data_4MWL # _entry.id 4MWL # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4MWL RCSB RCSB082456 WWPDB D_1000082456 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MWJ . unspecified PDB 4MWQ . unspecified PDB 4MWR . unspecified PDB 4MWU . unspecified PDB 4MWV . unspecified PDB 4MWW . unspecified PDB 4MWX . unspecified PDB 4MWY . unspecified PDB 4MX0 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MWL _pdbx_database_status.recvd_initial_deposition_date 2013-09-25 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.methods_development_category ? _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.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Wu, Y.' 1 'Qi, J.X.' 2 'Gao, F.' 3 'Gao, G.F.' 4 # _citation.id primary _citation.title 'Characterization of two distinct neuraminidases from avian-origin human-infecting H7N9 influenza viruses' _citation.journal_abbrev 'Cell Res.' _citation.journal_volume 23 _citation.page_first 1347 _citation.page_last 1355 _citation.year 2013 _citation.journal_id_ASTM ? _citation.country CN _citation.journal_id_ISSN 1001-0602 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24165891 _citation.pdbx_database_id_DOI 10.1038/cr.2013.144 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Wu, Y.' 1 primary 'Bi, Y.H.' 2 primary 'Vavricka, C.J.' 3 primary 'Sun, X.M.' 4 primary 'Zhang, Y.F.' 5 primary 'Gao, F.' 6 primary 'Zhao, M.' 7 primary 'Xiao, H.X.' 8 primary 'Qin, C.F.' 9 primary 'He, J.H.' 10 primary 'Liu, W.J.' 11 primary 'Yan, J.H.' 12 primary 'Qi, J.X.' 13 primary 'Gao, G.F.' 14 # _cell.entry_id 4MWL _cell.length_a 181.003 _cell.length_b 181.003 _cell.length_c 181.003 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 48 _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 4MWL _symmetry.space_group_name_H-M 'I 4 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 211 _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 Neuraminidase 43525.500 1 ? ? 'UNP residues 78-465' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 6 ? ? ? ? 5 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 6 water nat water 18.015 575 ? ? ? ? # _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 ;RNFNNLTKGLCTINSWHIYGKDNAVRIGESSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISW PLSSPPTVYNSRVECIGWSSTSCHDGKSRMSICISGPNNNASAVVWYNRRPVAEINTWARNILRTQESECVCHNGVCPVV FTDGSATGPADTRIYYFKEGKILKWESLTGTAKHIEECSCYGERTGITCTCKDNWQGSNRPVIQIDPVAMTHTSQYICSP VLTDNPRPNDPNIGKCNDPYPGNNNNGVKGFSYLDGANTWLGRTISTASRSGYEMLKVPNALTDDRSKPIQGQTIVLNAD WSGYSGSFMDYWAEGDCYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWNWPDGAKIEYFL ; _entity_poly.pdbx_seq_one_letter_code_can ;RNFNNLTKGLCTINSWHIYGKDNAVRIGESSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISW PLSSPPTVYNSRVECIGWSSTSCHDGKSRMSICISGPNNNASAVVWYNRRPVAEINTWARNILRTQESECVCHNGVCPVV FTDGSATGPADTRIYYFKEGKILKWESLTGTAKHIEECSCYGERTGITCTCKDNWQGSNRPVIQIDPVAMTHTSQYICSP VLTDNPRPNDPNIGKCNDPYPGNNNNGVKGFSYLDGANTWLGRTISTASRSGYEMLKVPNALTDDRSKPIQGQTIVLNAD WSGYSGSFMDYWAEGDCYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWNWPDGAKIEYFL ; _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 ARG n 1 2 ASN n 1 3 PHE n 1 4 ASN n 1 5 ASN n 1 6 LEU n 1 7 THR n 1 8 LYS n 1 9 GLY n 1 10 LEU n 1 11 CYS n 1 12 THR n 1 13 ILE n 1 14 ASN n 1 15 SER n 1 16 TRP n 1 17 HIS n 1 18 ILE n 1 19 TYR n 1 20 GLY n 1 21 LYS n 1 22 ASP n 1 23 ASN n 1 24 ALA n 1 25 VAL n 1 26 ARG n 1 27 ILE n 1 28 GLY n 1 29 GLU n 1 30 SER n 1 31 SER n 1 32 ASP n 1 33 VAL n 1 34 LEU n 1 35 VAL n 1 36 THR n 1 37 ARG n 1 38 GLU n 1 39 PRO n 1 40 TYR n 1 41 VAL n 1 42 SER n 1 43 CYS n 1 44 ASP n 1 45 PRO n 1 46 ASP n 1 47 GLU n 1 48 CYS n 1 49 ARG n 1 50 PHE n 1 51 TYR n 1 52 ALA n 1 53 LEU n 1 54 SER n 1 55 GLN n 1 56 GLY n 1 57 THR n 1 58 THR n 1 59 ILE n 1 60 ARG n 1 61 GLY n 1 62 LYS n 1 63 HIS n 1 64 SER n 1 65 ASN n 1 66 GLY n 1 67 THR n 1 68 ILE n 1 69 HIS n 1 70 ASP n 1 71 ARG n 1 72 SER n 1 73 GLN n 1 74 TYR n 1 75 ARG n 1 76 ALA n 1 77 LEU n 1 78 ILE n 1 79 SER n 1 80 TRP n 1 81 PRO n 1 82 LEU n 1 83 SER n 1 84 SER n 1 85 PRO n 1 86 PRO n 1 87 THR n 1 88 VAL n 1 89 TYR n 1 90 ASN n 1 91 SER n 1 92 ARG n 1 93 VAL n 1 94 GLU n 1 95 CYS n 1 96 ILE n 1 97 GLY n 1 98 TRP n 1 99 SER n 1 100 SER n 1 101 THR n 1 102 SER n 1 103 CYS n 1 104 HIS n 1 105 ASP n 1 106 GLY n 1 107 LYS n 1 108 SER n 1 109 ARG n 1 110 MET n 1 111 SER n 1 112 ILE n 1 113 CYS n 1 114 ILE n 1 115 SER n 1 116 GLY n 1 117 PRO n 1 118 ASN n 1 119 ASN n 1 120 ASN n 1 121 ALA n 1 122 SER n 1 123 ALA n 1 124 VAL n 1 125 VAL n 1 126 TRP n 1 127 TYR n 1 128 ASN n 1 129 ARG n 1 130 ARG n 1 131 PRO n 1 132 VAL n 1 133 ALA n 1 134 GLU n 1 135 ILE n 1 136 ASN n 1 137 THR n 1 138 TRP n 1 139 ALA n 1 140 ARG n 1 141 ASN n 1 142 ILE n 1 143 LEU n 1 144 ARG n 1 145 THR n 1 146 GLN n 1 147 GLU n 1 148 SER n 1 149 GLU n 1 150 CYS n 1 151 VAL n 1 152 CYS n 1 153 HIS n 1 154 ASN n 1 155 GLY n 1 156 VAL n 1 157 CYS n 1 158 PRO n 1 159 VAL n 1 160 VAL n 1 161 PHE n 1 162 THR n 1 163 ASP n 1 164 GLY n 1 165 SER n 1 166 ALA n 1 167 THR n 1 168 GLY n 1 169 PRO n 1 170 ALA n 1 171 ASP n 1 172 THR n 1 173 ARG n 1 174 ILE n 1 175 TYR n 1 176 TYR n 1 177 PHE n 1 178 LYS n 1 179 GLU n 1 180 GLY n 1 181 LYS n 1 182 ILE n 1 183 LEU n 1 184 LYS n 1 185 TRP n 1 186 GLU n 1 187 SER n 1 188 LEU n 1 189 THR n 1 190 GLY n 1 191 THR n 1 192 ALA n 1 193 LYS n 1 194 HIS n 1 195 ILE n 1 196 GLU n 1 197 GLU n 1 198 CYS n 1 199 SER n 1 200 CYS n 1 201 TYR n 1 202 GLY n 1 203 GLU n 1 204 ARG n 1 205 THR n 1 206 GLY n 1 207 ILE n 1 208 THR n 1 209 CYS n 1 210 THR n 1 211 CYS n 1 212 LYS n 1 213 ASP n 1 214 ASN n 1 215 TRP n 1 216 GLN n 1 217 GLY n 1 218 SER n 1 219 ASN n 1 220 ARG n 1 221 PRO n 1 222 VAL n 1 223 ILE n 1 224 GLN n 1 225 ILE n 1 226 ASP n 1 227 PRO n 1 228 VAL n 1 229 ALA n 1 230 MET n 1 231 THR n 1 232 HIS n 1 233 THR n 1 234 SER n 1 235 GLN n 1 236 TYR n 1 237 ILE n 1 238 CYS n 1 239 SER n 1 240 PRO n 1 241 VAL n 1 242 LEU n 1 243 THR n 1 244 ASP n 1 245 ASN n 1 246 PRO n 1 247 ARG n 1 248 PRO n 1 249 ASN n 1 250 ASP n 1 251 PRO n 1 252 ASN n 1 253 ILE n 1 254 GLY n 1 255 LYS n 1 256 CYS n 1 257 ASN n 1 258 ASP n 1 259 PRO n 1 260 TYR n 1 261 PRO n 1 262 GLY n 1 263 ASN n 1 264 ASN n 1 265 ASN n 1 266 ASN n 1 267 GLY n 1 268 VAL n 1 269 LYS n 1 270 GLY n 1 271 PHE n 1 272 SER n 1 273 TYR n 1 274 LEU n 1 275 ASP n 1 276 GLY n 1 277 ALA n 1 278 ASN n 1 279 THR n 1 280 TRP n 1 281 LEU n 1 282 GLY n 1 283 ARG n 1 284 THR n 1 285 ILE n 1 286 SER n 1 287 THR n 1 288 ALA n 1 289 SER n 1 290 ARG n 1 291 SER n 1 292 GLY n 1 293 TYR n 1 294 GLU n 1 295 MET n 1 296 LEU n 1 297 LYS n 1 298 VAL n 1 299 PRO n 1 300 ASN n 1 301 ALA n 1 302 LEU n 1 303 THR n 1 304 ASP n 1 305 ASP n 1 306 ARG n 1 307 SER n 1 308 LYS n 1 309 PRO n 1 310 ILE n 1 311 GLN n 1 312 GLY n 1 313 GLN n 1 314 THR n 1 315 ILE n 1 316 VAL n 1 317 LEU n 1 318 ASN n 1 319 ALA n 1 320 ASP n 1 321 TRP n 1 322 SER n 1 323 GLY n 1 324 TYR n 1 325 SER n 1 326 GLY n 1 327 SER n 1 328 PHE n 1 329 MET n 1 330 ASP n 1 331 TYR n 1 332 TRP n 1 333 ALA n 1 334 GLU n 1 335 GLY n 1 336 ASP n 1 337 CYS n 1 338 TYR n 1 339 ARG n 1 340 ALA n 1 341 CYS n 1 342 PHE n 1 343 TYR n 1 344 VAL n 1 345 GLU n 1 346 LEU n 1 347 ILE n 1 348 ARG n 1 349 GLY n 1 350 ARG n 1 351 PRO n 1 352 LYS n 1 353 GLU n 1 354 ASP n 1 355 LYS n 1 356 VAL n 1 357 TRP n 1 358 TRP n 1 359 THR n 1 360 SER n 1 361 ASN n 1 362 SER n 1 363 ILE n 1 364 VAL n 1 365 SER n 1 366 MET n 1 367 CYS n 1 368 SER n 1 369 SER n 1 370 THR n 1 371 GLU n 1 372 PHE n 1 373 LEU n 1 374 GLY n 1 375 GLN n 1 376 TRP n 1 377 ASN n 1 378 TRP n 1 379 PRO n 1 380 ASP n 1 381 GLY n 1 382 ALA n 1 383 LYS n 1 384 ILE n 1 385 GLU n 1 386 TYR n 1 387 PHE n 1 388 LEU n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene NA _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'A/Shanghai/1/2013(H7N9)' _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 'Influenza A virus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11320 _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 'fall armyworm' _entity_src_gen.pdbx_host_org_scientific_name 'Spodoptera frugiperda' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type Baculovirus _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 4MWL _struct_ref.pdbx_db_accession 4MWL _struct_ref.entity_id 1 _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4MWL _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 388 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 4MWL _struct_ref_seq.db_align_beg 83 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 470 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 83 _struct_ref_seq.pdbx_auth_seq_align_end 470 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4MWL _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.84 _exptl_crystal.density_percent_sol 56.67 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 291 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.5 _exptl_crystal_grow.pdbx_details ;5%(v/v)(+/-)-2-Methyl-2,4-pentanediol, 0.1M HEPES, 10% Polyethylene glycol 10000, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K ; _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 CCD _diffrn_detector.type 'ADSC QUANTUM 315' _diffrn_detector.pdbx_collection_date 2013-05-19 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator GRAPHITE _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9793 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SSRF BEAMLINE BL17U' _diffrn_source.pdbx_synchrotron_site SSRF _diffrn_source.pdbx_synchrotron_beamline BL17U _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.9793 # _reflns.entry_id 4MWL _reflns.observed_criterion_sigma_I 3.0 _reflns.observed_criterion_sigma_F 2.0 _reflns.d_resolution_low 50 _reflns.d_resolution_high 1.8 _reflns.number_obs 46782 _reflns.number_all 46782 _reflns.percent_possible_obs 100 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 13.270 _reflns.pdbx_redundancy ? _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 1.8 _reflns_shell.d_res_low ? _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 4MWL _refine.ls_number_reflns_obs 46781 _refine.ls_number_reflns_all 46804 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.34 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 42.663 _refine.ls_d_res_high 1.800 _refine.ls_percent_reflns_obs 99.95 _refine.ls_R_factor_obs 0.1382 _refine.ls_R_factor_all 0.1382 _refine.ls_R_factor_R_work 0.1372 _refine.ls_R_factor_R_free 0.1560 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.05 _refine.ls_number_reflns_R_free 2361 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.B_iso_mean 12.6387 _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.11 _refine.overall_FOM_work_R_set 0.9216 _refine.B_iso_max 62.870 _refine.B_iso_min 2.290 _refine.pdbx_overall_phase_error 13.5400 _refine.occupancy_max 1.000 _refine.occupancy_min 0.370 _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_redundancy_reflns_obs ? _refine.overall_SU_B ? _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.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _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 3053 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 134 _refine_hist.number_atoms_solvent 575 _refine_hist.number_atoms_total 3762 _refine_hist.d_res_high 1.800 _refine_hist.d_res_low 42.663 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' f_bond_d 3318 0.006 ? ? ? 'X-RAY DIFFRACTION' f_angle_d 4528 1.086 ? ? ? 'X-RAY DIFFRACTION' f_chiral_restr 506 0.074 ? ? ? 'X-RAY DIFFRACTION' f_plane_restr 570 0.005 ? ? ? 'X-RAY DIFFRACTION' f_dihedral_angle_d 1253 22.922 ? ? ? # loop_ _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.percent_reflns_obs _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_R_work _refine_ls_shell.R_factor_R_free _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.pdbx_refine_id _refine_ls_shell.redundancy_reflns_obs 1.8000 1.8367 17 100.0000 2561 . 0.1584 0.1760 . 128 . 2689 . 'X-RAY DIFFRACTION' . 1.8367 1.8767 17 100.0000 2575 . 0.1430 0.1689 . 135 . 2710 . 'X-RAY DIFFRACTION' . 1.8767 1.9203 17 100.0000 2581 . 0.1388 0.1516 . 133 . 2714 . 'X-RAY DIFFRACTION' . 1.9203 1.9683 17 100.0000 2569 . 0.1385 0.1557 . 139 . 2708 . 'X-RAY DIFFRACTION' . 1.9683 2.0216 17 100.0000 2575 . 0.1387 0.1662 . 149 . 2724 . 'X-RAY DIFFRACTION' . 2.0216 2.0810 17 100.0000 2585 . 0.1329 0.1555 . 136 . 2721 . 'X-RAY DIFFRACTION' . 2.0810 2.1482 17 100.0000 2574 . 0.1326 0.1692 . 134 . 2708 . 'X-RAY DIFFRACTION' . 2.1482 2.2250 17 100.0000 2588 . 0.1340 0.1512 . 135 . 2723 . 'X-RAY DIFFRACTION' . 2.2250 2.3141 17 100.0000 2575 . 0.1308 0.1622 . 143 . 2718 . 'X-RAY DIFFRACTION' . 2.3141 2.4194 17 100.0000 2609 . 0.1364 0.1774 . 146 . 2755 . 'X-RAY DIFFRACTION' . 2.4194 2.5469 17 100.0000 2584 . 0.1402 0.1734 . 145 . 2729 . 'X-RAY DIFFRACTION' . 2.5469 2.7065 17 100.0000 2601 . 0.1426 0.1804 . 152 . 2753 . 'X-RAY DIFFRACTION' . 2.7065 2.9154 17 100.0000 2616 . 0.1400 0.1695 . 143 . 2759 . 'X-RAY DIFFRACTION' . 2.9154 3.2087 17 100.0000 2655 . 0.1394 0.1484 . 115 . 2770 . 'X-RAY DIFFRACTION' . 3.2087 3.6728 17 100.0000 2648 . 0.1301 0.1221 . 146 . 2794 . 'X-RAY DIFFRACTION' . 3.6728 4.6264 17 100.0000 2691 . 0.1199 0.1314 . 131 . 2822 . 'X-RAY DIFFRACTION' . 4.6264 42.6748 17 100.0000 2833 . 0.1565 0.1630 . 151 . 2984 . 'X-RAY DIFFRACTION' . # _struct.entry_id 4MWL _struct.title 'Shanghai N9' _struct.pdbx_descriptor Neuraminidase _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MWL _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text '6-BLADED BETA-PROPELLER, HYDROLASE, Glycosylation' # 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 3 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 4 ? M N N 5 ? N N N 6 ? # _struct_biol.id 1 _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 ASN A 23 ? GLU A 29 ? ASN A 105 GLU A 111 1 ? 7 HELX_P HELX_P2 2 GLY A 61 ? ASN A 65 ? GLY A 143 ASN A 147 5 ? 5 HELX_P HELX_P3 3 ASP A 275 ? ASN A 278 ? ASP A 357 ASN A 360 5 ? 4 HELX_P HELX_P4 4 LYS A 383 ? LEU A 388 ? LYS A 465 LEU A 470 5 ? 6 # _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 337 SG ? ? A CYS 93 A CYS 419 1_555 ? ? ? ? ? ? ? 2.041 ? disulf2 disulf ? ? A CYS 43 SG ? ? ? 1_555 A CYS 48 SG ? ? A CYS 125 A CYS 130 1_555 ? ? ? ? ? ? ? 2.039 ? disulf3 disulf ? ? A CYS 95 SG ? ? ? 1_555 A CYS 113 SG ? ? A CYS 177 A CYS 195 1_555 ? ? ? ? ? ? ? 2.038 ? disulf4 disulf ? ? A CYS 103 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 185 A CYS 232 1_555 ? ? ? ? ? ? ? 2.030 ? disulf5 disulf ? ? A CYS 152 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 234 A CYS 239 1_555 ? ? ? ? ? ? ? 2.035 ? disulf6 disulf ? ? A CYS 198 SG ? ? ? 1_555 A CYS 211 SG ? ? A CYS 280 A CYS 293 1_555 ? ? ? ? ? ? ? 2.050 ? disulf7 disulf ? ? A CYS 200 SG ? ? ? 1_555 A CYS 209 SG ? ? A CYS 282 A CYS 291 1_555 ? ? ? ? ? ? ? 2.047 ? disulf8 disulf ? ? A CYS 238 SG ? ? ? 1_555 A CYS 256 SG ? ? A CYS 320 A CYS 338 1_555 ? ? ? ? ? ? ? 2.029 ? disulf9 disulf ? ? A CYS 341 SG ? ? ? 1_555 A CYS 367 SG ? ? A CYS 423 A CYS 449 1_555 ? ? ? ? ? ? ? 2.042 ? covale1 covale ? ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 505 A MAN 506 1_555 ? ? ? ? ? ? ? 1.435 ? covale2 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 504 A BMA 505 1_555 ? ? ? ? ? ? ? 1.437 ? covale3 covale ? ? G MAN . O2 ? ? ? 1_555 H MAN . C1 ? ? A MAN 506 A MAN 507 1_555 ? ? ? ? ? ? ? 1.437 ? covale4 covale ? ? F BMA . O6 ? ? ? 1_555 J MAN . C1 ? ? A BMA 505 A MAN 509 1_555 ? ? ? ? ? ? ? 1.438 ? covale5 covale ? ? H MAN . O2 ? ? ? 1_555 I MAN . C1 ? ? A MAN 507 A MAN 508 1_555 ? ? ? ? ? ? ? 1.438 ? covale6 covale ? ? J MAN . O6 ? ? ? 1_555 K MAN . C1 ? ? A MAN 509 A MAN 510 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 503 A NAG 504 1_555 ? ? ? ? ? ? ? 1.443 ? covale8 covale ? ? A ASN 5 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 87 A NAG 501 1_555 ? ? ? ? ? ? ? 1.443 ? covale9 covale ? ? A ASN 65 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 147 A NAG 502 1_555 ? ? ? ? ? ? ? 1.443 ? covale10 covale ? ? J MAN . O3 ? ? ? 1_555 L MAN . C1 ? ? A MAN 509 A MAN 511 1_555 ? ? ? ? ? ? ? 1.444 ? covale11 covale ? ? A ASN 120 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 202 A NAG 503 1_555 ? ? ? ? ? ? ? 1.448 ? metalc1 metalc ? ? A GLY 217 O ? ? ? 1_555 M CA . CA ? ? A GLY 299 A CA 512 1_555 ? ? ? ? ? ? ? 2.351 ? metalc2 metalc ? ? A ASP 244 OD2 ? ? ? 1_555 M CA . CA ? ? A ASP 326 A CA 512 1_555 ? ? ? ? ? ? ? 2.386 ? metalc3 metalc ? ? M CA . CA ? ? ? 1_555 N HOH . O ? ? A CA 512 A HOH 639 1_555 ? ? ? ? ? ? ? 2.413 ? metalc4 metalc ? ? A ASP 213 O ? ? ? 1_555 M CA . CA ? ? A ASP 295 A CA 512 1_555 ? ? ? ? ? ? ? 2.431 ? metalc5 metalc ? ? A ASN 266 O ? ? ? 1_555 M CA . CA ? ? A ASN 348 A CA 512 1_555 ? ? ? ? ? ? ? 2.525 ? metalc6 metalc ? ? M CA . CA ? ? ? 1_555 N HOH . O ? ? A CA 512 A HOH 621 1_555 ? ? ? ? ? ? ? 2.529 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 245 A . ? ASN 327 A PRO 246 A ? PRO 328 A 1 -1.30 2 ARG 350 A . ? ARG 432 A PRO 351 A ? PRO 433 A 1 5.26 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 3 ? F ? 4 ? G ? 4 ? # 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 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? 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 F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? 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 GLY A 9 ? LEU A 10 ? GLY A 91 LEU A 92 A 2 CYS A 337 ? TYR A 338 ? CYS A 419 TYR A 420 B 1 SER A 15 ? LYS A 21 ? SER A 97 LYS A 103 B 2 THR A 359 ? SER A 369 ? THR A 441 SER A 451 B 3 ALA A 340 ? GLY A 349 ? ALA A 422 GLY A 431 B 4 SER A 325 ? MET A 329 ? SER A 407 MET A 411 C 1 LEU A 34 ? CYS A 43 ? LEU A 116 CYS A 125 C 2 CYS A 48 ? THR A 58 ? CYS A 130 THR A 140 C 3 ALA A 76 ? PRO A 81 ? ALA A 158 PRO A 163 C 4 ARG A 92 ? ILE A 96 ? ARG A 174 ILE A 178 D 1 SER A 99 ? HIS A 104 ? SER A 181 HIS A 186 D 2 ARG A 109 ? SER A 115 ? ARG A 191 SER A 197 D 3 SER A 122 ? TYR A 127 ? SER A 204 TYR A 209 D 4 ARG A 130 ? ASN A 136 ? ARG A 212 ASN A 218 E 1 CYS A 157 ? GLY A 164 ? CYS A 239 GLY A 246 E 2 ALA A 170 ? LYS A 178 ? ALA A 252 LYS A 260 E 3 LYS A 181 ? SER A 187 ? LYS A 263 SER A 269 F 1 GLU A 196 ? GLU A 203 ? GLU A 278 GLU A 285 F 2 GLY A 206 ? LYS A 212 ? GLY A 288 LYS A 294 F 3 PRO A 221 ? ASP A 226 ? PRO A 303 ASP A 308 F 4 THR A 231 ? TYR A 236 ? THR A 313 TYR A 318 G 1 SER A 272 ? TYR A 273 ? SER A 354 TYR A 355 G 2 TRP A 280 ? ARG A 283 ? TRP A 362 ARG A 365 G 3 SER A 291 ? LYS A 297 ? SER A 373 LYS A 379 G 4 GLN A 311 ? TRP A 321 ? GLN A 393 TRP A 403 # 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 GLY A 9 ? N GLY A 91 O TYR A 338 ? O TYR A 420 B 1 2 N HIS A 17 ? N HIS A 99 O CYS A 367 ? O CYS A 449 B 2 3 O VAL A 364 ? O VAL A 446 N VAL A 344 ? N VAL A 426 B 3 4 O TYR A 343 ? O TYR A 425 N GLY A 326 ? N GLY A 408 C 1 2 N TYR A 40 ? N TYR A 122 O TYR A 51 ? O TYR A 133 C 2 3 N SER A 54 ? N SER A 136 O ALA A 76 ? O ALA A 158 C 3 4 N SER A 79 ? N SER A 161 O ARG A 92 ? O ARG A 174 D 1 2 N CYS A 103 ? N CYS A 185 O MET A 110 ? O MET A 192 D 2 3 N SER A 111 ? N SER A 193 O TRP A 126 ? O TRP A 208 D 3 4 N VAL A 125 ? N VAL A 207 O ALA A 133 ? O ALA A 215 E 1 2 N CYS A 157 ? N CYS A 239 O PHE A 177 ? O PHE A 259 E 2 3 N TYR A 176 ? N TYR A 258 O LEU A 183 ? O LEU A 265 F 1 2 N GLU A 203 ? N GLU A 285 O GLY A 206 ? O GLY A 288 F 2 3 N ILE A 207 ? N ILE A 289 O ILE A 225 ? O ILE A 307 F 3 4 N VAL A 222 ? N VAL A 304 O GLN A 235 ? O GLN A 317 G 1 2 N TYR A 273 ? N TYR A 355 O TRP A 280 ? O TRP A 362 G 2 3 N LEU A 281 ? N LEU A 363 O LEU A 296 ? O LEU A 378 G 3 4 N TYR A 293 ? N TYR A 375 O ILE A 315 ? O ILE A 397 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 512' AC2 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A 501 BOUND TO ASN A 87' AC3 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG A 502 BOUND TO ASN A 147' AC4 Software ? ? ? ? 46 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 202 RESIDUES 503 TO 511' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASP A 213 ? ASP A 295 . ? 1_555 ? 2 AC1 6 GLY A 217 ? GLY A 299 . ? 1_555 ? 3 AC1 6 ASP A 244 ? ASP A 326 . ? 1_555 ? 4 AC1 6 ASN A 266 ? ASN A 348 . ? 1_555 ? 5 AC1 6 HOH N . ? HOH A 621 . ? 1_555 ? 6 AC1 6 HOH N . ? HOH A 639 . ? 1_555 ? 7 AC2 5 ASN A 2 ? ASN A 84 . ? 1_555 ? 8 AC2 5 PHE A 3 ? PHE A 85 . ? 1_555 ? 9 AC2 5 ASN A 5 ? ASN A 87 . ? 1_555 ? 10 AC2 5 ASN A 154 ? ASN A 236 . ? 1_555 ? 11 AC2 5 HOH N . ? HOH A 1071 . ? 1_555 ? 12 AC3 4 ASN A 65 ? ASN A 147 . ? 1_555 ? 13 AC3 4 TRP A 357 ? TRP A 439 . ? 1_555 ? 14 AC3 4 HOH N . ? HOH A 1091 . ? 1_555 ? 15 AC3 4 HOH N . ? HOH A 1143 . ? 1_555 ? 16 AC4 46 ASN A 120 ? ASN A 202 . ? 1_555 ? 17 AC4 46 ARG A 247 ? ARG A 329 . ? 15_555 ? 18 AC4 46 ASN A 249 ? ASN A 331 . ? 15_555 ? 19 AC4 46 ASP A 250 ? ASP A 332 . ? 15_555 ? 20 AC4 46 ARG A 283 ? ARG A 365 . ? 15_555 ? 21 AC4 46 ILE A 285 ? ILE A 367 . ? 15_555 ? 22 AC4 46 THR A 287 ? THR A 369 . ? 15_555 ? 23 AC4 46 GLU A 294 ? GLU A 376 . ? 15_555 ? 24 AC4 46 LEU A 296 ? LEU A 378 . ? 15_555 ? 25 AC4 46 PRO A 309 ? PRO A 391 . ? 15_555 ? 26 AC4 46 ILE A 310 ? ILE A 392 . ? 15_555 ? 27 AC4 46 GLN A 311 ? GLN A 393 . ? 15_555 ? 28 AC4 46 GLY A 312 ? GLY A 394 . ? 15_555 ? 29 AC4 46 LEU A 373 ? LEU A 455 . ? 15_555 ? 30 AC4 46 GLY A 374 ? GLY A 456 . ? 15_555 ? 31 AC4 46 GLN A 375 ? GLN A 457 . ? 15_555 ? 32 AC4 46 HOH N . ? HOH A 611 . ? 15_555 ? 33 AC4 46 HOH N . ? HOH A 645 . ? 15_555 ? 34 AC4 46 HOH N . ? HOH A 654 . ? 15_555 ? 35 AC4 46 HOH N . ? HOH A 661 . ? 1_555 ? 36 AC4 46 HOH N . ? HOH A 772 . ? 1_555 ? 37 AC4 46 HOH N . ? HOH A 808 . ? 15_555 ? 38 AC4 46 HOH N . ? HOH A 851 . ? 1_555 ? 39 AC4 46 HOH N . ? HOH A 852 . ? 1_555 ? 40 AC4 46 HOH N . ? HOH A 855 . ? 1_555 ? 41 AC4 46 HOH N . ? HOH A 862 . ? 1_555 ? 42 AC4 46 HOH N . ? HOH A 889 . ? 1_555 ? 43 AC4 46 HOH N . ? HOH A 896 . ? 1_555 ? 44 AC4 46 HOH N . ? HOH A 916 . ? 1_555 ? 45 AC4 46 HOH N . ? HOH A 922 . ? 1_555 ? 46 AC4 46 HOH N . ? HOH A 927 . ? 1_555 ? 47 AC4 46 HOH N . ? HOH A 936 . ? 1_555 ? 48 AC4 46 HOH N . ? HOH A 963 . ? 1_555 ? 49 AC4 46 HOH N . ? HOH A 964 . ? 1_555 ? 50 AC4 46 HOH N . ? HOH A 986 . ? 1_555 ? 51 AC4 46 HOH N . ? HOH A 1008 . ? 15_555 ? 52 AC4 46 HOH N . ? HOH A 1030 . ? 1_555 ? 53 AC4 46 HOH N . ? HOH A 1033 . ? 15_555 ? 54 AC4 46 HOH N . ? HOH A 1050 . ? 1_555 ? 55 AC4 46 HOH N . ? HOH A 1060 . ? 1_555 ? 56 AC4 46 HOH N . ? HOH A 1070 . ? 15_555 ? 57 AC4 46 HOH N . ? HOH A 1087 . ? 1_555 ? 58 AC4 46 HOH N . ? HOH A 1100 . ? 1_555 ? 59 AC4 46 HOH N . ? HOH A 1103 . ? 1_555 ? 60 AC4 46 HOH N . ? HOH A 1111 . ? 1_555 ? 61 AC4 46 HOH N . ? HOH A 1147 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MWL _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4MWL _atom_sites.fract_transf_matrix[1][1] 0.005525 _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] 0.005525 _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] 0.005525 _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 CA 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 . ARG A 1 1 ? 10.331 7.955 30.247 1.00 41.32 ? 83 ARG A N 1 ATOM 2 C CA . ARG A 1 1 ? 10.709 9.094 31.077 1.00 26.86 ? 83 ARG A CA 1 ATOM 3 C C . ARG A 1 1 ? 11.979 9.779 30.575 1.00 28.19 ? 83 ARG A C 1 ATOM 4 O O . ARG A 1 1 ? 12.876 9.132 30.032 1.00 26.83 ? 83 ARG A O 1 ATOM 5 C CB . ARG A 1 1 ? 10.906 8.658 32.531 1.00 32.28 ? 83 ARG A CB 1 ATOM 6 C CG . ARG A 1 1 ? 9.639 8.612 33.373 1.00 38.07 ? 83 ARG A CG 1 ATOM 7 C CD . ARG A 1 1 ? 9.999 8.398 34.835 1.00 35.24 ? 83 ARG A CD 1 ATOM 8 N NE . ARG A 1 1 ? 8.837 8.428 35.717 1.00 48.32 ? 83 ARG A NE 1 ATOM 9 C CZ . ARG A 1 1 ? 8.900 8.272 37.035 1.00 41.23 ? 83 ARG A CZ 1 ATOM 10 N NH1 . ARG A 1 1 ? 10.072 8.078 37.624 1.00 40.02 ? 83 ARG A NH1 1 ATOM 11 N NH2 . ARG A 1 1 ? 7.794 8.311 37.767 1.00 38.28 ? 83 ARG A NH2 1 ATOM 12 N N . ASN A 1 2 ? 12.049 11.094 30.761 1.00 22.69 ? 84 ASN A N 1 ATOM 13 C CA . ASN A 1 2 ? 13.242 11.854 30.403 1.00 21.09 ? 84 ASN A CA 1 ATOM 14 C C . ASN A 1 2 ? 13.895 12.474 31.632 1.00 16.96 ? 84 ASN A C 1 ATOM 15 O O . ASN A 1 2 ? 13.219 12.719 32.633 1.00 17.89 ? 84 ASN A O 1 ATOM 16 C CB . ASN A 1 2 ? 12.897 12.955 29.400 1.00 25.32 ? 84 ASN A CB 1 ATOM 17 C CG . ASN A 1 2 ? 12.448 12.406 28.062 1.00 37.20 ? 84 ASN A CG 1 ATOM 18 O OD1 . ASN A 1 2 ? 13.254 11.880 27.294 1.00 37.47 ? 84 ASN A OD1 1 ATOM 19 N ND2 . ASN A 1 2 ? 11.159 12.535 27.770 1.00 38.80 ? 84 ASN A ND2 1 ATOM 20 N N . PHE A 1 3 ? 15.203 12.720 31.560 1.00 11.74 ? 85 PHE A N 1 ATOM 21 C CA . PHE A 1 3 ? 15.890 13.448 32.622 1.00 11.60 ? 85 PHE A CA 1 ATOM 22 C C . PHE A 1 3 ? 15.305 14.848 32.702 1.00 15.18 ? 85 PHE A C 1 ATOM 23 O O . PHE A 1 3 ? 15.028 15.465 31.676 1.00 14.08 ? 85 PHE A O 1 ATOM 24 C CB . PHE A 1 3 ? 17.386 13.560 32.329 1.00 11.30 ? 85 PHE A CB 1 ATOM 25 C CG . PHE A 1 3 ? 18.141 12.273 32.493 1.00 17.01 ? 85 PHE A CG 1 ATOM 26 C CD1 . PHE A 1 3 ? 18.000 11.511 33.645 1.00 10.79 ? 85 PHE A CD1 1 ATOM 27 C CD2 . PHE A 1 3 ? 19.000 11.830 31.496 1.00 14.04 ? 85 PHE A CD2 1 ATOM 28 C CE1 . PHE A 1 3 ? 18.700 10.328 33.800 1.00 14.12 ? 85 PHE A CE1 1 ATOM 29 C CE2 . PHE A 1 3 ? 19.704 10.651 31.643 1.00 13.69 ? 85 PHE A CE2 1 ATOM 30 C CZ . PHE A 1 3 ? 19.555 9.895 32.796 1.00 12.90 ? 85 PHE A CZ 1 ATOM 31 N N . ASN A 1 4 ? 15.114 15.355 33.913 1.00 12.57 ? 86 ASN A N 1 ATOM 32 C CA . ASN A 1 4 ? 14.634 16.719 34.062 1.00 11.32 ? 86 ASN A CA 1 ATOM 33 C C . ASN A 1 4 ? 15.726 17.738 33.756 1.00 10.98 ? 86 ASN A C 1 ATOM 34 O O . ASN A 1 4 ? 16.871 17.573 34.178 1.00 11.72 ? 86 ASN A O 1 ATOM 35 C CB . ASN A 1 4 ? 14.099 16.949 35.473 1.00 9.80 ? 86 ASN A CB 1 ATOM 36 C CG . ASN A 1 4 ? 13.576 18.350 35.662 1.00 13.67 ? 86 ASN A CG 1 ATOM 37 O OD1 . ASN A 1 4 ? 14.101 19.123 36.465 1.00 14.91 ? 86 ASN A OD1 1 ATOM 38 N ND2 . ASN A 1 4 ? 12.545 18.696 34.904 1.00 8.54 ? 86 ASN A ND2 1 ATOM 39 N N . ASN A 1 5 ? 15.369 18.792 33.026 1.00 10.38 ? 87 ASN A N 1 ATOM 40 C CA . ASN A 1 5 ? 16.277 19.912 32.807 1.00 9.59 ? 87 ASN A CA 1 ATOM 41 C C . ASN A 1 5 ? 15.781 21.135 33.563 1.00 8.54 ? 87 ASN A C 1 ATOM 42 O O . ASN A 1 5 ? 14.577 21.347 33.679 1.00 12.19 ? 87 ASN A O 1 ATOM 43 C CB . ASN A 1 5 ? 16.382 20.237 31.317 1.00 12.90 ? 87 ASN A CB 1 ATOM 44 C CG . ASN A 1 5 ? 16.847 19.054 30.497 1.00 21.79 ? 87 ASN A CG 1 ATOM 45 O OD1 . ASN A 1 5 ? 17.806 18.371 30.865 1.00 16.80 ? 87 ASN A OD1 1 ATOM 46 N ND2 . ASN A 1 5 ? 16.154 18.796 29.384 1.00 24.28 ? 87 ASN A ND2 1 ATOM 47 N N . LEU A 1 6 ? 16.708 21.934 34.077 1.00 9.89 ? 88 LEU A N 1 ATOM 48 C CA . LEU A 1 6 ? 16.349 23.134 34.819 1.00 9.14 ? 88 LEU A CA 1 ATOM 49 C C . LEU A 1 6 ? 16.090 24.298 33.863 1.00 12.63 ? 88 LEU A C 1 ATOM 50 O O . LEU A 1 6 ? 16.965 25.132 33.647 1.00 16.92 ? 88 LEU A O 1 ATOM 51 C CB . LEU A 1 6 ? 17.469 23.493 35.792 1.00 8.24 ? 88 LEU A CB 1 ATOM 52 C CG . LEU A 1 6 ? 17.796 22.399 36.813 1.00 10.10 ? 88 LEU A CG 1 ATOM 53 C CD1 . LEU A 1 6 ? 19.062 22.747 37.581 1.00 11.39 ? 88 LEU A CD1 1 ATOM 54 C CD2 . LEU A 1 6 ? 16.618 22.198 37.766 1.00 9.83 ? 88 LEU A CD2 1 ATOM 55 N N . THR A 1 7 ? 14.882 24.360 33.312 1.00 12.37 ? 89 THR A N 1 ATOM 56 C CA . THR A 1 7 ? 14.578 25.300 32.231 1.00 12.63 ? 89 THR A CA 1 ATOM 57 C C . THR A 1 7 ? 13.823 26.542 32.688 1.00 17.94 ? 89 THR A C 1 ATOM 58 O O . THR A 1 7 ? 13.613 27.464 31.900 1.00 16.30 ? 89 THR A O 1 ATOM 59 C CB . THR A 1 7 ? 13.730 24.629 31.139 1.00 10.35 ? 89 THR A CB 1 ATOM 60 O OG1 . THR A 1 7 ? 12.451 24.266 31.680 1.00 15.98 ? 89 THR A OG1 1 ATOM 61 C CG2 . THR A 1 7 ? 14.426 23.391 30.602 1.00 12.39 ? 89 THR A CG2 1 ATOM 62 N N . LYS A 1 8 ? 13.404 26.563 33.949 1.00 10.46 ? 90 LYS A N 1 ATOM 63 C CA . LYS A 1 8 ? 12.572 27.655 34.449 1.00 12.24 ? 90 LYS A CA 1 ATOM 64 C C . LYS A 1 8 ? 13.300 28.521 35.475 1.00 14.83 ? 90 LYS A C 1 ATOM 65 O O . LYS A 1 8 ? 14.284 28.094 36.081 1.00 12.83 ? 90 LYS A O 1 ATOM 66 C CB . LYS A 1 8 ? 11.288 27.092 35.065 1.00 11.49 ? 90 LYS A CB 1 ATOM 67 C CG . LYS A 1 8 ? 10.528 26.148 34.137 1.00 12.55 ? 90 LYS A CG 1 ATOM 68 C CD . LYS A 1 8 ? 9.351 25.486 34.843 1.00 15.50 ? 90 LYS A CD 1 ATOM 69 C CE . LYS A 1 8 ? 8.565 24.600 33.884 1.00 16.85 ? 90 LYS A CE 1 ATOM 70 N NZ . LYS A 1 8 ? 7.462 23.872 34.570 1.00 16.96 ? 90 LYS A NZ 1 ATOM 71 N N . GLY A 1 9 ? 12.817 29.744 35.661 1.00 10.03 ? 91 GLY A N 1 ATOM 72 C CA . GLY A 1 9 ? 13.313 30.589 36.732 1.00 10.35 ? 91 GLY A CA 1 ATOM 73 C C . GLY A 1 9 ? 12.428 30.413 37.950 1.00 12.51 ? 91 GLY A C 1 ATOM 74 O O . GLY A 1 9 ? 11.422 29.698 37.887 1.00 10.41 ? 91 GLY A O 1 ATOM 75 N N . LEU A 1 10 ? 12.795 31.047 39.060 1.00 9.78 ? 92 LEU A N 1 ATOM 76 C CA . LEU A 1 10 ? 11.963 31.003 40.260 1.00 10.44 ? 92 LEU A CA 1 ATOM 77 C C . LEU A 1 10 ? 10.703 31.828 40.060 1.00 13.59 ? 92 LEU A C 1 ATOM 78 O O . LEU A 1 10 ? 10.737 32.880 39.417 1.00 8.75 ? 92 LEU A O 1 ATOM 79 C CB . LEU A 1 10 ? 12.721 31.551 41.471 1.00 7.28 ? 92 LEU A CB 1 ATOM 80 C CG . LEU A 1 10 ? 14.011 30.853 41.898 1.00 11.12 ? 92 LEU A CG 1 ATOM 81 C CD1 . LEU A 1 10 ? 14.535 31.468 43.182 1.00 7.86 ? 92 LEU A CD1 1 ATOM 82 C CD2 . LEU A 1 10 ? 13.786 29.365 42.068 1.00 10.59 ? 92 LEU A CD2 1 ATOM 83 N N . CYS A 1 11 ? 9.593 31.357 40.616 1.00 9.05 ? 93 CYS A N 1 ATOM 84 C CA . CYS A 1 11 ? 8.390 32.173 40.689 1.00 10.75 ? 93 CYS A CA 1 ATOM 85 C C . CYS A 1 11 ? 8.673 33.379 41.573 1.00 9.85 ? 93 CYS A C 1 ATOM 86 O O . CYS A 1 11 ? 9.516 33.317 42.472 1.00 9.65 ? 93 CYS A O 1 ATOM 87 C CB . CYS A 1 11 ? 7.227 31.369 41.277 1.00 9.12 ? 93 CYS A CB 1 ATOM 88 S SG . CYS A 1 11 ? 6.762 29.929 40.301 1.00 11.82 ? 93 CYS A SG 1 ATOM 89 N N . THR A 1 12 ? 7.976 34.478 41.314 1.00 9.66 ? 94 THR A N 1 ATOM 90 C CA . THR A 1 12 ? 8.077 35.655 42.172 1.00 9.18 ? 94 THR A CA 1 ATOM 91 C C . THR A 1 12 ? 7.532 35.344 43.563 1.00 10.62 ? 94 THR A C 1 ATOM 92 O O . THR A 1 12 ? 6.390 34.898 43.707 1.00 10.14 ? 94 THR A O 1 ATOM 93 C CB . THR A 1 12 ? 7.321 36.843 41.560 1.00 12.71 ? 94 THR A CB 1 ATOM 94 O OG1 . THR A 1 12 ? 7.920 37.173 40.301 1.00 12.34 ? 94 THR A OG1 1 ATOM 95 C CG2 . THR A 1 12 ? 7.382 38.058 42.478 1.00 11.95 ? 94 THR A CG2 1 ATOM 96 N N . ILE A 1 13 ? 8.357 35.579 44.579 1.00 8.76 ? 95 ILE A N 1 ATOM 97 C CA . ILE A 1 13 ? 7.997 35.287 45.961 1.00 7.55 ? 95 ILE A CA 1 ATOM 98 C C . ILE A 1 13 ? 7.446 36.528 46.666 1.00 7.90 ? 95 ILE A C 1 ATOM 99 O O . ILE A 1 13 ? 8.202 37.438 47.009 1.00 8.74 ? 95 ILE A O 1 ATOM 100 C CB . ILE A 1 13 ? 9.225 34.772 46.750 1.00 5.43 ? 95 ILE A CB 1 ATOM 101 C CG1 . ILE A 1 13 ? 9.829 33.538 46.074 1.00 8.18 ? 95 ILE A CG1 1 ATOM 102 C CG2 . ILE A 1 13 ? 8.841 34.455 48.189 1.00 8.73 ? 95 ILE A CG2 1 ATOM 103 C CD1 . ILE A 1 13 ? 11.261 33.242 46.507 1.00 7.92 ? 95 ILE A CD1 1 ATOM 104 N N . ASN A 1 14 ? 6.134 36.561 46.888 1.00 6.93 ? 96 ASN A N 1 ATOM 105 C CA . ASN A 1 14 ? 5.513 37.682 47.599 1.00 7.75 ? 96 ASN A CA 1 ATOM 106 C C . ASN A 1 14 ? 5.061 37.334 49.018 1.00 9.01 ? 96 ASN A C 1 ATOM 107 O O . ASN A 1 14 ? 4.789 38.224 49.830 1.00 9.35 ? 96 ASN A O 1 ATOM 108 C CB . ASN A 1 14 ? 4.361 38.276 46.776 1.00 7.49 ? 96 ASN A CB 1 ATOM 109 C CG . ASN A 1 14 ? 4.856 39.040 45.556 1.00 8.42 ? 96 ASN A CG 1 ATOM 110 O OD1 . ASN A 1 14 ? 5.902 39.692 45.605 1.00 9.95 ? 96 ASN A OD1 1 ATOM 111 N ND2 . ASN A 1 14 ? 4.119 38.949 44.453 1.00 9.21 ? 96 ASN A ND2 1 ATOM 112 N N . SER A 1 15 ? 4.994 36.034 49.302 1.00 7.83 ? 97 SER A N 1 ATOM 113 C CA . SER A 1 15 ? 4.734 35.519 50.646 1.00 7.06 ? 97 SER A CA 1 ATOM 114 C C . SER A 1 15 ? 4.947 34.010 50.640 1.00 8.75 ? 97 SER A C 1 ATOM 115 O O . SER A 1 15 ? 5.325 33.433 49.620 1.00 6.66 ? 97 SER A O 1 ATOM 116 C CB . SER A 1 15 ? 3.311 35.847 51.116 1.00 7.25 ? 97 SER A CB 1 ATOM 117 O OG . SER A 1 15 ? 2.335 35.249 50.277 1.00 9.44 ? 97 SER A OG 1 ATOM 118 N N . TRP A 1 16 ? 4.712 33.373 51.782 1.00 6.15 ? 98 TRP A N 1 ATOM 119 C CA . TRP A 1 16 ? 4.874 31.930 51.888 1.00 6.32 ? 98 TRP A CA 1 ATOM 120 C C . TRP A 1 16 ? 3.590 31.299 52.398 1.00 6.60 ? 98 TRP A C 1 ATOM 121 O O . TRP A 1 16 ? 2.952 31.839 53.309 1.00 8.20 ? 98 TRP A O 1 ATOM 122 C CB . TRP A 1 16 ? 6.043 31.604 52.817 1.00 5.36 ? 98 TRP A CB 1 ATOM 123 C CG . TRP A 1 16 ? 7.334 32.202 52.340 1.00 6.42 ? 98 TRP A CG 1 ATOM 124 C CD1 . TRP A 1 16 ? 7.829 33.442 52.641 1.00 9.54 ? 98 TRP A CD1 1 ATOM 125 C CD2 . TRP A 1 16 ? 8.285 31.592 51.457 1.00 6.02 ? 98 TRP A CD2 1 ATOM 126 N NE1 . TRP A 1 16 ? 9.037 33.635 52.005 1.00 7.25 ? 98 TRP A NE1 1 ATOM 127 C CE2 . TRP A 1 16 ? 9.336 32.516 51.271 1.00 9.15 ? 98 TRP A CE2 1 ATOM 128 C CE3 . TRP A 1 16 ? 8.349 30.353 50.807 1.00 9.31 ? 98 TRP A CE3 1 ATOM 129 C CZ2 . TRP A 1 16 ? 10.443 32.236 50.464 1.00 9.45 ? 98 TRP A CZ2 1 ATOM 130 C CZ3 . TRP A 1 16 ? 9.446 30.078 49.998 1.00 7.34 ? 98 TRP A CZ3 1 ATOM 131 C CH2 . TRP A 1 16 ? 10.479 31.016 49.836 1.00 6.46 ? 98 TRP A CH2 1 ATOM 132 N N . HIS A 1 17 ? 3.197 30.177 51.796 1.00 5.66 ? 99 HIS A N 1 ATOM 133 C CA . HIS A 1 17 ? 1.989 29.463 52.226 1.00 4.55 ? 99 HIS A CA 1 ATOM 134 C C . HIS A 1 17 ? 2.337 28.106 52.827 1.00 4.98 ? 99 HIS A C 1 ATOM 135 O O . HIS A 1 17 ? 3.357 27.511 52.479 1.00 3.75 ? 99 HIS A O 1 ATOM 136 C CB . HIS A 1 17 ? 1.005 29.286 51.060 1.00 5.18 ? 99 HIS A CB 1 ATOM 137 C CG . HIS A 1 17 ? 1.445 28.289 50.026 1.00 5.43 ? 99 HIS A CG 1 ATOM 138 N ND1 . HIS A 1 17 ? 1.285 26.930 50.186 1.00 6.70 ? 99 HIS A ND1 1 ATOM 139 C CD2 . HIS A 1 17 ? 2.024 28.458 48.811 1.00 6.14 ? 99 HIS A CD2 1 ATOM 140 C CE1 . HIS A 1 17 ? 1.755 26.302 49.120 1.00 9.02 ? 99 HIS A CE1 1 ATOM 141 N NE2 . HIS A 1 17 ? 2.208 27.206 48.271 1.00 7.62 ? 99 HIS A NE2 1 ATOM 142 N N . ILE A 1 18 ? 1.490 27.618 53.728 1.00 4.86 ? 100 ILE A N 1 ATOM 143 C CA . ILE A 1 18 ? 1.706 26.303 54.319 1.00 6.17 ? 100 ILE A CA 1 ATOM 144 C C . ILE A 1 18 ? 1.662 25.213 53.243 1.00 6.11 ? 100 ILE A C 1 ATOM 145 O O . ILE A 1 18 ? 0.779 25.203 52.375 1.00 8.83 ? 100 ILE A O 1 ATOM 146 C CB . ILE A 1 18 ? 0.707 26.026 55.478 1.00 5.86 ? 100 ILE A CB 1 ATOM 147 C CG1 . ILE A 1 18 ? 1.076 24.739 56.223 1.00 7.38 ? 100 ILE A CG1 1 ATOM 148 C CG2 . ILE A 1 18 ? -0.728 25.986 54.970 1.00 5.54 ? 100 ILE A CG2 1 ATOM 149 C CD1 . ILE A 1 18 ? 2.419 24.804 56.938 1.00 6.22 ? 100 ILE A CD1 1 ATOM 150 N N . TYR A 1 19 ? 2.645 24.317 53.280 1.00 3.41 ? 101 TYR A N 1 ATOM 151 C CA . TYR A 1 19 ? 2.749 23.237 52.298 1.00 5.20 ? 101 TYR A CA 1 ATOM 152 C C . TYR A 1 19 ? 2.554 21.890 52.980 1.00 5.61 ? 101 TYR A C 1 ATOM 153 O O . TYR A 1 19 ? 1.736 21.077 52.544 1.00 7.17 ? 101 TYR A O 1 ATOM 154 C CB . TYR A 1 19 ? 4.111 23.297 51.605 1.00 6.01 ? 101 TYR A CB 1 ATOM 155 C CG . TYR A 1 19 ? 4.403 22.164 50.634 1.00 6.30 ? 101 TYR A CG 1 ATOM 156 C CD1 . TYR A 1 19 ? 3.791 22.112 49.386 1.00 9.32 ? 101 TYR A CD1 1 ATOM 157 C CD2 . TYR A 1 19 ? 5.318 21.169 50.957 1.00 7.32 ? 101 TYR A CD2 1 ATOM 158 C CE1 . TYR A 1 19 ? 4.068 21.083 48.489 1.00 10.75 ? 101 TYR A CE1 1 ATOM 159 C CE2 . TYR A 1 19 ? 5.607 20.138 50.065 1.00 8.80 ? 101 TYR A CE2 1 ATOM 160 C CZ . TYR A 1 19 ? 4.978 20.104 48.836 1.00 10.57 ? 101 TYR A CZ 1 ATOM 161 O OH . TYR A 1 19 ? 5.261 19.086 47.949 1.00 10.79 ? 101 TYR A OH 1 ATOM 162 N N . GLY A 1 20 ? 3.302 21.656 54.056 1.00 4.27 ? 102 GLY A N 1 ATOM 163 C CA . GLY A 1 20 ? 3.164 20.418 54.804 1.00 5.24 ? 102 GLY A CA 1 ATOM 164 C C . GLY A 1 20 ? 3.543 20.557 56.264 1.00 6.51 ? 102 GLY A C 1 ATOM 165 O O . GLY A 1 20 ? 4.300 21.451 56.637 1.00 8.24 ? 102 GLY A O 1 ATOM 166 N N . LYS A 1 21 ? 3.007 19.668 57.093 1.00 4.35 ? 103 LYS A N 1 ATOM 167 C CA . LYS A 1 21 ? 3.326 19.649 58.513 1.00 3.26 ? 103 LYS A CA 1 ATOM 168 C C . LYS A 1 21 ? 2.902 18.289 59.026 1.00 7.77 ? 103 LYS A C 1 ATOM 169 O O . LYS A 1 21 ? 1.777 17.863 58.764 1.00 4.24 ? 103 LYS A O 1 ATOM 170 C CB . LYS A 1 21 ? 2.551 20.744 59.251 1.00 5.84 ? 103 LYS A CB 1 ATOM 171 C CG . LYS A 1 21 ? 3.011 20.949 60.691 1.00 4.43 ? 103 LYS A CG 1 ATOM 172 C CD . LYS A 1 21 ? 2.107 21.917 61.436 1.00 6.18 ? 103 LYS A CD 1 ATOM 173 C CE . LYS A 1 21 ? 2.758 22.410 62.730 1.00 4.97 ? 103 LYS A CE 1 ATOM 174 N NZ . LYS A 1 21 ? 3.016 21.307 63.708 1.00 4.28 ? 103 LYS A NZ 1 ATOM 175 N N . ASP A 1 22 ? 3.778 17.597 59.750 1.00 5.53 ? 104 ASP A N 1 ATOM 176 C CA . ASP A 1 22 ? 3.436 16.231 60.151 1.00 4.74 ? 104 ASP A CA 1 ATOM 177 C C . ASP A 1 22 ? 3.020 16.028 61.607 1.00 4.95 ? 104 ASP A C 1 ATOM 178 O O . ASP A 1 22 ? 2.497 14.968 61.943 1.00 6.66 ? 104 ASP A O 1 ATOM 179 C CB . ASP A 1 22 ? 4.513 15.210 59.739 1.00 4.82 ? 104 ASP A CB 1 ATOM 180 C CG . ASP A 1 22 ? 5.857 15.454 60.404 1.00 5.66 ? 104 ASP A CG 1 ATOM 181 O OD1 . ASP A 1 22 ? 5.968 16.374 61.240 1.00 5.89 ? 104 ASP A OD1 1 ATOM 182 O OD2 . ASP A 1 22 ? 6.809 14.701 60.100 1.00 6.63 ? 104 ASP A OD2 1 ATOM 183 N N . ASN A 1 23 ? 3.247 17.027 62.458 1.00 3.93 ? 105 ASN A N 1 ATOM 184 C CA . ASN A 1 23 ? 2.889 16.922 63.872 1.00 2.71 ? 105 ASN A CA 1 ATOM 185 C C . ASN A 1 23 ? 3.410 15.634 64.512 1.00 6.70 ? 105 ASN A C 1 ATOM 186 O O . ASN A 1 23 ? 2.716 15.004 65.316 1.00 4.98 ? 105 ASN A O 1 ATOM 187 C CB . ASN A 1 23 ? 1.367 17.013 64.030 1.00 5.48 ? 105 ASN A CB 1 ATOM 188 C CG . ASN A 1 23 ? 0.806 18.315 63.487 1.00 7.21 ? 105 ASN A CG 1 ATOM 189 O OD1 . ASN A 1 23 ? 1.081 19.387 64.026 1.00 7.46 ? 105 ASN A OD1 1 ATOM 190 N ND2 . ASN A 1 23 ? 0.026 18.231 62.412 1.00 6.93 ? 105 ASN A ND2 1 ATOM 191 N N . ALA A 1 24 ? 4.628 15.241 64.143 1.00 4.60 ? 106 ALA A N 1 ATOM 192 C CA . ALA A 1 24 ? 5.147 13.914 64.486 1.00 5.71 ? 106 ALA A CA 1 ATOM 193 C C . ALA A 1 24 ? 5.278 13.666 65.987 1.00 6.98 ? 106 ALA A C 1 ATOM 194 O O . ALA A 1 24 ? 5.044 12.549 66.456 1.00 5.25 ? 106 ALA A O 1 ATOM 195 C CB . ALA A 1 24 ? 6.489 13.662 63.795 1.00 4.29 ? 106 ALA A CB 1 ATOM 196 N N . VAL A 1 25 ? 5.681 14.691 66.734 1.00 5.29 ? 107 VAL A N 1 ATOM 197 C CA . VAL A 1 25 ? 5.925 14.523 68.166 1.00 4.76 ? 107 VAL A CA 1 ATOM 198 C C . VAL A 1 25 ? 4.595 14.425 68.923 1.00 6.03 ? 107 VAL A C 1 ATOM 199 O O . VAL A 1 25 ? 4.442 13.575 69.809 1.00 5.27 ? 107 VAL A O 1 ATOM 200 C CB . VAL A 1 25 ? 6.837 15.640 68.728 1.00 4.99 ? 107 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 25 ? 7.144 15.407 70.211 1.00 5.03 ? 107 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 25 ? 8.130 15.701 67.926 1.00 6.76 ? 107 VAL A CG2 1 ATOM 203 N N . ARG A 1 26 ? 3.627 15.269 68.553 1.00 3.96 ? 108 ARG A N 1 ATOM 204 C CA . ARG A 1 26 ? 2.267 15.163 69.096 1.00 3.90 ? 108 ARG A CA 1 ATOM 205 C C . ARG A 1 26 ? 1.726 13.752 68.898 1.00 6.50 ? 108 ARG A C 1 ATOM 206 O O . ARG A 1 26 ? 1.254 13.110 69.836 1.00 7.03 ? 108 ARG A O 1 ATOM 207 C CB . ARG A 1 26 ? 1.316 16.141 68.392 1.00 6.14 ? 108 ARG A CB 1 ATOM 208 C CG . ARG A 1 26 ? 1.471 17.605 68.776 1.00 4.29 ? 108 ARG A CG 1 ATOM 209 C CD . ARG A 1 26 ? 0.594 18.499 67.883 1.00 4.80 ? 108 ARG A CD 1 ATOM 210 N NE . ARG A 1 26 ? -0.827 18.135 67.921 1.00 6.23 ? 108 ARG A NE 1 ATOM 211 C CZ . ARG A 1 26 ? -1.695 18.580 68.827 1.00 7.66 ? 108 ARG A CZ 1 ATOM 212 N NH1 . ARG A 1 26 ? -1.294 19.395 69.797 1.00 8.30 ? 108 ARG A NH1 1 ATOM 213 N NH2 . ARG A 1 26 ? -2.968 18.202 68.773 1.00 6.48 ? 108 ARG A NH2 1 ATOM 214 N N . ILE A 1 27 ? 1.791 13.274 67.661 1.00 4.39 ? 109 ILE A N 1 ATOM 215 C CA . ILE A 1 27 ? 1.216 11.974 67.324 1.00 4.94 ? 109 ILE A CA 1 ATOM 216 C C . ILE A 1 27 ? 2.007 10.835 67.980 1.00 6.33 ? 109 ILE A C 1 ATOM 217 O O . ILE A 1 27 ? 1.423 9.881 68.511 1.00 7.16 ? 109 ILE A O 1 ATOM 218 C CB . ILE A 1 27 ? 1.108 11.806 65.792 1.00 5.11 ? 109 ILE A CB 1 ATOM 219 C CG1 . ILE A 1 27 ? 0.040 12.763 65.246 1.00 5.26 ? 109 ILE A CG1 1 ATOM 220 C CG2 . ILE A 1 27 ? 0.737 10.374 65.420 1.00 6.39 ? 109 ILE A CG2 1 ATOM 221 C CD1 . ILE A 1 27 ? 0.048 12.904 63.714 1.00 3.89 ? 109 ILE A CD1 1 ATOM 222 N N . GLY A 1 28 ? 3.332 10.961 67.974 1.00 6.04 ? 110 GLY A N 1 ATOM 223 C CA . GLY A 1 28 ? 4.209 9.959 68.558 1.00 5.51 ? 110 GLY A CA 1 ATOM 224 C C . GLY A 1 28 ? 4.092 9.778 70.061 1.00 6.14 ? 110 GLY A C 1 ATOM 225 O O . GLY A 1 28 ? 4.622 8.812 70.609 1.00 7.08 ? 110 GLY A O 1 ATOM 226 N N . GLU A 1 29 ? 3.422 10.707 70.739 1.00 5.12 ? 111 GLU A N 1 ATOM 227 C CA . GLU A 1 29 ? 3.139 10.528 72.163 1.00 4.92 ? 111 GLU A CA 1 ATOM 228 C C . GLU A 1 29 ? 2.331 9.252 72.385 1.00 8.02 ? 111 GLU A C 1 ATOM 229 O O . GLU A 1 29 ? 2.431 8.609 73.439 1.00 6.37 ? 111 GLU A O 1 ATOM 230 C CB . GLU A 1 29 ? 2.378 11.738 72.722 1.00 6.88 ? 111 GLU A CB 1 ATOM 231 C CG . GLU A 1 29 ? 2.205 11.730 74.244 1.00 7.31 ? 111 GLU A CG 1 ATOM 232 C CD . GLU A 1 29 ? 1.002 10.919 74.711 1.00 8.31 ? 111 GLU A CD 1 ATOM 233 O OE1 . GLU A 1 29 ? -0.004 10.863 73.974 1.00 7.80 ? 111 GLU A OE1 1 ATOM 234 O OE2 . GLU A 1 29 ? 1.069 10.331 75.813 1.00 11.67 ? 111 GLU A OE2 1 ATOM 235 N N . SER A 1 30 ? 1.529 8.886 71.389 1.00 6.37 ? 112 SER A N 1 ATOM 236 C CA . SER A 1 30 ? 0.705 7.686 71.486 1.00 5.27 ? 112 SER A CA 1 ATOM 237 C C . SER A 1 30 ? 0.505 6.983 70.148 1.00 13.62 ? 112 SER A C 1 ATOM 238 O O . SER A 1 30 ? -0.625 6.692 69.747 1.00 22.68 ? 112 SER A O 1 ATOM 239 C CB . SER A 1 30 ? -0.654 8.008 72.101 1.00 10.69 ? 112 SER A CB 1 ATOM 240 O OG . SER A 1 30 ? -1.421 6.827 72.262 1.00 25.76 ? 112 SER A OG 1 ATOM 241 N N A SER A 1 31 ? 1.610 6.705 69.470 0.40 6.79 ? 113 SER A N 1 ATOM 242 N N B SER A 1 31 ? 1.614 6.747 69.449 0.60 6.76 ? 113 SER A N 1 ATOM 243 C CA A SER A 1 31 ? 1.601 5.825 68.308 0.40 5.68 ? 113 SER A CA 1 ATOM 244 C CA B SER A 1 31 ? 1.629 6.002 68.189 0.60 5.63 ? 113 SER A CA 1 ATOM 245 C C A SER A 1 31 ? 3.048 5.509 67.972 0.40 6.77 ? 113 SER A C 1 ATOM 246 C C B SER A 1 31 ? 3.056 5.529 67.962 0.60 6.76 ? 113 SER A C 1 ATOM 247 O O A SER A 1 31 ? 3.966 6.076 68.564 0.40 6.85 ? 113 SER A O 1 ATOM 248 O O B SER A 1 31 ? 3.969 5.993 68.643 0.60 6.85 ? 113 SER A O 1 ATOM 249 C CB A SER A 1 31 ? 0.900 6.469 67.114 0.40 5.49 ? 113 SER A CB 1 ATOM 250 C CB B SER A 1 31 ? 1.180 6.878 67.022 0.60 6.08 ? 113 SER A CB 1 ATOM 251 O OG A SER A 1 31 ? 1.557 7.657 66.727 0.40 8.02 ? 113 SER A OG 1 ATOM 252 O OG B SER A 1 31 ? -0.216 7.074 67.041 0.60 4.88 ? 113 SER A OG 1 ATOM 253 N N . ASP A 1 32 ? 3.252 4.608 67.021 1.00 5.05 ? 114 ASP A N 1 ATOM 254 C CA . ASP A 1 32 ? 4.587 4.081 66.765 1.00 4.27 ? 114 ASP A CA 1 ATOM 255 C C . ASP A 1 32 ? 5.356 4.935 65.765 1.00 7.23 ? 114 ASP A C 1 ATOM 256 O O . ASP A 1 32 ? 5.599 4.540 64.623 1.00 6.07 ? 114 ASP A O 1 ATOM 257 C CB . ASP A 1 32 ? 4.515 2.607 66.363 1.00 4.65 ? 114 ASP A CB 1 ATOM 258 C CG . ASP A 1 32 ? 3.934 1.736 67.469 1.00 9.88 ? 114 ASP A CG 1 ATOM 259 O OD1 . ASP A 1 32 ? 4.194 2.040 68.654 1.00 9.87 ? 114 ASP A OD1 1 ATOM 260 O OD2 . ASP A 1 32 ? 3.215 0.759 67.164 1.00 9.18 ? 114 ASP A OD2 1 ATOM 261 N N . VAL A 1 33 ? 5.729 6.123 66.228 1.00 5.02 ? 115 VAL A N 1 ATOM 262 C CA . VAL A 1 33 ? 6.439 7.103 65.417 1.00 5.61 ? 115 VAL A CA 1 ATOM 263 C C . VAL A 1 33 ? 7.933 6.993 65.681 1.00 5.39 ? 115 VAL A C 1 ATOM 264 O O . VAL A 1 33 ? 8.368 6.989 66.831 1.00 4.65 ? 115 VAL A O 1 ATOM 265 C CB . VAL A 1 33 ? 5.955 8.524 65.750 1.00 4.78 ? 115 VAL A CB 1 ATOM 266 C CG1 . VAL A 1 33 ? 6.838 9.572 65.082 1.00 6.08 ? 115 VAL A CG1 1 ATOM 267 C CG2 . VAL A 1 33 ? 4.502 8.692 65.320 1.00 5.38 ? 115 VAL A CG2 1 ATOM 268 N N . LEU A 1 34 ? 8.720 6.885 64.617 1.00 3.18 ? 116 LEU A N 1 ATOM 269 C CA . LEU A 1 34 ? 10.163 6.746 64.765 1.00 2.79 ? 116 LEU A CA 1 ATOM 270 C C . LEU A 1 34 ? 10.791 8.046 65.251 1.00 4.92 ? 116 LEU A C 1 ATOM 271 O O . LEU A 1 34 ? 10.392 9.131 64.834 1.00 5.94 ? 116 LEU A O 1 ATOM 272 C CB . LEU A 1 34 ? 10.798 6.337 63.431 1.00 3.60 ? 116 LEU A CB 1 ATOM 273 C CG . LEU A 1 34 ? 10.479 4.932 62.927 1.00 3.94 ? 116 LEU A CG 1 ATOM 274 C CD1 . LEU A 1 34 ? 10.802 4.818 61.439 1.00 4.11 ? 116 LEU A CD1 1 ATOM 275 C CD2 . LEU A 1 34 ? 11.282 3.908 63.723 1.00 2.50 ? 116 LEU A CD2 1 ATOM 276 N N . VAL A 1 35 ? 11.769 7.932 66.143 1.00 2.51 ? 117 VAL A N 1 ATOM 277 C CA . VAL A 1 35 ? 12.606 9.074 66.487 1.00 4.35 ? 117 VAL A CA 1 ATOM 278 C C . VAL A 1 35 ? 13.442 9.439 65.264 1.00 5.78 ? 117 VAL A C 1 ATOM 279 O O . VAL A 1 35 ? 14.058 8.567 64.647 1.00 6.24 ? 117 VAL A O 1 ATOM 280 C CB . VAL A 1 35 ? 13.550 8.745 67.654 1.00 3.70 ? 117 VAL A CB 1 ATOM 281 C CG1 . VAL A 1 35 ? 14.526 9.887 67.889 1.00 3.05 ? 117 VAL A CG1 1 ATOM 282 C CG2 . VAL A 1 35 ? 12.749 8.467 68.916 1.00 4.85 ? 117 VAL A CG2 1 ATOM 283 N N . THR A 1 36 ? 13.451 10.720 64.903 1.00 5.04 ? 118 THR A N 1 ATOM 284 C CA . THR A 1 36 ? 14.260 11.186 63.779 1.00 2.56 ? 118 THR A CA 1 ATOM 285 C C . THR A 1 36 ? 15.058 12.427 64.146 1.00 4.38 ? 118 THR A C 1 ATOM 286 O O . THR A 1 36 ? 14.945 12.946 65.255 1.00 6.49 ? 118 THR A O 1 ATOM 287 C CB . THR A 1 36 ? 13.379 11.534 62.558 1.00 5.09 ? 118 THR A CB 1 ATOM 288 O OG1 . THR A 1 36 ? 12.467 12.581 62.906 1.00 7.05 ? 118 THR A OG1 1 ATOM 289 C CG2 . THR A 1 36 ? 12.582 10.320 62.093 1.00 4.14 ? 118 THR A CG2 1 ATOM 290 N N . ARG A 1 37 ? 15.883 12.873 63.209 1.00 3.58 ? 119 ARG A N 1 ATOM 291 C CA . ARG A 1 37 ? 16.373 14.249 63.151 1.00 3.50 ? 119 ARG A CA 1 ATOM 292 C C . ARG A 1 37 ? 16.910 14.477 61.738 1.00 4.70 ? 119 ARG A C 1 ATOM 293 O O . ARG A 1 37 ? 16.909 13.553 60.918 1.00 4.65 ? 119 ARG A O 1 ATOM 294 C CB . ARG A 1 37 ? 17.434 14.566 64.220 1.00 4.01 ? 119 ARG A CB 1 ATOM 295 C CG . ARG A 1 37 ? 16.893 15.404 65.397 1.00 5.28 ? 119 ARG A CG 1 ATOM 296 C CD . ARG A 1 37 ? 17.927 16.408 65.932 1.00 5.65 ? 119 ARG A CD 1 ATOM 297 N NE . ARG A 1 37 ? 18.215 17.443 64.938 1.00 5.41 ? 119 ARG A NE 1 ATOM 298 C CZ . ARG A 1 37 ? 19.359 18.113 64.849 1.00 7.69 ? 119 ARG A CZ 1 ATOM 299 N NH1 . ARG A 1 37 ? 20.344 17.878 65.705 1.00 5.98 ? 119 ARG A NH1 1 ATOM 300 N NH2 . ARG A 1 37 ? 19.517 19.023 63.894 1.00 7.14 ? 119 ARG A NH2 1 ATOM 301 N N . GLU A 1 38 ? 17.352 15.700 61.458 1.00 4.86 ? 120 GLU A N 1 ATOM 302 C CA . GLU A 1 38 ? 17.852 16.069 60.131 1.00 3.76 ? 120 GLU A CA 1 ATOM 303 C C . GLU A 1 38 ? 16.865 15.742 59.001 1.00 4.53 ? 120 GLU A C 1 ATOM 304 O O . GLU A 1 38 ? 17.205 15.022 58.060 1.00 6.00 ? 120 GLU A O 1 ATOM 305 C CB . GLU A 1 38 ? 19.220 15.411 59.865 1.00 5.77 ? 120 GLU A CB 1 ATOM 306 C CG . GLU A 1 38 ? 20.333 15.822 60.853 1.00 5.54 ? 120 GLU A CG 1 ATOM 307 C CD . GLU A 1 38 ? 20.311 15.034 62.155 1.00 6.92 ? 120 GLU A CD 1 ATOM 308 O OE1 . GLU A 1 38 ? 19.859 13.873 62.142 1.00 6.20 ? 120 GLU A OE1 1 ATOM 309 O OE2 . GLU A 1 38 ? 20.747 15.573 63.200 1.00 4.96 ? 120 GLU A OE2 1 ATOM 310 N N . PRO A 1 39 ? 15.640 16.285 59.075 1.00 4.90 ? 121 PRO A N 1 ATOM 311 C CA . PRO A 1 39 ? 14.635 15.973 58.055 1.00 3.64 ? 121 PRO A CA 1 ATOM 312 C C . PRO A 1 39 ? 14.831 16.807 56.799 1.00 3.90 ? 121 PRO A C 1 ATOM 313 O O . PRO A 1 39 ? 15.582 17.784 56.812 1.00 5.79 ? 121 PRO A O 1 ATOM 314 C CB . PRO A 1 39 ? 13.335 16.410 58.726 1.00 3.38 ? 121 PRO A CB 1 ATOM 315 C CG . PRO A 1 39 ? 13.750 17.609 59.533 1.00 5.59 ? 121 PRO A CG 1 ATOM 316 C CD . PRO A 1 39 ? 15.141 17.281 60.042 1.00 5.35 ? 121 PRO A CD 1 ATOM 317 N N . TYR A 1 40 ? 14.163 16.408 55.722 1.00 4.39 ? 122 TYR A N 1 ATOM 318 C CA . TYR A 1 40 ? 14.016 17.259 54.548 1.00 4.84 ? 122 TYR A CA 1 ATOM 319 C C . TYR A 1 40 ? 12.829 16.819 53.706 1.00 5.31 ? 122 TYR A C 1 ATOM 320 O O . TYR A 1 40 ? 12.073 15.942 54.113 1.00 4.93 ? 122 TYR A O 1 ATOM 321 C CB . TYR A 1 40 ? 15.307 17.357 53.717 1.00 5.01 ? 122 TYR A CB 1 ATOM 322 C CG . TYR A 1 40 ? 16.012 16.066 53.315 1.00 4.99 ? 122 TYR A CG 1 ATOM 323 C CD1 . TYR A 1 40 ? 16.816 15.371 54.218 1.00 5.21 ? 122 TYR A CD1 1 ATOM 324 C CD2 . TYR A 1 40 ? 15.953 15.605 52.002 1.00 4.59 ? 122 TYR A CD2 1 ATOM 325 C CE1 . TYR A 1 40 ? 17.498 14.213 53.834 1.00 5.36 ? 122 TYR A CE1 1 ATOM 326 C CE2 . TYR A 1 40 ? 16.633 14.452 51.608 1.00 4.76 ? 122 TYR A CE2 1 ATOM 327 C CZ . TYR A 1 40 ? 17.405 13.769 52.525 1.00 5.84 ? 122 TYR A CZ 1 ATOM 328 O OH . TYR A 1 40 ? 18.083 12.637 52.126 1.00 5.61 ? 122 TYR A OH 1 ATOM 329 N N . VAL A 1 41 ? 12.643 17.460 52.557 1.00 5.42 ? 123 VAL A N 1 ATOM 330 C CA . VAL A 1 41 ? 11.551 17.118 51.653 1.00 4.55 ? 123 VAL A CA 1 ATOM 331 C C . VAL A 1 41 ? 12.151 16.965 50.260 1.00 3.89 ? 123 VAL A C 1 ATOM 332 O O . VAL A 1 41 ? 13.090 17.682 49.908 1.00 5.52 ? 123 VAL A O 1 ATOM 333 C CB . VAL A 1 41 ? 10.466 18.222 51.630 1.00 5.99 ? 123 VAL A CB 1 ATOM 334 C CG1 . VAL A 1 41 ? 9.248 17.775 50.826 1.00 5.41 ? 123 VAL A CG1 1 ATOM 335 C CG2 . VAL A 1 41 ? 10.053 18.601 53.050 1.00 5.41 ? 123 VAL A CG2 1 ATOM 336 N N . SER A 1 42 ? 11.631 16.032 49.472 1.00 4.37 ? 124 SER A N 1 ATOM 337 C CA . SER A 1 42 ? 12.121 15.866 48.105 1.00 6.59 ? 124 SER A CA 1 ATOM 338 C C . SER A 1 42 ? 11.019 15.307 47.227 1.00 9.19 ? 124 SER A C 1 ATOM 339 O O . SER A 1 42 ? 10.253 14.449 47.663 1.00 5.69 ? 124 SER A O 1 ATOM 340 C CB . SER A 1 42 ? 13.338 14.937 48.082 1.00 6.60 ? 124 SER A CB 1 ATOM 341 O OG . SER A 1 42 ? 13.998 14.989 46.828 1.00 6.76 ? 124 SER A OG 1 ATOM 342 N N . CYS A 1 43 ? 10.939 15.786 45.988 1.00 5.79 ? 125 CYS A N 1 ATOM 343 C CA . CYS A 1 43 ? 9.888 15.333 45.084 1.00 6.24 ? 125 CYS A CA 1 ATOM 344 C C . CYS A 1 43 ? 10.372 14.346 44.035 1.00 8.41 ? 125 CYS A C 1 ATOM 345 O O . CYS A 1 43 ? 11.492 14.452 43.539 1.00 6.93 ? 125 CYS A O 1 ATOM 346 C CB . CYS A 1 43 ? 9.243 16.524 44.377 1.00 7.57 ? 125 CYS A CB 1 ATOM 347 S SG . CYS A 1 43 ? 8.445 17.678 45.502 1.00 9.38 ? 125 CYS A SG 1 ATOM 348 N N . ASP A 1 44 ? 9.503 13.383 43.730 1.00 6.56 ? 126 ASP A N 1 ATOM 349 C CA . ASP A 1 44 ? 9.583 12.551 42.536 1.00 7.37 ? 126 ASP A CA 1 ATOM 350 C C . ASP A 1 44 ? 8.654 13.196 41.502 1.00 9.44 ? 126 ASP A C 1 ATOM 351 O O . ASP A 1 44 ? 7.900 14.107 41.841 1.00 8.73 ? 126 ASP A O 1 ATOM 352 C CB . ASP A 1 44 ? 9.066 11.146 42.856 1.00 7.55 ? 126 ASP A CB 1 ATOM 353 C CG . ASP A 1 44 ? 10.015 10.345 43.722 1.00 11.16 ? 126 ASP A CG 1 ATOM 354 O OD1 . ASP A 1 44 ? 11.002 10.911 44.229 1.00 11.09 ? 126 ASP A OD1 1 ATOM 355 O OD2 . ASP A 1 44 ? 9.761 9.133 43.895 1.00 11.89 ? 126 ASP A OD2 1 ATOM 356 N N . PRO A 1 45 ? 8.689 12.728 40.238 1.00 9.25 ? 127 PRO A N 1 ATOM 357 C CA . PRO A 1 45 ? 7.770 13.306 39.249 1.00 7.35 ? 127 PRO A CA 1 ATOM 358 C C . PRO A 1 45 ? 6.289 13.108 39.572 1.00 11.01 ? 127 PRO A C 1 ATOM 359 O O . PRO A 1 45 ? 5.459 13.826 39.014 1.00 12.22 ? 127 PRO A O 1 ATOM 360 C CB . PRO A 1 45 ? 8.126 12.547 37.963 1.00 9.31 ? 127 PRO A CB 1 ATOM 361 C CG . PRO A 1 45 ? 9.572 12.209 38.130 1.00 6.73 ? 127 PRO A CG 1 ATOM 362 C CD . PRO A 1 45 ? 9.706 11.871 39.599 1.00 8.63 ? 127 PRO A CD 1 ATOM 363 N N . ASP A 1 46 ? 5.959 12.159 40.444 1.00 8.68 ? 128 ASP A N 1 ATOM 364 C CA . ASP A 1 46 ? 4.556 11.859 40.717 1.00 13.40 ? 128 ASP A CA 1 ATOM 365 C C . ASP A 1 46 ? 4.172 11.969 42.192 1.00 13.33 ? 128 ASP A C 1 ATOM 366 O O . ASP A 1 46 ? 3.018 11.729 42.551 1.00 12.34 ? 128 ASP A O 1 ATOM 367 C CB . ASP A 1 46 ? 4.205 10.465 40.191 1.00 16.27 ? 128 ASP A CB 1 ATOM 368 C CG . ASP A 1 46 ? 4.987 9.360 40.887 1.00 24.25 ? 128 ASP A CG 1 ATOM 369 O OD1 . ASP A 1 46 ? 6.038 9.648 41.508 1.00 18.69 ? 128 ASP A OD1 1 ATOM 370 O OD2 . ASP A 1 46 ? 4.555 8.191 40.802 1.00 39.45 ? 128 ASP A OD2 1 ATOM 371 N N . GLU A 1 47 ? 5.126 12.337 43.042 1.00 8.53 ? 129 GLU A N 1 ATOM 372 C CA . GLU A 1 47 ? 4.869 12.387 44.482 1.00 9.61 ? 129 GLU A CA 1 ATOM 373 C C . GLU A 1 47 ? 5.950 13.192 45.193 1.00 9.69 ? 129 GLU A C 1 ATOM 374 O O . GLU A 1 47 ? 7.121 13.132 44.814 1.00 10.50 ? 129 GLU A O 1 ATOM 375 C CB . GLU A 1 47 ? 4.831 10.961 45.053 1.00 10.22 ? 129 GLU A CB 1 ATOM 376 C CG . GLU A 1 47 ? 4.539 10.870 46.546 1.00 22.03 ? 129 GLU A CG 1 ATOM 377 C CD . GLU A 1 47 ? 4.742 9.463 47.106 1.00 24.61 ? 129 GLU A CD 1 ATOM 378 O OE1 . GLU A 1 47 ? 5.220 8.580 46.358 1.00 16.82 ? 129 GLU A OE1 1 ATOM 379 O OE2 . GLU A 1 47 ? 4.427 9.243 48.302 1.00 18.95 ? 129 GLU A OE2 1 ATOM 380 N N . CYS A 1 48 ? 5.564 13.938 46.227 1.00 9.02 ? 130 CYS A N 1 ATOM 381 C CA . CYS A 1 48 ? 6.547 14.572 47.107 1.00 6.04 ? 130 CYS A CA 1 ATOM 382 C C . CYS A 1 48 ? 6.497 13.915 48.489 1.00 5.20 ? 130 CYS A C 1 ATOM 383 O O . CYS A 1 48 ? 5.416 13.586 48.992 1.00 5.66 ? 130 CYS A O 1 ATOM 384 C CB . CYS A 1 48 ? 6.310 16.083 47.203 1.00 8.07 ? 130 CYS A CB 1 ATOM 385 S SG . CYS A 1 48 ? 6.541 16.958 45.615 1.00 11.94 ? 130 CYS A SG 1 ATOM 386 N N . ARG A 1 49 ? 7.666 13.713 49.095 1.00 6.03 ? 131 ARG A N 1 ATOM 387 C CA . ARG A 1 49 ? 7.761 12.950 50.340 1.00 3.40 ? 131 ARG A CA 1 ATOM 388 C C . ARG A 1 49 ? 8.629 13.635 51.390 1.00 5.32 ? 131 ARG A C 1 ATOM 389 O O . ARG A 1 49 ? 9.513 14.434 51.060 1.00 4.98 ? 131 ARG A O 1 ATOM 390 C CB . ARG A 1 49 ? 8.308 11.545 50.058 1.00 4.84 ? 131 ARG A CB 1 ATOM 391 C CG . ARG A 1 49 ? 7.359 10.670 49.247 1.00 5.10 ? 131 ARG A CG 1 ATOM 392 C CD . ARG A 1 49 ? 8.048 9.410 48.724 1.00 8.18 ? 131 ARG A CD 1 ATOM 393 N NE . ARG A 1 49 ? 8.401 8.458 49.780 1.00 8.62 ? 131 ARG A NE 1 ATOM 394 C CZ . ARG A 1 49 ? 7.561 7.561 50.293 1.00 11.14 ? 131 ARG A CZ 1 ATOM 395 N NH1 . ARG A 1 49 ? 6.308 7.506 49.863 1.00 10.77 ? 131 ARG A NH1 1 ATOM 396 N NH2 . ARG A 1 49 ? 7.967 6.719 51.238 1.00 8.26 ? 131 ARG A NH2 1 ATOM 397 N N . PHE A 1 50 ? 8.372 13.317 52.656 1.00 6.30 ? 132 PHE A N 1 ATOM 398 C CA . PHE A 1 50 ? 9.237 13.751 53.749 1.00 5.49 ? 132 PHE A CA 1 ATOM 399 C C . PHE A 1 50 ? 10.381 12.751 53.902 1.00 5.05 ? 132 PHE A C 1 ATOM 400 O O . PHE A 1 50 ? 10.195 11.556 53.663 1.00 6.14 ? 132 PHE A O 1 ATOM 401 C CB . PHE A 1 50 ? 8.454 13.827 55.061 1.00 3.18 ? 132 PHE A CB 1 ATOM 402 C CG . PHE A 1 50 ? 7.606 15.072 55.213 1.00 6.38 ? 132 PHE A CG 1 ATOM 403 C CD1 . PHE A 1 50 ? 7.574 16.053 54.226 1.00 7.53 ? 132 PHE A CD1 1 ATOM 404 C CD2 . PHE A 1 50 ? 6.848 15.257 56.365 1.00 7.48 ? 132 PHE A CD2 1 ATOM 405 C CE1 . PHE A 1 50 ? 6.792 17.202 54.391 1.00 9.78 ? 132 PHE A CE1 1 ATOM 406 C CE2 . PHE A 1 50 ? 6.067 16.392 56.539 1.00 4.51 ? 132 PHE A CE2 1 ATOM 407 C CZ . PHE A 1 50 ? 6.037 17.368 55.551 1.00 6.95 ? 132 PHE A CZ 1 ATOM 408 N N . TYR A 1 51 ? 11.555 13.248 54.291 1.00 3.85 ? 133 TYR A N 1 ATOM 409 C CA . TYR A 1 51 ? 12.750 12.425 54.495 1.00 4.55 ? 133 TYR A CA 1 ATOM 410 C C . TYR A 1 51 ? 13.353 12.780 55.844 1.00 2.87 ? 133 TYR A C 1 ATOM 411 O O . TYR A 1 51 ? 13.160 13.893 56.322 1.00 5.40 ? 133 TYR A O 1 ATOM 412 C CB . TYR A 1 51 ? 13.796 12.717 53.408 1.00 3.87 ? 133 TYR A CB 1 ATOM 413 C CG . TYR A 1 51 ? 13.422 12.185 52.046 1.00 5.34 ? 133 TYR A CG 1 ATOM 414 C CD1 . TYR A 1 51 ? 12.410 12.785 51.301 1.00 4.96 ? 133 TYR A CD1 1 ATOM 415 C CD2 . TYR A 1 51 ? 14.075 11.084 51.505 1.00 7.02 ? 133 TYR A CD2 1 ATOM 416 C CE1 . TYR A 1 51 ? 12.054 12.299 50.060 1.00 5.15 ? 133 TYR A CE1 1 ATOM 417 C CE2 . TYR A 1 51 ? 13.730 10.592 50.259 1.00 7.97 ? 133 TYR A CE2 1 ATOM 418 C CZ . TYR A 1 51 ? 12.720 11.202 49.544 1.00 7.48 ? 133 TYR A CZ 1 ATOM 419 O OH . TYR A 1 51 ? 12.364 10.708 48.308 1.00 7.79 ? 133 TYR A OH 1 ATOM 420 N N . ALA A 1 52 ? 14.091 11.848 56.445 1.00 5.03 ? 134 ALA A N 1 ATOM 421 C CA . ALA A 1 52 ? 14.839 12.129 57.674 1.00 3.95 ? 134 ALA A CA 1 ATOM 422 C C . ALA A 1 52 ? 15.766 10.980 58.034 1.00 5.04 ? 134 ALA A C 1 ATOM 423 O O . ALA A 1 52 ? 15.686 9.895 57.454 1.00 4.69 ? 134 ALA A O 1 ATOM 424 C CB . ALA A 1 52 ? 13.888 12.416 58.839 1.00 2.74 ? 134 ALA A CB 1 ATOM 425 N N . LEU A 1 53 ? 16.647 11.223 58.996 1.00 2.94 ? 135 LEU A N 1 ATOM 426 C CA . LEU A 1 53 ? 17.470 10.157 59.546 1.00 5.32 ? 135 LEU A CA 1 ATOM 427 C C . LEU A 1 53 ? 16.778 9.567 60.772 1.00 5.69 ? 135 LEU A C 1 ATOM 428 O O . LEU A 1 53 ? 16.675 10.219 61.811 1.00 5.94 ? 135 LEU A O 1 ATOM 429 C CB . LEU A 1 53 ? 18.860 10.679 59.917 1.00 5.51 ? 135 LEU A CB 1 ATOM 430 C CG . LEU A 1 53 ? 19.727 11.156 58.748 1.00 7.84 ? 135 LEU A CG 1 ATOM 431 C CD1 . LEU A 1 53 ? 21.022 11.782 59.243 1.00 7.16 ? 135 LEU A CD1 1 ATOM 432 C CD2 . LEU A 1 53 ? 20.036 10.007 57.794 1.00 4.77 ? 135 LEU A CD2 1 ATOM 433 N N . SER A 1 54 ? 16.279 8.341 60.634 1.00 3.65 ? 136 SER A N 1 ATOM 434 C CA . SER A 1 54 ? 15.718 7.621 61.770 1.00 4.35 ? 136 SER A CA 1 ATOM 435 C C . SER A 1 54 ? 16.810 7.332 62.791 1.00 5.51 ? 136 SER A C 1 ATOM 436 O O . SER A 1 54 ? 18.001 7.334 62.457 1.00 4.62 ? 136 SER A O 1 ATOM 437 C CB . SER A 1 54 ? 15.100 6.301 61.308 1.00 5.66 ? 136 SER A CB 1 ATOM 438 O OG . SER A 1 54 ? 14.591 5.574 62.416 1.00 4.99 ? 136 SER A OG 1 ATOM 439 N N . GLN A 1 55 ? 16.403 7.079 64.031 1.00 4.15 ? 137 GLN A N 1 ATOM 440 C CA . GLN A 1 55 ? 17.318 6.621 65.074 1.00 5.40 ? 137 GLN A CA 1 ATOM 441 C C . GLN A 1 55 ? 17.062 5.156 65.421 1.00 6.35 ? 137 GLN A C 1 ATOM 442 O O . GLN A 1 55 ? 17.660 4.625 66.355 1.00 6.06 ? 137 GLN A O 1 ATOM 443 C CB . GLN A 1 55 ? 17.184 7.481 66.343 1.00 3.81 ? 137 GLN A CB 1 ATOM 444 C CG . GLN A 1 55 ? 17.680 8.925 66.203 1.00 3.83 ? 137 GLN A CG 1 ATOM 445 C CD . GLN A 1 55 ? 19.174 9.072 66.427 1.00 6.08 ? 137 GLN A CD 1 ATOM 446 O OE1 . GLN A 1 55 ? 19.919 8.093 66.401 1.00 5.91 ? 137 GLN A OE1 1 ATOM 447 N NE2 . GLN A 1 55 ? 19.622 10.305 66.655 1.00 5.10 ? 137 GLN A NE2 1 ATOM 448 N N . GLY A 1 56 ? 16.180 4.497 64.673 1.00 5.08 ? 138 GLY A N 1 ATOM 449 C CA . GLY A 1 56 ? 15.982 3.069 64.859 1.00 3.99 ? 138 GLY A CA 1 ATOM 450 C C . GLY A 1 56 ? 15.291 2.721 66.165 1.00 3.13 ? 138 GLY A C 1 ATOM 451 O O . GLY A 1 56 ? 15.616 1.719 66.809 1.00 5.72 ? 138 GLY A O 1 ATOM 452 N N . THR A 1 57 ? 14.328 3.556 66.547 1.00 4.04 ? 139 THR A N 1 ATOM 453 C CA . THR A 1 57 ? 13.525 3.346 67.743 1.00 4.07 ? 139 THR A CA 1 ATOM 454 C C . THR A 1 57 ? 12.326 4.285 67.644 1.00 4.29 ? 139 THR A C 1 ATOM 455 O O . THR A 1 57 ? 12.398 5.287 66.931 1.00 3.94 ? 139 THR A O 1 ATOM 456 C CB . THR A 1 57 ? 14.333 3.682 69.015 1.00 4.83 ? 139 THR A CB 1 ATOM 457 O OG1 . THR A 1 57 ? 13.490 3.556 70.164 1.00 6.39 ? 139 THR A OG1 1 ATOM 458 C CG2 . THR A 1 57 ? 14.877 5.109 68.946 1.00 6.85 ? 139 THR A CG2 1 ATOM 459 N N . THR A 1 58 ? 11.221 3.972 68.321 1.00 4.29 ? 140 THR A N 1 ATOM 460 C CA . THR A 1 58 ? 10.123 4.939 68.416 1.00 5.12 ? 140 THR A CA 1 ATOM 461 C C . THR A 1 58 ? 10.356 5.879 69.596 1.00 5.41 ? 140 THR A C 1 ATOM 462 O O . THR A 1 58 ? 11.229 5.625 70.424 1.00 6.27 ? 140 THR A O 1 ATOM 463 C CB . THR A 1 58 ? 8.738 4.281 68.564 1.00 6.30 ? 140 THR A CB 1 ATOM 464 O OG1 . THR A 1 58 ? 8.665 3.589 69.814 1.00 5.03 ? 140 THR A OG1 1 ATOM 465 C CG2 . THR A 1 58 ? 8.464 3.301 67.423 1.00 4.86 ? 140 THR A CG2 1 ATOM 466 N N . ILE A 1 59 ? 9.574 6.957 69.675 1.00 4.24 ? 141 ILE A N 1 ATOM 467 C CA . ILE A 1 59 ? 9.747 7.945 70.745 1.00 5.70 ? 141 ILE A CA 1 ATOM 468 C C . ILE A 1 59 ? 9.389 7.379 72.114 1.00 6.54 ? 141 ILE A C 1 ATOM 469 O O . ILE A 1 59 ? 10.093 7.619 73.098 1.00 8.31 ? 141 ILE A O 1 ATOM 470 C CB . ILE A 1 59 ? 8.895 9.210 70.523 1.00 8.47 ? 141 ILE A CB 1 ATOM 471 C CG1 . ILE A 1 59 ? 9.034 9.731 69.098 1.00 14.20 ? 141 ILE A CG1 1 ATOM 472 C CG2 . ILE A 1 59 ? 9.301 10.298 71.513 1.00 8.80 ? 141 ILE A CG2 1 ATOM 473 C CD1 . ILE A 1 59 ? 8.208 10.988 68.834 1.00 17.23 ? 141 ILE A CD1 1 ATOM 474 N N . ARG A 1 60 ? 8.282 6.645 72.174 1.00 7.39 ? 142 ARG A N 1 ATOM 475 C CA . ARG A 1 60 ? 7.828 6.053 73.423 1.00 8.53 ? 142 ARG A CA 1 ATOM 476 C C . ARG A 1 60 ? 8.637 4.811 73.779 1.00 8.47 ? 142 ARG A C 1 ATOM 477 O O . ARG A 1 60 ? 8.590 4.333 74.911 1.00 7.30 ? 142 ARG A O 1 ATOM 478 C CB . ARG A 1 60 ? 6.336 5.721 73.353 1.00 9.96 ? 142 ARG A CB 1 ATOM 479 C CG . ARG A 1 60 ? 5.432 6.928 73.588 1.00 12.34 ? 142 ARG A CG 1 ATOM 480 C CD . ARG A 1 60 ? 5.656 7.514 74.982 1.00 11.80 ? 142 ARG A CD 1 ATOM 481 N NE . ARG A 1 60 ? 4.545 8.360 75.424 1.00 10.41 ? 142 ARG A NE 1 ATOM 482 C CZ . ARG A 1 60 ? 4.492 8.953 76.612 1.00 15.75 ? 142 ARG A CZ 1 ATOM 483 N NH1 . ARG A 1 60 ? 5.490 8.791 77.472 1.00 13.39 ? 142 ARG A NH1 1 ATOM 484 N NH2 . ARG A 1 60 ? 3.446 9.706 76.945 1.00 11.68 ? 142 ARG A NH2 1 ATOM 485 N N . GLY A 1 61 ? 9.382 4.292 72.811 1.00 5.07 ? 143 GLY A N 1 ATOM 486 C CA . GLY A 1 61 ? 10.251 3.155 73.060 1.00 6.45 ? 143 GLY A CA 1 ATOM 487 C C . GLY A 1 61 ? 11.384 3.507 74.001 1.00 7.13 ? 143 GLY A C 1 ATOM 488 O O . GLY A 1 61 ? 11.884 4.635 73.989 1.00 6.88 ? 143 GLY A O 1 ATOM 489 N N . LYS A 1 62 ? 11.801 2.540 74.814 1.00 4.98 ? 144 LYS A N 1 ATOM 490 C CA . LYS A 1 62 ? 12.884 2.773 75.759 1.00 5.34 ? 144 LYS A CA 1 ATOM 491 C C . LYS A 1 62 ? 14.212 3.082 75.071 1.00 5.35 ? 144 LYS A C 1 ATOM 492 O O . LYS A 1 62 ? 15.091 3.714 75.663 1.00 6.29 ? 144 LYS A O 1 ATOM 493 C CB . LYS A 1 62 ? 13.032 1.585 76.717 1.00 4.31 ? 144 LYS A CB 1 ATOM 494 C CG . LYS A 1 62 ? 11.853 1.411 77.669 1.00 8.91 ? 144 LYS A CG 1 ATOM 495 C CD . LYS A 1 62 ? 12.038 0.172 78.548 1.00 10.97 ? 144 LYS A CD 1 ATOM 496 C CE . LYS A 1 62 ? 10.854 -0.032 79.486 1.00 13.73 ? 144 LYS A CE 1 ATOM 497 N NZ . LYS A 1 62 ? 11.043 -1.237 80.360 1.00 14.28 ? 144 LYS A NZ 1 ATOM 498 N N . HIS A 1 63 ? 14.365 2.646 73.822 1.00 4.94 ? 145 HIS A N 1 ATOM 499 C CA . HIS A 1 63 ? 15.590 2.936 73.085 1.00 4.83 ? 145 HIS A CA 1 ATOM 500 C C . HIS A 1 63 ? 15.671 4.401 72.618 1.00 5.96 ? 145 HIS A C 1 ATOM 501 O O . HIS A 1 63 ? 16.672 4.813 72.032 1.00 7.17 ? 145 HIS A O 1 ATOM 502 C CB . HIS A 1 63 ? 15.769 1.970 71.905 1.00 4.98 ? 145 HIS A CB 1 ATOM 503 C CG . HIS A 1 63 ? 15.992 0.544 72.310 1.00 6.56 ? 145 HIS A CG 1 ATOM 504 N ND1 . HIS A 1 63 ? 14.973 -0.384 72.364 1.00 5.87 ? 145 HIS A ND1 1 ATOM 505 C CD2 . HIS A 1 63 ? 17.119 -0.116 72.674 1.00 7.19 ? 145 HIS A CD2 1 ATOM 506 C CE1 . HIS A 1 63 ? 15.461 -1.552 72.743 1.00 7.31 ? 145 HIS A CE1 1 ATOM 507 N NE2 . HIS A 1 63 ? 16.760 -1.417 72.939 1.00 6.87 ? 145 HIS A NE2 1 ATOM 508 N N . SER A 1 64 ? 14.637 5.196 72.893 1.00 5.33 ? 146 SER A N 1 ATOM 509 C CA . SER A 1 64 ? 14.699 6.630 72.585 1.00 6.75 ? 146 SER A CA 1 ATOM 510 C C . SER A 1 64 ? 15.701 7.329 73.507 1.00 5.65 ? 146 SER A C 1 ATOM 511 O O . SER A 1 64 ? 16.168 8.435 73.217 1.00 5.89 ? 146 SER A O 1 ATOM 512 C CB . SER A 1 64 ? 13.317 7.293 72.691 1.00 5.08 ? 146 SER A CB 1 ATOM 513 O OG . SER A 1 64 ? 12.884 7.405 74.037 1.00 8.15 ? 146 SER A OG 1 ATOM 514 N N . ASN A 1 65 ? 16.030 6.671 74.616 1.00 6.33 ? 147 ASN A N 1 ATOM 515 C CA . ASN A 1 65 ? 17.011 7.189 75.568 1.00 9.76 ? 147 ASN A CA 1 ATOM 516 C C . ASN A 1 65 ? 18.393 7.247 74.927 1.00 9.83 ? 147 ASN A C 1 ATOM 517 O O . ASN A 1 65 ? 18.947 6.216 74.543 1.00 9.67 ? 147 ASN A O 1 ATOM 518 C CB . ASN A 1 65 ? 17.043 6.282 76.805 1.00 9.25 ? 147 ASN A CB 1 ATOM 519 C CG . ASN A 1 65 ? 17.778 6.904 77.983 1.00 13.78 ? 147 ASN A CG 1 ATOM 520 O OD1 . ASN A 1 65 ? 18.534 7.870 77.829 1.00 9.45 ? 147 ASN A OD1 1 ATOM 521 N ND2 . ASN A 1 65 ? 17.555 6.336 79.175 1.00 18.25 ? 147 ASN A ND2 1 ATOM 522 N N . GLY A 1 66 ? 18.946 8.450 74.802 1.00 6.18 ? 148 GLY A N 1 ATOM 523 C CA . GLY A 1 66 ? 20.272 8.617 74.228 1.00 9.14 ? 148 GLY A CA 1 ATOM 524 C C . GLY A 1 66 ? 20.287 9.103 72.785 1.00 10.08 ? 148 GLY A C 1 ATOM 525 O O . GLY A 1 66 ? 21.351 9.213 72.179 1.00 7.84 ? 148 GLY A O 1 ATOM 526 N N . THR A 1 67 ? 19.116 9.416 72.236 1.00 5.73 ? 149 THR A N 1 ATOM 527 C CA . THR A 1 67 ? 19.030 9.799 70.825 1.00 8.26 ? 149 THR A CA 1 ATOM 528 C C . THR A 1 67 ? 19.505 11.220 70.506 1.00 8.03 ? 149 THR A C 1 ATOM 529 O O . THR A 1 67 ? 19.371 11.669 69.370 1.00 7.62 ? 149 THR A O 1 ATOM 530 C CB . THR A 1 67 ? 17.611 9.581 70.231 1.00 5.57 ? 149 THR A CB 1 ATOM 531 O OG1 . THR A 1 67 ? 16.622 10.080 71.137 1.00 5.81 ? 149 THR A OG1 1 ATOM 532 C CG2 . THR A 1 67 ? 17.358 8.095 69.972 1.00 6.67 ? 149 THR A CG2 1 ATOM 533 N N . ILE A 1 68 ? 20.079 11.925 71.480 1.00 5.60 ? 150 ILE A N 1 ATOM 534 C CA . ILE A 1 68 ? 20.759 13.184 71.154 1.00 5.10 ? 150 ILE A CA 1 ATOM 535 C C . ILE A 1 68 ? 21.984 12.879 70.280 1.00 7.23 ? 150 ILE A C 1 ATOM 536 O O . ILE A 1 68 ? 22.450 13.729 69.516 1.00 8.18 ? 150 ILE A O 1 ATOM 537 C CB . ILE A 1 68 ? 21.176 13.980 72.422 1.00 10.60 ? 150 ILE A CB 1 ATOM 538 C CG1 . ILE A 1 68 ? 21.610 15.409 72.050 1.00 11.05 ? 150 ILE A CG1 1 ATOM 539 C CG2 . ILE A 1 68 ? 22.264 13.245 73.197 1.00 10.23 ? 150 ILE A CG2 1 ATOM 540 C CD1 . ILE A 1 68 ? 21.908 16.319 73.248 1.00 15.98 ? 150 ILE A CD1 1 ATOM 541 N N . HIS A 1 69 ? 22.486 11.654 70.386 1.00 11.56 ? 151 HIS A N 1 ATOM 542 C CA . HIS A 1 69 ? 23.692 11.275 69.667 1.00 13.15 ? 151 HIS A CA 1 ATOM 543 C C . HIS A 1 69 ? 23.473 11.241 68.162 1.00 12.28 ? 151 HIS A C 1 ATOM 544 O O . HIS A 1 69 ? 22.443 10.778 67.674 1.00 10.88 ? 151 HIS A O 1 ATOM 545 C CB . HIS A 1 69 ? 24.233 9.944 70.184 1.00 14.92 ? 151 HIS A CB 1 ATOM 546 C CG . HIS A 1 69 ? 24.739 10.014 71.590 1.00 16.98 ? 151 HIS A CG 1 ATOM 547 N ND1 . HIS A 1 69 ? 25.668 10.948 71.998 1.00 21.23 ? 151 HIS A ND1 1 ATOM 548 C CD2 . HIS A 1 69 ? 24.443 9.275 72.685 1.00 20.86 ? 151 HIS A CD2 1 ATOM 549 C CE1 . HIS A 1 69 ? 25.923 10.780 73.282 1.00 18.09 ? 151 HIS A CE1 1 ATOM 550 N NE2 . HIS A 1 69 ? 25.193 9.770 73.723 1.00 25.67 ? 151 HIS A NE2 1 ATOM 551 N N . ASP A 1 70 ? 24.461 11.744 67.434 1.00 8.07 ? 152 ASP A N 1 ATOM 552 C CA . ASP A 1 70 ? 24.342 11.933 65.982 1.00 7.40 ? 152 ASP A CA 1 ATOM 553 C C . ASP A 1 70 ? 24.603 10.697 65.134 1.00 7.86 ? 152 ASP A C 1 ATOM 554 O O . ASP A 1 70 ? 23.977 10.513 64.090 1.00 6.97 ? 152 ASP A O 1 ATOM 555 C CB . ASP A 1 70 ? 25.301 13.029 65.507 1.00 9.22 ? 152 ASP A CB 1 ATOM 556 C CG . ASP A 1 70 ? 24.906 14.403 65.986 1.00 13.28 ? 152 ASP A CG 1 ATOM 557 O OD1 . ASP A 1 70 ? 23.716 14.765 65.858 1.00 11.15 ? 152 ASP A OD1 1 ATOM 558 O OD2 . ASP A 1 70 ? 25.794 15.126 66.481 1.00 13.98 ? 152 ASP A OD2 1 ATOM 559 N N . ARG A 1 71 ? 25.549 9.868 65.558 1.00 5.75 ? 153 ARG A N 1 ATOM 560 C CA . ARG A 1 71 ? 26.043 8.806 64.690 1.00 6.30 ? 153 ARG A CA 1 ATOM 561 C C . ARG A 1 71 ? 26.037 7.464 65.400 1.00 15.36 ? 153 ARG A C 1 ATOM 562 O O . ARG A 1 71 ? 26.828 7.226 66.316 1.00 25.90 ? 153 ARG A O 1 ATOM 563 C CB . ARG A 1 71 ? 27.453 9.140 64.177 1.00 5.87 ? 153 ARG A CB 1 ATOM 564 C CG . ARG A 1 71 ? 27.525 10.441 63.372 1.00 7.24 ? 153 ARG A CG 1 ATOM 565 C CD . ARG A 1 71 ? 28.950 10.742 62.904 1.00 5.99 ? 153 ARG A CD 1 ATOM 566 N NE . ARG A 1 71 ? 29.869 10.831 64.035 1.00 10.56 ? 153 ARG A NE 1 ATOM 567 C CZ . ARG A 1 71 ? 29.981 11.893 64.828 1.00 11.80 ? 153 ARG A CZ 1 ATOM 568 N NH1 . ARG A 1 71 ? 29.222 12.965 64.627 1.00 7.71 ? 153 ARG A NH1 1 ATOM 569 N NH2 . ARG A 1 71 ? 30.845 11.878 65.836 1.00 11.50 ? 153 ARG A NH2 1 ATOM 570 N N . SER A 1 72 ? 25.113 6.602 64.993 1.00 11.07 ? 154 SER A N 1 ATOM 571 C CA . SER A 1 72 ? 25.054 5.240 65.506 1.00 7.30 ? 154 SER A CA 1 ATOM 572 C C . SER A 1 72 ? 24.760 4.313 64.341 1.00 8.24 ? 154 SER A C 1 ATOM 573 O O . SER A 1 72 ? 24.370 4.763 63.255 1.00 5.89 ? 154 SER A O 1 ATOM 574 C CB . SER A 1 72 ? 23.940 5.097 66.535 1.00 8.60 ? 154 SER A CB 1 ATOM 575 O OG . SER A 1 72 ? 22.694 4.915 65.884 1.00 7.79 ? 154 SER A OG 1 ATOM 576 N N . GLN A 1 73 ? 24.912 3.015 64.587 1.00 4.97 ? 155 GLN A N 1 ATOM 577 C CA . GLN A 1 73 ? 24.654 1.992 63.586 1.00 5.39 ? 155 GLN A CA 1 ATOM 578 C C . GLN A 1 73 ? 23.164 1.766 63.363 1.00 7.32 ? 155 GLN A C 1 ATOM 579 O O . GLN A 1 73 ? 22.776 0.940 62.533 1.00 6.76 ? 155 GLN A O 1 ATOM 580 C CB . GLN A 1 73 ? 25.301 0.673 64.019 1.00 5.84 ? 155 GLN A CB 1 ATOM 581 C CG . GLN A 1 73 ? 26.832 0.704 64.083 1.00 6.16 ? 155 GLN A CG 1 ATOM 582 C CD . GLN A 1 73 ? 27.377 0.976 65.469 1.00 8.98 ? 155 GLN A CD 1 ATOM 583 O OE1 . GLN A 1 73 ? 26.803 1.750 66.246 1.00 7.81 ? 155 GLN A OE1 1 ATOM 584 N NE2 . GLN A 1 73 ? 28.504 0.339 65.793 1.00 7.66 ? 155 GLN A NE2 1 ATOM 585 N N . TYR A 1 74 ? 22.331 2.501 64.094 1.00 5.73 ? 156 TYR A N 1 ATOM 586 C CA . TYR A 1 74 ? 20.895 2.238 64.099 1.00 3.13 ? 156 TYR A CA 1 ATOM 587 C C . TYR A 1 74 ? 20.152 3.308 63.313 1.00 5.47 ? 156 TYR A C 1 ATOM 588 O O . TYR A 1 74 ? 18.923 3.330 63.287 1.00 5.25 ? 156 TYR A O 1 ATOM 589 C CB . TYR A 1 74 ? 20.392 2.121 65.545 1.00 3.87 ? 156 TYR A CB 1 ATOM 590 C CG . TYR A 1 74 ? 21.396 1.354 66.364 1.00 6.14 ? 156 TYR A CG 1 ATOM 591 C CD1 . TYR A 1 74 ? 21.772 0.070 65.986 1.00 6.18 ? 156 TYR A CD1 1 ATOM 592 C CD2 . TYR A 1 74 ? 22.022 1.927 67.465 1.00 9.19 ? 156 TYR A CD2 1 ATOM 593 C CE1 . TYR A 1 74 ? 22.729 -0.634 66.691 1.00 4.65 ? 156 TYR A CE1 1 ATOM 594 C CE2 . TYR A 1 74 ? 22.977 1.224 68.185 1.00 7.97 ? 156 TYR A CE2 1 ATOM 595 C CZ . TYR A 1 74 ? 23.323 -0.055 67.789 1.00 8.19 ? 156 TYR A CZ 1 ATOM 596 O OH . TYR A 1 74 ? 24.271 -0.768 68.492 1.00 9.72 ? 156 TYR A OH 1 ATOM 597 N N . ARG A 1 75 ? 20.909 4.173 62.646 1.00 4.63 ? 157 ARG A N 1 ATOM 598 C CA . ARG A 1 75 ? 20.314 5.244 61.853 1.00 3.03 ? 157 ARG A CA 1 ATOM 599 C C . ARG A 1 75 ? 20.165 4.855 60.392 1.00 4.40 ? 157 ARG A C 1 ATOM 600 O O . ARG A 1 75 ? 20.925 4.033 59.869 1.00 6.55 ? 157 ARG A O 1 ATOM 601 C CB . ARG A 1 75 ? 21.137 6.530 61.971 1.00 4.57 ? 157 ARG A CB 1 ATOM 602 C CG . ARG A 1 75 ? 21.270 7.042 63.401 1.00 4.76 ? 157 ARG A CG 1 ATOM 603 C CD . ARG A 1 75 ? 21.508 8.542 63.424 1.00 4.93 ? 157 ARG A CD 1 ATOM 604 N NE . ARG A 1 75 ? 20.268 9.306 63.253 1.00 5.20 ? 157 ARG A NE 1 ATOM 605 C CZ . ARG A 1 75 ? 20.186 10.624 63.399 1.00 5.62 ? 157 ARG A CZ 1 ATOM 606 N NH1 . ARG A 1 75 ? 19.021 11.245 63.243 1.00 4.55 ? 157 ARG A NH1 1 ATOM 607 N NH2 . ARG A 1 75 ? 21.273 11.321 63.708 1.00 4.99 ? 157 ARG A NH2 1 ATOM 608 N N . ALA A 1 76 ? 19.176 5.448 59.736 1.00 3.54 ? 158 ALA A N 1 ATOM 609 C CA . ALA A 1 76 ? 18.944 5.211 58.317 1.00 4.03 ? 158 ALA A CA 1 ATOM 610 C C . ALA A 1 76 ? 18.188 6.384 57.730 1.00 5.92 ? 158 ALA A C 1 ATOM 611 O O . ALA A 1 76 ? 17.434 7.056 58.437 1.00 4.86 ? 158 ALA A O 1 ATOM 612 C CB . ALA A 1 76 ? 18.142 3.931 58.120 1.00 7.41 ? 158 ALA A CB 1 ATOM 613 N N . LEU A 1 77 ? 18.387 6.634 56.439 1.00 5.14 ? 159 LEU A N 1 ATOM 614 C CA . LEU A 1 77 ? 17.561 7.606 55.734 1.00 3.43 ? 159 LEU A CA 1 ATOM 615 C C . LEU A 1 77 ? 16.230 6.931 55.424 1.00 4.30 ? 159 LEU A C 1 ATOM 616 O O . LEU A 1 77 ? 16.197 5.873 54.793 1.00 5.94 ? 159 LEU A O 1 ATOM 617 C CB . LEU A 1 77 ? 18.233 8.057 54.436 1.00 5.02 ? 159 LEU A CB 1 ATOM 618 C CG . LEU A 1 77 ? 17.354 8.911 53.517 1.00 4.51 ? 159 LEU A CG 1 ATOM 619 C CD1 . LEU A 1 77 ? 17.012 10.234 54.190 1.00 4.18 ? 159 LEU A CD1 1 ATOM 620 C CD2 . LEU A 1 77 ? 18.037 9.148 52.176 1.00 4.26 ? 159 LEU A CD2 1 ATOM 621 N N . ILE A 1 78 ? 15.141 7.525 55.897 1.00 4.73 ? 160 ILE A N 1 ATOM 622 C CA . ILE A 1 78 ? 13.805 7.032 55.584 1.00 4.80 ? 160 ILE A CA 1 ATOM 623 C C . ILE A 1 78 ? 12.997 8.097 54.856 1.00 5.46 ? 160 ILE A C 1 ATOM 624 O O . ILE A 1 78 ? 13.274 9.290 54.977 1.00 6.03 ? 160 ILE A O 1 ATOM 625 C CB . ILE A 1 78 ? 13.034 6.612 56.849 1.00 4.84 ? 160 ILE A CB 1 ATOM 626 C CG1 . ILE A 1 78 ? 13.023 7.744 57.882 1.00 4.16 ? 160 ILE A CG1 1 ATOM 627 C CG2 . ILE A 1 78 ? 13.642 5.347 57.450 1.00 3.79 ? 160 ILE A CG2 1 ATOM 628 C CD1 . ILE A 1 78 ? 11.990 7.532 59.003 1.00 3.60 ? 160 ILE A CD1 1 ATOM 629 N N . SER A 1 79 ? 12.001 7.665 54.095 1.00 3.64 ? 161 SER A N 1 ATOM 630 C CA . SER A 1 79 ? 11.055 8.602 53.505 1.00 5.54 ? 161 SER A CA 1 ATOM 631 C C . SER A 1 79 ? 9.645 8.121 53.798 1.00 5.69 ? 161 SER A C 1 ATOM 632 O O . SER A 1 79 ? 9.427 6.932 54.051 1.00 6.61 ? 161 SER A O 1 ATOM 633 C CB . SER A 1 79 ? 11.276 8.756 51.998 1.00 6.32 ? 161 SER A CB 1 ATOM 634 O OG . SER A 1 79 ? 10.920 7.579 51.301 1.00 7.80 ? 161 SER A OG 1 ATOM 635 N N . TRP A 1 80 ? 8.688 9.043 53.782 1.00 5.24 ? 162 TRP A N 1 ATOM 636 C CA . TRP A 1 80 ? 7.302 8.697 54.089 1.00 6.78 ? 162 TRP A CA 1 ATOM 637 C C . TRP A 1 80 ? 6.367 9.731 53.458 1.00 5.53 ? 162 TRP A C 1 ATOM 638 O O . TRP A 1 80 ? 6.817 10.816 53.083 1.00 6.74 ? 162 TRP A O 1 ATOM 639 C CB . TRP A 1 80 ? 7.106 8.555 55.610 1.00 5.98 ? 162 TRP A CB 1 ATOM 640 C CG . TRP A 1 80 ? 7.266 9.827 56.394 1.00 4.35 ? 162 TRP A CG 1 ATOM 641 C CD1 . TRP A 1 80 ? 6.272 10.671 56.789 1.00 3.48 ? 162 TRP A CD1 1 ATOM 642 C CD2 . TRP A 1 80 ? 8.489 10.381 56.895 1.00 4.05 ? 162 TRP A CD2 1 ATOM 643 N NE1 . TRP A 1 80 ? 6.798 11.721 57.501 1.00 4.85 ? 162 TRP A NE1 1 ATOM 644 C CE2 . TRP A 1 80 ? 8.159 11.566 57.580 1.00 5.44 ? 162 TRP A CE2 1 ATOM 645 C CE3 . TRP A 1 80 ? 9.833 9.991 56.826 1.00 4.16 ? 162 TRP A CE3 1 ATOM 646 C CZ2 . TRP A 1 80 ? 9.120 12.367 58.193 1.00 3.64 ? 162 TRP A CZ2 1 ATOM 647 C CZ3 . TRP A 1 80 ? 10.792 10.791 57.433 1.00 2.80 ? 162 TRP A CZ3 1 ATOM 648 C CH2 . TRP A 1 80 ? 10.429 11.964 58.109 1.00 4.73 ? 162 TRP A CH2 1 ATOM 649 N N . PRO A 1 81 ? 5.073 9.392 53.305 1.00 6.23 ? 163 PRO A N 1 ATOM 650 C CA . PRO A 1 81 ? 4.163 10.291 52.578 1.00 6.91 ? 163 PRO A CA 1 ATOM 651 C C . PRO A 1 81 ? 4.073 11.694 53.167 1.00 6.50 ? 163 PRO A C 1 ATOM 652 O O . PRO A 1 81 ? 4.094 11.860 54.390 1.00 5.69 ? 163 PRO A O 1 ATOM 653 C CB . PRO A 1 81 ? 2.812 9.579 52.687 1.00 7.85 ? 163 PRO A CB 1 ATOM 654 C CG . PRO A 1 81 ? 3.181 8.121 52.788 1.00 8.41 ? 163 PRO A CG 1 ATOM 655 C CD . PRO A 1 81 ? 4.415 8.116 53.650 1.00 6.56 ? 163 PRO A CD 1 ATOM 656 N N . LEU A 1 82 ? 3.979 12.685 52.282 1.00 6.76 ? 164 LEU A N 1 ATOM 657 C CA . LEU A 1 82 ? 3.904 14.096 52.653 1.00 5.22 ? 164 LEU A CA 1 ATOM 658 C C . LEU A 1 82 ? 2.924 14.346 53.796 1.00 4.98 ? 164 LEU A C 1 ATOM 659 O O . LEU A 1 82 ? 1.758 13.958 53.712 1.00 6.06 ? 164 LEU A O 1 ATOM 660 C CB . LEU A 1 82 ? 3.486 14.933 51.438 1.00 7.90 ? 164 LEU A CB 1 ATOM 661 C CG . LEU A 1 82 ? 3.694 16.445 51.558 1.00 14.60 ? 164 LEU A CG 1 ATOM 662 C CD1 . LEU A 1 82 ? 5.167 16.771 51.399 1.00 16.76 ? 164 LEU A CD1 1 ATOM 663 C CD2 . LEU A 1 82 ? 2.855 17.204 50.529 1.00 9.97 ? 164 LEU A CD2 1 ATOM 664 N N . SER A 1 83 ? 3.428 14.969 54.864 1.00 5.34 ? 165 SER A N 1 ATOM 665 C CA . SER A 1 83 ? 2.639 15.389 56.037 1.00 5.53 ? 165 SER A CA 1 ATOM 666 C C . SER A 1 83 ? 2.107 14.277 56.947 1.00 5.63 ? 165 SER A C 1 ATOM 667 O O . SER A 1 83 ? 1.481 14.561 57.969 1.00 6.04 ? 165 SER A O 1 ATOM 668 C CB . SER A 1 83 ? 1.518 16.357 55.644 1.00 5.46 ? 165 SER A CB 1 ATOM 669 O OG . SER A 1 83 ? 2.060 17.560 55.130 1.00 5.91 ? 165 SER A OG 1 ATOM 670 N N . SER A 1 84 ? 2.341 13.019 56.582 1.00 5.48 ? 166 SER A N 1 ATOM 671 C CA . SER A 1 84 ? 2.173 11.935 57.539 1.00 6.32 ? 166 SER A CA 1 ATOM 672 C C . SER A 1 84 ? 3.379 11.984 58.466 1.00 5.45 ? 166 SER A C 1 ATOM 673 O O . SER A 1 84 ? 4.393 12.592 58.118 1.00 6.57 ? 166 SER A O 1 ATOM 674 C CB . SER A 1 84 ? 2.124 10.582 56.823 1.00 9.85 ? 166 SER A CB 1 ATOM 675 O OG . SER A 1 84 ? 0.838 10.343 56.290 1.00 16.77 ? 166 SER A OG 1 ATOM 676 N N . PRO A 1 85 ? 3.284 11.358 59.651 1.00 6.24 ? 167 PRO A N 1 ATOM 677 C CA . PRO A 1 85 ? 4.491 11.277 60.476 1.00 7.31 ? 167 PRO A CA 1 ATOM 678 C C . PRO A 1 85 ? 5.332 10.063 60.086 1.00 4.99 ? 167 PRO A C 1 ATOM 679 O O . PRO A 1 85 ? 4.823 9.143 59.437 1.00 6.41 ? 167 PRO A O 1 ATOM 680 C CB . PRO A 1 85 ? 3.925 11.116 61.893 1.00 9.71 ? 167 PRO A CB 1 ATOM 681 C CG . PRO A 1 85 ? 2.648 10.390 61.703 1.00 8.88 ? 167 PRO A CG 1 ATOM 682 C CD . PRO A 1 85 ? 2.112 10.775 60.334 1.00 5.74 ? 167 PRO A CD 1 ATOM 683 N N . PRO A 1 86 ? 6.618 10.055 60.464 1.00 4.20 ? 168 PRO A N 1 ATOM 684 C CA . PRO A 1 86 ? 7.449 8.898 60.125 1.00 4.08 ? 168 PRO A CA 1 ATOM 685 C C . PRO A 1 86 ? 7.181 7.724 61.068 1.00 7.68 ? 168 PRO A C 1 ATOM 686 O O . PRO A 1 86 ? 7.748 7.665 62.154 1.00 8.78 ? 168 PRO A O 1 ATOM 687 C CB . PRO A 1 86 ? 8.871 9.430 60.312 1.00 5.93 ? 168 PRO A CB 1 ATOM 688 C CG . PRO A 1 86 ? 8.740 10.502 61.362 1.00 7.12 ? 168 PRO A CG 1 ATOM 689 C CD . PRO A 1 86 ? 7.379 11.120 61.145 1.00 4.77 ? 168 PRO A CD 1 ATOM 690 N N . THR A 1 87 ? 6.324 6.794 60.661 1.00 6.89 ? 169 THR A N 1 ATOM 691 C CA . THR A 1 87 ? 5.978 5.687 61.548 1.00 6.38 ? 169 THR A CA 1 ATOM 692 C C . THR A 1 87 ? 6.739 4.429 61.160 1.00 5.49 ? 169 THR A C 1 ATOM 693 O O . THR A 1 87 ? 7.298 4.340 60.065 1.00 5.22 ? 169 THR A O 1 ATOM 694 C CB . THR A 1 87 ? 4.475 5.379 61.516 1.00 6.78 ? 169 THR A CB 1 ATOM 695 O OG1 . THR A 1 87 ? 4.169 4.657 60.321 1.00 11.25 ? 169 THR A OG1 1 ATOM 696 C CG2 . THR A 1 87 ? 3.664 6.671 61.548 1.00 8.51 ? 169 THR A CG2 1 ATOM 697 N N . VAL A 1 88 ? 6.755 3.459 62.068 1.00 4.71 ? 170 VAL A N 1 ATOM 698 C CA . VAL A 1 88 ? 7.377 2.167 61.805 1.00 5.89 ? 170 VAL A CA 1 ATOM 699 C C . VAL A 1 88 ? 6.749 1.516 60.576 1.00 6.45 ? 170 VAL A C 1 ATOM 700 O O . VAL A 1 88 ? 7.428 0.845 59.807 1.00 9.56 ? 170 VAL A O 1 ATOM 701 C CB . VAL A 1 88 ? 7.238 1.238 63.028 1.00 7.04 ? 170 VAL A CB 1 ATOM 702 C CG1 . VAL A 1 88 ? 7.785 -0.163 62.732 1.00 7.36 ? 170 VAL A CG1 1 ATOM 703 C CG2 . VAL A 1 88 ? 7.960 1.844 64.220 1.00 5.92 ? 170 VAL A CG2 1 ATOM 704 N N . TYR A 1 89 ? 5.457 1.762 60.378 1.00 6.67 ? 171 TYR A N 1 ATOM 705 C CA . TYR A 1 89 ? 4.677 1.032 59.379 1.00 7.93 ? 171 TYR A CA 1 ATOM 706 C C . TYR A 1 89 ? 4.532 1.736 58.019 1.00 10.89 ? 171 TYR A C 1 ATOM 707 O O . TYR A 1 89 ? 4.078 1.122 57.054 1.00 14.96 ? 171 TYR A O 1 ATOM 708 C CB . TYR A 1 89 ? 3.293 0.685 59.952 1.00 7.80 ? 171 TYR A CB 1 ATOM 709 C CG . TYR A 1 89 ? 3.351 0.220 61.394 1.00 6.78 ? 171 TYR A CG 1 ATOM 710 C CD1 . TYR A 1 89 ? 4.070 -0.911 61.743 1.00 6.52 ? 171 TYR A CD1 1 ATOM 711 C CD2 . TYR A 1 89 ? 2.697 0.920 62.403 1.00 8.31 ? 171 TYR A CD2 1 ATOM 712 C CE1 . TYR A 1 89 ? 4.143 -1.339 63.057 1.00 5.24 ? 171 TYR A CE1 1 ATOM 713 C CE2 . TYR A 1 89 ? 2.760 0.502 63.719 1.00 5.71 ? 171 TYR A CE2 1 ATOM 714 C CZ . TYR A 1 89 ? 3.487 -0.633 64.037 1.00 6.12 ? 171 TYR A CZ 1 ATOM 715 O OH . TYR A 1 89 ? 3.564 -1.065 65.339 1.00 7.18 ? 171 TYR A OH 1 ATOM 716 N N . ASN A 1 90 ? 4.912 3.010 57.934 1.00 9.61 ? 172 ASN A N 1 ATOM 717 C CA . ASN A 1 90 ? 4.766 3.751 56.675 1.00 10.23 ? 172 ASN A CA 1 ATOM 718 C C . ASN A 1 90 ? 6.087 4.296 56.139 1.00 12.19 ? 172 ASN A C 1 ATOM 719 O O . ASN A 1 90 ? 6.121 4.919 55.077 1.00 21.12 ? 172 ASN A O 1 ATOM 720 C CB . ASN A 1 90 ? 3.755 4.903 56.814 1.00 11.90 ? 172 ASN A CB 1 ATOM 721 C CG . ASN A 1 90 ? 4.300 6.076 57.631 1.00 18.70 ? 172 ASN A CG 1 ATOM 722 O OD1 . ASN A 1 90 ? 5.205 5.911 58.444 1.00 21.15 ? 172 ASN A OD1 1 ATOM 723 N ND2 . ASN A 1 90 ? 3.740 7.264 57.417 1.00 12.20 ? 172 ASN A ND2 1 ATOM 724 N N . SER A 1 91 ? 7.171 4.074 56.876 1.00 8.44 ? 173 SER A N 1 ATOM 725 C CA . SER A 1 91 ? 8.462 4.642 56.500 1.00 6.07 ? 173 SER A CA 1 ATOM 726 C C . SER A 1 91 ? 9.233 3.696 55.590 1.00 12.34 ? 173 SER A C 1 ATOM 727 O O . SER A 1 91 ? 9.366 2.514 55.888 1.00 14.12 ? 173 SER A O 1 ATOM 728 C CB . SER A 1 91 ? 9.305 4.953 57.739 1.00 6.12 ? 173 SER A CB 1 ATOM 729 O OG . SER A 1 91 ? 8.765 6.029 58.490 1.00 11.31 ? 173 SER A OG 1 ATOM 730 N N . ARG A 1 92 ? 9.750 4.226 54.486 1.00 5.35 ? 174 ARG A N 1 ATOM 731 C CA . ARG A 1 92 ? 10.528 3.427 53.544 1.00 5.67 ? 174 ARG A CA 1 ATOM 732 C C . ARG A 1 92 ? 12.009 3.738 53.708 1.00 7.09 ? 174 ARG A C 1 ATOM 733 O O . ARG A 1 92 ? 12.409 4.901 53.634 1.00 8.04 ? 174 ARG A O 1 ATOM 734 C CB . ARG A 1 92 ? 10.086 3.744 52.114 1.00 8.15 ? 174 ARG A CB 1 ATOM 735 C CG . ARG A 1 92 ? 10.927 3.089 51.035 1.00 12.63 ? 174 ARG A CG 1 ATOM 736 C CD . ARG A 1 92 ? 10.237 3.210 49.683 1.00 18.73 ? 174 ARG A CD 1 ATOM 737 N NE . ARG A 1 92 ? 10.305 4.566 49.142 1.00 17.40 ? 174 ARG A NE 1 ATOM 738 C CZ . ARG A 1 92 ? 9.378 5.101 48.351 1.00 22.59 ? 174 ARG A CZ 1 ATOM 739 N NH1 . ARG A 1 92 ? 8.302 4.400 48.020 1.00 17.65 ? 174 ARG A NH1 1 ATOM 740 N NH2 . ARG A 1 92 ? 9.520 6.337 47.898 1.00 17.07 ? 174 ARG A NH2 1 ATOM 741 N N . VAL A 1 93 ? 12.823 2.711 53.945 1.00 5.51 ? 175 VAL A N 1 ATOM 742 C CA . VAL A 1 93 ? 14.256 2.927 54.138 1.00 4.56 ? 175 VAL A CA 1 ATOM 743 C C . VAL A 1 93 ? 14.956 3.109 52.796 1.00 6.97 ? 175 VAL A C 1 ATOM 744 O O . VAL A 1 93 ? 14.867 2.245 51.919 1.00 8.67 ? 175 VAL A O 1 ATOM 745 C CB . VAL A 1 93 ? 14.919 1.761 54.899 1.00 6.92 ? 175 VAL A CB 1 ATOM 746 C CG1 . VAL A 1 93 ? 16.439 1.972 54.967 1.00 6.80 ? 175 VAL A CG1 1 ATOM 747 C CG2 . VAL A 1 93 ? 14.331 1.642 56.298 1.00 5.98 ? 175 VAL A CG2 1 ATOM 748 N N . GLU A 1 94 ? 15.652 4.231 52.638 1.00 5.32 ? 176 GLU A N 1 ATOM 749 C CA . GLU A 1 94 ? 16.353 4.524 51.391 1.00 5.65 ? 176 GLU A CA 1 ATOM 750 C C . GLU A 1 94 ? 17.783 3.976 51.413 1.00 9.09 ? 176 GLU A C 1 ATOM 751 O O . GLU A 1 94 ? 18.288 3.498 50.395 1.00 9.37 ? 176 GLU A O 1 ATOM 752 C CB . GLU A 1 94 ? 16.352 6.032 51.123 1.00 5.40 ? 176 GLU A CB 1 ATOM 753 C CG . GLU A 1 94 ? 14.958 6.681 51.141 1.00 7.39 ? 176 GLU A CG 1 ATOM 754 C CD . GLU A 1 94 ? 14.079 6.256 49.973 1.00 19.83 ? 176 GLU A CD 1 ATOM 755 O OE1 . GLU A 1 94 ? 14.622 5.757 48.965 1.00 23.05 ? 176 GLU A OE1 1 ATOM 756 O OE2 . GLU A 1 94 ? 12.838 6.413 50.058 1.00 17.61 ? 176 GLU A OE2 1 ATOM 757 N N . CYS A 1 95 ? 18.427 4.057 52.575 1.00 5.77 ? 177 CYS A N 1 ATOM 758 C CA . CYS A 1 95 ? 19.770 3.509 52.785 1.00 4.68 ? 177 CYS A CA 1 ATOM 759 C C . CYS A 1 95 ? 20.156 3.643 54.254 1.00 6.58 ? 177 CYS A C 1 ATOM 760 O O . CYS A 1 95 ? 19.476 4.331 55.018 1.00 6.07 ? 177 CYS A O 1 ATOM 761 C CB . CYS A 1 95 ? 20.824 4.176 51.876 1.00 7.83 ? 177 CYS A CB 1 ATOM 762 S SG . CYS A 1 95 ? 20.709 5.976 51.677 1.00 10.94 ? 177 CYS A SG 1 ATOM 763 N N . ILE A 1 96 ? 21.247 2.986 54.641 1.00 6.56 ? 178 ILE A N 1 ATOM 764 C CA . ILE A 1 96 ? 21.676 2.940 56.038 1.00 5.25 ? 178 ILE A CA 1 ATOM 765 C C . ILE A 1 96 ? 22.824 3.918 56.307 1.00 5.84 ? 178 ILE A C 1 ATOM 766 O O . ILE A 1 96 ? 23.805 3.935 55.567 1.00 6.58 ? 178 ILE A O 1 ATOM 767 C CB . ILE A 1 96 ? 22.137 1.512 56.412 1.00 3.46 ? 178 ILE A CB 1 ATOM 768 C CG1 . ILE A 1 96 ? 21.058 0.481 56.050 1.00 6.81 ? 178 ILE A CG1 1 ATOM 769 C CG2 . ILE A 1 96 ? 22.536 1.438 57.888 1.00 5.40 ? 178 ILE A CG2 1 ATOM 770 C CD1 . ILE A 1 96 ? 19.741 0.675 56.795 1.00 10.73 ? 178 ILE A CD1 1 ATOM 771 N N . GLY A 1 97 ? 22.708 4.730 57.360 1.00 5.20 ? 179 GLY A N 1 ATOM 772 C CA . GLY A 1 97 ? 23.758 5.684 57.689 1.00 3.82 ? 179 GLY A CA 1 ATOM 773 C C . GLY A 1 97 ? 23.288 6.864 58.520 1.00 7.98 ? 179 GLY A C 1 ATOM 774 O O . GLY A 1 97 ? 22.122 6.921 58.918 1.00 5.41 ? 179 GLY A O 1 ATOM 775 N N . TRP A 1 98 ? 24.195 7.809 58.774 1.00 5.52 ? 180 TRP A N 1 ATOM 776 C CA . TRP A 1 98 ? 23.923 8.931 59.679 1.00 3.06 ? 180 TRP A CA 1 ATOM 777 C C . TRP A 1 98 ? 24.160 10.312 59.056 1.00 5.13 ? 180 TRP A C 1 ATOM 778 O O . TRP A 1 98 ? 24.205 11.327 59.764 1.00 7.09 ? 180 TRP A O 1 ATOM 779 C CB . TRP A 1 98 ? 24.716 8.779 60.987 1.00 2.29 ? 180 TRP A CB 1 ATOM 780 C CG . TRP A 1 98 ? 26.129 8.258 60.821 1.00 5.00 ? 180 TRP A CG 1 ATOM 781 C CD1 . TRP A 1 98 ? 26.596 7.028 61.200 1.00 5.87 ? 180 TRP A CD1 1 ATOM 782 C CD2 . TRP A 1 98 ? 27.250 8.953 60.249 1.00 5.95 ? 180 TRP A CD2 1 ATOM 783 N NE1 . TRP A 1 98 ? 27.934 6.916 60.896 1.00 4.53 ? 180 TRP A NE1 1 ATOM 784 C CE2 . TRP A 1 98 ? 28.359 8.080 60.312 1.00 4.28 ? 180 TRP A CE2 1 ATOM 785 C CE3 . TRP A 1 98 ? 27.421 10.225 59.687 1.00 5.27 ? 180 TRP A CE3 1 ATOM 786 C CZ2 . TRP A 1 98 ? 29.625 8.438 59.832 1.00 6.68 ? 180 TRP A CZ2 1 ATOM 787 C CZ3 . TRP A 1 98 ? 28.672 10.580 59.210 1.00 5.61 ? 180 TRP A CZ3 1 ATOM 788 C CH2 . TRP A 1 98 ? 29.761 9.689 59.284 1.00 6.66 ? 180 TRP A CH2 1 ATOM 789 N N . SER A 1 99 ? 24.317 10.340 57.734 1.00 6.79 ? 181 SER A N 1 ATOM 790 C CA . SER A 1 99 ? 24.384 11.588 56.966 1.00 6.12 ? 181 SER A CA 1 ATOM 791 C C . SER A 1 99 ? 23.904 11.254 55.563 1.00 6.89 ? 181 SER A C 1 ATOM 792 O O . SER A 1 99 ? 24.297 10.218 55.014 1.00 7.40 ? 181 SER A O 1 ATOM 793 C CB . SER A 1 99 ? 25.813 12.132 56.909 1.00 6.39 ? 181 SER A CB 1 ATOM 794 O OG . SER A 1 99 ? 25.851 13.377 56.227 1.00 5.96 ? 181 SER A OG 1 ATOM 795 N N . SER A 1 100 ? 23.067 12.110 54.976 1.00 3.71 ? 182 SER A N 1 ATOM 796 C CA . SER A 1 100 ? 22.426 11.747 53.711 1.00 4.93 ? 182 SER A CA 1 ATOM 797 C C . SER A 1 100 ? 22.089 12.903 52.777 1.00 6.38 ? 182 SER A C 1 ATOM 798 O O . SER A 1 100 ? 22.111 14.078 53.158 1.00 5.21 ? 182 SER A O 1 ATOM 799 C CB . SER A 1 100 ? 21.129 10.974 53.982 1.00 6.14 ? 182 SER A CB 1 ATOM 800 O OG . SER A 1 100 ? 20.050 11.874 54.208 1.00 8.05 ? 182 SER A OG 1 ATOM 801 N N . THR A 1 101 ? 21.773 12.533 51.541 1.00 4.66 ? 183 THR A N 1 ATOM 802 C CA . THR A 1 101 ? 21.110 13.412 50.591 1.00 5.16 ? 183 THR A CA 1 ATOM 803 C C . THR A 1 101 ? 20.337 12.509 49.643 1.00 4.63 ? 183 THR A C 1 ATOM 804 O O . THR A 1 101 ? 20.548 11.291 49.618 1.00 6.91 ? 183 THR A O 1 ATOM 805 C CB . THR A 1 101 ? 22.101 14.271 49.788 1.00 5.18 ? 183 THR A CB 1 ATOM 806 O OG1 . THR A 1 101 ? 21.376 15.218 48.988 1.00 5.79 ? 183 THR A OG1 1 ATOM 807 C CG2 . THR A 1 101 ? 22.949 13.393 48.876 1.00 7.25 ? 183 THR A CG2 1 ATOM 808 N N . SER A 1 102 ? 19.442 13.098 48.863 1.00 5.41 ? 184 SER A N 1 ATOM 809 C CA . SER A 1 102 ? 18.617 12.317 47.951 1.00 8.39 ? 184 SER A CA 1 ATOM 810 C C . SER A 1 102 ? 18.009 13.251 46.916 1.00 7.49 ? 184 SER A C 1 ATOM 811 O O . SER A 1 102 ? 17.668 14.388 47.239 1.00 7.02 ? 184 SER A O 1 ATOM 812 C CB . SER A 1 102 ? 17.506 11.606 48.733 1.00 5.89 ? 184 SER A CB 1 ATOM 813 O OG . SER A 1 102 ? 16.819 10.665 47.925 1.00 6.79 ? 184 SER A OG 1 ATOM 814 N N . CYS A 1 103 ? 17.882 12.786 45.675 1.00 7.59 ? 185 CYS A N 1 ATOM 815 C CA . CYS A 1 103 ? 17.197 13.567 44.642 1.00 6.22 ? 185 CYS A CA 1 ATOM 816 C C . CYS A 1 103 ? 16.752 12.708 43.464 1.00 7.07 ? 185 CYS A C 1 ATOM 817 O O . CYS A 1 103 ? 17.367 11.684 43.161 1.00 6.65 ? 185 CYS A O 1 ATOM 818 C CB . CYS A 1 103 ? 18.061 14.743 44.158 1.00 5.97 ? 185 CYS A CB 1 ATOM 819 S SG . CYS A 1 103 ? 19.783 14.351 43.737 1.00 8.91 ? 185 CYS A SG 1 ATOM 820 N N . HIS A 1 104 ? 15.673 13.130 42.813 1.00 6.97 ? 186 HIS A N 1 ATOM 821 C CA . HIS A 1 104 ? 15.183 12.452 41.618 1.00 7.95 ? 186 HIS A CA 1 ATOM 822 C C . HIS A 1 104 ? 15.692 13.189 40.380 1.00 7.16 ? 186 HIS A C 1 ATOM 823 O O . HIS A 1 104 ? 15.673 14.416 40.344 1.00 7.99 ? 186 HIS A O 1 ATOM 824 C CB . HIS A 1 104 ? 13.652 12.426 41.620 1.00 6.27 ? 186 HIS A CB 1 ATOM 825 C CG . HIS A 1 104 ? 13.066 11.290 40.841 1.00 8.17 ? 186 HIS A CG 1 ATOM 826 N ND1 . HIS A 1 104 ? 13.050 11.260 39.462 1.00 10.33 ? 186 HIS A ND1 1 ATOM 827 C CD2 . HIS A 1 104 ? 12.472 10.143 41.248 1.00 7.89 ? 186 HIS A CD2 1 ATOM 828 C CE1 . HIS A 1 104 ? 12.472 10.144 39.054 1.00 7.40 ? 186 HIS A CE1 1 ATOM 829 N NE2 . HIS A 1 104 ? 12.108 9.450 40.118 1.00 7.47 ? 186 HIS A NE2 1 ATOM 830 N N . ASP A 1 105 ? 16.156 12.449 39.372 1.00 8.43 ? 187 ASP A N 1 ATOM 831 C CA . ASP A 1 105 ? 16.682 13.083 38.161 1.00 6.91 ? 187 ASP A CA 1 ATOM 832 C C . ASP A 1 105 ? 15.661 13.170 37.027 1.00 12.20 ? 187 ASP A C 1 ATOM 833 O O . ASP A 1 105 ? 15.988 13.607 35.920 1.00 9.85 ? 187 ASP A O 1 ATOM 834 C CB . ASP A 1 105 ? 17.976 12.390 37.678 1.00 5.82 ? 187 ASP A CB 1 ATOM 835 C CG . ASP A 1 105 ? 17.764 10.931 37.264 1.00 7.20 ? 187 ASP A CG 1 ATOM 836 O OD1 . ASP A 1 105 ? 16.623 10.530 36.956 1.00 9.16 ? 187 ASP A OD1 1 ATOM 837 O OD2 . ASP A 1 105 ? 18.763 10.179 37.229 1.00 12.02 ? 187 ASP A OD2 1 ATOM 838 N N . GLY A 1 106 ? 14.430 12.745 37.304 1.00 7.34 ? 188 GLY A N 1 ATOM 839 C CA . GLY A 1 106 ? 13.384 12.714 36.295 1.00 7.11 ? 188 GLY A CA 1 ATOM 840 C C . GLY A 1 106 ? 13.063 11.293 35.877 1.00 11.70 ? 188 GLY A C 1 ATOM 841 O O . GLY A 1 106 ? 11.924 10.987 35.523 1.00 12.13 ? 188 GLY A O 1 ATOM 842 N N . LYS A 1 107 ? 14.071 10.422 35.914 1.00 9.64 ? 189 LYS A N 1 ATOM 843 C CA . LYS A 1 107 ? 13.872 9.002 35.618 1.00 7.16 ? 189 LYS A CA 1 ATOM 844 C C . LYS A 1 107 ? 13.829 8.153 36.888 1.00 9.76 ? 189 LYS A C 1 ATOM 845 O O . LYS A 1 107 ? 12.879 7.395 37.106 1.00 10.45 ? 189 LYS A O 1 ATOM 846 C CB . LYS A 1 107 ? 14.980 8.485 34.698 1.00 10.46 ? 189 LYS A CB 1 ATOM 847 C CG . LYS A 1 107 ? 15.006 9.136 33.325 1.00 11.12 ? 189 LYS A CG 1 ATOM 848 C CD . LYS A 1 107 ? 16.077 8.493 32.462 1.00 15.76 ? 189 LYS A CD 1 ATOM 849 C CE . LYS A 1 107 ? 16.096 9.082 31.069 1.00 20.74 ? 189 LYS A CE 1 ATOM 850 N NZ . LYS A 1 107 ? 17.026 8.315 30.183 1.00 26.13 ? 189 LYS A NZ 1 ATOM 851 N N . SER A 1 108 ? 14.867 8.276 37.712 1.00 8.85 ? 190 SER A N 1 ATOM 852 C CA . SER A 1 108 ? 14.945 7.544 38.975 1.00 8.06 ? 190 SER A CA 1 ATOM 853 C C . SER A 1 108 ? 15.548 8.408 40.074 1.00 9.66 ? 190 SER A C 1 ATOM 854 O O . SER A 1 108 ? 16.064 9.496 39.806 1.00 8.61 ? 190 SER A O 1 ATOM 855 C CB . SER A 1 108 ? 15.769 6.265 38.819 1.00 11.14 ? 190 SER A CB 1 ATOM 856 O OG . SER A 1 108 ? 15.091 5.318 38.013 1.00 15.72 ? 190 SER A OG 1 ATOM 857 N N . ARG A 1 109 ? 15.481 7.916 41.309 1.00 8.48 ? 191 ARG A N 1 ATOM 858 C CA . ARG A 1 109 ? 15.999 8.651 42.460 1.00 7.93 ? 191 ARG A CA 1 ATOM 859 C C . ARG A 1 109 ? 17.380 8.157 42.859 1.00 6.48 ? 191 ARG A C 1 ATOM 860 O O . ARG A 1 109 ? 17.632 6.949 42.880 1.00 7.51 ? 191 ARG A O 1 ATOM 861 C CB . ARG A 1 109 ? 15.040 8.510 43.647 1.00 6.11 ? 191 ARG A CB 1 ATOM 862 C CG . ARG A 1 109 ? 15.578 9.059 44.969 1.00 7.14 ? 191 ARG A CG 1 ATOM 863 C CD . ARG A 1 109 ? 14.448 9.320 45.964 1.00 6.92 ? 191 ARG A CD 1 ATOM 864 N NE . ARG A 1 109 ? 13.564 10.400 45.524 1.00 5.18 ? 191 ARG A NE 1 ATOM 865 C CZ . ARG A 1 109 ? 13.779 11.693 45.766 1.00 6.96 ? 191 ARG A CZ 1 ATOM 866 N NH1 . ARG A 1 109 ? 14.854 12.083 46.448 1.00 5.39 ? 191 ARG A NH1 1 ATOM 867 N NH2 . ARG A 1 109 ? 12.915 12.604 45.329 1.00 6.19 ? 191 ARG A NH2 1 ATOM 868 N N . MET A 1 110 ? 18.276 9.094 43.158 1.00 5.83 ? 192 MET A N 1 ATOM 869 C CA . MET A 1 110 ? 19.560 8.772 43.774 1.00 7.36 ? 192 MET A CA 1 ATOM 870 C C . MET A 1 110 ? 19.484 9.091 45.263 1.00 5.36 ? 192 MET A C 1 ATOM 871 O O . MET A 1 110 ? 19.032 10.167 45.637 1.00 6.51 ? 192 MET A O 1 ATOM 872 C CB . MET A 1 110 ? 20.685 9.603 43.146 1.00 7.03 ? 192 MET A CB 1 ATOM 873 C CG . MET A 1 110 ? 22.049 9.395 43.809 1.00 8.44 ? 192 MET A CG 1 ATOM 874 S SD . MET A 1 110 ? 23.375 10.422 43.120 1.00 7.66 ? 192 MET A SD 1 ATOM 875 C CE . MET A 1 110 ? 22.896 12.056 43.691 1.00 10.82 ? 192 MET A CE 1 ATOM 876 N N . SER A 1 111 ? 19.919 8.160 46.109 1.00 7.04 ? 193 SER A N 1 ATOM 877 C CA . SER A 1 111 ? 20.039 8.433 47.545 1.00 6.67 ? 193 SER A CA 1 ATOM 878 C C . SER A 1 111 ? 21.440 8.070 48.006 1.00 5.36 ? 193 SER A C 1 ATOM 879 O O . SER A 1 111 ? 21.995 7.053 47.589 1.00 8.61 ? 193 SER A O 1 ATOM 880 C CB . SER A 1 111 ? 19.003 7.647 48.353 1.00 7.04 ? 193 SER A CB 1 ATOM 881 O OG . SER A 1 111 ? 17.684 8.038 48.025 1.00 7.07 ? 193 SER A OG 1 ATOM 882 N N . ILE A 1 112 ? 22.013 8.902 48.870 1.00 5.34 ? 194 ILE A N 1 ATOM 883 C CA . ILE A 1 112 ? 23.363 8.665 49.359 1.00 5.37 ? 194 ILE A CA 1 ATOM 884 C C . ILE A 1 112 ? 23.350 8.667 50.877 1.00 5.62 ? 194 ILE A C 1 ATOM 885 O O . ILE A 1 112 ? 22.816 9.593 51.486 1.00 4.78 ? 194 ILE A O 1 ATOM 886 C CB . ILE A 1 112 ? 24.347 9.739 48.857 1.00 6.13 ? 194 ILE A CB 1 ATOM 887 C CG1 . ILE A 1 112 ? 24.311 9.819 47.328 1.00 6.80 ? 194 ILE A CG1 1 ATOM 888 C CG2 . ILE A 1 112 ? 25.767 9.432 49.342 1.00 7.59 ? 194 ILE A CG2 1 ATOM 889 C CD1 . ILE A 1 112 ? 25.273 10.848 46.727 1.00 7.78 ? 194 ILE A CD1 1 ATOM 890 N N . CYS A 1 113 ? 23.907 7.621 51.480 1.00 4.76 ? 195 CYS A N 1 ATOM 891 C CA . CYS A 1 113 ? 24.019 7.531 52.934 1.00 7.67 ? 195 CYS A CA 1 ATOM 892 C C . CYS A 1 113 ? 25.461 7.267 53.314 1.00 6.89 ? 195 CYS A C 1 ATOM 893 O O . CYS A 1 113 ? 26.120 6.429 52.700 1.00 6.27 ? 195 CYS A O 1 ATOM 894 C CB . CYS A 1 113 ? 23.175 6.381 53.483 1.00 9.57 ? 195 CYS A CB 1 ATOM 895 S SG . CYS A 1 113 ? 21.384 6.641 53.481 1.00 13.15 ? 195 CYS A SG 1 ATOM 896 N N . ILE A 1 114 ? 25.939 7.965 54.338 1.00 6.20 ? 196 ILE A N 1 ATOM 897 C CA . ILE A 1 114 ? 27.277 7.733 54.876 1.00 5.30 ? 196 ILE A CA 1 ATOM 898 C C . ILE A 1 114 ? 27.175 7.017 56.220 1.00 4.90 ? 196 ILE A C 1 ATOM 899 O O . ILE A 1 114 ? 26.371 7.405 57.071 1.00 6.54 ? 196 ILE A O 1 ATOM 900 C CB . ILE A 1 114 ? 28.032 9.067 55.049 1.00 3.31 ? 196 ILE A CB 1 ATOM 901 C CG1 . ILE A 1 114 ? 28.190 9.759 53.691 1.00 5.60 ? 196 ILE A CG1 1 ATOM 902 C CG2 . ILE A 1 114 ? 29.401 8.851 55.712 1.00 3.24 ? 196 ILE A CG2 1 ATOM 903 C CD1 . ILE A 1 114 ? 28.527 11.252 53.796 1.00 7.89 ? 196 ILE A CD1 1 ATOM 904 N N . SER A 1 115 ? 27.975 5.967 56.410 1.00 4.75 ? 197 SER A N 1 ATOM 905 C CA . SER A 1 115 ? 28.042 5.284 57.703 1.00 5.76 ? 197 SER A CA 1 ATOM 906 C C . SER A 1 115 ? 29.490 5.007 58.065 1.00 8.39 ? 197 SER A C 1 ATOM 907 O O . SER A 1 115 ? 30.393 5.215 57.253 1.00 7.55 ? 197 SER A O 1 ATOM 908 C CB . SER A 1 115 ? 27.261 3.966 57.688 1.00 6.98 ? 197 SER A CB 1 ATOM 909 O OG . SER A 1 115 ? 27.974 2.957 56.987 1.00 6.35 ? 197 SER A OG 1 ATOM 910 N N . GLY A 1 116 ? 29.712 4.545 59.290 1.00 5.32 ? 198 GLY A N 1 ATOM 911 C CA . GLY A 1 116 ? 31.047 4.157 59.714 1.00 5.57 ? 198 GLY A CA 1 ATOM 912 C C . GLY A 1 116 ? 31.500 4.890 60.961 1.00 6.22 ? 198 GLY A C 1 ATOM 913 O O . GLY A 1 116 ? 30.804 5.779 61.457 1.00 6.86 ? 198 GLY A O 1 ATOM 914 N N . PRO A 1 117 ? 32.674 4.516 61.486 1.00 6.07 ? 199 PRO A N 1 ATOM 915 C CA . PRO A 1 117 ? 33.245 5.248 62.618 1.00 6.28 ? 199 PRO A CA 1 ATOM 916 C C . PRO A 1 117 ? 33.825 6.565 62.112 1.00 8.60 ? 199 PRO A C 1 ATOM 917 O O . PRO A 1 117 ? 33.924 6.746 60.896 1.00 7.03 ? 199 PRO A O 1 ATOM 918 C CB . PRO A 1 117 ? 34.368 4.326 63.094 1.00 7.29 ? 199 PRO A CB 1 ATOM 919 C CG . PRO A 1 117 ? 34.811 3.620 61.852 1.00 7.77 ? 199 PRO A CG 1 ATOM 920 C CD . PRO A 1 117 ? 33.564 3.443 61.006 1.00 7.05 ? 199 PRO A CD 1 ATOM 921 N N . ASN A 1 118 ? 34.201 7.463 63.017 1.00 7.33 ? 200 ASN A N 1 ATOM 922 C CA . ASN A 1 118 ? 34.691 8.778 62.614 1.00 7.97 ? 200 ASN A CA 1 ATOM 923 C C . ASN A 1 118 ? 35.883 8.738 61.660 1.00 6.04 ? 200 ASN A C 1 ATOM 924 O O . ASN A 1 118 ? 35.999 9.577 60.768 1.00 7.95 ? 200 ASN A O 1 ATOM 925 C CB . ASN A 1 118 ? 35.058 9.618 63.840 1.00 10.35 ? 200 ASN A CB 1 ATOM 926 C CG . ASN A 1 118 ? 33.870 9.905 64.732 1.00 11.56 ? 200 ASN A CG 1 ATOM 927 O OD1 . ASN A 1 118 ? 32.729 9.617 64.381 1.00 10.45 ? 200 ASN A OD1 1 ATOM 928 N ND2 . ASN A 1 118 ? 34.134 10.494 65.893 1.00 13.64 ? 200 ASN A ND2 1 ATOM 929 N N . ASN A 1 119 ? 36.764 7.762 61.846 1.00 7.72 ? 201 ASN A N 1 ATOM 930 C CA . ASN A 1 119 ? 38.001 7.711 61.075 1.00 8.14 ? 201 ASN A CA 1 ATOM 931 C C . ASN A 1 119 ? 37.968 6.758 59.879 1.00 9.30 ? 201 ASN A C 1 ATOM 932 O O . ASN A 1 119 ? 38.997 6.510 59.249 1.00 9.67 ? 201 ASN A O 1 ATOM 933 C CB . ASN A 1 119 ? 39.181 7.364 61.995 1.00 9.84 ? 201 ASN A CB 1 ATOM 934 C CG . ASN A 1 119 ? 39.066 5.975 62.607 1.00 14.82 ? 201 ASN A CG 1 ATOM 935 O OD1 . ASN A 1 119 ? 38.134 5.221 62.313 1.00 10.03 ? 201 ASN A OD1 1 ATOM 936 N ND2 . ASN A 1 119 ? 40.024 5.628 63.460 1.00 11.98 ? 201 ASN A ND2 1 ATOM 937 N N . ASN A 1 120 ? 36.795 6.220 59.563 1.00 9.73 ? 202 ASN A N 1 ATOM 938 C CA . ASN A 1 120 ? 36.712 5.196 58.520 1.00 7.33 ? 202 ASN A CA 1 ATOM 939 C C . ASN A 1 120 ? 35.331 5.149 57.874 1.00 6.71 ? 202 ASN A C 1 ATOM 940 O O . ASN A 1 120 ? 34.837 4.080 57.527 1.00 7.24 ? 202 ASN A O 1 ATOM 941 C CB . ASN A 1 120 ? 37.062 3.819 59.108 1.00 6.62 ? 202 ASN A CB 1 ATOM 942 C CG . ASN A 1 120 ? 38.259 3.155 58.421 1.00 6.17 ? 202 ASN A CG 1 ATOM 943 O OD1 . ASN A 1 120 ? 38.676 3.557 57.332 1.00 8.11 ? 202 ASN A OD1 1 ATOM 944 N ND2 . ASN A 1 120 ? 38.809 2.122 59.074 1.00 10.04 ? 202 ASN A ND2 1 ATOM 945 N N . ALA A 1 121 ? 34.714 6.315 57.705 1.00 6.12 ? 203 ALA A N 1 ATOM 946 C CA . ALA A 1 121 ? 33.366 6.390 57.143 1.00 3.99 ? 203 ALA A CA 1 ATOM 947 C C . ALA A 1 121 ? 33.368 6.204 55.632 1.00 8.25 ? 203 ALA A C 1 ATOM 948 O O . ALA A 1 121 ? 34.391 6.395 54.979 1.00 7.88 ? 203 ALA A O 1 ATOM 949 C CB . ALA A 1 121 ? 32.711 7.708 57.510 1.00 6.00 ? 203 ALA A CB 1 ATOM 950 N N . SER A 1 122 ? 32.213 5.848 55.076 1.00 6.55 ? 204 SER A N 1 ATOM 951 C CA . SER A 1 122 ? 32.085 5.685 53.632 1.00 8.01 ? 204 SER A CA 1 ATOM 952 C C . SER A 1 122 ? 30.678 6.022 53.173 1.00 8.01 ? 204 SER A C 1 ATOM 953 O O . SER A 1 122 ? 29.705 5.794 53.896 1.00 6.87 ? 204 SER A O 1 ATOM 954 C CB . SER A 1 122 ? 32.461 4.263 53.198 1.00 6.68 ? 204 SER A CB 1 ATOM 955 O OG . SER A 1 122 ? 31.631 3.288 53.818 1.00 8.30 ? 204 SER A OG 1 ATOM 956 N N . ALA A 1 123 ? 30.585 6.583 51.972 1.00 6.66 ? 205 ALA A N 1 ATOM 957 C CA . ALA A 1 123 ? 29.308 6.886 51.341 1.00 4.55 ? 205 ALA A CA 1 ATOM 958 C C . ALA A 1 123 ? 28.926 5.750 50.403 1.00 6.80 ? 205 ALA A C 1 ATOM 959 O O . ALA A 1 123 ? 29.770 5.237 49.664 1.00 8.70 ? 205 ALA A O 1 ATOM 960 C CB . ALA A 1 123 ? 29.406 8.203 50.559 1.00 6.83 ? 205 ALA A CB 1 ATOM 961 N N . VAL A 1 124 ? 27.661 5.344 50.440 1.00 5.96 ? 206 VAL A N 1 ATOM 962 C CA . VAL A 1 124 ? 27.147 4.424 49.433 1.00 6.55 ? 206 VAL A CA 1 ATOM 963 C C . VAL A 1 124 ? 26.105 5.161 48.602 1.00 8.14 ? 206 VAL A C 1 ATOM 964 O O . VAL A 1 124 ? 25.166 5.748 49.147 1.00 6.79 ? 206 VAL A O 1 ATOM 965 C CB . VAL A 1 124 ? 26.529 3.155 50.050 1.00 6.44 ? 206 VAL A CB 1 ATOM 966 C CG1 . VAL A 1 124 ? 26.060 2.210 48.953 1.00 8.40 ? 206 VAL A CG1 1 ATOM 967 C CG2 . VAL A 1 124 ? 27.543 2.450 50.938 1.00 5.98 ? 206 VAL A CG2 1 ATOM 968 N N . VAL A 1 125 ? 26.285 5.145 47.285 1.00 5.58 ? 207 VAL A N 1 ATOM 969 C CA . VAL A 1 125 ? 25.384 5.846 46.379 1.00 6.41 ? 207 VAL A CA 1 ATOM 970 C C . VAL A 1 125 ? 24.397 4.863 45.772 1.00 8.18 ? 207 VAL A C 1 ATOM 971 O O . VAL A 1 125 ? 24.798 3.928 45.075 1.00 9.28 ? 207 VAL A O 1 ATOM 972 C CB . VAL A 1 125 ? 26.161 6.535 45.246 1.00 6.22 ? 207 VAL A CB 1 ATOM 973 C CG1 . VAL A 1 125 ? 25.212 7.338 44.374 1.00 7.31 ? 207 VAL A CG1 1 ATOM 974 C CG2 . VAL A 1 125 ? 27.237 7.448 45.827 1.00 8.79 ? 207 VAL A CG2 1 ATOM 975 N N . TRP A 1 126 ? 23.112 5.074 46.049 1.00 6.70 ? 208 TRP A N 1 ATOM 976 C CA . TRP A 1 126 ? 22.041 4.221 45.539 1.00 7.83 ? 208 TRP A CA 1 ATOM 977 C C . TRP A 1 126 ? 21.364 4.928 44.378 1.00 9.24 ? 208 TRP A C 1 ATOM 978 O O . TRP A 1 126 ? 21.192 6.142 44.415 1.00 6.91 ? 208 TRP A O 1 ATOM 979 C CB . TRP A 1 126 ? 20.996 3.968 46.634 1.00 6.61 ? 208 TRP A CB 1 ATOM 980 C CG . TRP A 1 126 ? 21.487 3.134 47.781 1.00 6.03 ? 208 TRP A CG 1 ATOM 981 C CD1 . TRP A 1 126 ? 22.467 3.461 48.677 1.00 5.89 ? 208 TRP A CD1 1 ATOM 982 C CD2 . TRP A 1 126 ? 21.005 1.844 48.165 1.00 6.20 ? 208 TRP A CD2 1 ATOM 983 N NE1 . TRP A 1 126 ? 22.635 2.444 49.585 1.00 5.20 ? 208 TRP A NE1 1 ATOM 984 C CE2 . TRP A 1 126 ? 21.744 1.441 49.295 1.00 8.53 ? 208 TRP A CE2 1 ATOM 985 C CE3 . TRP A 1 126 ? 20.020 0.987 47.660 1.00 7.89 ? 208 TRP A CE3 1 ATOM 986 C CZ2 . TRP A 1 126 ? 21.529 0.216 49.930 1.00 10.05 ? 208 TRP A CZ2 1 ATOM 987 C CZ3 . TRP A 1 126 ? 19.805 -0.229 48.297 1.00 7.16 ? 208 TRP A CZ3 1 ATOM 988 C CH2 . TRP A 1 126 ? 20.560 -0.602 49.414 1.00 9.36 ? 208 TRP A CH2 1 ATOM 989 N N . TYR A 1 127 ? 20.986 4.174 43.351 1.00 6.70 ? 209 TYR A N 1 ATOM 990 C CA . TYR A 1 127 ? 20.226 4.720 42.230 1.00 6.30 ? 209 TYR A CA 1 ATOM 991 C C . TYR A 1 127 ? 19.161 3.711 41.824 1.00 7.52 ? 209 TYR A C 1 ATOM 992 O O . TYR A 1 127 ? 19.463 2.528 41.647 1.00 6.17 ? 209 TYR A O 1 ATOM 993 C CB . TYR A 1 127 ? 21.138 5.031 41.037 1.00 7.61 ? 209 TYR A CB 1 ATOM 994 C CG . TYR A 1 127 ? 20.412 5.739 39.911 1.00 6.97 ? 209 TYR A CG 1 ATOM 995 C CD1 . TYR A 1 127 ? 20.050 7.075 40.029 1.00 8.76 ? 209 TYR A CD1 1 ATOM 996 C CD2 . TYR A 1 127 ? 20.080 5.069 38.741 1.00 10.27 ? 209 TYR A CD2 1 ATOM 997 C CE1 . TYR A 1 127 ? 19.378 7.728 39.009 1.00 10.38 ? 209 TYR A CE1 1 ATOM 998 C CE2 . TYR A 1 127 ? 19.408 5.710 37.717 1.00 8.46 ? 209 TYR A CE2 1 ATOM 999 C CZ . TYR A 1 127 ? 19.062 7.040 37.858 1.00 11.37 ? 209 TYR A CZ 1 ATOM 1000 O OH . TYR A 1 127 ? 18.393 7.687 36.842 1.00 9.29 ? 209 TYR A OH 1 ATOM 1001 N N . ASN A 1 128 ? 17.922 4.183 41.686 1.00 7.78 ? 210 ASN A N 1 ATOM 1002 C CA . ASN A 1 128 ? 16.781 3.308 41.428 1.00 11.81 ? 210 ASN A CA 1 ATOM 1003 C C . ASN A 1 128 ? 16.735 2.166 42.442 1.00 10.30 ? 210 ASN A C 1 ATOM 1004 O O . ASN A 1 128 ? 16.518 1.006 42.082 1.00 9.76 ? 210 ASN A O 1 ATOM 1005 C CB . ASN A 1 128 ? 16.820 2.764 39.995 1.00 13.40 ? 210 ASN A CB 1 ATOM 1006 C CG . ASN A 1 128 ? 15.496 2.152 39.561 1.00 18.60 ? 210 ASN A CG 1 ATOM 1007 O OD1 . ASN A 1 128 ? 14.433 2.525 40.055 1.00 18.87 ? 210 ASN A OD1 1 ATOM 1008 N ND2 . ASN A 1 128 ? 15.560 1.208 38.632 1.00 24.22 ? 210 ASN A ND2 1 ATOM 1009 N N . ARG A 1 129 ? 16.980 2.521 43.703 1.00 11.40 ? 211 ARG A N 1 ATOM 1010 C CA . ARG A 1 129 ? 16.864 1.622 44.858 1.00 12.61 ? 211 ARG A CA 1 ATOM 1011 C C . ARG A 1 129 ? 17.895 0.498 44.902 1.00 10.29 ? 211 ARG A C 1 ATOM 1012 O O . ARG A 1 129 ? 17.695 -0.499 45.597 1.00 8.61 ? 211 ARG A O 1 ATOM 1013 C CB . ARG A 1 129 ? 15.443 1.052 44.975 1.00 11.33 ? 211 ARG A CB 1 ATOM 1014 C CG . ARG A 1 129 ? 14.348 2.083 44.704 1.00 24.82 ? 211 ARG A CG 1 ATOM 1015 C CD . ARG A 1 129 ? 13.074 1.781 45.470 1.00 32.30 ? 211 ARG A CD 1 ATOM 1016 N NE . ARG A 1 129 ? 12.771 2.865 46.397 1.00 44.14 ? 211 ARG A NE 1 ATOM 1017 C CZ . ARG A 1 129 ? 13.346 3.010 47.587 1.00 37.55 ? 211 ARG A CZ 1 ATOM 1018 N NH1 . ARG A 1 129 ? 14.252 2.138 48.009 1.00 41.28 ? 211 ARG A NH1 1 ATOM 1019 N NH2 . ARG A 1 129 ? 13.016 4.030 48.357 1.00 38.14 ? 211 ARG A NH2 1 ATOM 1020 N N . ARG A 1 130 ? 18.999 0.671 44.175 1.00 6.31 ? 212 ARG A N 1 ATOM 1021 C CA . ARG A 1 130 ? 20.103 -0.291 44.183 1.00 5.68 ? 212 ARG A CA 1 ATOM 1022 C C . ARG A 1 130 ? 21.424 0.417 44.442 1.00 6.38 ? 212 ARG A C 1 ATOM 1023 O O . ARG A 1 130 ? 21.639 1.522 43.946 1.00 6.81 ? 212 ARG A O 1 ATOM 1024 C CB . ARG A 1 130 ? 20.211 -0.999 42.830 1.00 6.31 ? 212 ARG A CB 1 ATOM 1025 C CG . ARG A 1 130 ? 18.968 -1.756 42.393 1.00 7.88 ? 212 ARG A CG 1 ATOM 1026 C CD . ARG A 1 130 ? 19.201 -2.475 41.063 1.00 9.40 ? 212 ARG A CD 1 ATOM 1027 N NE . ARG A 1 130 ? 18.099 -3.383 40.740 1.00 8.98 ? 212 ARG A NE 1 ATOM 1028 C CZ . ARG A 1 130 ? 17.111 -3.086 39.903 1.00 18.04 ? 212 ARG A CZ 1 ATOM 1029 N NH1 . ARG A 1 130 ? 17.091 -1.905 39.299 1.00 21.44 ? 212 ARG A NH1 1 ATOM 1030 N NH2 . ARG A 1 130 ? 16.144 -3.964 39.668 1.00 12.75 ? 212 ARG A NH2 1 ATOM 1031 N N . PRO A 1 131 ? 22.330 -0.225 45.199 1.00 8.00 ? 213 PRO A N 1 ATOM 1032 C CA . PRO A 1 131 ? 23.653 0.376 45.407 1.00 7.79 ? 213 PRO A CA 1 ATOM 1033 C C . PRO A 1 131 ? 24.453 0.358 44.110 1.00 8.19 ? 213 PRO A C 1 ATOM 1034 O O . PRO A 1 131 ? 24.479 -0.673 43.434 1.00 11.01 ? 213 PRO A O 1 ATOM 1035 C CB . PRO A 1 131 ? 24.298 -0.542 46.452 1.00 10.04 ? 213 PRO A CB 1 ATOM 1036 C CG . PRO A 1 131 ? 23.594 -1.862 46.290 1.00 10.72 ? 213 PRO A CG 1 ATOM 1037 C CD . PRO A 1 131 ? 22.179 -1.511 45.906 1.00 8.40 ? 213 PRO A CD 1 ATOM 1038 N N . VAL A 1 132 ? 25.088 1.479 43.768 1.00 5.33 ? 214 VAL A N 1 ATOM 1039 C CA . VAL A 1 132 ? 25.793 1.607 42.491 1.00 8.26 ? 214 VAL A CA 1 ATOM 1040 C C . VAL A 1 132 ? 27.265 1.996 42.637 1.00 10.46 ? 214 VAL A C 1 ATOM 1041 O O . VAL A 1 132 ? 28.128 1.451 41.944 1.00 12.20 ? 214 VAL A O 1 ATOM 1042 C CB . VAL A 1 132 ? 25.084 2.616 41.561 1.00 10.46 ? 214 VAL A CB 1 ATOM 1043 C CG1 . VAL A 1 132 ? 25.946 2.939 40.340 1.00 15.68 ? 214 VAL A CG1 1 ATOM 1044 C CG2 . VAL A 1 132 ? 23.752 2.061 41.128 1.00 10.66 ? 214 VAL A CG2 1 ATOM 1045 N N . ALA A 1 133 ? 27.549 2.943 43.525 1.00 7.30 ? 215 ALA A N 1 ATOM 1046 C CA . ALA A 1 133 ? 28.920 3.411 43.731 1.00 7.71 ? 215 ALA A CA 1 ATOM 1047 C C . ALA A 1 133 ? 29.205 3.660 45.208 1.00 8.25 ? 215 ALA A C 1 ATOM 1048 O O . ALA A 1 133 ? 28.286 3.897 45.999 1.00 7.27 ? 215 ALA A O 1 ATOM 1049 C CB . ALA A 1 133 ? 29.196 4.673 42.915 1.00 8.23 ? 215 ALA A CB 1 ATOM 1050 N N . GLU A 1 134 ? 30.478 3.600 45.583 1.00 6.60 ? 216 GLU A N 1 ATOM 1051 C CA . GLU A 1 134 ? 30.869 3.816 46.975 1.00 7.40 ? 216 GLU A CA 1 ATOM 1052 C C . GLU A 1 134 ? 32.064 4.756 47.033 1.00 9.75 ? 216 GLU A C 1 ATOM 1053 O O . GLU A 1 134 ? 32.916 4.742 46.143 1.00 12.09 ? 216 GLU A O 1 ATOM 1054 C CB . GLU A 1 134 ? 31.223 2.490 47.660 1.00 7.07 ? 216 GLU A CB 1 ATOM 1055 C CG . GLU A 1 134 ? 30.181 1.378 47.497 1.00 11.15 ? 216 GLU A CG 1 ATOM 1056 C CD . GLU A 1 134 ? 30.207 0.745 46.116 1.00 11.29 ? 216 GLU A CD 1 ATOM 1057 O OE1 . GLU A 1 134 ? 31.304 0.373 45.646 1.00 13.30 ? 216 GLU A OE1 1 ATOM 1058 O OE2 . GLU A 1 134 ? 29.129 0.640 45.494 1.00 10.14 ? 216 GLU A OE2 1 ATOM 1059 N N . ILE A 1 135 ? 32.120 5.580 48.076 1.00 6.14 ? 217 ILE A N 1 ATOM 1060 C CA . ILE A 1 135 ? 33.206 6.539 48.234 1.00 6.27 ? 217 ILE A CA 1 ATOM 1061 C C . ILE A 1 135 ? 33.779 6.450 49.643 1.00 11.28 ? 217 ILE A C 1 ATOM 1062 O O . ILE A 1 135 ? 33.070 6.680 50.623 1.00 8.81 ? 217 ILE A O 1 ATOM 1063 C CB . ILE A 1 135 ? 32.727 7.986 47.992 1.00 8.04 ? 217 ILE A CB 1 ATOM 1064 C CG1 . ILE A 1 135 ? 32.062 8.119 46.621 1.00 9.52 ? 217 ILE A CG1 1 ATOM 1065 C CG2 . ILE A 1 135 ? 33.893 8.961 48.118 1.00 8.27 ? 217 ILE A CG2 1 ATOM 1066 C CD1 . ILE A 1 135 ? 31.206 9.371 46.482 1.00 12.24 ? 217 ILE A CD1 1 ATOM 1067 N N . ASN A 1 136 ? 35.062 6.119 49.747 1.00 8.36 ? 218 ASN A N 1 ATOM 1068 C CA . ASN A 1 136 ? 35.707 6.043 51.050 1.00 8.51 ? 218 ASN A CA 1 ATOM 1069 C C . ASN A 1 136 ? 36.112 7.415 51.576 1.00 8.18 ? 218 ASN A C 1 ATOM 1070 O O . ASN A 1 136 ? 36.379 8.335 50.796 1.00 9.62 ? 218 ASN A O 1 ATOM 1071 C CB . ASN A 1 136 ? 36.941 5.147 50.990 1.00 7.93 ? 218 ASN A CB 1 ATOM 1072 C CG . ASN A 1 136 ? 37.323 4.604 52.348 1.00 10.00 ? 218 ASN A CG 1 ATOM 1073 O OD1 . ASN A 1 136 ? 36.456 4.223 53.136 1.00 10.18 ? 218 ASN A OD1 1 ATOM 1074 N ND2 . ASN A 1 136 ? 38.620 4.578 52.639 1.00 10.76 ? 218 ASN A ND2 1 ATOM 1075 N N . THR A 1 137 ? 36.158 7.543 52.901 1.00 6.52 ? 219 THR A N 1 ATOM 1076 C CA . THR A 1 137 ? 36.646 8.761 53.544 1.00 6.88 ? 219 THR A CA 1 ATOM 1077 C C . THR A 1 137 ? 38.013 9.161 52.982 1.00 10.87 ? 219 THR A C 1 ATOM 1078 O O . THR A 1 137 ? 38.872 8.301 52.740 1.00 8.18 ? 219 THR A O 1 ATOM 1079 C CB . THR A 1 137 ? 36.723 8.590 55.083 1.00 6.00 ? 219 THR A CB 1 ATOM 1080 O OG1 . THR A 1 137 ? 37.248 9.782 55.681 1.00 6.88 ? 219 THR A OG1 1 ATOM 1081 C CG2 . THR A 1 137 ? 37.595 7.396 55.462 1.00 9.42 ? 219 THR A CG2 1 ATOM 1082 N N . TRP A 1 138 ? 38.201 10.458 52.746 1.00 7.67 ? 220 TRP A N 1 ATOM 1083 C CA . TRP A 1 138 ? 39.474 10.955 52.214 1.00 12.75 ? 220 TRP A CA 1 ATOM 1084 C C . TRP A 1 138 ? 40.293 11.738 53.236 1.00 13.67 ? 220 TRP A C 1 ATOM 1085 O O . TRP A 1 138 ? 41.476 12.014 53.012 1.00 12.07 ? 220 TRP A O 1 ATOM 1086 C CB . TRP A 1 138 ? 39.274 11.784 50.936 1.00 8.81 ? 220 TRP A CB 1 ATOM 1087 C CG . TRP A 1 138 ? 38.290 12.921 51.040 1.00 8.61 ? 220 TRP A CG 1 ATOM 1088 C CD1 . TRP A 1 138 ? 38.531 14.183 51.510 1.00 9.83 ? 220 TRP A CD1 1 ATOM 1089 C CD2 . TRP A 1 138 ? 36.918 12.903 50.623 1.00 7.60 ? 220 TRP A CD2 1 ATOM 1090 N NE1 . TRP A 1 138 ? 37.388 14.947 51.420 1.00 9.91 ? 220 TRP A NE1 1 ATOM 1091 C CE2 . TRP A 1 138 ? 36.386 14.184 50.878 1.00 8.78 ? 220 TRP A CE2 1 ATOM 1092 C CE3 . TRP A 1 138 ? 36.091 11.928 50.055 1.00 8.96 ? 220 TRP A CE3 1 ATOM 1093 C CZ2 . TRP A 1 138 ? 35.059 14.513 50.591 1.00 8.97 ? 220 TRP A CZ2 1 ATOM 1094 C CZ3 . TRP A 1 138 ? 34.773 12.256 49.768 1.00 8.82 ? 220 TRP A CZ3 1 ATOM 1095 C CH2 . TRP A 1 138 ? 34.271 13.538 50.037 1.00 6.85 ? 220 TRP A CH2 1 ATOM 1096 N N . ALA A 1 139 ? 39.666 12.086 54.356 1.00 7.88 ? 221 ALA A N 1 ATOM 1097 C CA . ALA A 1 139 ? 40.342 12.837 55.409 1.00 9.29 ? 221 ALA A CA 1 ATOM 1098 C C . ALA A 1 139 ? 40.213 12.162 56.773 1.00 10.19 ? 221 ALA A C 1 ATOM 1099 O O . ALA A 1 139 ? 40.732 12.667 57.771 1.00 9.37 ? 221 ALA A O 1 ATOM 1100 C CB . ALA A 1 139 ? 39.815 14.270 55.465 1.00 9.11 ? 221 ALA A CB 1 ATOM 1101 N N . ARG A 1 140 ? 39.505 11.033 56.809 1.00 8.02 ? 222 ARG A N 1 ATOM 1102 C CA . ARG A 1 140 ? 39.373 10.231 58.026 1.00 7.29 ? 222 ARG A CA 1 ATOM 1103 C C . ARG A 1 140 ? 38.841 11.019 59.225 1.00 9.28 ? 222 ARG A C 1 ATOM 1104 O O . ARG A 1 140 ? 39.293 10.835 60.359 1.00 9.08 ? 222 ARG A O 1 ATOM 1105 C CB . ARG A 1 140 ? 40.709 9.561 58.358 1.00 9.63 ? 222 ARG A CB 1 ATOM 1106 C CG . ARG A 1 140 ? 41.126 8.543 57.304 1.00 14.91 ? 222 ARG A CG 1 ATOM 1107 C CD . ARG A 1 140 ? 42.636 8.486 57.125 1.00 30.01 ? 222 ARG A CD 1 ATOM 1108 N NE . ARG A 1 140 ? 43.001 8.780 55.740 1.00 58.55 ? 222 ARG A NE 1 ATOM 1109 C CZ . ARG A 1 140 ? 43.427 9.962 55.300 1.00 41.41 ? 222 ARG A CZ 1 ATOM 1110 N NH1 . ARG A 1 140 ? 43.573 10.985 56.136 1.00 26.89 ? 222 ARG A NH1 1 ATOM 1111 N NH2 . ARG A 1 140 ? 43.721 10.114 54.016 1.00 45.93 ? 222 ARG A NH2 1 ATOM 1112 N N . ASN A 1 141 ? 37.876 11.894 58.969 1.00 8.31 ? 223 ASN A N 1 ATOM 1113 C CA . ASN A 1 141 ? 37.286 12.689 60.036 1.00 7.41 ? 223 ASN A CA 1 ATOM 1114 C C . ASN A 1 141 ? 35.838 13.039 59.733 1.00 8.62 ? 223 ASN A C 1 ATOM 1115 O O . ASN A 1 141 ? 35.540 14.164 59.337 1.00 7.60 ? 223 ASN A O 1 ATOM 1116 C CB . ASN A 1 141 ? 38.110 13.961 60.264 1.00 8.89 ? 223 ASN A CB 1 ATOM 1117 C CG . ASN A 1 141 ? 37.705 14.705 61.519 1.00 11.10 ? 223 ASN A CG 1 ATOM 1118 O OD1 . ASN A 1 141 ? 36.729 14.353 62.181 1.00 8.81 ? 223 ASN A OD1 1 ATOM 1119 N ND2 . ASN A 1 141 ? 38.459 15.744 61.855 1.00 13.32 ? 223 ASN A ND2 1 ATOM 1120 N N . ILE A 1 142 ? 34.948 12.065 59.919 1.00 7.48 ? 224 ILE A N 1 ATOM 1121 C CA . ILE A 1 142 ? 33.506 12.264 59.760 1.00 7.15 ? 224 ILE A CA 1 ATOM 1122 C C . ILE A 1 142 ? 33.097 12.783 58.375 1.00 5.90 ? 224 ILE A C 1 ATOM 1123 O O . ILE A 1 142 ? 32.604 13.907 58.229 1.00 6.66 ? 224 ILE A O 1 ATOM 1124 C CB . ILE A 1 142 ? 32.918 13.147 60.891 1.00 6.91 ? 224 ILE A CB 1 ATOM 1125 C CG1 . ILE A 1 142 ? 33.493 12.730 62.251 1.00 6.60 ? 224 ILE A CG1 1 ATOM 1126 C CG2 . ILE A 1 142 ? 31.392 13.033 60.925 1.00 6.61 ? 224 ILE A CG2 1 ATOM 1127 C CD1 . ILE A 1 142 ? 32.947 13.531 63.434 1.00 10.88 ? 224 ILE A CD1 1 ATOM 1128 N N . LEU A 1 143 ? 33.310 11.947 57.360 1.00 7.16 ? 225 LEU A N 1 ATOM 1129 C CA . LEU A 1 143 ? 32.779 12.206 56.028 1.00 6.60 ? 225 LEU A CA 1 ATOM 1130 C C . LEU A 1 143 ? 31.293 12.519 56.170 1.00 7.42 ? 225 LEU A C 1 ATOM 1131 O O . LEU A 1 143 ? 30.575 11.800 56.866 1.00 6.34 ? 225 LEU A O 1 ATOM 1132 C CB . LEU A 1 143 ? 32.989 10.981 55.136 1.00 6.50 ? 225 LEU A CB 1 ATOM 1133 C CG . LEU A 1 143 ? 32.386 11.027 53.732 1.00 5.80 ? 225 LEU A CG 1 ATOM 1134 C CD1 . LEU A 1 143 ? 33.012 12.143 52.920 1.00 7.16 ? 225 LEU A CD1 1 ATOM 1135 C CD2 . LEU A 1 143 ? 32.582 9.693 53.026 1.00 6.74 ? 225 LEU A CD2 1 ATOM 1136 N N . ARG A 1 144 ? 30.839 13.608 55.553 1.00 5.37 ? 226 ARG A N 1 ATOM 1137 C CA . ARG A 1 144 ? 29.471 14.081 55.777 1.00 7.88 ? 226 ARG A CA 1 ATOM 1138 C C . ARG A 1 144 ? 28.935 14.896 54.602 1.00 6.56 ? 226 ARG A C 1 ATOM 1139 O O . ARG A 1 144 ? 29.705 15.442 53.805 1.00 6.69 ? 226 ARG A O 1 ATOM 1140 C CB . ARG A 1 144 ? 29.390 14.874 57.084 1.00 6.00 ? 226 ARG A CB 1 ATOM 1141 C CG . ARG A 1 144 ? 30.370 16.044 57.186 1.00 6.83 ? 226 ARG A CG 1 ATOM 1142 C CD . ARG A 1 144 ? 30.639 16.379 58.652 1.00 5.91 ? 226 ARG A CD 1 ATOM 1143 N NE . ARG A 1 144 ? 31.414 17.608 58.840 1.00 7.17 ? 226 ARG A NE 1 ATOM 1144 C CZ . ARG A 1 144 ? 32.743 17.665 58.870 1.00 12.87 ? 226 ARG A CZ 1 ATOM 1145 N NH1 . ARG A 1 144 ? 33.471 16.566 58.698 1.00 8.04 ? 226 ARG A NH1 1 ATOM 1146 N NH2 . ARG A 1 144 ? 33.349 18.831 59.067 1.00 7.06 ? 226 ARG A NH2 1 ATOM 1147 N N . THR A 1 145 ? 27.612 14.965 54.479 1.00 6.41 ? 227 THR A N 1 ATOM 1148 C CA . THR A 1 145 ? 27.020 15.600 53.310 1.00 5.24 ? 227 THR A CA 1 ATOM 1149 C C . THR A 1 145 ? 25.839 16.523 53.654 1.00 4.39 ? 227 THR A C 1 ATOM 1150 O O . THR A 1 145 ? 25.779 17.068 54.758 1.00 6.96 ? 227 THR A O 1 ATOM 1151 C CB . THR A 1 145 ? 26.711 14.553 52.195 1.00 7.60 ? 227 THR A CB 1 ATOM 1152 O OG1 . THR A 1 145 ? 26.355 15.217 50.975 1.00 6.97 ? 227 THR A OG1 1 ATOM 1153 C CG2 . THR A 1 145 ? 25.601 13.588 52.616 1.00 5.61 ? 227 THR A CG2 1 ATOM 1154 N N . GLN A 1 146 ? 24.917 16.710 52.714 1.00 4.47 ? 228 GLN A N 1 ATOM 1155 C CA . GLN A 1 146 ? 24.010 17.864 52.757 1.00 4.95 ? 228 GLN A CA 1 ATOM 1156 C C . GLN A 1 146 ? 22.938 17.875 53.852 1.00 4.79 ? 228 GLN A C 1 ATOM 1157 O O . GLN A 1 146 ? 22.666 18.925 54.445 1.00 6.39 ? 228 GLN A O 1 ATOM 1158 C CB . GLN A 1 146 ? 23.382 18.085 51.374 1.00 4.79 ? 228 GLN A CB 1 ATOM 1159 C CG . GLN A 1 146 ? 24.447 18.304 50.305 1.00 5.56 ? 228 GLN A CG 1 ATOM 1160 C CD . GLN A 1 146 ? 23.904 18.595 48.925 1.00 8.92 ? 228 GLN A CD 1 ATOM 1161 O OE1 . GLN A 1 146 ? 24.677 18.721 47.975 1.00 11.51 ? 228 GLN A OE1 1 ATOM 1162 N NE2 . GLN A 1 146 ? 22.584 18.708 48.798 1.00 7.90 ? 228 GLN A NE2 1 ATOM 1163 N N . GLU A 1 147 ? 22.345 16.714 54.117 1.00 5.55 ? 229 GLU A N 1 ATOM 1164 C CA . GLU A 1 147 ? 21.161 16.589 54.985 1.00 3.66 ? 229 GLU A CA 1 ATOM 1165 C C . GLU A 1 147 ? 19.912 17.280 54.413 1.00 4.24 ? 229 GLU A C 1 ATOM 1166 O O . GLU A 1 147 ? 18.967 17.569 55.144 1.00 4.89 ? 229 GLU A O 1 ATOM 1167 C CB . GLU A 1 147 ? 21.419 17.028 56.445 1.00 5.68 ? 229 GLU A CB 1 ATOM 1168 C CG . GLU A 1 147 ? 22.826 16.756 57.008 1.00 6.91 ? 229 GLU A CG 1 ATOM 1169 C CD . GLU A 1 147 ? 23.200 15.280 57.087 1.00 10.01 ? 229 GLU A CD 1 ATOM 1170 O OE1 . GLU A 1 147 ? 22.383 14.408 56.723 1.00 6.90 ? 229 GLU A OE1 1 ATOM 1171 O OE2 . GLU A 1 147 ? 24.337 14.992 57.516 1.00 8.74 ? 229 GLU A OE2 1 ATOM 1172 N N . SER A 1 148 ? 19.923 17.547 53.108 1.00 5.16 ? 230 SER A N 1 ATOM 1173 C CA . SER A 1 148 ? 18.713 17.914 52.374 1.00 4.23 ? 230 SER A CA 1 ATOM 1174 C C . SER A 1 148 ? 18.893 17.497 50.921 1.00 6.43 ? 230 SER A C 1 ATOM 1175 O O . SER A 1 148 ? 19.934 16.939 50.558 1.00 7.09 ? 230 SER A O 1 ATOM 1176 C CB . SER A 1 148 ? 18.380 19.404 52.493 1.00 6.16 ? 230 SER A CB 1 ATOM 1177 O OG . SER A 1 148 ? 19.397 20.210 51.923 1.00 8.03 ? 230 SER A OG 1 ATOM 1178 N N . GLU A 1 149 ? 17.888 17.745 50.089 1.00 4.55 ? 231 GLU A N 1 ATOM 1179 C CA . GLU A 1 149 ? 17.899 17.161 48.749 1.00 6.86 ? 231 GLU A CA 1 ATOM 1180 C C . GLU A 1 149 ? 18.999 17.739 47.870 1.00 9.21 ? 231 GLU A C 1 ATOM 1181 O O . GLU A 1 149 ? 19.386 18.902 48.019 1.00 7.45 ? 231 GLU A O 1 ATOM 1182 C CB . GLU A 1 149 ? 16.539 17.300 48.056 1.00 3.98 ? 231 GLU A CB 1 ATOM 1183 C CG . GLU A 1 149 ? 16.277 18.656 47.401 1.00 7.00 ? 231 GLU A CG 1 ATOM 1184 C CD . GLU A 1 149 ? 15.068 18.620 46.478 1.00 8.42 ? 231 GLU A CD 1 ATOM 1185 O OE1 . GLU A 1 149 ? 14.382 17.572 46.439 1.00 6.76 ? 231 GLU A OE1 1 ATOM 1186 O OE2 . GLU A 1 149 ? 14.802 19.634 45.793 1.00 7.44 ? 231 GLU A OE2 1 ATOM 1187 N N . CYS A 1 150 ? 19.513 16.906 46.970 1.00 6.62 ? 232 CYS A N 1 ATOM 1188 C CA . CYS A 1 150 ? 20.368 17.382 45.887 1.00 8.65 ? 232 CYS A CA 1 ATOM 1189 C C . CYS A 1 150 ? 19.492 17.816 44.708 1.00 8.09 ? 232 CYS A C 1 ATOM 1190 O O . CYS A 1 150 ? 18.266 17.793 44.804 1.00 7.17 ? 232 CYS A O 1 ATOM 1191 C CB . CYS A 1 150 ? 21.379 16.303 45.479 1.00 9.25 ? 232 CYS A CB 1 ATOM 1192 S SG . CYS A 1 150 ? 20.759 14.584 45.502 1.00 9.33 ? 232 CYS A SG 1 ATOM 1193 N N . VAL A 1 151 ? 20.115 18.253 43.615 1.00 8.60 ? 233 VAL A N 1 ATOM 1194 C CA . VAL A 1 151 ? 19.375 18.733 42.446 1.00 5.79 ? 233 VAL A CA 1 ATOM 1195 C C . VAL A 1 151 ? 20.024 18.171 41.183 1.00 7.84 ? 233 VAL A C 1 ATOM 1196 O O . VAL A 1 151 ? 21.240 18.011 41.135 1.00 9.72 ? 233 VAL A O 1 ATOM 1197 C CB . VAL A 1 151 ? 19.370 20.280 42.366 1.00 9.95 ? 233 VAL A CB 1 ATOM 1198 C CG1 . VAL A 1 151 ? 18.465 20.762 41.242 1.00 12.09 ? 233 VAL A CG1 1 ATOM 1199 C CG2 . VAL A 1 151 ? 18.898 20.887 43.671 1.00 13.76 ? 233 VAL A CG2 1 ATOM 1200 N N . CYS A 1 152 ? 19.221 17.874 40.166 1.00 6.79 ? 234 CYS A N 1 ATOM 1201 C CA . CYS A 1 152 ? 19.741 17.260 38.950 1.00 7.72 ? 234 CYS A CA 1 ATOM 1202 C C . CYS A 1 152 ? 19.442 18.095 37.709 1.00 10.10 ? 234 CYS A C 1 ATOM 1203 O O . CYS A 1 152 ? 18.415 18.779 37.635 1.00 9.11 ? 234 CYS A O 1 ATOM 1204 C CB . CYS A 1 152 ? 19.157 15.856 38.770 1.00 9.85 ? 234 CYS A CB 1 ATOM 1205 S SG . CYS A 1 152 ? 19.438 14.741 40.170 1.00 9.15 ? 234 CYS A SG 1 ATOM 1206 N N . HIS A 1 153 ? 20.342 18.025 36.731 1.00 9.29 ? 235 HIS A N 1 ATOM 1207 C CA . HIS A 1 153 ? 20.102 18.626 35.419 1.00 11.11 ? 235 HIS A CA 1 ATOM 1208 C C . HIS A 1 153 ? 20.590 17.702 34.305 1.00 10.06 ? 235 HIS A C 1 ATOM 1209 O O . HIS A 1 153 ? 21.776 17.374 34.245 1.00 9.86 ? 235 HIS A O 1 ATOM 1210 C CB . HIS A 1 153 ? 20.804 19.977 35.289 1.00 8.36 ? 235 HIS A CB 1 ATOM 1211 C CG . HIS A 1 153 ? 20.679 20.578 33.924 1.00 12.04 ? 235 HIS A CG 1 ATOM 1212 N ND1 . HIS A 1 153 ? 19.551 21.255 33.509 1.00 14.48 ? 235 HIS A ND1 1 ATOM 1213 C CD2 . HIS A 1 153 ? 21.522 20.567 32.864 1.00 14.29 ? 235 HIS A CD2 1 ATOM 1214 C CE1 . HIS A 1 153 ? 19.714 21.654 32.260 1.00 17.02 ? 235 HIS A CE1 1 ATOM 1215 N NE2 . HIS A 1 153 ? 20.901 21.248 31.843 1.00 13.50 ? 235 HIS A NE2 1 ATOM 1216 N N . ASN A 1 154 ? 19.675 17.299 33.427 1.00 8.71 ? 236 ASN A N 1 ATOM 1217 C CA . ASN A 1 154 ? 19.981 16.355 32.347 1.00 11.21 ? 236 ASN A CA 1 ATOM 1218 C C . ASN A 1 154 ? 20.733 15.122 32.846 1.00 10.98 ? 236 ASN A C 1 ATOM 1219 O O . ASN A 1 154 ? 21.713 14.678 32.235 1.00 10.73 ? 236 ASN A O 1 ATOM 1220 C CB . ASN A 1 154 ? 20.758 17.046 31.222 1.00 11.78 ? 236 ASN A CB 1 ATOM 1221 C CG . ASN A 1 154 ? 20.808 16.215 29.956 1.00 17.43 ? 236 ASN A CG 1 ATOM 1222 O OD1 . ASN A 1 154 ? 19.901 15.426 29.683 1.00 15.04 ? 236 ASN A OD1 1 ATOM 1223 N ND2 . ASN A 1 154 ? 21.875 16.376 29.185 1.00 20.85 ? 236 ASN A ND2 1 ATOM 1224 N N . GLY A 1 155 ? 20.289 14.596 33.982 1.00 10.12 ? 237 GLY A N 1 ATOM 1225 C CA . GLY A 1 155 ? 20.875 13.391 34.541 1.00 11.92 ? 237 GLY A CA 1 ATOM 1226 C C . GLY A 1 155 ? 22.064 13.600 35.460 1.00 13.19 ? 237 GLY A C 1 ATOM 1227 O O . GLY A 1 155 ? 22.469 12.672 36.163 1.00 10.70 ? 237 GLY A O 1 ATOM 1228 N N . VAL A 1 156 ? 22.644 14.798 35.453 1.00 8.56 ? 238 VAL A N 1 ATOM 1229 C CA . VAL A 1 156 ? 23.792 15.073 36.311 1.00 7.63 ? 238 VAL A CA 1 ATOM 1230 C C . VAL A 1 156 ? 23.335 15.667 37.638 1.00 10.09 ? 238 VAL A C 1 ATOM 1231 O O . VAL A 1 156 ? 22.663 16.696 37.656 1.00 8.00 ? 238 VAL A O 1 ATOM 1232 C CB . VAL A 1 156 ? 24.785 16.045 35.647 1.00 11.33 ? 238 VAL A CB 1 ATOM 1233 C CG1 . VAL A 1 156 ? 25.945 16.337 36.589 1.00 8.97 ? 238 VAL A CG1 1 ATOM 1234 C CG2 . VAL A 1 156 ? 25.291 15.463 34.339 1.00 13.06 ? 238 VAL A CG2 1 ATOM 1235 N N . CYS A 1 157 ? 23.712 15.018 38.739 1.00 8.36 ? 239 CYS A N 1 ATOM 1236 C CA . CYS A 1 157 ? 23.287 15.430 40.077 1.00 9.14 ? 239 CYS A CA 1 ATOM 1237 C C . CYS A 1 157 ? 24.499 15.736 40.941 1.00 7.00 ? 239 CYS A C 1 ATOM 1238 O O . CYS A 1 157 ? 25.156 14.818 41.442 1.00 7.89 ? 239 CYS A O 1 ATOM 1239 C CB . CYS A 1 157 ? 22.475 14.318 40.748 1.00 8.69 ? 239 CYS A CB 1 ATOM 1240 S SG . CYS A 1 157 ? 21.107 13.651 39.761 1.00 9.20 ? 239 CYS A SG 1 ATOM 1241 N N . PRO A 1 158 ? 24.811 17.028 41.119 1.00 8.01 ? 240 PRO A N 1 ATOM 1242 C CA . PRO A 1 158 ? 25.950 17.391 41.970 1.00 7.62 ? 240 PRO A CA 1 ATOM 1243 C C . PRO A 1 158 ? 25.620 17.234 43.453 1.00 7.89 ? 240 PRO A C 1 ATOM 1244 O O . PRO A 1 158 ? 24.476 17.464 43.856 1.00 6.88 ? 240 PRO A O 1 ATOM 1245 C CB . PRO A 1 158 ? 26.185 18.873 41.642 1.00 8.28 ? 240 PRO A CB 1 ATOM 1246 C CG . PRO A 1 158 ? 25.421 19.129 40.365 1.00 11.12 ? 240 PRO A CG 1 ATOM 1247 C CD . PRO A 1 158 ? 24.255 18.195 40.413 1.00 8.30 ? 240 PRO A CD 1 ATOM 1248 N N . VAL A 1 159 ? 26.612 16.835 44.243 1.00 6.10 ? 241 VAL A N 1 ATOM 1249 C CA . VAL A 1 159 ? 26.450 16.700 45.691 1.00 7.95 ? 241 VAL A CA 1 ATOM 1250 C C . VAL A 1 159 ? 27.681 17.257 46.400 1.00 9.19 ? 241 VAL A C 1 ATOM 1251 O O . VAL A 1 159 ? 28.811 16.981 45.989 1.00 8.85 ? 241 VAL A O 1 ATOM 1252 C CB . VAL A 1 159 ? 26.259 15.222 46.112 1.00 6.61 ? 241 VAL A CB 1 ATOM 1253 C CG1 . VAL A 1 159 ? 26.183 15.100 47.636 1.00 5.18 ? 241 VAL A CG1 1 ATOM 1254 C CG2 . VAL A 1 159 ? 25.009 14.629 45.468 1.00 5.79 ? 241 VAL A CG2 1 ATOM 1255 N N . VAL A 1 160 ? 27.473 18.035 47.463 1.00 4.56 ? 242 VAL A N 1 ATOM 1256 C CA . VAL A 1 160 ? 28.594 18.563 48.239 1.00 6.82 ? 242 VAL A CA 1 ATOM 1257 C C . VAL A 1 160 ? 28.897 17.696 49.467 1.00 8.09 ? 242 VAL A C 1 ATOM 1258 O O . VAL A 1 160 ? 27.994 17.390 50.249 1.00 7.78 ? 242 VAL A O 1 ATOM 1259 C CB . VAL A 1 160 ? 28.339 20.025 48.686 1.00 4.95 ? 242 VAL A CB 1 ATOM 1260 C CG1 . VAL A 1 160 ? 29.581 20.594 49.381 1.00 6.42 ? 242 VAL A CG1 1 ATOM 1261 C CG2 . VAL A 1 160 ? 27.951 20.890 47.485 1.00 8.11 ? 242 VAL A CG2 1 ATOM 1262 N N . PHE A 1 161 ? 30.166 17.303 49.620 1.00 6.64 ? 243 PHE A N 1 ATOM 1263 C CA . PHE A 1 161 ? 30.634 16.521 50.766 1.00 6.16 ? 243 PHE A CA 1 ATOM 1264 C C . PHE A 1 161 ? 31.721 17.289 51.506 1.00 9.19 ? 243 PHE A C 1 ATOM 1265 O O . PHE A 1 161 ? 32.447 18.082 50.903 1.00 10.25 ? 243 PHE A O 1 ATOM 1266 C CB . PHE A 1 161 ? 31.290 15.213 50.304 1.00 6.65 ? 243 PHE A CB 1 ATOM 1267 C CG . PHE A 1 161 ? 30.350 14.215 49.700 1.00 8.36 ? 243 PHE A CG 1 ATOM 1268 C CD1 . PHE A 1 161 ? 30.028 14.274 48.352 1.00 7.87 ? 243 PHE A CD1 1 ATOM 1269 C CD2 . PHE A 1 161 ? 29.837 13.176 50.468 1.00 7.16 ? 243 PHE A CD2 1 ATOM 1270 C CE1 . PHE A 1 161 ? 29.186 13.334 47.781 1.00 8.87 ? 243 PHE A CE1 1 ATOM 1271 C CE2 . PHE A 1 161 ? 28.991 12.229 49.905 1.00 7.09 ? 243 PHE A CE2 1 ATOM 1272 C CZ . PHE A 1 161 ? 28.666 12.309 48.559 1.00 10.53 ? 243 PHE A CZ 1 ATOM 1273 N N . THR A 1 162 ? 31.865 17.019 52.800 1.00 5.33 ? 244 THR A N 1 ATOM 1274 C CA . THR A 1 162 ? 32.999 17.532 53.563 1.00 5.87 ? 244 THR A CA 1 ATOM 1275 C C . THR A 1 162 ? 33.583 16.403 54.406 1.00 9.44 ? 244 THR A C 1 ATOM 1276 O O . THR A 1 162 ? 32.846 15.578 54.949 1.00 6.03 ? 244 THR A O 1 ATOM 1277 C CB . THR A 1 162 ? 32.594 18.731 54.459 1.00 7.93 ? 244 THR A CB 1 ATOM 1278 O OG1 . THR A 1 162 ? 32.107 19.802 53.639 1.00 8.67 ? 244 THR A OG1 1 ATOM 1279 C CG2 . THR A 1 162 ? 33.786 19.233 55.277 1.00 8.62 ? 244 THR A CG2 1 ATOM 1280 N N . ASP A 1 163 ? 34.909 16.352 54.491 1.00 7.65 ? 245 ASP A N 1 ATOM 1281 C CA . ASP A 1 163 ? 35.599 15.386 55.337 1.00 8.46 ? 245 ASP A CA 1 ATOM 1282 C C . ASP A 1 163 ? 36.730 16.159 56.010 1.00 9.42 ? 245 ASP A C 1 ATOM 1283 O O . ASP A 1 163 ? 37.477 16.875 55.345 1.00 10.02 ? 245 ASP A O 1 ATOM 1284 C CB . ASP A 1 163 ? 36.149 14.241 54.476 1.00 8.11 ? 245 ASP A CB 1 ATOM 1285 C CG . ASP A 1 163 ? 36.491 12.991 55.282 1.00 8.99 ? 245 ASP A CG 1 ATOM 1286 O OD1 . ASP A 1 163 ? 36.602 13.068 56.525 1.00 7.91 ? 245 ASP A OD1 1 ATOM 1287 O OD2 . ASP A 1 163 ? 36.676 11.921 54.658 1.00 10.69 ? 245 ASP A OD2 1 ATOM 1288 N N . GLY A 1 164 ? 36.842 16.051 57.329 1.00 6.18 ? 246 GLY A N 1 ATOM 1289 C CA . GLY A 1 164 ? 37.839 16.820 58.049 1.00 8.90 ? 246 GLY A CA 1 ATOM 1290 C C . GLY A 1 164 ? 37.248 17.605 59.199 1.00 11.31 ? 246 GLY A C 1 ATOM 1291 O O . GLY A 1 164 ? 36.105 17.380 59.593 1.00 8.65 ? 246 GLY A O 1 ATOM 1292 N N . SER A 1 165 ? 38.027 18.538 59.733 1.00 10.01 ? 247 SER A N 1 ATOM 1293 C CA . SER A 1 165 ? 37.654 19.255 60.952 1.00 7.62 ? 247 SER A CA 1 ATOM 1294 C C . SER A 1 165 ? 36.352 20.046 60.838 1.00 8.10 ? 247 SER A C 1 ATOM 1295 O O . SER A 1 165 ? 36.020 20.565 59.774 1.00 9.70 ? 247 SER A O 1 ATOM 1296 C CB . SER A 1 165 ? 38.784 20.204 61.363 1.00 11.61 ? 247 SER A CB 1 ATOM 1297 O OG . SER A 1 165 ? 38.485 20.843 62.590 1.00 13.35 ? 247 SER A OG 1 ATOM 1298 N N . ALA A 1 166 ? 35.624 20.144 61.948 1.00 9.62 ? 248 ALA A N 1 ATOM 1299 C CA . ALA A 1 166 ? 34.461 21.026 62.021 1.00 8.84 ? 248 ALA A CA 1 ATOM 1300 C C . ALA A 1 166 ? 34.851 22.376 62.621 1.00 10.97 ? 248 ALA A C 1 ATOM 1301 O O . ALA A 1 166 ? 34.033 23.300 62.679 1.00 11.42 ? 248 ALA A O 1 ATOM 1302 C CB . ALA A 1 166 ? 33.346 20.383 62.838 1.00 12.40 ? 248 ALA A CB 1 ATOM 1303 N N . THR A 1 167 ? 36.104 22.479 63.062 1.00 11.51 ? 249 THR A N 1 ATOM 1304 C CA . THR A 1 167 ? 36.584 23.658 63.787 1.00 14.00 ? 249 THR A CA 1 ATOM 1305 C C . THR A 1 167 ? 37.882 24.225 63.198 1.00 17.92 ? 249 THR A C 1 ATOM 1306 O O . THR A 1 167 ? 38.670 24.874 63.895 1.00 17.00 ? 249 THR A O 1 ATOM 1307 C CB . THR A 1 167 ? 36.812 23.324 65.269 1.00 12.96 ? 249 THR A CB 1 ATOM 1308 O OG1 . THR A 1 167 ? 37.769 22.261 65.376 1.00 14.68 ? 249 THR A OG1 1 ATOM 1309 C CG2 . THR A 1 167 ? 35.508 22.881 65.923 1.00 16.90 ? 249 THR A CG2 1 ATOM 1310 N N . GLY A 1 168 ? 38.088 23.977 61.910 1.00 10.93 ? 250 GLY A N 1 ATOM 1311 C CA . GLY A 1 168 ? 39.276 24.417 61.200 1.00 11.07 ? 250 GLY A CA 1 ATOM 1312 C C . GLY A 1 168 ? 39.103 24.039 59.744 1.00 13.56 ? 250 GLY A C 1 ATOM 1313 O O . GLY A 1 168 ? 38.042 23.541 59.366 1.00 11.67 ? 250 GLY A O 1 ATOM 1314 N N . PRO A 1 169 ? 40.138 24.268 58.918 1.00 12.28 ? 251 PRO A N 1 ATOM 1315 C CA . PRO A 1 169 ? 40.064 23.940 57.489 1.00 14.73 ? 251 PRO A CA 1 ATOM 1316 C C . PRO A 1 169 ? 39.774 22.456 57.269 1.00 14.01 ? 251 PRO A C 1 ATOM 1317 O O . PRO A 1 169 ? 40.342 21.609 57.964 1.00 14.14 ? 251 PRO A O 1 ATOM 1318 C CB . PRO A 1 169 ? 41.466 24.293 56.978 1.00 18.43 ? 251 PRO A CB 1 ATOM 1319 C CG . PRO A 1 169 ? 41.961 25.336 57.944 1.00 17.51 ? 251 PRO A CG 1 ATOM 1320 C CD . PRO A 1 169 ? 41.413 24.916 59.273 1.00 14.00 ? 251 PRO A CD 1 ATOM 1321 N N . ALA A 1 170 ? 38.884 22.161 56.325 1.00 10.58 ? 252 ALA A N 1 ATOM 1322 C CA . ALA A 1 170 ? 38.488 20.791 56.022 1.00 15.02 ? 252 ALA A CA 1 ATOM 1323 C C . ALA A 1 170 ? 38.572 20.550 54.519 1.00 13.94 ? 252 ALA A C 1 ATOM 1324 O O . ALA A 1 170 ? 38.821 21.482 53.750 1.00 12.64 ? 252 ALA A O 1 ATOM 1325 C CB . ALA A 1 170 ? 37.077 20.527 56.524 1.00 8.50 ? 252 ALA A CB 1 ATOM 1326 N N . ASP A 1 171 ? 38.356 19.304 54.102 1.00 9.13 ? 253 ASP A N 1 ATOM 1327 C CA . ASP A 1 171 ? 38.441 18.947 52.690 1.00 8.50 ? 253 ASP A CA 1 ATOM 1328 C C . ASP A 1 171 ? 37.058 18.738 52.090 1.00 12.41 ? 253 ASP A C 1 ATOM 1329 O O . ASP A 1 171 ? 36.462 17.666 52.231 1.00 9.95 ? 253 ASP A O 1 ATOM 1330 C CB . ASP A 1 171 ? 39.286 17.681 52.501 1.00 11.10 ? 253 ASP A CB 1 ATOM 1331 C CG . ASP A 1 171 ? 40.705 17.846 53.005 1.00 24.83 ? 253 ASP A CG 1 ATOM 1332 O OD1 . ASP A 1 171 ? 41.249 18.961 52.878 1.00 20.50 ? 253 ASP A OD1 1 ATOM 1333 O OD2 . ASP A 1 171 ? 41.276 16.864 53.525 1.00 25.05 ? 253 ASP A OD2 1 ATOM 1334 N N . THR A 1 172 ? 36.556 19.772 51.422 1.00 8.12 ? 254 THR A N 1 ATOM 1335 C CA . THR A 1 172 ? 35.240 19.728 50.796 1.00 6.29 ? 254 THR A CA 1 ATOM 1336 C C . THR A 1 172 ? 35.387 19.360 49.330 1.00 9.23 ? 254 THR A C 1 ATOM 1337 O O . THR A 1 172 ? 36.279 19.860 48.644 1.00 11.69 ? 254 THR A O 1 ATOM 1338 C CB . THR A 1 172 ? 34.528 21.081 50.944 1.00 10.18 ? 254 THR A CB 1 ATOM 1339 O OG1 . THR A 1 172 ? 34.214 21.288 52.328 1.00 7.95 ? 254 THR A OG1 1 ATOM 1340 C CG2 . THR A 1 172 ? 33.245 21.126 50.113 1.00 6.91 ? 254 THR A CG2 1 ATOM 1341 N N . ARG A 1 173 ? 34.527 18.459 48.864 1.00 7.67 ? 255 ARG A N 1 ATOM 1342 C CA . ARG A 1 173 ? 34.526 18.036 47.471 1.00 7.08 ? 255 ARG A CA 1 ATOM 1343 C C . ARG A 1 173 ? 33.128 18.171 46.896 1.00 11.43 ? 255 ARG A C 1 ATOM 1344 O O . ARG A 1 173 ? 32.139 17.949 47.597 1.00 10.45 ? 255 ARG A O 1 ATOM 1345 C CB . ARG A 1 173 ? 34.956 16.573 47.355 1.00 7.50 ? 255 ARG A CB 1 ATOM 1346 C CG . ARG A 1 173 ? 36.402 16.301 47.708 1.00 9.67 ? 255 ARG A CG 1 ATOM 1347 C CD . ARG A 1 173 ? 36.755 14.837 47.471 1.00 7.24 ? 255 ARG A CD 1 ATOM 1348 N NE . ARG A 1 173 ? 38.151 14.566 47.805 1.00 11.16 ? 255 ARG A NE 1 ATOM 1349 C CZ . ARG A 1 173 ? 38.750 13.391 47.636 1.00 11.14 ? 255 ARG A CZ 1 ATOM 1350 N NH1 . ARG A 1 173 ? 38.076 12.365 47.141 1.00 11.07 ? 255 ARG A NH1 1 ATOM 1351 N NH2 . ARG A 1 173 ? 40.025 13.246 47.962 1.00 12.71 ? 255 ARG A NH2 1 ATOM 1352 N N . ILE A 1 174 ? 33.045 18.530 45.620 1.00 7.87 ? 256 ILE A N 1 ATOM 1353 C CA . ILE A 1 174 ? 31.778 18.487 44.905 1.00 10.37 ? 256 ILE A CA 1 ATOM 1354 C C . ILE A 1 174 ? 31.818 17.303 43.946 1.00 12.84 ? 256 ILE A C 1 ATOM 1355 O O . ILE A 1 174 ? 32.686 17.236 43.068 1.00 11.47 ? 256 ILE A O 1 ATOM 1356 C CB . ILE A 1 174 ? 31.502 19.783 44.114 1.00 10.70 ? 256 ILE A CB 1 ATOM 1357 C CG1 . ILE A 1 174 ? 31.311 20.974 45.058 1.00 13.83 ? 256 ILE A CG1 1 ATOM 1358 C CG2 . ILE A 1 174 ? 30.257 19.618 43.254 1.00 10.17 ? 256 ILE A CG2 1 ATOM 1359 C CD1 . ILE A 1 174 ? 32.593 21.651 45.484 1.00 20.39 ? 256 ILE A CD1 1 ATOM 1360 N N . TYR A 1 175 ? 30.895 16.362 44.133 1.00 8.44 ? 257 TYR A N 1 ATOM 1361 C CA . TYR A 1 175 ? 30.801 15.186 43.276 1.00 8.75 ? 257 TYR A CA 1 ATOM 1362 C C . TYR A 1 175 ? 29.694 15.351 42.256 1.00 10.90 ? 257 TYR A C 1 ATOM 1363 O O . TYR A 1 175 ? 28.658 15.944 42.546 1.00 11.17 ? 257 TYR A O 1 ATOM 1364 C CB . TYR A 1 175 ? 30.530 13.933 44.111 1.00 8.76 ? 257 TYR A CB 1 ATOM 1365 C CG . TYR A 1 175 ? 31.780 13.283 44.642 1.00 8.88 ? 257 TYR A CG 1 ATOM 1366 C CD1 . TYR A 1 175 ? 32.441 13.804 45.747 1.00 10.62 ? 257 TYR A CD1 1 ATOM 1367 C CD2 . TYR A 1 175 ? 32.301 12.145 44.038 1.00 9.35 ? 257 TYR A CD2 1 ATOM 1368 C CE1 . TYR A 1 175 ? 33.590 13.210 46.239 1.00 8.02 ? 257 TYR A CE1 1 ATOM 1369 C CE2 . TYR A 1 175 ? 33.448 11.545 44.521 1.00 10.52 ? 257 TYR A CE2 1 ATOM 1370 C CZ . TYR A 1 175 ? 34.090 12.083 45.615 1.00 10.54 ? 257 TYR A CZ 1 ATOM 1371 O OH . TYR A 1 175 ? 35.236 11.489 46.095 1.00 10.72 ? 257 TYR A OH 1 ATOM 1372 N N . TYR A 1 176 ? 29.916 14.823 41.058 1.00 8.18 ? 258 TYR A N 1 ATOM 1373 C CA . TYR A 1 176 ? 28.916 14.888 40.003 1.00 7.84 ? 258 TYR A CA 1 ATOM 1374 C C . TYR A 1 176 ? 28.528 13.467 39.639 1.00 10.49 ? 258 TYR A C 1 ATOM 1375 O O . TYR A 1 176 ? 29.360 12.701 39.154 1.00 11.08 ? 258 TYR A O 1 ATOM 1376 C CB . TYR A 1 176 ? 29.472 15.636 38.785 1.00 10.62 ? 258 TYR A CB 1 ATOM 1377 C CG . TYR A 1 176 ? 29.877 17.061 39.100 1.00 8.92 ? 258 TYR A CG 1 ATOM 1378 C CD1 . TYR A 1 176 ? 31.148 17.352 39.580 1.00 9.36 ? 258 TYR A CD1 1 ATOM 1379 C CD2 . TYR A 1 176 ? 28.977 18.109 38.941 1.00 9.65 ? 258 TYR A CD2 1 ATOM 1380 C CE1 . TYR A 1 176 ? 31.517 18.645 39.882 1.00 10.00 ? 258 TYR A CE1 1 ATOM 1381 C CE2 . TYR A 1 176 ? 29.338 19.411 39.240 1.00 11.13 ? 258 TYR A CE2 1 ATOM 1382 C CZ . TYR A 1 176 ? 30.613 19.671 39.705 1.00 11.04 ? 258 TYR A CZ 1 ATOM 1383 O OH . TYR A 1 176 ? 30.995 20.962 40.010 1.00 11.37 ? 258 TYR A OH 1 ATOM 1384 N N . PHE A 1 177 ? 27.272 13.112 39.905 1.00 8.41 ? 259 PHE A N 1 ATOM 1385 C CA . PHE A 1 177 ? 26.791 11.754 39.666 1.00 8.56 ? 259 PHE A CA 1 ATOM 1386 C C . PHE A 1 177 ? 25.838 11.695 38.482 1.00 8.80 ? 259 PHE A C 1 ATOM 1387 O O . PHE A 1 177 ? 25.105 12.649 38.216 1.00 11.32 ? 259 PHE A O 1 ATOM 1388 C CB . PHE A 1 177 ? 26.056 11.211 40.901 1.00 7.13 ? 259 PHE A CB 1 ATOM 1389 C CG . PHE A 1 177 ? 26.899 11.151 42.147 1.00 6.53 ? 259 PHE A CG 1 ATOM 1390 C CD1 . PHE A 1 177 ? 27.741 10.070 42.386 1.00 7.56 ? 259 PHE A CD1 1 ATOM 1391 C CD2 . PHE A 1 177 ? 26.821 12.160 43.098 1.00 7.46 ? 259 PHE A CD2 1 ATOM 1392 C CE1 . PHE A 1 177 ? 28.510 10.008 43.542 1.00 7.90 ? 259 PHE A CE1 1 ATOM 1393 C CE2 . PHE A 1 177 ? 27.578 12.105 44.254 1.00 8.03 ? 259 PHE A CE2 1 ATOM 1394 C CZ . PHE A 1 177 ? 28.424 11.031 44.482 1.00 6.37 ? 259 PHE A CZ 1 ATOM 1395 N N . LYS A 1 178 ? 25.840 10.570 37.774 1.00 7.89 ? 260 LYS A N 1 ATOM 1396 C CA . LYS A 1 178 ? 24.784 10.290 36.805 1.00 7.72 ? 260 LYS A CA 1 ATOM 1397 C C . LYS A 1 178 ? 24.427 8.816 36.872 1.00 11.83 ? 260 LYS A C 1 ATOM 1398 O O . LYS A 1 178 ? 25.295 7.951 36.699 1.00 11.55 ? 260 LYS A O 1 ATOM 1399 C CB . LYS A 1 178 ? 25.201 10.675 35.383 1.00 10.37 ? 260 LYS A CB 1 ATOM 1400 C CG . LYS A 1 178 ? 24.094 10.471 34.361 1.00 9.41 ? 260 LYS A CG 1 ATOM 1401 C CD . LYS A 1 178 ? 24.490 11.040 33.009 1.00 14.04 ? 260 LYS A CD 1 ATOM 1402 C CE . LYS A 1 178 ? 23.411 10.789 31.972 1.00 23.39 ? 260 LYS A CE 1 ATOM 1403 N NZ . LYS A 1 178 ? 23.890 11.107 30.599 1.00 33.69 ? 260 LYS A NZ 1 ATOM 1404 N N . GLU A 1 179 ? 23.151 8.541 37.136 1.00 9.55 ? 261 GLU A N 1 ATOM 1405 C CA . GLU A 1 179 ? 22.669 7.179 37.364 1.00 9.11 ? 261 GLU A CA 1 ATOM 1406 C C . GLU A 1 179 ? 23.472 6.489 38.462 1.00 12.40 ? 261 GLU A C 1 ATOM 1407 O O . GLU A 1 179 ? 23.709 5.279 38.412 1.00 10.31 ? 261 GLU A O 1 ATOM 1408 C CB . GLU A 1 179 ? 22.667 6.372 36.061 1.00 11.45 ? 261 GLU A CB 1 ATOM 1409 C CG . GLU A 1 179 ? 21.683 6.927 35.037 1.00 9.85 ? 261 GLU A CG 1 ATOM 1410 C CD . GLU A 1 179 ? 21.720 6.190 33.716 1.00 21.84 ? 261 GLU A CD 1 ATOM 1411 O OE1 . GLU A 1 179 ? 22.733 5.517 33.435 1.00 30.12 ? 261 GLU A OE1 1 ATOM 1412 O OE2 . GLU A 1 179 ? 20.733 6.290 32.960 1.00 30.56 ? 261 GLU A OE2 1 ATOM 1413 N N . GLY A 1 180 ? 23.894 7.278 39.450 1.00 10.15 ? 262 GLY A N 1 ATOM 1414 C CA . GLY A 1 180 ? 24.603 6.759 40.607 1.00 11.41 ? 262 GLY A CA 1 ATOM 1415 C C . GLY A 1 180 ? 26.104 6.635 40.417 1.00 14.27 ? 262 GLY A C 1 ATOM 1416 O O . GLY A 1 180 ? 26.839 6.392 41.373 1.00 11.63 ? 262 GLY A O 1 ATOM 1417 N N . LYS A 1 181 ? 26.561 6.802 39.180 1.00 8.41 ? 263 LYS A N 1 ATOM 1418 C CA . LYS A 1 181 ? 27.984 6.689 38.877 1.00 11.06 ? 263 LYS A CA 1 ATOM 1419 C C . LYS A 1 181 ? 28.697 8.027 39.001 1.00 12.62 ? 263 LYS A C 1 ATOM 1420 O O . LYS A 1 181 ? 28.124 9.075 38.708 1.00 13.30 ? 263 LYS A O 1 ATOM 1421 C CB . LYS A 1 181 ? 28.191 6.150 37.464 1.00 14.97 ? 263 LYS A CB 1 ATOM 1422 C CG . LYS A 1 181 ? 27.721 4.723 37.257 1.00 26.77 ? 263 LYS A CG 1 ATOM 1423 C CD . LYS A 1 181 ? 28.074 4.264 35.851 1.00 32.43 ? 263 LYS A CD 1 ATOM 1424 C CE . LYS A 1 181 ? 27.501 2.895 35.542 1.00 47.94 ? 263 LYS A CE 1 ATOM 1425 N NZ . LYS A 1 181 ? 27.762 2.518 34.123 1.00 51.75 ? 263 LYS A NZ 1 ATOM 1426 N N . ILE A 1 182 ? 29.956 7.978 39.419 1.00 10.39 ? 264 ILE A N 1 ATOM 1427 C CA . ILE A 1 182 ? 30.771 9.180 39.560 1.00 8.57 ? 264 ILE A CA 1 ATOM 1428 C C . ILE A 1 182 ? 31.322 9.621 38.205 1.00 14.03 ? 264 ILE A C 1 ATOM 1429 O O . ILE A 1 182 ? 32.142 8.924 37.603 1.00 11.43 ? 264 ILE A O 1 ATOM 1430 C CB . ILE A 1 182 ? 31.943 8.931 40.530 1.00 10.33 ? 264 ILE A CB 1 ATOM 1431 C CG1 . ILE A 1 182 ? 31.415 8.468 41.891 1.00 14.93 ? 264 ILE A CG1 1 ATOM 1432 C CG2 . ILE A 1 182 ? 32.815 10.178 40.671 1.00 11.57 ? 264 ILE A CG2 1 ATOM 1433 C CD1 . ILE A 1 182 ? 32.491 7.908 42.804 1.00 18.60 ? 264 ILE A CD1 1 ATOM 1434 N N . LEU A 1 183 ? 30.861 10.773 37.724 1.00 9.75 ? 265 LEU A N 1 ATOM 1435 C CA . LEU A 1 183 ? 31.387 11.346 36.491 1.00 11.91 ? 265 LEU A CA 1 ATOM 1436 C C . LEU A 1 183 ? 32.681 12.081 36.777 1.00 13.53 ? 265 LEU A C 1 ATOM 1437 O O . LEU A 1 183 ? 33.628 12.027 35.992 1.00 13.12 ? 265 LEU A O 1 ATOM 1438 C CB . LEU A 1 183 ? 30.385 12.326 35.878 1.00 11.49 ? 265 LEU A CB 1 ATOM 1439 C CG . LEU A 1 183 ? 29.031 11.755 35.473 1.00 12.89 ? 265 LEU A CG 1 ATOM 1440 C CD1 . LEU A 1 183 ? 28.156 12.813 34.811 1.00 13.32 ? 265 LEU A CD1 1 ATOM 1441 C CD2 . LEU A 1 183 ? 29.239 10.566 34.558 1.00 18.04 ? 265 LEU A CD2 1 ATOM 1442 N N . LYS A 1 184 ? 32.711 12.768 37.915 1.00 9.52 ? 266 LYS A N 1 ATOM 1443 C CA . LYS A 1 184 ? 33.774 13.711 38.224 1.00 12.00 ? 266 LYS A CA 1 ATOM 1444 C C . LYS A 1 184 ? 33.625 14.158 39.675 1.00 11.89 ? 266 LYS A C 1 ATOM 1445 O O . LYS A 1 184 ? 32.516 14.163 40.213 1.00 10.63 ? 266 LYS A O 1 ATOM 1446 C CB . LYS A 1 184 ? 33.644 14.920 37.290 1.00 15.14 ? 266 LYS A CB 1 ATOM 1447 C CG . LYS A 1 184 ? 34.560 16.102 37.589 1.00 15.72 ? 266 LYS A CG 1 ATOM 1448 C CD . LYS A 1 184 ? 34.274 17.250 36.620 1.00 15.85 ? 266 LYS A CD 1 ATOM 1449 C CE . LYS A 1 184 ? 35.187 18.439 36.870 1.00 18.67 ? 266 LYS A CE 1 ATOM 1450 N NZ . LYS A 1 184 ? 34.909 19.556 35.916 1.00 20.04 ? 266 LYS A NZ 1 ATOM 1451 N N . TRP A 1 185 ? 34.739 14.494 40.314 1.00 11.25 ? 267 TRP A N 1 ATOM 1452 C CA . TRP A 1 185 ? 34.694 15.273 41.547 1.00 11.32 ? 267 TRP A CA 1 ATOM 1453 C C . TRP A 1 185 ? 35.765 16.342 41.507 1.00 11.97 ? 267 TRP A C 1 ATOM 1454 O O . TRP A 1 185 ? 36.755 16.217 40.781 1.00 13.47 ? 267 TRP A O 1 ATOM 1455 C CB . TRP A 1 185 ? 34.833 14.405 42.807 1.00 9.23 ? 267 TRP A CB 1 ATOM 1456 C CG . TRP A 1 185 ? 36.151 13.710 42.987 1.00 10.12 ? 267 TRP A CG 1 ATOM 1457 C CD1 . TRP A 1 185 ? 36.453 12.424 42.633 1.00 13.22 ? 267 TRP A CD1 1 ATOM 1458 C CD2 . TRP A 1 185 ? 37.336 14.245 43.595 1.00 9.32 ? 267 TRP A CD2 1 ATOM 1459 N NE1 . TRP A 1 185 ? 37.754 12.133 42.969 1.00 12.69 ? 267 TRP A NE1 1 ATOM 1460 C CE2 . TRP A 1 185 ? 38.316 13.233 43.564 1.00 11.99 ? 267 TRP A CE2 1 ATOM 1461 C CE3 . TRP A 1 185 ? 37.662 15.483 44.164 1.00 9.71 ? 267 TRP A CE3 1 ATOM 1462 C CZ2 . TRP A 1 185 ? 39.602 13.420 44.079 1.00 10.48 ? 267 TRP A CZ2 1 ATOM 1463 C CZ3 . TRP A 1 185 ? 38.941 15.668 44.668 1.00 12.93 ? 267 TRP A CZ3 1 ATOM 1464 C CH2 . TRP A 1 185 ? 39.894 14.641 44.622 1.00 13.33 ? 267 TRP A CH2 1 ATOM 1465 N N . GLU A 1 186 ? 35.550 17.409 42.264 1.00 9.26 ? 268 GLU A N 1 ATOM 1466 C CA . GLU A 1 186 ? 36.403 18.566 42.403 1.00 11.66 ? 268 GLU A CA 1 ATOM 1467 C C . GLU A 1 186 ? 36.639 18.945 43.856 1.00 12.63 ? 268 GLU A C 1 ATOM 1468 O O . GLU A 1 186 ? 35.732 18.952 44.605 1.00 12.10 ? 268 GLU A O 1 ATOM 1469 C CB . GLU A 1 186 ? 35.741 19.828 41.851 1.00 24.28 ? 268 GLU A CB 1 ATOM 1470 C CG . GLU A 1 186 ? 35.286 19.784 40.466 1.00 25.63 ? 268 GLU A CG 1 ATOM 1471 C CD . GLU A 1 186 ? 34.704 21.126 40.069 1.00 18.99 ? 268 GLU A CD 1 ATOM 1472 O OE1 . GLU A 1 186 ? 33.594 21.413 40.389 1.00 14.92 ? 268 GLU A OE1 1 ATOM 1473 O OE2 . GLU A 1 186 ? 35.433 21.815 39.420 1.00 27.67 ? 268 GLU A OE2 1 ATOM 1474 N N A SER A 1 187 ? 37.803 19.476 44.167 0.37 10.18 ? 269 SER A N 1 ATOM 1475 N N B SER A 1 187 ? 37.807 19.492 44.149 0.63 10.12 ? 269 SER A N 1 ATOM 1476 C CA A SER A 1 187 ? 37.964 20.082 45.479 0.37 11.68 ? 269 SER A CA 1 ATOM 1477 C CA B SER A 1 187 ? 38.000 20.126 45.447 0.63 11.71 ? 269 SER A CA 1 ATOM 1478 C C A SER A 1 187 ? 37.341 21.470 45.469 0.37 11.38 ? 269 SER A C 1 ATOM 1479 C C B SER A 1 187 ? 37.320 21.483 45.454 0.63 11.36 ? 269 SER A C 1 ATOM 1480 O O A SER A 1 187 ? 37.296 22.129 44.428 0.37 10.84 ? 269 SER A O 1 ATOM 1481 O O B SER A 1 187 ? 37.224 22.138 44.415 0.63 10.81 ? 269 SER A O 1 ATOM 1482 C CB A SER A 1 187 ? 39.441 20.170 45.850 0.37 14.15 ? 269 SER A CB 1 ATOM 1483 C CB B SER A 1 187 ? 39.489 20.300 45.750 0.63 14.13 ? 269 SER A CB 1 ATOM 1484 O OG A SER A 1 187 ? 40.181 20.777 44.809 0.37 13.98 ? 269 SER A OG 1 ATOM 1485 O OG B SER A 1 187 ? 40.122 19.052 45.957 0.63 15.03 ? 269 SER A OG 1 ATOM 1486 N N . LEU A 1 188 ? 36.849 21.900 46.627 1.00 12.32 ? 270 LEU A N 1 ATOM 1487 C CA . LEU A 1 188 ? 36.229 23.213 46.774 1.00 12.72 ? 270 LEU A CA 1 ATOM 1488 C C . LEU A 1 188 ? 37.173 24.319 46.318 1.00 11.31 ? 270 LEU A C 1 ATOM 1489 O O . LEU A 1 188 ? 38.356 24.321 46.664 1.00 11.72 ? 270 LEU A O 1 ATOM 1490 C CB . LEU A 1 188 ? 35.838 23.454 48.236 1.00 9.12 ? 270 LEU A CB 1 ATOM 1491 C CG . LEU A 1 188 ? 35.294 24.843 48.597 1.00 10.43 ? 270 LEU A CG 1 ATOM 1492 C CD1 . LEU A 1 188 ? 33.937 25.073 47.973 1.00 8.01 ? 270 LEU A CD1 1 ATOM 1493 C CD2 . LEU A 1 188 ? 35.218 25.007 50.103 1.00 10.93 ? 270 LEU A CD2 1 ATOM 1494 N N . THR A 1 189 ? 36.648 25.246 45.526 1.00 9.26 ? 271 THR A N 1 ATOM 1495 C CA . THR A 1 189 ? 37.402 26.441 45.154 1.00 11.68 ? 271 THR A CA 1 ATOM 1496 C C . THR A 1 189 ? 36.591 27.668 45.551 1.00 16.21 ? 271 THR A C 1 ATOM 1497 O O . THR A 1 189 ? 35.449 27.544 46.003 1.00 12.79 ? 271 THR A O 1 ATOM 1498 C CB . THR A 1 189 ? 37.728 26.471 43.642 1.00 10.89 ? 271 THR A CB 1 ATOM 1499 O OG1 . THR A 1 189 ? 38.635 27.547 43.364 1.00 24.31 ? 271 THR A OG1 1 ATOM 1500 C CG2 . THR A 1 189 ? 36.468 26.674 42.828 1.00 10.21 ? 271 THR A CG2 1 ATOM 1501 N N . GLY A 1 190 ? 37.175 28.851 45.404 1.00 14.83 ? 272 GLY A N 1 ATOM 1502 C CA . GLY A 1 190 ? 36.466 30.068 45.751 1.00 14.11 ? 272 GLY A CA 1 ATOM 1503 C C . GLY A 1 190 ? 36.823 30.570 47.134 1.00 11.19 ? 272 GLY A C 1 ATOM 1504 O O . GLY A 1 190 ? 37.829 30.154 47.716 1.00 12.95 ? 272 GLY A O 1 ATOM 1505 N N . THR A 1 191 ? 35.989 31.456 47.675 1.00 8.58 ? 273 THR A N 1 ATOM 1506 C CA . THR A 1 191 ? 36.335 32.155 48.909 1.00 10.50 ? 273 THR A CA 1 ATOM 1507 C C . THR A 1 191 ? 35.633 31.642 50.168 1.00 9.08 ? 273 THR A C 1 ATOM 1508 O O . THR A 1 191 ? 35.934 32.097 51.272 1.00 8.45 ? 273 THR A O 1 ATOM 1509 C CB . THR A 1 191 ? 36.131 33.674 48.767 1.00 10.57 ? 273 THR A CB 1 ATOM 1510 O OG1 . THR A 1 191 ? 34.768 33.951 48.429 1.00 9.82 ? 273 THR A OG1 1 ATOM 1511 C CG2 . THR A 1 191 ? 37.030 34.213 47.665 1.00 12.55 ? 273 THR A CG2 1 ATOM 1512 N N . ALA A 1 192 ? 34.711 30.696 50.019 1.00 8.70 ? 274 ALA A N 1 ATOM 1513 C CA . ALA A 1 192 ? 34.151 30.044 51.202 1.00 9.40 ? 274 ALA A CA 1 ATOM 1514 C C . ALA A 1 192 ? 35.275 29.319 51.952 1.00 11.06 ? 274 ALA A C 1 ATOM 1515 O O . ALA A 1 192 ? 36.067 28.595 51.341 1.00 11.05 ? 274 ALA A O 1 ATOM 1516 C CB . ALA A 1 192 ? 33.030 29.077 50.811 1.00 7.92 ? 274 ALA A CB 1 ATOM 1517 N N . LYS A 1 193 ? 35.358 29.532 53.266 1.00 7.28 ? 275 LYS A N 1 ATOM 1518 C CA . LYS A 1 193 ? 36.476 29.011 54.061 1.00 10.77 ? 275 LYS A CA 1 ATOM 1519 C C . LYS A 1 193 ? 36.143 27.736 54.841 1.00 14.18 ? 275 LYS A C 1 ATOM 1520 O O . LYS A 1 193 ? 37.040 27.052 55.345 1.00 10.07 ? 275 LYS A O 1 ATOM 1521 C CB . LYS A 1 193 ? 37.010 30.081 55.018 1.00 10.16 ? 275 LYS A CB 1 ATOM 1522 C CG . LYS A 1 193 ? 37.509 31.354 54.325 1.00 10.36 ? 275 LYS A CG 1 ATOM 1523 C CD . LYS A 1 193 ? 38.542 31.032 53.244 1.00 10.27 ? 275 LYS A CD 1 ATOM 1524 C CE . LYS A 1 193 ? 39.229 32.297 52.731 1.00 11.13 ? 275 LYS A CE 1 ATOM 1525 N NZ . LYS A 1 193 ? 38.266 33.287 52.169 1.00 10.86 ? 275 LYS A NZ 1 ATOM 1526 N N . HIS A 1 194 ? 34.855 27.426 54.946 1.00 9.54 ? 276 HIS A N 1 ATOM 1527 C CA . HIS A 1 194 ? 34.417 26.179 55.576 1.00 8.93 ? 276 HIS A CA 1 ATOM 1528 C C . HIS A 1 194 ? 33.012 25.865 55.077 1.00 9.31 ? 276 HIS A C 1 ATOM 1529 O O . HIS A 1 194 ? 32.177 26.765 54.974 1.00 10.71 ? 276 HIS A O 1 ATOM 1530 C CB . HIS A 1 194 ? 34.440 26.302 57.102 1.00 9.60 ? 276 HIS A CB 1 ATOM 1531 C CG . HIS A 1 194 ? 34.361 24.985 57.816 1.00 9.33 ? 276 HIS A CG 1 ATOM 1532 N ND1 . HIS A 1 194 ? 33.205 24.529 58.413 1.00 9.97 ? 276 HIS A ND1 1 ATOM 1533 C CD2 . HIS A 1 194 ? 35.295 24.025 58.020 1.00 9.51 ? 276 HIS A CD2 1 ATOM 1534 C CE1 . HIS A 1 194 ? 33.431 23.344 58.957 1.00 11.36 ? 276 HIS A CE1 1 ATOM 1535 N NE2 . HIS A 1 194 ? 34.692 23.018 58.738 1.00 10.11 ? 276 HIS A NE2 1 ATOM 1536 N N . ILE A 1 195 ? 32.761 24.599 54.752 1.00 8.53 ? 277 ILE A N 1 ATOM 1537 C CA . ILE A 1 195 ? 31.492 24.186 54.155 1.00 6.95 ? 277 ILE A CA 1 ATOM 1538 C C . ILE A 1 195 ? 30.909 22.954 54.850 1.00 9.87 ? 277 ILE A C 1 ATOM 1539 O O . ILE A 1 195 ? 31.584 21.928 54.977 1.00 8.64 ? 277 ILE A O 1 ATOM 1540 C CB . ILE A 1 195 ? 31.669 23.848 52.656 1.00 6.91 ? 277 ILE A CB 1 ATOM 1541 C CG1 . ILE A 1 195 ? 32.039 25.096 51.856 1.00 10.59 ? 277 ILE A CG1 1 ATOM 1542 C CG2 . ILE A 1 195 ? 30.402 23.190 52.093 1.00 7.33 ? 277 ILE A CG2 1 ATOM 1543 C CD1 . ILE A 1 195 ? 30.875 26.034 51.622 1.00 11.00 ? 277 ILE A CD1 1 ATOM 1544 N N . GLU A 1 196 ? 29.658 23.066 55.300 1.00 6.73 ? 278 GLU A N 1 ATOM 1545 C CA . GLU A 1 196 ? 28.890 21.918 55.779 1.00 8.12 ? 278 GLU A CA 1 ATOM 1546 C C . GLU A 1 196 ? 27.418 22.044 55.381 1.00 6.65 ? 278 GLU A C 1 ATOM 1547 O O . GLU A 1 196 ? 26.911 23.156 55.199 1.00 9.82 ? 278 GLU A O 1 ATOM 1548 C CB . GLU A 1 196 ? 28.983 21.786 57.306 1.00 7.46 ? 278 GLU A CB 1 ATOM 1549 C CG . GLU A 1 196 ? 30.345 21.358 57.845 1.00 8.34 ? 278 GLU A CG 1 ATOM 1550 C CD . GLU A 1 196 ? 30.305 21.009 59.317 1.00 14.08 ? 278 GLU A CD 1 ATOM 1551 O OE1 . GLU A 1 196 ? 31.343 20.571 59.859 1.00 12.47 ? 278 GLU A OE1 1 ATOM 1552 O OE2 . GLU A 1 196 ? 29.232 21.161 59.934 1.00 22.14 ? 278 GLU A OE2 1 ATOM 1553 N N . GLU A 1 197 ? 26.751 20.899 55.234 1.00 5.51 ? 279 GLU A N 1 ATOM 1554 C CA . GLU A 1 197 ? 25.282 20.835 55.179 1.00 5.69 ? 279 GLU A CA 1 ATOM 1555 C C . GLU A 1 197 ? 24.631 21.784 54.172 1.00 5.07 ? 279 GLU A C 1 ATOM 1556 O O . GLU A 1 197 ? 23.740 22.568 54.521 1.00 5.69 ? 279 GLU A O 1 ATOM 1557 C CB . GLU A 1 197 ? 24.695 21.053 56.584 1.00 6.98 ? 279 GLU A CB 1 ATOM 1558 C CG . GLU A 1 197 ? 25.128 19.976 57.591 1.00 8.29 ? 279 GLU A CG 1 ATOM 1559 C CD . GLU A 1 197 ? 24.675 20.247 59.019 1.00 10.99 ? 279 GLU A CD 1 ATOM 1560 O OE1 . GLU A 1 197 ? 24.360 21.411 59.347 1.00 9.38 ? 279 GLU A OE1 1 ATOM 1561 O OE2 . GLU A 1 197 ? 24.641 19.290 59.823 1.00 10.01 ? 279 GLU A OE2 1 ATOM 1562 N N . CYS A 1 198 ? 25.070 21.702 52.920 1.00 5.83 ? 280 CYS A N 1 ATOM 1563 C CA . CYS A 1 198 ? 24.545 22.569 51.872 1.00 6.78 ? 280 CYS A CA 1 ATOM 1564 C C . CYS A 1 198 ? 23.076 22.310 51.561 1.00 7.98 ? 280 CYS A C 1 ATOM 1565 O O . CYS A 1 198 ? 22.648 21.159 51.449 1.00 5.43 ? 280 CYS A O 1 ATOM 1566 C CB . CYS A 1 198 ? 25.372 22.417 50.597 1.00 6.59 ? 280 CYS A CB 1 ATOM 1567 S SG . CYS A 1 198 ? 27.049 23.060 50.770 1.00 11.32 ? 280 CYS A SG 1 ATOM 1568 N N . SER A 1 199 ? 22.314 23.395 51.439 1.00 7.05 ? 281 SER A N 1 ATOM 1569 C CA . SER A 1 199 ? 20.931 23.344 50.977 1.00 9.03 ? 281 SER A CA 1 ATOM 1570 C C . SER A 1 199 ? 20.876 23.900 49.562 1.00 9.33 ? 281 SER A C 1 ATOM 1571 O O . SER A 1 199 ? 21.226 25.061 49.333 1.00 8.67 ? 281 SER A O 1 ATOM 1572 C CB . SER A 1 199 ? 20.030 24.183 51.880 1.00 7.29 ? 281 SER A CB 1 ATOM 1573 O OG . SER A 1 199 ? 20.118 23.756 53.222 1.00 7.41 ? 281 SER A OG 1 ATOM 1574 N N . CYS A 1 200 ? 20.417 23.087 48.615 1.00 6.67 ? 282 CYS A N 1 ATOM 1575 C CA . CYS A 1 200 ? 20.525 23.449 47.208 1.00 7.39 ? 282 CYS A CA 1 ATOM 1576 C C . CYS A 1 200 ? 19.178 23.534 46.493 1.00 8.53 ? 282 CYS A C 1 ATOM 1577 O O . CYS A 1 200 ? 18.185 22.934 46.915 1.00 7.48 ? 282 CYS A O 1 ATOM 1578 C CB . CYS A 1 200 ? 21.430 22.454 46.483 1.00 8.52 ? 282 CYS A CB 1 ATOM 1579 S SG . CYS A 1 200 ? 23.030 22.191 47.283 1.00 9.73 ? 282 CYS A SG 1 ATOM 1580 N N . TYR A 1 201 ? 19.151 24.300 45.410 1.00 5.88 ? 283 TYR A N 1 ATOM 1581 C CA . TYR A 1 201 ? 17.995 24.337 44.525 1.00 7.46 ? 283 TYR A CA 1 ATOM 1582 C C . TYR A 1 201 ? 18.507 24.657 43.126 1.00 8.78 ? 283 TYR A C 1 ATOM 1583 O O . TYR A 1 201 ? 19.615 25.176 42.972 1.00 9.22 ? 283 TYR A O 1 ATOM 1584 C CB . TYR A 1 201 ? 16.974 25.379 44.993 1.00 7.74 ? 283 TYR A CB 1 ATOM 1585 C CG . TYR A 1 201 ? 17.457 26.803 44.850 1.00 8.51 ? 283 TYR A CG 1 ATOM 1586 C CD1 . TYR A 1 201 ? 18.154 27.428 45.878 1.00 7.98 ? 283 TYR A CD1 1 ATOM 1587 C CD2 . TYR A 1 201 ? 17.216 27.524 43.681 1.00 10.84 ? 283 TYR A CD2 1 ATOM 1588 C CE1 . TYR A 1 201 ? 18.604 28.732 45.745 1.00 6.30 ? 283 TYR A CE1 1 ATOM 1589 C CE2 . TYR A 1 201 ? 17.664 28.821 43.540 1.00 8.81 ? 283 TYR A CE2 1 ATOM 1590 C CZ . TYR A 1 201 ? 18.351 29.418 44.572 1.00 10.45 ? 283 TYR A CZ 1 ATOM 1591 O OH . TYR A 1 201 ? 18.790 30.716 44.421 1.00 10.70 ? 283 TYR A OH 1 ATOM 1592 N N . GLY A 1 202 ? 17.711 24.342 42.112 1.00 8.42 ? 284 GLY A N 1 ATOM 1593 C CA . GLY A 1 202 ? 18.131 24.580 40.744 1.00 10.27 ? 284 GLY A CA 1 ATOM 1594 C C . GLY A 1 202 ? 17.157 25.443 39.973 1.00 9.13 ? 284 GLY A C 1 ATOM 1595 O O . GLY A 1 202 ? 15.954 25.425 40.220 1.00 8.72 ? 284 GLY A O 1 ATOM 1596 N N . GLU A 1 203 ? 17.691 26.213 39.035 1.00 10.49 ? 285 GLU A N 1 ATOM 1597 C CA . GLU A 1 203 ? 16.869 26.994 38.127 1.00 9.87 ? 285 GLU A CA 1 ATOM 1598 C C . GLU A 1 203 ? 17.750 27.307 36.924 1.00 14.88 ? 285 GLU A C 1 ATOM 1599 O O . GLU A 1 203 ? 18.948 27.040 36.964 1.00 19.51 ? 285 GLU A O 1 ATOM 1600 C CB . GLU A 1 203 ? 16.341 28.265 38.809 1.00 9.55 ? 285 GLU A CB 1 ATOM 1601 C CG . GLU A 1 203 ? 17.420 29.186 39.381 1.00 14.90 ? 285 GLU A CG 1 ATOM 1602 C CD . GLU A 1 203 ? 17.361 30.581 38.787 1.00 21.84 ? 285 GLU A CD 1 ATOM 1603 O OE1 . GLU A 1 203 ? 17.194 30.694 37.556 1.00 21.94 ? 285 GLU A OE1 1 ATOM 1604 O OE2 . GLU A 1 203 ? 17.467 31.562 39.551 1.00 35.41 ? 285 GLU A OE2 1 ATOM 1605 N N . ARG A 1 204 ? 17.162 27.839 35.856 1.00 10.68 ? 286 ARG A N 1 ATOM 1606 C CA . ARG A 1 204 ? 17.893 28.061 34.601 1.00 12.20 ? 286 ARG A CA 1 ATOM 1607 C C . ARG A 1 204 ? 19.316 28.626 34.750 1.00 18.78 ? 286 ARG A C 1 ATOM 1608 O O . ARG A 1 204 ? 20.189 28.339 33.932 1.00 14.60 ? 286 ARG A O 1 ATOM 1609 C CB . ARG A 1 204 ? 17.066 28.930 33.649 1.00 25.71 ? 286 ARG A CB 1 ATOM 1610 C CG . ARG A 1 204 ? 16.631 30.254 34.240 1.00 14.93 ? 286 ARG A CG 1 ATOM 1611 C CD . ARG A 1 204 ? 15.696 30.987 33.296 1.00 28.89 ? 286 ARG A CD 1 ATOM 1612 N NE . ARG A 1 204 ? 15.065 32.136 33.938 1.00 20.83 ? 286 ARG A NE 1 ATOM 1613 C CZ . ARG A 1 204 ? 13.931 32.688 33.521 1.00 24.50 ? 286 ARG A CZ 1 ATOM 1614 N NH1 . ARG A 1 204 ? 13.306 32.190 32.462 1.00 22.40 ? 286 ARG A NH1 1 ATOM 1615 N NH2 . ARG A 1 204 ? 13.419 33.729 34.163 1.00 25.61 ? 286 ARG A NH2 1 ATOM 1616 N N . THR A 1 205 ? 19.555 29.407 35.802 1.00 32.23 ? 287 THR A N 1 ATOM 1617 C CA . THR A 1 205 ? 20.883 29.979 36.033 1.00 28.38 ? 287 THR A CA 1 ATOM 1618 C C . THR A 1 205 ? 21.903 28.934 36.496 1.00 38.20 ? 287 THR A C 1 ATOM 1619 O O . THR A 1 205 ? 23.111 29.177 36.437 1.00 37.05 ? 287 THR A O 1 ATOM 1620 C CB . THR A 1 205 ? 20.859 31.121 37.069 1.00 39.85 ? 287 THR A CB 1 ATOM 1621 O OG1 . THR A 1 205 ? 20.552 30.592 38.365 1.00 42.26 ? 287 THR A OG1 1 ATOM 1622 C CG2 . THR A 1 205 ? 19.833 32.186 36.694 1.00 33.01 ? 287 THR A CG2 1 ATOM 1623 N N . GLY A 1 206 ? 21.419 27.782 36.959 1.00 23.83 ? 288 GLY A N 1 ATOM 1624 C CA . GLY A 1 206 ? 22.293 26.728 37.455 1.00 15.58 ? 288 GLY A CA 1 ATOM 1625 C C . GLY A 1 206 ? 21.808 26.170 38.778 1.00 16.91 ? 288 GLY A C 1 ATOM 1626 O O . GLY A 1 206 ? 20.617 26.224 39.076 1.00 16.42 ? 288 GLY A O 1 ATOM 1627 N N . ILE A 1 207 ? 22.724 25.630 39.573 1.00 10.86 ? 289 ILE A N 1 ATOM 1628 C CA . ILE A 1 207 ? 22.368 25.121 40.895 1.00 8.36 ? 289 ILE A CA 1 ATOM 1629 C C . ILE A 1 207 ? 23.009 26.004 41.959 1.00 11.14 ? 289 ILE A C 1 ATOM 1630 O O . ILE A 1 207 ? 24.199 26.316 41.881 1.00 11.84 ? 289 ILE A O 1 ATOM 1631 C CB . ILE A 1 207 ? 22.796 23.643 41.064 1.00 8.20 ? 289 ILE A CB 1 ATOM 1632 C CG1 . ILE A 1 207 ? 21.928 22.745 40.178 1.00 9.25 ? 289 ILE A CG1 1 ATOM 1633 C CG2 . ILE A 1 207 ? 22.679 23.206 42.527 1.00 8.67 ? 289 ILE A CG2 1 ATOM 1634 C CD1 . ILE A 1 207 ? 22.484 21.341 39.970 1.00 10.52 ? 289 ILE A CD1 1 ATOM 1635 N N . THR A 1 208 ? 22.207 26.434 42.931 1.00 7.94 ? 290 THR A N 1 ATOM 1636 C CA . THR A 1 208 ? 22.682 27.314 43.992 1.00 5.98 ? 290 THR A CA 1 ATOM 1637 C C . THR A 1 208 ? 22.587 26.594 45.334 1.00 9.90 ? 290 THR A C 1 ATOM 1638 O O . THR A 1 208 ? 21.528 26.069 45.678 1.00 9.10 ? 290 THR A O 1 ATOM 1639 C CB . THR A 1 208 ? 21.851 28.621 44.051 1.00 9.34 ? 290 THR A CB 1 ATOM 1640 O OG1 . THR A 1 208 ? 21.992 29.342 42.818 1.00 11.93 ? 290 THR A OG1 1 ATOM 1641 C CG2 . THR A 1 208 ? 22.319 29.499 45.192 1.00 9.98 ? 290 THR A CG2 1 ATOM 1642 N N . CYS A 1 209 ? 23.688 26.553 46.082 1.00 10.07 ? 291 CYS A N 1 ATOM 1643 C CA . CYS A 1 209 ? 23.687 25.918 47.399 1.00 9.54 ? 291 CYS A CA 1 ATOM 1644 C C . CYS A 1 209 ? 24.048 26.918 48.483 1.00 10.48 ? 291 CYS A C 1 ATOM 1645 O O . CYS A 1 209 ? 25.057 27.617 48.381 1.00 12.93 ? 291 CYS A O 1 ATOM 1646 C CB . CYS A 1 209 ? 24.671 24.748 47.454 1.00 7.38 ? 291 CYS A CB 1 ATOM 1647 S SG . CYS A 1 209 ? 24.325 23.427 46.290 1.00 10.15 ? 291 CYS A SG 1 ATOM 1648 N N . THR A 1 210 ? 23.219 26.983 49.520 1.00 6.93 ? 292 THR A N 1 ATOM 1649 C CA . THR A 1 210 ? 23.514 27.814 50.681 1.00 7.96 ? 292 THR A CA 1 ATOM 1650 C C . THR A 1 210 ? 23.915 26.879 51.804 1.00 8.42 ? 292 THR A C 1 ATOM 1651 O O . THR A 1 210 ? 23.153 25.984 52.173 1.00 7.16 ? 292 THR A O 1 ATOM 1652 C CB . THR A 1 210 ? 22.290 28.633 51.105 1.00 7.13 ? 292 THR A CB 1 ATOM 1653 O OG1 . THR A 1 210 ? 21.820 29.393 49.984 1.00 10.71 ? 292 THR A OG1 1 ATOM 1654 C CG2 . THR A 1 210 ? 22.642 29.574 52.252 1.00 8.28 ? 292 THR A CG2 1 ATOM 1655 N N . CYS A 1 211 ? 25.114 27.069 52.340 1.00 7.60 ? 293 CYS A N 1 ATOM 1656 C CA . CYS A 1 211 ? 25.665 26.102 53.279 1.00 8.64 ? 293 CYS A CA 1 ATOM 1657 C C . CYS A 1 211 ? 25.882 26.725 54.651 1.00 7.97 ? 293 CYS A C 1 ATOM 1658 O O . CYS A 1 211 ? 25.338 27.791 54.954 1.00 6.46 ? 293 CYS A O 1 ATOM 1659 C CB . CYS A 1 211 ? 26.972 25.534 52.720 1.00 8.74 ? 293 CYS A CB 1 ATOM 1660 S SG . CYS A 1 211 ? 26.834 25.089 50.968 1.00 9.73 ? 293 CYS A SG 1 ATOM 1661 N N . LYS A 1 212 ? 26.658 26.035 55.482 1.00 7.11 ? 294 LYS A N 1 ATOM 1662 C CA . LYS A 1 212 ? 27.006 26.514 56.813 1.00 7.34 ? 294 LYS A CA 1 ATOM 1663 C C . LYS A 1 212 ? 28.523 26.524 56.989 1.00 9.43 ? 294 LYS A C 1 ATOM 1664 O O . LYS A 1 212 ? 29.199 25.546 56.662 1.00 10.92 ? 294 LYS A O 1 ATOM 1665 C CB . LYS A 1 212 ? 26.374 25.614 57.885 1.00 11.90 ? 294 LYS A CB 1 ATOM 1666 C CG . LYS A 1 212 ? 26.969 25.795 59.280 1.00 14.56 ? 294 LYS A CG 1 ATOM 1667 C CD . LYS A 1 212 ? 26.438 24.782 60.289 1.00 14.47 ? 294 LYS A CD 1 ATOM 1668 C CE . LYS A 1 212 ? 27.030 23.402 60.076 1.00 14.28 ? 294 LYS A CE 1 ATOM 1669 N NZ . LYS A 1 212 ? 27.090 22.624 61.345 1.00 15.35 ? 294 LYS A NZ 1 ATOM 1670 N N . ASP A 1 213 ? 29.049 27.637 57.493 1.00 6.57 ? 295 ASP A N 1 ATOM 1671 C CA . ASP A 1 213 ? 30.439 27.715 57.936 1.00 7.10 ? 295 ASP A CA 1 ATOM 1672 C C . ASP A 1 213 ? 30.436 27.416 59.433 1.00 8.65 ? 295 ASP A C 1 ATOM 1673 O O . ASP A 1 213 ? 30.025 28.251 60.237 1.00 7.23 ? 295 ASP A O 1 ATOM 1674 C CB . ASP A 1 213 ? 30.998 29.122 57.647 1.00 7.89 ? 295 ASP A CB 1 ATOM 1675 C CG . ASP A 1 213 ? 32.461 29.293 58.064 1.00 9.88 ? 295 ASP A CG 1 ATOM 1676 O OD1 . ASP A 1 213 ? 32.904 28.659 59.044 1.00 10.86 ? 295 ASP A OD1 1 ATOM 1677 O OD2 . ASP A 1 213 ? 33.169 30.100 57.418 1.00 10.25 ? 295 ASP A OD2 1 ATOM 1678 N N . ASN A 1 214 ? 30.879 26.224 59.818 1.00 6.03 ? 296 ASN A N 1 ATOM 1679 C CA . ASN A 1 214 ? 30.863 25.856 61.230 1.00 6.98 ? 296 ASN A CA 1 ATOM 1680 C C . ASN A 1 214 ? 32.037 26.450 62.001 1.00 11.71 ? 296 ASN A C 1 ATOM 1681 O O . ASN A 1 214 ? 31.986 26.576 63.217 1.00 13.76 ? 296 ASN A O 1 ATOM 1682 C CB . ASN A 1 214 ? 30.858 24.334 61.408 1.00 7.84 ? 296 ASN A CB 1 ATOM 1683 C CG . ASN A 1 214 ? 30.363 23.915 62.779 1.00 9.99 ? 296 ASN A CG 1 ATOM 1684 O OD1 . ASN A 1 214 ? 29.172 24.025 63.070 1.00 11.02 ? 296 ASN A OD1 1 ATOM 1685 N ND2 . ASN A 1 214 ? 31.269 23.428 63.628 1.00 10.14 ? 296 ASN A ND2 1 ATOM 1686 N N . TRP A 1 215 ? 33.090 26.815 61.281 1.00 9.35 ? 297 TRP A N 1 ATOM 1687 C CA . TRP A 1 215 ? 34.356 27.193 61.902 1.00 10.30 ? 297 TRP A CA 1 ATOM 1688 C C . TRP A 1 215 ? 34.354 28.626 62.447 1.00 10.55 ? 297 TRP A C 1 ATOM 1689 O O . TRP A 1 215 ? 34.442 28.829 63.657 1.00 12.75 ? 297 TRP A O 1 ATOM 1690 C CB . TRP A 1 215 ? 35.486 26.964 60.894 1.00 11.13 ? 297 TRP A CB 1 ATOM 1691 C CG . TRP A 1 215 ? 36.861 27.421 61.312 1.00 14.98 ? 297 TRP A CG 1 ATOM 1692 C CD1 . TRP A 1 215 ? 37.322 27.644 62.580 1.00 14.20 ? 297 TRP A CD1 1 ATOM 1693 C CD2 . TRP A 1 215 ? 37.952 27.716 60.431 1.00 12.25 ? 297 TRP A CD2 1 ATOM 1694 N NE1 . TRP A 1 215 ? 38.637 28.065 62.536 1.00 13.18 ? 297 TRP A NE1 1 ATOM 1695 C CE2 . TRP A 1 215 ? 39.043 28.116 61.227 1.00 14.64 ? 297 TRP A CE2 1 ATOM 1696 C CE3 . TRP A 1 215 ? 38.109 27.680 59.041 1.00 15.76 ? 297 TRP A CE3 1 ATOM 1697 C CZ2 . TRP A 1 215 ? 40.274 28.475 60.679 1.00 13.86 ? 297 TRP A CZ2 1 ATOM 1698 C CZ3 . TRP A 1 215 ? 39.333 28.041 58.498 1.00 17.36 ? 297 TRP A CZ3 1 ATOM 1699 C CH2 . TRP A 1 215 ? 40.399 28.431 59.317 1.00 14.96 ? 297 TRP A CH2 1 ATOM 1700 N N . GLN A 1 216 ? 34.240 29.615 61.566 1.00 10.66 ? 298 GLN A N 1 ATOM 1701 C CA . GLN A 1 216 ? 34.375 31.008 61.988 1.00 13.30 ? 298 GLN A CA 1 ATOM 1702 C C . GLN A 1 216 ? 33.216 31.914 61.594 1.00 11.21 ? 298 GLN A C 1 ATOM 1703 O O . GLN A 1 216 ? 33.122 33.035 62.090 1.00 11.95 ? 298 GLN A O 1 ATOM 1704 C CB . GLN A 1 216 ? 35.645 31.622 61.395 1.00 15.32 ? 298 GLN A CB 1 ATOM 1705 C CG . GLN A 1 216 ? 36.940 30.954 61.800 1.00 15.82 ? 298 GLN A CG 1 ATOM 1706 C CD . GLN A 1 216 ? 38.114 31.464 60.986 1.00 25.14 ? 298 GLN A CD 1 ATOM 1707 O OE1 . GLN A 1 216 ? 39.043 32.061 61.525 1.00 28.58 ? 298 GLN A OE1 1 ATOM 1708 N NE2 . GLN A 1 216 ? 38.074 31.232 59.676 1.00 19.20 ? 298 GLN A NE2 1 ATOM 1709 N N . GLY A 1 217 ? 32.359 31.453 60.689 1.00 9.04 ? 299 GLY A N 1 ATOM 1710 C CA . GLY A 1 217 ? 31.406 32.343 60.047 1.00 10.04 ? 299 GLY A CA 1 ATOM 1711 C C . GLY A 1 217 ? 29.977 32.315 60.539 1.00 15.63 ? 299 GLY A C 1 ATOM 1712 O O . GLY A 1 217 ? 29.436 31.261 60.859 1.00 11.41 ? 299 GLY A O 1 ATOM 1713 N N . SER A 1 218 ? 29.356 33.488 60.581 1.00 10.47 ? 300 SER A N 1 ATOM 1714 C CA . SER A 1 218 ? 27.940 33.575 60.908 1.00 5.90 ? 300 SER A CA 1 ATOM 1715 C C . SER A 1 218 ? 27.136 34.100 59.729 1.00 11.29 ? 300 SER A C 1 ATOM 1716 O O . SER A 1 218 ? 25.902 34.138 59.772 1.00 10.09 ? 300 SER A O 1 ATOM 1717 C CB . SER A 1 218 ? 27.721 34.435 62.145 1.00 8.12 ? 300 SER A CB 1 ATOM 1718 O OG . SER A 1 218 ? 28.220 33.776 63.294 1.00 12.46 ? 300 SER A OG 1 ATOM 1719 N N . ASN A 1 219 ? 27.841 34.532 58.688 1.00 8.35 ? 301 ASN A N 1 ATOM 1720 C CA . ASN A 1 219 ? 27.236 34.629 57.372 1.00 7.24 ? 301 ASN A CA 1 ATOM 1721 C C . ASN A 1 219 ? 27.338 33.251 56.723 1.00 8.30 ? 301 ASN A C 1 ATOM 1722 O O . ASN A 1 219 ? 28.153 32.428 57.142 1.00 10.01 ? 301 ASN A O 1 ATOM 1723 C CB . ASN A 1 219 ? 27.932 35.697 56.514 1.00 8.51 ? 301 ASN A CB 1 ATOM 1724 C CG . ASN A 1 219 ? 29.450 35.537 56.479 1.00 10.30 ? 301 ASN A CG 1 ATOM 1725 O OD1 . ASN A 1 219 ? 30.035 34.810 57.286 1.00 8.23 ? 301 ASN A OD1 1 ATOM 1726 N ND2 . ASN A 1 219 ? 30.095 36.238 55.547 1.00 10.74 ? 301 ASN A ND2 1 ATOM 1727 N N . ARG A 1 220 ? 26.509 32.980 55.726 1.00 6.21 ? 302 ARG A N 1 ATOM 1728 C CA . ARG A 1 220 ? 26.496 31.647 55.123 1.00 6.85 ? 302 ARG A CA 1 ATOM 1729 C C . ARG A 1 220 ? 27.307 31.579 53.849 1.00 9.57 ? 302 ARG A C 1 ATOM 1730 O O . ARG A 1 220 ? 27.182 32.441 52.980 1.00 9.22 ? 302 ARG A O 1 ATOM 1731 C CB . ARG A 1 220 ? 25.061 31.197 54.845 1.00 3.96 ? 302 ARG A CB 1 ATOM 1732 C CG . ARG A 1 220 ? 24.276 30.923 56.108 1.00 7.23 ? 302 ARG A CG 1 ATOM 1733 C CD . ARG A 1 220 ? 22.963 30.196 55.824 1.00 7.49 ? 302 ARG A CD 1 ATOM 1734 N NE . ARG A 1 220 ? 22.289 29.889 57.080 1.00 7.50 ? 302 ARG A NE 1 ATOM 1735 C CZ . ARG A 1 220 ? 22.586 28.842 57.843 1.00 6.06 ? 302 ARG A CZ 1 ATOM 1736 N NH1 . ARG A 1 220 ? 23.539 27.989 57.468 1.00 5.10 ? 302 ARG A NH1 1 ATOM 1737 N NH2 . ARG A 1 220 ? 21.933 28.647 58.981 1.00 4.82 ? 302 ARG A NH2 1 ATOM 1738 N N . PRO A 1 221 ? 28.148 30.544 53.728 1.00 7.27 ? 303 PRO A N 1 ATOM 1739 C CA . PRO A 1 221 ? 28.842 30.360 52.455 1.00 7.84 ? 303 PRO A CA 1 ATOM 1740 C C . PRO A 1 221 ? 27.866 29.894 51.377 1.00 9.28 ? 303 PRO A C 1 ATOM 1741 O O . PRO A 1 221 ? 26.842 29.271 51.694 1.00 9.98 ? 303 PRO A O 1 ATOM 1742 C CB . PRO A 1 221 ? 29.898 29.292 52.772 1.00 9.55 ? 303 PRO A CB 1 ATOM 1743 C CG . PRO A 1 221 ? 29.412 28.593 53.998 1.00 10.38 ? 303 PRO A CG 1 ATOM 1744 C CD . PRO A 1 221 ? 28.581 29.587 54.764 1.00 6.75 ? 303 PRO A CD 1 ATOM 1745 N N . VAL A 1 222 ? 28.161 30.231 50.125 1.00 6.93 ? 304 VAL A N 1 ATOM 1746 C CA . VAL A 1 222 ? 27.324 29.856 48.993 1.00 8.60 ? 304 VAL A CA 1 ATOM 1747 C C . VAL A 1 222 ? 28.188 29.158 47.957 1.00 12.22 ? 304 VAL A C 1 ATOM 1748 O O . VAL A 1 222 ? 29.286 29.627 47.645 1.00 12.02 ? 304 VAL A O 1 ATOM 1749 C CB . VAL A 1 222 ? 26.671 31.092 48.336 1.00 10.09 ? 304 VAL A CB 1 ATOM 1750 C CG1 . VAL A 1 222 ? 25.936 30.704 47.059 1.00 10.64 ? 304 VAL A CG1 1 ATOM 1751 C CG2 . VAL A 1 222 ? 25.723 31.770 49.303 1.00 9.27 ? 304 VAL A CG2 1 ATOM 1752 N N . ILE A 1 223 ? 27.705 28.030 47.443 1.00 6.40 ? 305 ILE A N 1 ATOM 1753 C CA . ILE A 1 223 ? 28.355 27.365 46.316 1.00 8.25 ? 305 ILE A CA 1 ATOM 1754 C C . ILE A 1 223 ? 27.429 27.416 45.108 1.00 10.24 ? 305 ILE A C 1 ATOM 1755 O O . ILE A 1 223 ? 26.260 27.035 45.193 1.00 10.21 ? 305 ILE A O 1 ATOM 1756 C CB . ILE A 1 223 ? 28.717 25.899 46.636 1.00 9.96 ? 305 ILE A CB 1 ATOM 1757 C CG1 . ILE A 1 223 ? 29.690 25.832 47.817 1.00 7.90 ? 305 ILE A CG1 1 ATOM 1758 C CG2 . ILE A 1 223 ? 29.311 25.217 45.403 1.00 11.69 ? 305 ILE A CG2 1 ATOM 1759 C CD1 . ILE A 1 223 ? 29.962 24.412 48.328 1.00 10.89 ? 305 ILE A CD1 1 ATOM 1760 N N . GLN A 1 224 ? 27.945 27.904 43.983 1.00 7.05 ? 306 GLN A N 1 ATOM 1761 C CA . GLN A 1 224 ? 27.154 27.981 42.763 1.00 8.06 ? 306 GLN A CA 1 ATOM 1762 C C . GLN A 1 224 ? 27.695 26.988 41.742 1.00 10.87 ? 306 GLN A C 1 ATOM 1763 O O . GLN A 1 224 ? 28.856 27.064 41.350 1.00 12.47 ? 306 GLN A O 1 ATOM 1764 C CB . GLN A 1 224 ? 27.163 29.414 42.216 1.00 10.91 ? 306 GLN A CB 1 ATOM 1765 C CG . GLN A 1 224 ? 26.501 30.408 43.176 1.00 18.08 ? 306 GLN A CG 1 ATOM 1766 C CD . GLN A 1 224 ? 26.600 31.851 42.721 1.00 24.75 ? 306 GLN A CD 1 ATOM 1767 O OE1 . GLN A 1 224 ? 27.620 32.508 42.926 1.00 28.31 ? 306 GLN A OE1 1 ATOM 1768 N NE2 . GLN A 1 224 ? 25.533 32.356 42.109 1.00 28.85 ? 306 GLN A NE2 1 ATOM 1769 N N . ILE A 1 225 ? 26.849 26.054 41.321 1.00 9.67 ? 307 ILE A N 1 ATOM 1770 C CA . ILE A 1 225 ? 27.300 24.922 40.515 1.00 9.26 ? 307 ILE A CA 1 ATOM 1771 C C . ILE A 1 225 ? 26.697 24.921 39.111 1.00 12.96 ? 307 ILE A C 1 ATOM 1772 O O . ILE A 1 225 ? 25.483 25.041 38.944 1.00 12.53 ? 307 ILE A O 1 ATOM 1773 C CB . ILE A 1 225 ? 26.950 23.579 41.214 1.00 10.58 ? 307 ILE A CB 1 ATOM 1774 C CG1 . ILE A 1 225 ? 27.541 23.539 42.626 1.00 9.88 ? 307 ILE A CG1 1 ATOM 1775 C CG2 . ILE A 1 225 ? 27.449 22.391 40.390 1.00 9.40 ? 307 ILE A CG2 1 ATOM 1776 C CD1 . ILE A 1 225 ? 27.032 22.360 43.484 1.00 7.80 ? 307 ILE A CD1 1 ATOM 1777 N N . ASP A 1 226 ? 27.561 24.793 38.108 1.00 10.49 ? 308 ASP A N 1 ATOM 1778 C CA . ASP A 1 226 ? 27.138 24.610 36.722 1.00 12.59 ? 308 ASP A CA 1 ATOM 1779 C C . ASP A 1 226 ? 27.158 23.110 36.454 1.00 11.12 ? 308 ASP A C 1 ATOM 1780 O O . ASP A 1 226 ? 28.231 22.521 36.351 1.00 10.50 ? 308 ASP A O 1 ATOM 1781 C CB . ASP A 1 226 ? 28.128 25.332 35.802 1.00 11.53 ? 308 ASP A CB 1 ATOM 1782 C CG . ASP A 1 226 ? 27.777 25.215 34.326 1.00 16.66 ? 308 ASP A CG 1 ATOM 1783 O OD1 . ASP A 1 226 ? 26.971 24.344 33.936 1.00 15.61 ? 308 ASP A OD1 1 ATOM 1784 O OD2 . ASP A 1 226 ? 28.340 26.007 33.543 1.00 18.26 ? 308 ASP A OD2 1 ATOM 1785 N N . PRO A 1 227 ? 25.973 22.482 36.350 1.00 10.33 ? 309 PRO A N 1 ATOM 1786 C CA . PRO A 1 227 ? 25.891 21.021 36.230 1.00 9.90 ? 309 PRO A CA 1 ATOM 1787 C C . PRO A 1 227 ? 26.193 20.517 34.823 1.00 11.24 ? 309 PRO A C 1 ATOM 1788 O O . PRO A 1 227 ? 26.268 19.307 34.611 1.00 11.42 ? 309 PRO A O 1 ATOM 1789 C CB . PRO A 1 227 ? 24.430 20.729 36.585 1.00 11.16 ? 309 PRO A CB 1 ATOM 1790 C CG . PRO A 1 227 ? 23.702 21.952 36.151 1.00 12.25 ? 309 PRO A CG 1 ATOM 1791 C CD . PRO A 1 227 ? 24.639 23.104 36.416 1.00 12.57 ? 309 PRO A CD 1 ATOM 1792 N N . VAL A 1 228 ? 26.345 21.432 33.871 1.00 13.04 ? 310 VAL A N 1 ATOM 1793 C CA . VAL A 1 228 ? 26.705 21.051 32.507 1.00 13.75 ? 310 VAL A CA 1 ATOM 1794 C C . VAL A 1 228 ? 28.224 21.023 32.364 1.00 15.18 ? 310 VAL A C 1 ATOM 1795 O O . VAL A 1 228 ? 28.805 20.015 31.965 1.00 14.17 ? 310 VAL A O 1 ATOM 1796 C CB . VAL A 1 228 ? 26.083 22.004 31.463 1.00 14.17 ? 310 VAL A CB 1 ATOM 1797 C CG1 . VAL A 1 228 ? 26.566 21.646 30.063 1.00 15.38 ? 310 VAL A CG1 1 ATOM 1798 C CG2 . VAL A 1 228 ? 24.564 21.950 31.526 1.00 12.22 ? 310 VAL A CG2 1 ATOM 1799 N N . ALA A 1 229 ? 28.868 22.129 32.716 1.00 11.33 ? 311 ALA A N 1 ATOM 1800 C CA . ALA A 1 229 ? 30.322 22.197 32.716 1.00 15.32 ? 311 ALA A CA 1 ATOM 1801 C C . ALA A 1 229 ? 30.913 21.390 33.869 1.00 16.31 ? 311 ALA A C 1 ATOM 1802 O O . ALA A 1 229 ? 32.096 21.032 33.850 1.00 13.58 ? 311 ALA A O 1 ATOM 1803 C CB . ALA A 1 229 ? 30.777 23.644 32.801 1.00 15.12 ? 311 ALA A CB 1 ATOM 1804 N N . MET A 1 230 ? 30.078 21.115 34.871 1.00 11.37 ? 312 MET A N 1 ATOM 1805 C CA . MET A 1 230 ? 30.512 20.446 36.098 1.00 11.01 ? 312 MET A CA 1 ATOM 1806 C C . MET A 1 230 ? 31.636 21.225 36.780 1.00 11.64 ? 312 MET A C 1 ATOM 1807 O O . MET A 1 230 ? 32.708 20.686 37.082 1.00 11.90 ? 312 MET A O 1 ATOM 1808 C CB . MET A 1 230 ? 30.875 18.980 35.837 1.00 9.21 ? 312 MET A CB 1 ATOM 1809 C CG . MET A 1 230 ? 29.695 18.192 35.260 1.00 10.66 ? 312 MET A CG 1 ATOM 1810 S SD . MET A 1 230 ? 29.919 16.407 35.169 1.00 14.93 ? 312 MET A SD 1 ATOM 1811 C CE . MET A 1 230 ? 31.268 16.296 33.992 1.00 19.54 ? 312 MET A CE 1 ATOM 1812 N N . THR A 1 231 ? 31.369 22.513 36.999 1.00 10.50 ? 313 THR A N 1 ATOM 1813 C CA . THR A 1 231 ? 32.285 23.418 37.685 1.00 10.22 ? 313 THR A CA 1 ATOM 1814 C C . THR A 1 231 ? 31.510 24.201 38.734 1.00 11.52 ? 313 THR A C 1 ATOM 1815 O O . THR A 1 231 ? 30.275 24.199 38.735 1.00 12.17 ? 313 THR A O 1 ATOM 1816 C CB . THR A 1 231 ? 32.947 24.413 36.707 1.00 13.18 ? 313 THR A CB 1 ATOM 1817 O OG1 . THR A 1 231 ? 31.937 25.069 35.926 1.00 13.98 ? 313 THR A OG1 1 ATOM 1818 C CG2 . THR A 1 231 ? 33.893 23.684 35.776 1.00 16.38 ? 313 THR A CG2 1 ATOM 1819 N N . HIS A 1 232 ? 32.225 24.866 39.632 1.00 9.74 ? 314 HIS A N 1 ATOM 1820 C CA . HIS A 1 232 ? 31.559 25.631 40.679 1.00 11.20 ? 314 HIS A CA 1 ATOM 1821 C C . HIS A 1 232 ? 32.391 26.828 41.114 1.00 12.51 ? 314 HIS A C 1 ATOM 1822 O O . HIS A 1 232 ? 33.592 26.904 40.836 1.00 12.97 ? 314 HIS A O 1 ATOM 1823 C CB . HIS A 1 232 ? 31.294 24.746 41.899 1.00 8.95 ? 314 HIS A CB 1 ATOM 1824 C CG . HIS A 1 232 ? 32.518 24.485 42.717 1.00 9.29 ? 314 HIS A CG 1 ATOM 1825 N ND1 . HIS A 1 232 ? 33.473 23.562 42.350 1.00 11.40 ? 314 HIS A ND1 1 ATOM 1826 C CD2 . HIS A 1 232 ? 32.958 25.042 43.872 1.00 10.46 ? 314 HIS A CD2 1 ATOM 1827 C CE1 . HIS A 1 232 ? 34.445 23.555 43.247 1.00 13.73 ? 314 HIS A CE1 1 ATOM 1828 N NE2 . HIS A 1 232 ? 34.156 24.445 44.181 1.00 10.44 ? 314 HIS A NE2 1 ATOM 1829 N N . THR A 1 233 ? 31.739 27.761 41.801 1.00 11.94 ? 315 THR A N 1 ATOM 1830 C CA . THR A 1 233 ? 32.419 28.858 42.473 1.00 10.48 ? 315 THR A CA 1 ATOM 1831 C C . THR A 1 233 ? 31.898 28.874 43.903 1.00 13.37 ? 315 THR A C 1 ATOM 1832 O O . THR A 1 233 ? 30.900 28.212 44.211 1.00 11.17 ? 315 THR A O 1 ATOM 1833 C CB . THR A 1 233 ? 32.116 30.219 41.811 1.00 15.71 ? 315 THR A CB 1 ATOM 1834 O OG1 . THR A 1 233 ? 30.698 30.440 41.785 1.00 16.01 ? 315 THR A OG1 1 ATOM 1835 C CG2 . THR A 1 233 ? 32.644 30.254 40.392 1.00 23.61 ? 315 THR A CG2 1 ATOM 1836 N N . SER A 1 234 ? 32.568 29.607 44.784 1.00 9.70 ? 316 SER A N 1 ATOM 1837 C CA . SER A 1 234 ? 32.037 29.790 46.131 1.00 8.31 ? 316 SER A CA 1 ATOM 1838 C C . SER A 1 234 ? 32.365 31.171 46.683 1.00 11.72 ? 316 SER A C 1 ATOM 1839 O O . SER A 1 234 ? 33.354 31.797 46.287 1.00 11.01 ? 316 SER A O 1 ATOM 1840 C CB . SER A 1 234 ? 32.530 28.698 47.088 1.00 9.23 ? 316 SER A CB 1 ATOM 1841 O OG . SER A 1 234 ? 33.851 28.943 47.540 1.00 8.81 ? 316 SER A OG 1 ATOM 1842 N N . GLN A 1 235 ? 31.507 31.639 47.584 1.00 10.00 ? 317 GLN A N 1 ATOM 1843 C CA . GLN A 1 235 ? 31.730 32.871 48.337 1.00 8.30 ? 317 GLN A CA 1 ATOM 1844 C C . GLN A 1 235 ? 30.818 32.830 49.560 1.00 10.06 ? 317 GLN A C 1 ATOM 1845 O O . GLN A 1 235 ? 30.413 31.751 49.986 1.00 9.32 ? 317 GLN A O 1 ATOM 1846 C CB . GLN A 1 235 ? 31.438 34.100 47.477 1.00 9.70 ? 317 GLN A CB 1 ATOM 1847 C CG . GLN A 1 235 ? 30.001 34.220 47.003 1.00 9.98 ? 317 GLN A CG 1 ATOM 1848 C CD . GLN A 1 235 ? 29.752 35.537 46.291 1.00 18.56 ? 317 GLN A CD 1 ATOM 1849 O OE1 . GLN A 1 235 ? 30.037 35.673 45.100 1.00 16.05 ? 317 GLN A OE1 1 ATOM 1850 N NE2 . GLN A 1 235 ? 29.233 36.518 47.021 1.00 13.40 ? 317 GLN A NE2 1 ATOM 1851 N N . TYR A 1 236 ? 30.508 33.989 50.136 1.00 8.82 ? 318 TYR A N 1 ATOM 1852 C CA . TYR A 1 236 ? 29.516 34.066 51.207 1.00 8.84 ? 318 TYR A CA 1 ATOM 1853 C C . TYR A 1 236 ? 28.375 34.960 50.740 1.00 9.10 ? 318 TYR A C 1 ATOM 1854 O O . TYR A 1 236 ? 28.544 35.738 49.800 1.00 10.23 ? 318 TYR A O 1 ATOM 1855 C CB . TYR A 1 236 ? 30.128 34.660 52.484 1.00 8.11 ? 318 TYR A CB 1 ATOM 1856 C CG . TYR A 1 236 ? 31.088 33.747 53.213 1.00 8.29 ? 318 TYR A CG 1 ATOM 1857 C CD1 . TYR A 1 236 ? 32.415 33.644 52.813 1.00 8.38 ? 318 TYR A CD1 1 ATOM 1858 C CD2 . TYR A 1 236 ? 30.671 32.994 54.307 1.00 7.44 ? 318 TYR A CD2 1 ATOM 1859 C CE1 . TYR A 1 236 ? 33.303 32.812 53.477 1.00 9.73 ? 318 TYR A CE1 1 ATOM 1860 C CE2 . TYR A 1 236 ? 31.556 32.154 54.979 1.00 8.19 ? 318 TYR A CE2 1 ATOM 1861 C CZ . TYR A 1 236 ? 32.870 32.070 54.552 1.00 8.15 ? 318 TYR A CZ 1 ATOM 1862 O OH . TYR A 1 236 ? 33.765 31.246 55.205 1.00 9.77 ? 318 TYR A OH 1 ATOM 1863 N N . ILE A 1 237 ? 27.213 34.848 51.381 1.00 8.80 ? 319 ILE A N 1 ATOM 1864 C CA . ILE A 1 237 ? 26.175 35.853 51.195 1.00 7.51 ? 319 ILE A CA 1 ATOM 1865 C C . ILE A 1 237 ? 26.741 37.178 51.710 1.00 6.68 ? 319 ILE A C 1 ATOM 1866 O O . ILE A 1 237 ? 27.122 37.277 52.880 1.00 9.24 ? 319 ILE A O 1 ATOM 1867 C CB . ILE A 1 237 ? 24.885 35.498 51.968 1.00 8.71 ? 319 ILE A CB 1 ATOM 1868 C CG1 . ILE A 1 237 ? 24.328 34.156 51.489 1.00 8.40 ? 319 ILE A CG1 1 ATOM 1869 C CG2 . ILE A 1 237 ? 23.830 36.579 51.788 1.00 8.23 ? 319 ILE A CG2 1 ATOM 1870 C CD1 . ILE A 1 237 ? 23.068 33.710 52.233 1.00 9.26 ? 319 ILE A CD1 1 ATOM 1871 N N . CYS A 1 238 ? 26.805 38.179 50.830 1.00 9.06 ? 320 CYS A N 1 ATOM 1872 C CA . CYS A 1 238 ? 27.401 39.486 51.146 1.00 10.40 ? 320 CYS A CA 1 ATOM 1873 C C . CYS A 1 238 ? 26.625 40.269 52.199 1.00 11.93 ? 320 CYS A C 1 ATOM 1874 O O . CYS A 1 238 ? 27.198 41.083 52.923 1.00 10.96 ? 320 CYS A O 1 ATOM 1875 C CB . CYS A 1 238 ? 27.481 40.360 49.885 1.00 11.35 ? 320 CYS A CB 1 ATOM 1876 S SG . CYS A 1 238 ? 28.733 39.892 48.668 1.00 15.95 ? 320 CYS A SG 1 ATOM 1877 N N . SER A 1 239 ? 25.318 40.042 52.252 1.00 11.56 ? 321 SER A N 1 ATOM 1878 C CA . SER A 1 239 ? 24.421 40.821 53.107 1.00 12.24 ? 321 SER A CA 1 ATOM 1879 C C . SER A 1 239 ? 24.804 40.830 54.586 1.00 9.14 ? 321 SER A C 1 ATOM 1880 O O . SER A 1 239 ? 25.235 39.810 55.129 1.00 9.70 ? 321 SER A O 1 ATOM 1881 C CB . SER A 1 239 ? 22.993 40.288 52.970 1.00 9.53 ? 321 SER A CB 1 ATOM 1882 O OG . SER A 1 239 ? 22.096 41.036 53.762 1.00 8.62 ? 321 SER A OG 1 ATOM 1883 N N . PRO A 1 240 ? 24.620 41.984 55.250 1.00 10.04 ? 322 PRO A N 1 ATOM 1884 C CA . PRO A 1 240 ? 24.792 42.081 56.702 1.00 9.81 ? 322 PRO A CA 1 ATOM 1885 C C . PRO A 1 240 ? 23.610 41.481 57.461 1.00 9.41 ? 322 PRO A C 1 ATOM 1886 O O . PRO A 1 240 ? 23.628 41.469 58.694 1.00 9.76 ? 322 PRO A O 1 ATOM 1887 C CB . PRO A 1 240 ? 24.860 43.594 56.945 1.00 11.04 ? 322 PRO A CB 1 ATOM 1888 C CG . PRO A 1 240 ? 24.039 44.175 55.847 1.00 11.58 ? 322 PRO A CG 1 ATOM 1889 C CD . PRO A 1 240 ? 24.288 43.287 54.647 1.00 9.53 ? 322 PRO A CD 1 ATOM 1890 N N . VAL A 1 241 ? 22.598 40.989 56.747 1.00 7.92 ? 323 VAL A N 1 ATOM 1891 C CA . VAL A 1 241 ? 21.535 40.225 57.401 1.00 11.10 ? 323 VAL A CA 1 ATOM 1892 C C . VAL A 1 241 ? 22.068 38.805 57.608 1.00 8.15 ? 323 VAL A C 1 ATOM 1893 O O . VAL A 1 241 ? 22.008 37.970 56.701 1.00 8.69 ? 323 VAL A O 1 ATOM 1894 C CB . VAL A 1 241 ? 20.226 40.222 56.577 1.00 8.40 ? 323 VAL A CB 1 ATOM 1895 C CG1 . VAL A 1 241 ? 19.137 39.413 57.276 1.00 8.88 ? 323 VAL A CG1 1 ATOM 1896 C CG2 . VAL A 1 241 ? 19.744 41.645 56.354 1.00 7.99 ? 323 VAL A CG2 1 ATOM 1897 N N . LEU A 1 242 ? 22.619 38.554 58.794 1.00 6.30 ? 324 LEU A N 1 ATOM 1898 C CA . LEU A 1 242 ? 23.335 37.309 59.070 1.00 9.16 ? 324 LEU A CA 1 ATOM 1899 C C . LEU A 1 242 ? 22.350 36.180 59.349 1.00 7.12 ? 324 LEU A C 1 ATOM 1900 O O . LEU A 1 242 ? 21.348 36.382 60.041 1.00 8.32 ? 324 LEU A O 1 ATOM 1901 C CB . LEU A 1 242 ? 24.287 37.497 60.257 1.00 5.97 ? 324 LEU A CB 1 ATOM 1902 C CG . LEU A 1 242 ? 25.341 38.598 60.096 1.00 9.09 ? 324 LEU A CG 1 ATOM 1903 C CD1 . LEU A 1 242 ? 26.211 38.712 61.345 1.00 10.06 ? 324 LEU A CD1 1 ATOM 1904 C CD2 . LEU A 1 242 ? 26.197 38.341 58.865 1.00 9.68 ? 324 LEU A CD2 1 ATOM 1905 N N . THR A 1 243 ? 22.624 34.988 58.820 1.00 8.68 ? 325 THR A N 1 ATOM 1906 C CA . THR A 1 243 ? 21.621 33.922 58.893 1.00 8.05 ? 325 THR A CA 1 ATOM 1907 C C . THR A 1 243 ? 22.057 32.578 59.486 1.00 7.03 ? 325 THR A C 1 ATOM 1908 O O . THR A 1 243 ? 21.299 31.607 59.422 1.00 9.34 ? 325 THR A O 1 ATOM 1909 C CB . THR A 1 243 ? 20.937 33.681 57.525 1.00 8.18 ? 325 THR A CB 1 ATOM 1910 O OG1 . THR A 1 243 ? 21.898 33.204 56.579 1.00 6.77 ? 325 THR A OG1 1 ATOM 1911 C CG2 . THR A 1 243 ? 20.302 34.967 56.996 1.00 7.51 ? 325 THR A CG2 1 ATOM 1912 N N . ASP A 1 244 ? 23.248 32.508 60.077 1.00 6.74 ? 326 ASP A N 1 ATOM 1913 C CA . ASP A 1 244 ? 23.615 31.302 60.816 1.00 5.68 ? 326 ASP A CA 1 ATOM 1914 C C . ASP A 1 244 ? 23.044 31.400 62.231 1.00 7.54 ? 326 ASP A C 1 ATOM 1915 O O . ASP A 1 244 ? 22.392 32.388 62.581 1.00 9.80 ? 326 ASP A O 1 ATOM 1916 C CB . ASP A 1 244 ? 25.136 31.095 60.846 1.00 7.95 ? 326 ASP A CB 1 ATOM 1917 C CG . ASP A 1 244 ? 25.530 29.628 61.024 1.00 10.81 ? 326 ASP A CG 1 ATOM 1918 O OD1 . ASP A 1 244 ? 24.641 28.797 61.314 1.00 8.24 ? 326 ASP A OD1 1 ATOM 1919 O OD2 . ASP A 1 244 ? 26.728 29.303 60.887 1.00 10.13 ? 326 ASP A OD2 1 ATOM 1920 N N . ASN A 1 245 ? 23.259 30.362 63.031 1.00 5.97 ? 327 ASN A N 1 ATOM 1921 C CA . ASN A 1 245 ? 22.869 30.381 64.438 1.00 8.31 ? 327 ASN A CA 1 ATOM 1922 C C . ASN A 1 245 ? 23.770 29.450 65.230 1.00 8.85 ? 327 ASN A C 1 ATOM 1923 O O . ASN A 1 245 ? 23.949 28.300 64.843 1.00 8.14 ? 327 ASN A O 1 ATOM 1924 C CB . ASN A 1 245 ? 21.406 29.973 64.627 1.00 6.72 ? 327 ASN A CB 1 ATOM 1925 C CG . ASN A 1 245 ? 20.993 29.964 66.093 1.00 13.28 ? 327 ASN A CG 1 ATOM 1926 O OD1 . ASN A 1 245 ? 21.037 28.926 66.756 1.00 9.84 ? 327 ASN A OD1 1 ATOM 1927 N ND2 . ASN A 1 245 ? 20.607 31.129 66.610 1.00 9.67 ? 327 ASN A ND2 1 ATOM 1928 N N . PRO A 1 246 ? 24.352 29.939 66.337 1.00 9.32 ? 328 PRO A N 1 ATOM 1929 C CA . PRO A 1 246 ? 24.246 31.301 66.879 1.00 9.09 ? 328 PRO A CA 1 ATOM 1930 C C . PRO A 1 246 ? 24.973 32.305 65.991 1.00 10.12 ? 328 PRO A C 1 ATOM 1931 O O . PRO A 1 246 ? 25.685 31.896 65.075 1.00 10.83 ? 328 PRO A O 1 ATOM 1932 C CB . PRO A 1 246 ? 24.958 31.192 68.230 1.00 11.58 ? 328 PRO A CB 1 ATOM 1933 C CG . PRO A 1 246 ? 25.956 30.096 68.029 1.00 13.05 ? 328 PRO A CG 1 ATOM 1934 C CD . PRO A 1 246 ? 25.261 29.098 67.139 1.00 13.04 ? 328 PRO A CD 1 ATOM 1935 N N . ARG A 1 247 ? 24.785 33.596 66.247 1.00 7.52 ? 329 ARG A N 1 ATOM 1936 C CA . ARG A 1 247 ? 25.371 34.617 65.387 1.00 6.65 ? 329 ARG A CA 1 ATOM 1937 C C . ARG A 1 247 ? 25.443 35.952 66.117 1.00 11.04 ? 329 ARG A C 1 ATOM 1938 O O . ARG A 1 247 ? 24.733 36.168 67.101 1.00 7.94 ? 329 ARG A O 1 ATOM 1939 C CB . ARG A 1 247 ? 24.544 34.771 64.106 1.00 6.40 ? 329 ARG A CB 1 ATOM 1940 C CG . ARG A 1 247 ? 23.095 35.182 64.360 1.00 7.99 ? 329 ARG A CG 1 ATOM 1941 C CD . ARG A 1 247 ? 22.350 35.515 63.072 1.00 8.71 ? 329 ARG A CD 1 ATOM 1942 N NE . ARG A 1 247 ? 21.034 36.078 63.369 1.00 7.84 ? 329 ARG A NE 1 ATOM 1943 C CZ . ARG A 1 247 ? 19.921 35.360 63.512 1.00 8.56 ? 329 ARG A CZ 1 ATOM 1944 N NH1 . ARG A 1 247 ? 19.943 34.042 63.360 1.00 6.80 ? 329 ARG A NH1 1 ATOM 1945 N NH2 . ARG A 1 247 ? 18.780 35.965 63.802 1.00 6.50 ? 329 ARG A NH2 1 ATOM 1946 N N . PRO A 1 248 ? 26.312 36.857 65.641 1.00 10.72 ? 330 PRO A N 1 ATOM 1947 C CA . PRO A 1 248 ? 26.316 38.220 66.170 1.00 10.76 ? 330 PRO A CA 1 ATOM 1948 C C . PRO A 1 248 ? 25.075 38.967 65.713 1.00 11.64 ? 330 PRO A C 1 ATOM 1949 O O . PRO A 1 248 ? 24.315 38.471 64.877 1.00 11.64 ? 330 PRO A O 1 ATOM 1950 C CB . PRO A 1 248 ? 27.545 38.854 65.497 1.00 11.43 ? 330 PRO A CB 1 ATOM 1951 C CG . PRO A 1 248 ? 28.396 37.702 65.060 1.00 15.01 ? 330 PRO A CG 1 ATOM 1952 C CD . PRO A 1 248 ? 27.416 36.632 64.693 1.00 10.47 ? 330 PRO A CD 1 ATOM 1953 N N . ASN A 1 249 ? 24.869 40.157 66.256 1.00 10.43 ? 331 ASN A N 1 ATOM 1954 C CA . ASN A 1 249 ? 23.823 41.026 65.746 1.00 11.99 ? 331 ASN A CA 1 ATOM 1955 C C . ASN A 1 249 ? 24.152 41.518 64.338 1.00 11.83 ? 331 ASN A C 1 ATOM 1956 O O . ASN A 1 249 ? 25.318 41.543 63.944 1.00 12.03 ? 331 ASN A O 1 ATOM 1957 C CB . ASN A 1 249 ? 23.587 42.200 66.702 1.00 12.89 ? 331 ASN A CB 1 ATOM 1958 C CG . ASN A 1 249 ? 22.936 41.765 68.001 1.00 16.58 ? 331 ASN A CG 1 ATOM 1959 O OD1 . ASN A 1 249 ? 21.935 41.047 67.997 1.00 16.23 ? 331 ASN A OD1 1 ATOM 1960 N ND2 . ASN A 1 249 ? 23.511 42.181 69.120 1.00 18.89 ? 331 ASN A ND2 1 ATOM 1961 N N . ASP A 1 250 ? 23.126 41.897 63.581 1.00 7.22 ? 332 ASP A N 1 ATOM 1962 C CA . ASP A 1 250 ? 23.332 42.355 62.208 1.00 9.63 ? 332 ASP A CA 1 ATOM 1963 C C . ASP A 1 250 ? 24.086 43.681 62.166 1.00 12.88 ? 332 ASP A C 1 ATOM 1964 O O . ASP A 1 250 ? 23.641 44.667 62.757 1.00 14.48 ? 332 ASP A O 1 ATOM 1965 C CB . ASP A 1 250 ? 21.998 42.539 61.487 1.00 11.40 ? 332 ASP A CB 1 ATOM 1966 C CG . ASP A 1 250 ? 21.289 41.232 61.210 1.00 13.73 ? 332 ASP A CG 1 ATOM 1967 O OD1 . ASP A 1 250 ? 21.939 40.163 61.261 1.00 11.63 ? 332 ASP A OD1 1 ATOM 1968 O OD2 . ASP A 1 250 ? 20.074 41.288 60.922 1.00 12.54 ? 332 ASP A OD2 1 ATOM 1969 N N . PRO A 1 251 ? 25.225 43.711 61.456 1.00 8.99 ? 333 PRO A N 1 ATOM 1970 C CA . PRO A 1 251 ? 25.951 44.960 61.202 1.00 11.02 ? 333 PRO A CA 1 ATOM 1971 C C . PRO A 1 251 ? 25.332 45.702 60.019 1.00 11.43 ? 333 PRO A C 1 ATOM 1972 O O . PRO A 1 251 ? 24.229 45.350 59.597 1.00 10.87 ? 333 PRO A O 1 ATOM 1973 C CB . PRO A 1 251 ? 27.347 44.467 60.828 1.00 11.33 ? 333 PRO A CB 1 ATOM 1974 C CG . PRO A 1 251 ? 27.082 43.172 60.115 1.00 11.81 ? 333 PRO A CG 1 ATOM 1975 C CD . PRO A 1 251 ? 25.909 42.546 60.858 1.00 7.07 ? 333 PRO A CD 1 ATOM 1976 N N . ASN A 1 252 ? 26.022 46.714 59.491 1.00 9.08 ? 334 ASN A N 1 ATOM 1977 C CA . ASN A 1 252 ? 25.543 47.424 58.301 1.00 10.45 ? 334 ASN A CA 1 ATOM 1978 C C . ASN A 1 252 ? 26.377 47.101 57.070 1.00 9.78 ? 334 ASN A C 1 ATOM 1979 O O . ASN A 1 252 ? 26.019 47.471 55.948 1.00 10.61 ? 334 ASN A O 1 ATOM 1980 C CB . ASN A 1 252 ? 25.505 48.938 58.533 1.00 12.76 ? 334 ASN A CB 1 ATOM 1981 C CG . ASN A 1 252 ? 24.344 49.360 59.406 1.00 17.23 ? 334 ASN A CG 1 ATOM 1982 O OD1 . ASN A 1 252 ? 23.417 48.584 59.635 1.00 15.37 ? 334 ASN A OD1 1 ATOM 1983 N ND2 . ASN A 1 252 ? 24.378 50.596 59.886 1.00 13.44 ? 334 ASN A ND2 1 ATOM 1984 N N . ILE A 1 253 ? 27.495 46.419 57.295 1.00 12.30 ? 335 ILE A N 1 ATOM 1985 C CA . ILE A 1 253 ? 28.327 45.910 56.211 1.00 11.86 ? 335 ILE A CA 1 ATOM 1986 C C . ILE A 1 253 ? 28.598 44.430 56.445 1.00 10.79 ? 335 ILE A C 1 ATOM 1987 O O . ILE A 1 253 ? 29.111 44.048 57.497 1.00 10.36 ? 335 ILE A O 1 ATOM 1988 C CB . ILE A 1 253 ? 29.677 46.655 56.124 1.00 13.73 ? 335 ILE A CB 1 ATOM 1989 C CG1 . ILE A 1 253 ? 29.458 48.166 55.999 1.00 14.48 ? 335 ILE A CG1 1 ATOM 1990 C CG2 . ILE A 1 253 ? 30.493 46.142 54.940 1.00 11.76 ? 335 ILE A CG2 1 ATOM 1991 C CD1 . ILE A 1 253 ? 30.750 48.950 55.817 1.00 15.00 ? 335 ILE A CD1 1 ATOM 1992 N N . GLY A 1 254 ? 28.239 43.594 55.475 1.00 9.88 ? 336 GLY A N 1 ATOM 1993 C CA . GLY A 1 254 ? 28.497 42.168 55.586 1.00 10.22 ? 336 GLY A CA 1 ATOM 1994 C C . GLY A 1 254 ? 29.840 41.807 54.984 1.00 11.03 ? 336 GLY A C 1 ATOM 1995 O O . GLY A 1 254 ? 30.683 42.679 54.770 1.00 11.49 ? 336 GLY A O 1 ATOM 1996 N N . LYS A 1 255 ? 30.044 40.522 54.712 1.00 9.65 ? 337 LYS A N 1 ATOM 1997 C CA . LYS A 1 255 ? 31.309 40.051 54.154 1.00 9.81 ? 337 LYS A CA 1 ATOM 1998 C C . LYS A 1 255 ? 31.046 39.076 53.012 1.00 14.65 ? 337 LYS A C 1 ATOM 1999 O O . LYS A 1 255 ? 30.329 38.087 53.184 1.00 11.90 ? 337 LYS A O 1 ATOM 2000 C CB . LYS A 1 255 ? 32.158 39.387 55.241 1.00 9.71 ? 337 LYS A CB 1 ATOM 2001 C CG . LYS A 1 255 ? 32.737 40.355 56.266 1.00 13.83 ? 337 LYS A CG 1 ATOM 2002 C CD . LYS A 1 255 ? 33.947 41.108 55.715 1.00 16.03 ? 337 LYS A CD 1 ATOM 2003 C CE . LYS A 1 255 ? 35.201 40.230 55.731 1.00 18.47 ? 337 LYS A CE 1 ATOM 2004 N NZ . LYS A 1 255 ? 36.423 40.959 55.253 1.00 18.34 ? 337 LYS A NZ 1 ATOM 2005 N N . CYS A 1 256 ? 31.625 39.360 51.847 1.00 10.44 ? 338 CYS A N 1 ATOM 2006 C CA . CYS A 1 256 ? 31.406 38.548 50.651 1.00 12.05 ? 338 CYS A CA 1 ATOM 2007 C C . CYS A 1 256 ? 32.377 37.378 50.540 1.00 15.27 ? 338 CYS A C 1 ATOM 2008 O O . CYS A 1 256 ? 32.039 36.339 49.974 1.00 11.36 ? 338 CYS A O 1 ATOM 2009 C CB . CYS A 1 256 ? 31.560 39.398 49.387 1.00 13.74 ? 338 CYS A CB 1 ATOM 2010 S SG . CYS A 1 256 ? 30.445 40.812 49.252 1.00 17.04 ? 338 CYS A SG 1 ATOM 2011 N N . ASN A 1 257 ? 33.589 37.553 51.060 1.00 10.10 ? 339 ASN A N 1 ATOM 2012 C CA . ASN A 1 257 ? 34.668 36.612 50.762 1.00 13.22 ? 339 ASN A CA 1 ATOM 2013 C C . ASN A 1 257 ? 35.403 36.064 51.976 1.00 12.87 ? 339 ASN A C 1 ATOM 2014 O O . ASN A 1 257 ? 36.508 35.533 51.859 1.00 11.99 ? 339 ASN A O 1 ATOM 2015 C CB . ASN A 1 257 ? 35.659 37.259 49.787 1.00 12.46 ? 339 ASN A CB 1 ATOM 2016 C CG . ASN A 1 257 ? 35.014 37.624 48.470 1.00 16.57 ? 339 ASN A CG 1 ATOM 2017 O OD1 . ASN A 1 257 ? 34.920 38.801 48.115 1.00 20.81 ? 339 ASN A OD1 1 ATOM 2018 N ND2 . ASN A 1 257 ? 34.554 36.614 47.737 1.00 12.35 ? 339 ASN A ND2 1 ATOM 2019 N N . ASP A 1 258 ? 34.776 36.182 53.140 1.00 10.73 ? 340 ASP A N 1 ATOM 2020 C CA . ASP A 1 258 ? 35.357 35.699 54.380 1.00 9.37 ? 340 ASP A CA 1 ATOM 2021 C C . ASP A 1 258 ? 34.251 35.549 55.414 1.00 10.15 ? 340 ASP A C 1 ATOM 2022 O O . ASP A 1 258 ? 33.188 36.159 55.280 1.00 9.37 ? 340 ASP A O 1 ATOM 2023 C CB . ASP A 1 258 ? 36.444 36.663 54.887 1.00 12.29 ? 340 ASP A CB 1 ATOM 2024 C CG . ASP A 1 258 ? 37.850 36.226 54.496 1.00 20.70 ? 340 ASP A CG 1 ATOM 2025 O OD1 . ASP A 1 258 ? 38.125 35.007 54.491 1.00 14.23 ? 340 ASP A OD1 1 ATOM 2026 O OD2 . ASP A 1 258 ? 38.684 37.106 54.198 1.00 15.00 ? 340 ASP A OD2 1 ATOM 2027 N N . PRO A 1 259 ? 34.488 34.719 56.437 1.00 10.97 ? 341 PRO A N 1 ATOM 2028 C CA . PRO A 1 259 ? 33.494 34.550 57.498 1.00 10.59 ? 341 PRO A CA 1 ATOM 2029 C C . PRO A 1 259 ? 33.299 35.832 58.292 1.00 14.21 ? 341 PRO A C 1 ATOM 2030 O O . PRO A 1 259 ? 34.286 36.484 58.649 1.00 11.72 ? 341 PRO A O 1 ATOM 2031 C CB . PRO A 1 259 ? 34.135 33.490 58.400 1.00 10.03 ? 341 PRO A CB 1 ATOM 2032 C CG . PRO A 1 259 ? 35.604 33.555 58.097 1.00 12.83 ? 341 PRO A CG 1 ATOM 2033 C CD . PRO A 1 259 ? 35.650 33.833 56.633 1.00 9.40 ? 341 PRO A CD 1 ATOM 2034 N N . TYR A 1 260 ? 32.049 36.195 58.559 1.00 9.30 ? 342 TYR A N 1 ATOM 2035 C CA . TYR A 1 260 ? 31.775 37.267 59.506 1.00 11.06 ? 342 TYR A CA 1 ATOM 2036 C C . TYR A 1 260 ? 31.938 36.720 60.923 1.00 10.40 ? 342 TYR A C 1 ATOM 2037 O O . TYR A 1 260 ? 31.282 35.742 61.290 1.00 10.51 ? 342 TYR A O 1 ATOM 2038 C CB . TYR A 1 260 ? 30.371 37.845 59.308 1.00 10.18 ? 342 TYR A CB 1 ATOM 2039 C CG . TYR A 1 260 ? 30.202 39.137 60.070 1.00 9.61 ? 342 TYR A CG 1 ATOM 2040 C CD1 . TYR A 1 260 ? 29.746 39.136 61.382 1.00 14.00 ? 342 TYR A CD1 1 ATOM 2041 C CD2 . TYR A 1 260 ? 30.546 40.354 59.492 1.00 14.08 ? 342 TYR A CD2 1 ATOM 2042 C CE1 . TYR A 1 260 ? 29.618 40.309 62.092 1.00 16.01 ? 342 TYR A CE1 1 ATOM 2043 C CE2 . TYR A 1 260 ? 30.421 41.536 60.196 1.00 14.60 ? 342 TYR A CE2 1 ATOM 2044 C CZ . TYR A 1 260 ? 29.954 41.504 61.495 1.00 18.27 ? 342 TYR A CZ 1 ATOM 2045 O OH . TYR A 1 260 ? 29.816 42.674 62.204 1.00 23.90 ? 342 TYR A OH 1 ATOM 2046 N N . PRO A 1 261 ? 32.813 37.351 61.727 1.00 8.78 ? 343 PRO A N 1 ATOM 2047 C CA . PRO A 1 261 ? 33.291 36.818 63.010 1.00 10.03 ? 343 PRO A CA 1 ATOM 2048 C C . PRO A 1 261 ? 32.401 37.140 64.212 1.00 12.82 ? 343 PRO A C 1 ATOM 2049 O O . PRO A 1 261 ? 31.538 38.022 64.137 1.00 13.94 ? 343 PRO A O 1 ATOM 2050 C CB . PRO A 1 261 ? 34.634 37.527 63.182 1.00 14.82 ? 343 PRO A CB 1 ATOM 2051 C CG . PRO A 1 261 ? 34.383 38.878 62.584 1.00 13.28 ? 343 PRO A CG 1 ATOM 2052 C CD . PRO A 1 261 ? 33.457 38.639 61.402 1.00 14.34 ? 343 PRO A CD 1 ATOM 2053 N N . GLY A 1 262 ? 32.630 36.431 65.316 1.00 13.67 ? 344 GLY A N 1 ATOM 2054 C CA . GLY A 1 262 ? 31.877 36.643 66.540 1.00 13.39 ? 344 GLY A CA 1 ATOM 2055 C C . GLY A 1 262 ? 31.501 35.335 67.206 1.00 16.60 ? 344 GLY A C 1 ATOM 2056 O O . GLY A 1 262 ? 31.456 35.236 68.436 1.00 13.49 ? 344 GLY A O 1 ATOM 2057 N N . ASN A 1 263 ? 31.223 34.330 66.382 1.00 12.63 ? 345 ASN A N 1 ATOM 2058 C CA . ASN A 1 263 ? 30.864 33.004 66.864 1.00 11.22 ? 345 ASN A CA 1 ATOM 2059 C C . ASN A 1 263 ? 31.683 31.933 66.155 1.00 14.66 ? 345 ASN A C 1 ATOM 2060 O O . ASN A 1 263 ? 31.686 31.864 64.924 1.00 15.22 ? 345 ASN A O 1 ATOM 2061 C CB . ASN A 1 263 ? 29.369 32.751 66.646 1.00 13.67 ? 345 ASN A CB 1 ATOM 2062 C CG . ASN A 1 263 ? 28.502 33.583 67.565 1.00 19.37 ? 345 ASN A CG 1 ATOM 2063 O OD1 . ASN A 1 263 ? 28.185 34.737 67.268 1.00 14.56 ? 345 ASN A OD1 1 ATOM 2064 N ND2 . ASN A 1 263 ? 28.119 33.005 68.696 1.00 13.68 ? 345 ASN A ND2 1 ATOM 2065 N N . ASN A 1 264 ? 32.378 31.104 66.931 1.00 12.70 ? 346 ASN A N 1 ATOM 2066 C CA . ASN A 1 264 ? 33.204 30.037 66.367 1.00 14.62 ? 346 ASN A CA 1 ATOM 2067 C C . ASN A 1 264 ? 32.676 28.651 66.704 1.00 13.43 ? 346 ASN A C 1 ATOM 2068 O O . ASN A 1 264 ? 31.963 28.474 67.698 1.00 11.01 ? 346 ASN A O 1 ATOM 2069 C CB . ASN A 1 264 ? 34.657 30.151 66.850 1.00 17.65 ? 346 ASN A CB 1 ATOM 2070 C CG . ASN A 1 264 ? 35.429 31.251 66.138 1.00 21.34 ? 346 ASN A CG 1 ATOM 2071 O OD1 . ASN A 1 264 ? 34.958 32.379 66.022 1.00 21.72 ? 346 ASN A OD1 1 ATOM 2072 N ND2 . ASN A 1 264 ? 36.617 30.917 65.645 1.00 26.57 ? 346 ASN A ND2 1 ATOM 2073 N N . ASN A 1 265 ? 33.031 27.673 65.873 1.00 11.23 ? 347 ASN A N 1 ATOM 2074 C CA . ASN A 1 265 ? 32.769 26.267 66.177 1.00 8.77 ? 347 ASN A CA 1 ATOM 2075 C C . ASN A 1 265 ? 31.302 25.948 66.458 1.00 10.17 ? 347 ASN A C 1 ATOM 2076 O O . ASN A 1 265 ? 30.989 25.204 67.386 1.00 12.06 ? 347 ASN A O 1 ATOM 2077 C CB . ASN A 1 265 ? 33.638 25.803 67.348 1.00 11.67 ? 347 ASN A CB 1 ATOM 2078 C CG . ASN A 1 265 ? 35.117 26.069 67.119 1.00 16.68 ? 347 ASN A CG 1 ATOM 2079 O OD1 . ASN A 1 265 ? 35.545 26.345 66.000 1.00 17.67 ? 347 ASN A OD1 1 ATOM 2080 N ND2 . ASN A 1 265 ? 35.906 25.971 68.183 1.00 20.13 ? 347 ASN A ND2 1 ATOM 2081 N N . ASN A 1 266 ? 30.408 26.523 65.661 1.00 9.93 ? 348 ASN A N 1 ATOM 2082 C CA . ASN A 1 266 ? 28.984 26.221 65.772 1.00 9.77 ? 348 ASN A CA 1 ATOM 2083 C C . ASN A 1 266 ? 28.247 26.748 64.554 1.00 11.64 ? 348 ASN A C 1 ATOM 2084 O O . ASN A 1 266 ? 28.830 27.416 63.694 1.00 8.11 ? 348 ASN A O 1 ATOM 2085 C CB . ASN A 1 266 ? 28.385 26.820 67.053 1.00 11.03 ? 348 ASN A CB 1 ATOM 2086 C CG . ASN A 1 266 ? 27.148 26.066 67.537 1.00 21.85 ? 348 ASN A CG 1 ATOM 2087 O OD1 . ASN A 1 266 ? 26.547 25.278 66.799 1.00 22.01 ? 348 ASN A OD1 1 ATOM 2088 N ND2 . ASN A 1 266 ? 26.763 26.312 68.785 1.00 31.72 ? 348 ASN A ND2 1 ATOM 2089 N N . GLY A 1 267 ? 26.959 26.446 64.477 1.00 9.03 ? 349 GLY A N 1 ATOM 2090 C CA . GLY A 1 267 ? 26.174 26.845 63.330 1.00 7.82 ? 349 GLY A CA 1 ATOM 2091 C C . GLY A 1 267 ? 24.961 25.950 63.235 1.00 9.52 ? 349 GLY A C 1 ATOM 2092 O O . GLY A 1 267 ? 24.811 25.023 64.032 1.00 10.93 ? 349 GLY A O 1 ATOM 2093 N N . VAL A 1 268 ? 24.091 26.233 62.276 1.00 6.95 ? 350 VAL A N 1 ATOM 2094 C CA . VAL A 1 268 ? 22.947 25.373 62.008 1.00 5.32 ? 350 VAL A CA 1 ATOM 2095 C C . VAL A 1 268 ? 22.785 25.306 60.497 1.00 6.35 ? 350 VAL A C 1 ATOM 2096 O O . VAL A 1 268 ? 23.147 26.253 59.790 1.00 7.91 ? 350 VAL A O 1 ATOM 2097 C CB . VAL A 1 268 ? 21.647 25.902 62.705 1.00 5.37 ? 350 VAL A CB 1 ATOM 2098 C CG1 . VAL A 1 268 ? 21.144 27.177 62.042 1.00 6.76 ? 350 VAL A CG1 1 ATOM 2099 C CG2 . VAL A 1 268 ? 20.552 24.842 62.693 1.00 5.18 ? 350 VAL A CG2 1 ATOM 2100 N N . LYS A 1 269 ? 22.293 24.179 59.991 1.00 6.03 ? 351 LYS A N 1 ATOM 2101 C CA . LYS A 1 269 ? 21.955 24.085 58.576 1.00 5.91 ? 351 LYS A CA 1 ATOM 2102 C C . LYS A 1 269 ? 20.841 25.074 58.263 1.00 5.06 ? 351 LYS A C 1 ATOM 2103 O O . LYS A 1 269 ? 19.874 25.186 59.023 1.00 6.15 ? 351 LYS A O 1 ATOM 2104 C CB . LYS A 1 269 ? 21.501 22.669 58.221 1.00 4.58 ? 351 LYS A CB 1 ATOM 2105 C CG . LYS A 1 269 ? 21.073 22.495 56.768 1.00 3.79 ? 351 LYS A CG 1 ATOM 2106 C CD . LYS A 1 269 ? 20.624 21.060 56.508 1.00 6.45 ? 351 LYS A CD 1 ATOM 2107 C CE . LYS A 1 269 ? 20.047 20.908 55.107 1.00 7.01 ? 351 LYS A CE 1 ATOM 2108 N NZ . LYS A 1 269 ? 21.073 21.121 54.043 1.00 4.74 ? 351 LYS A NZ 1 ATOM 2109 N N . GLY A 1 270 ? 20.985 25.788 57.149 1.00 5.33 ? 352 GLY A N 1 ATOM 2110 C CA . GLY A 1 270 ? 20.015 26.789 56.734 1.00 5.65 ? 352 GLY A CA 1 ATOM 2111 C C . GLY A 1 270 ? 19.933 26.886 55.221 1.00 6.97 ? 352 GLY A C 1 ATOM 2112 O O . GLY A 1 270 ? 20.486 26.046 54.510 1.00 7.84 ? 352 GLY A O 1 ATOM 2113 N N . PHE A 1 271 ? 19.243 27.901 54.710 1.00 6.45 ? 353 PHE A N 1 ATOM 2114 C CA . PHE A 1 271 ? 19.060 27.989 53.265 1.00 4.91 ? 353 PHE A CA 1 ATOM 2115 C C . PHE A 1 271 ? 18.732 29.413 52.866 1.00 6.75 ? 353 PHE A C 1 ATOM 2116 O O . PHE A 1 271 ? 18.434 30.257 53.714 1.00 7.31 ? 353 PHE A O 1 ATOM 2117 C CB . PHE A 1 271 ? 17.907 27.080 52.818 1.00 3.90 ? 353 PHE A CB 1 ATOM 2118 C CG . PHE A 1 271 ? 16.558 27.674 53.077 1.00 4.47 ? 353 PHE A CG 1 ATOM 2119 C CD1 . PHE A 1 271 ? 15.994 27.612 54.340 1.00 6.58 ? 353 PHE A CD1 1 ATOM 2120 C CD2 . PHE A 1 271 ? 15.874 28.336 52.067 1.00 6.53 ? 353 PHE A CD2 1 ATOM 2121 C CE1 . PHE A 1 271 ? 14.761 28.187 54.593 1.00 5.48 ? 353 PHE A CE1 1 ATOM 2122 C CE2 . PHE A 1 271 ? 14.646 28.920 52.309 1.00 6.35 ? 353 PHE A CE2 1 ATOM 2123 C CZ . PHE A 1 271 ? 14.093 28.853 53.576 1.00 7.38 ? 353 PHE A CZ 1 ATOM 2124 N N . SER A 1 272 ? 18.767 29.673 51.566 1.00 4.65 ? 354 SER A N 1 ATOM 2125 C CA . SER A 1 272 ? 18.277 30.937 51.039 1.00 6.26 ? 354 SER A CA 1 ATOM 2126 C C . SER A 1 272 ? 17.855 30.740 49.597 1.00 7.20 ? 354 SER A C 1 ATOM 2127 O O . SER A 1 272 ? 18.213 29.739 48.969 1.00 7.68 ? 354 SER A O 1 ATOM 2128 C CB . SER A 1 272 ? 19.367 32.007 51.114 1.00 12.09 ? 354 SER A CB 1 ATOM 2129 O OG . SER A 1 272 ? 20.389 31.750 50.168 1.00 9.93 ? 354 SER A OG 1 ATOM 2130 N N . TYR A 1 273 ? 17.088 31.688 49.071 1.00 5.31 ? 355 TYR A N 1 ATOM 2131 C CA . TYR A 1 273 ? 16.844 31.744 47.639 1.00 6.67 ? 355 TYR A CA 1 ATOM 2132 C C . TYR A 1 273 ? 17.439 33.040 47.112 1.00 10.63 ? 355 TYR A C 1 ATOM 2133 O O . TYR A 1 273 ? 16.986 34.128 47.469 1.00 9.52 ? 355 TYR A O 1 ATOM 2134 C CB . TYR A 1 273 ? 15.350 31.634 47.329 1.00 6.25 ? 355 TYR A CB 1 ATOM 2135 C CG . TYR A 1 273 ? 14.852 30.205 47.393 1.00 6.46 ? 355 TYR A CG 1 ATOM 2136 C CD1 . TYR A 1 273 ? 14.922 29.378 46.277 1.00 7.02 ? 355 TYR A CD1 1 ATOM 2137 C CD2 . TYR A 1 273 ? 14.337 29.676 48.573 1.00 7.62 ? 355 TYR A CD2 1 ATOM 2138 C CE1 . TYR A 1 273 ? 14.480 28.059 46.326 1.00 6.00 ? 355 TYR A CE1 1 ATOM 2139 C CE2 . TYR A 1 273 ? 13.890 28.363 48.633 1.00 4.27 ? 355 TYR A CE2 1 ATOM 2140 C CZ . TYR A 1 273 ? 13.968 27.562 47.505 1.00 4.68 ? 355 TYR A CZ 1 ATOM 2141 O OH . TYR A 1 273 ? 13.531 26.257 47.551 1.00 5.90 ? 355 TYR A OH 1 ATOM 2142 N N . LEU A 1 274 ? 18.477 32.915 46.288 1.00 6.51 ? 356 LEU A N 1 ATOM 2143 C CA . LEU A 1 274 ? 19.239 34.076 45.833 1.00 8.12 ? 356 LEU A CA 1 ATOM 2144 C C . LEU A 1 274 ? 18.883 34.363 44.384 1.00 9.12 ? 356 LEU A C 1 ATOM 2145 O O . LEU A 1 274 ? 19.300 33.640 43.475 1.00 11.59 ? 356 LEU A O 1 ATOM 2146 C CB . LEU A 1 274 ? 20.736 33.805 45.989 1.00 8.22 ? 356 LEU A CB 1 ATOM 2147 C CG . LEU A 1 274 ? 21.110 33.348 47.403 1.00 9.68 ? 356 LEU A CG 1 ATOM 2148 C CD1 . LEU A 1 274 ? 22.544 32.843 47.497 1.00 9.93 ? 356 LEU A CD1 1 ATOM 2149 C CD2 . LEU A 1 274 ? 20.884 34.479 48.416 1.00 9.87 ? 356 LEU A CD2 1 ATOM 2150 N N . ASP A 1 275 ? 18.109 35.423 44.172 1.00 9.15 ? 357 ASP A N 1 ATOM 2151 C CA . ASP A 1 275 ? 17.495 35.657 42.876 1.00 8.85 ? 357 ASP A CA 1 ATOM 2152 C C . ASP A 1 275 ? 17.279 37.150 42.647 1.00 9.94 ? 357 ASP A C 1 ATOM 2153 O O . ASP A 1 275 ? 16.164 37.583 42.365 1.00 9.29 ? 357 ASP A O 1 ATOM 2154 C CB . ASP A 1 275 ? 16.155 34.906 42.811 1.00 9.66 ? 357 ASP A CB 1 ATOM 2155 C CG . ASP A 1 275 ? 15.542 34.903 41.421 1.00 12.49 ? 357 ASP A CG 1 ATOM 2156 O OD1 . ASP A 1 275 ? 16.299 34.939 40.428 1.00 13.08 ? 357 ASP A OD1 1 ATOM 2157 O OD2 . ASP A 1 275 ? 14.296 34.861 41.322 1.00 14.37 ? 357 ASP A OD2 1 ATOM 2158 N N . GLY A 1 276 ? 18.347 37.937 42.774 1.00 9.98 ? 358 GLY A N 1 ATOM 2159 C CA . GLY A 1 276 ? 18.258 39.369 42.540 1.00 11.42 ? 358 GLY A CA 1 ATOM 2160 C C . GLY A 1 276 ? 17.266 40.040 43.473 1.00 11.12 ? 358 GLY A C 1 ATOM 2161 O O . GLY A 1 276 ? 17.348 39.884 44.692 1.00 10.55 ? 358 GLY A O 1 ATOM 2162 N N . ALA A 1 277 ? 16.316 40.774 42.905 1.00 10.44 ? 359 ALA A N 1 ATOM 2163 C CA . ALA A 1 277 ? 15.309 41.468 43.707 1.00 11.44 ? 359 ALA A CA 1 ATOM 2164 C C . ALA A 1 277 ? 14.297 40.503 44.330 1.00 11.06 ? 359 ALA A C 1 ATOM 2165 O O . ALA A 1 277 ? 13.512 40.895 45.198 1.00 14.17 ? 359 ALA A O 1 ATOM 2166 C CB . ALA A 1 277 ? 14.589 42.510 42.867 1.00 11.23 ? 359 ALA A CB 1 ATOM 2167 N N . ASN A 1 278 ? 14.311 39.253 43.870 1.00 9.71 ? 360 ASN A N 1 ATOM 2168 C CA . ASN A 1 278 ? 13.402 38.213 44.361 1.00 8.96 ? 360 ASN A CA 1 ATOM 2169 C C . ASN A 1 278 ? 14.097 37.344 45.416 1.00 12.50 ? 360 ASN A C 1 ATOM 2170 O O . ASN A 1 278 ? 13.749 36.178 45.611 1.00 10.86 ? 360 ASN A O 1 ATOM 2171 C CB . ASN A 1 278 ? 12.938 37.353 43.175 1.00 10.58 ? 360 ASN A CB 1 ATOM 2172 C CG . ASN A 1 278 ? 11.803 36.397 43.525 1.00 9.87 ? 360 ASN A CG 1 ATOM 2173 O OD1 . ASN A 1 278 ? 10.867 36.750 44.247 1.00 10.85 ? 360 ASN A OD1 1 ATOM 2174 N ND2 . ASN A 1 278 ? 11.885 35.178 43.002 1.00 10.37 ? 360 ASN A ND2 1 ATOM 2175 N N . THR A 1 279 ? 15.084 37.919 46.099 1.00 6.99 ? 361 THR A N 1 ATOM 2176 C CA . THR A 1 279 ? 15.877 37.176 47.082 1.00 7.56 ? 361 THR A CA 1 ATOM 2177 C C . THR A 1 279 ? 15.211 37.099 48.463 1.00 9.46 ? 361 THR A C 1 ATOM 2178 O O . THR A 1 279 ? 14.791 38.119 49.010 1.00 9.09 ? 361 THR A O 1 ATOM 2179 C CB . THR A 1 279 ? 17.273 37.805 47.240 1.00 9.47 ? 361 THR A CB 1 ATOM 2180 O OG1 . THR A 1 279 ? 18.000 37.666 46.013 1.00 8.28 ? 361 THR A OG1 1 ATOM 2181 C CG2 . THR A 1 279 ? 18.047 37.117 48.354 1.00 6.94 ? 361 THR A CG2 1 ATOM 2182 N N . TRP A 1 280 ? 15.128 35.892 49.024 1.00 7.49 ? 362 TRP A N 1 ATOM 2183 C CA . TRP A 1 280 ? 14.621 35.707 50.385 1.00 7.72 ? 362 TRP A CA 1 ATOM 2184 C C . TRP A 1 280 ? 15.582 34.851 51.209 1.00 8.50 ? 362 TRP A C 1 ATOM 2185 O O . TRP A 1 280 ? 16.068 33.821 50.735 1.00 6.64 ? 362 TRP A O 1 ATOM 2186 C CB . TRP A 1 280 ? 13.246 35.041 50.362 1.00 7.61 ? 362 TRP A CB 1 ATOM 2187 C CG . TRP A 1 280 ? 12.121 35.935 49.926 1.00 7.05 ? 362 TRP A CG 1 ATOM 2188 C CD1 . TRP A 1 280 ? 11.835 36.347 48.653 1.00 7.68 ? 362 TRP A CD1 1 ATOM 2189 C CD2 . TRP A 1 280 ? 11.106 36.494 50.767 1.00 7.44 ? 362 TRP A CD2 1 ATOM 2190 N NE1 . TRP A 1 280 ? 10.707 37.140 48.656 1.00 7.66 ? 362 TRP A NE1 1 ATOM 2191 C CE2 . TRP A 1 280 ? 10.242 37.242 49.942 1.00 7.85 ? 362 TRP A CE2 1 ATOM 2192 C CE3 . TRP A 1 280 ? 10.848 36.437 52.142 1.00 6.59 ? 362 TRP A CE3 1 ATOM 2193 C CZ2 . TRP A 1 280 ? 9.137 37.931 50.450 1.00 9.39 ? 362 TRP A CZ2 1 ATOM 2194 C CZ3 . TRP A 1 280 ? 9.752 37.119 52.643 1.00 8.81 ? 362 TRP A CZ3 1 ATOM 2195 C CH2 . TRP A 1 280 ? 8.908 37.852 51.798 1.00 10.34 ? 362 TRP A CH2 1 ATOM 2196 N N . LEU A 1 281 ? 15.849 35.277 52.441 1.00 7.13 ? 363 LEU A N 1 ATOM 2197 C CA . LEU A 1 281 ? 16.737 34.542 53.336 1.00 7.97 ? 363 LEU A CA 1 ATOM 2198 C C . LEU A 1 281 ? 15.935 33.956 54.492 1.00 8.81 ? 363 LEU A C 1 ATOM 2199 O O . LEU A 1 281 ? 15.030 34.604 55.014 1.00 8.39 ? 363 LEU A O 1 ATOM 2200 C CB . LEU A 1 281 ? 17.814 35.463 53.913 1.00 7.72 ? 363 LEU A CB 1 ATOM 2201 C CG . LEU A 1 281 ? 18.606 36.380 52.979 1.00 11.62 ? 363 LEU A CG 1 ATOM 2202 C CD1 . LEU A 1 281 ? 19.638 37.173 53.779 1.00 6.95 ? 363 LEU A CD1 1 ATOM 2203 C CD2 . LEU A 1 281 ? 19.267 35.580 51.862 1.00 9.45 ? 363 LEU A CD2 1 ATOM 2204 N N . GLY A 1 282 ? 16.271 32.733 54.891 1.00 6.71 ? 364 GLY A N 1 ATOM 2205 C CA . GLY A 1 282 ? 15.692 32.147 56.088 1.00 5.41 ? 364 GLY A CA 1 ATOM 2206 C C . GLY A 1 282 ? 16.655 32.262 57.258 1.00 7.29 ? 364 GLY A C 1 ATOM 2207 O O . GLY A 1 282 ? 17.869 32.200 57.063 1.00 7.68 ? 364 GLY A O 1 ATOM 2208 N N . ARG A 1 283 ? 16.130 32.443 58.469 1.00 4.44 ? 365 ARG A N 1 ATOM 2209 C CA . ARG A 1 283 ? 16.972 32.375 59.669 1.00 5.29 ? 365 ARG A CA 1 ATOM 2210 C C . ARG A 1 283 ? 16.166 32.137 60.938 1.00 7.07 ? 365 ARG A C 1 ATOM 2211 O O . ARG A 1 283 ? 14.961 32.381 60.972 1.00 6.67 ? 365 ARG A O 1 ATOM 2212 C CB . ARG A 1 283 ? 17.834 33.638 59.830 1.00 5.35 ? 365 ARG A CB 1 ATOM 2213 C CG . ARG A 1 283 ? 17.068 34.920 60.157 1.00 7.48 ? 365 ARG A CG 1 ATOM 2214 C CD . ARG A 1 283 ? 18.062 36.056 60.346 1.00 6.97 ? 365 ARG A CD 1 ATOM 2215 N NE . ARG A 1 283 ? 17.455 37.344 60.685 1.00 9.74 ? 365 ARG A NE 1 ATOM 2216 C CZ . ARG A 1 283 ? 18.163 38.454 60.887 1.00 11.01 ? 365 ARG A CZ 1 ATOM 2217 N NH1 . ARG A 1 283 ? 19.485 38.419 60.784 1.00 7.99 ? 365 ARG A NH1 1 ATOM 2218 N NH2 . ARG A 1 283 ? 17.559 39.596 61.182 1.00 10.29 ? 365 ARG A NH2 1 ATOM 2219 N N . THR A 1 284 ? 16.834 31.650 61.980 1.00 5.60 ? 366 THR A N 1 ATOM 2220 C CA . THR A 1 284 ? 16.219 31.581 63.299 1.00 6.59 ? 366 THR A CA 1 ATOM 2221 C C . THR A 1 284 ? 16.020 33.009 63.778 1.00 10.19 ? 366 THR A C 1 ATOM 2222 O O . THR A 1 284 ? 16.782 33.906 63.404 1.00 8.30 ? 366 THR A O 1 ATOM 2223 C CB . THR A 1 284 ? 17.109 30.841 64.313 1.00 7.21 ? 366 THR A CB 1 ATOM 2224 O OG1 . THR A 1 284 ? 18.321 31.579 64.518 1.00 7.50 ? 366 THR A OG1 1 ATOM 2225 C CG2 . THR A 1 284 ? 17.453 29.450 63.810 1.00 5.68 ? 366 THR A CG2 1 ATOM 2226 N N . ILE A 1 285 ? 14.998 33.233 64.595 1.00 7.03 ? 367 ILE A N 1 ATOM 2227 C CA . ILE A 1 285 ? 14.777 34.569 65.142 1.00 6.53 ? 367 ILE A CA 1 ATOM 2228 C C . ILE A 1 285 ? 15.822 34.884 66.206 1.00 8.98 ? 367 ILE A C 1 ATOM 2229 O O . ILE A 1 285 ? 16.416 35.966 66.207 1.00 10.65 ? 367 ILE A O 1 ATOM 2230 C CB . ILE A 1 285 ? 13.346 34.737 65.695 1.00 10.22 ? 367 ILE A CB 1 ATOM 2231 C CG1 . ILE A 1 285 ? 12.336 34.654 64.547 1.00 10.17 ? 367 ILE A CG1 1 ATOM 2232 C CG2 . ILE A 1 285 ? 13.204 36.073 66.423 1.00 10.88 ? 367 ILE A CG2 1 ATOM 2233 C CD1 . ILE A 1 285 ? 10.882 34.660 64.996 1.00 11.47 ? 367 ILE A CD1 1 ATOM 2234 N N . SER A 1 286 ? 16.063 33.927 67.096 1.00 9.33 ? 368 SER A N 1 ATOM 2235 C CA . SER A 1 286 ? 17.088 34.084 68.125 1.00 11.06 ? 368 SER A CA 1 ATOM 2236 C C . SER A 1 286 ? 18.493 34.132 67.532 1.00 13.38 ? 368 SER A C 1 ATOM 2237 O O . SER A 1 286 ? 18.795 33.427 66.570 1.00 12.64 ? 368 SER A O 1 ATOM 2238 C CB . SER A 1 286 ? 17.009 32.936 69.130 1.00 9.96 ? 368 SER A CB 1 ATOM 2239 O OG . SER A 1 286 ? 18.072 33.004 70.067 1.00 9.68 ? 368 SER A OG 1 ATOM 2240 N N . THR A 1 287 ? 19.355 34.965 68.108 1.00 9.36 ? 369 THR A N 1 ATOM 2241 C CA . THR A 1 287 ? 20.761 34.977 67.716 1.00 8.86 ? 369 THR A CA 1 ATOM 2242 C C . THR A 1 287 ? 21.559 33.993 68.558 1.00 11.14 ? 369 THR A C 1 ATOM 2243 O O . THR A 1 287 ? 22.727 33.730 68.273 1.00 8.09 ? 369 THR A O 1 ATOM 2244 C CB . THR A 1 287 ? 21.400 36.361 67.902 1.00 9.32 ? 369 THR A CB 1 ATOM 2245 O OG1 . THR A 1 287 ? 21.237 36.777 69.265 1.00 9.27 ? 369 THR A OG1 1 ATOM 2246 C CG2 . THR A 1 287 ? 20.766 37.391 66.964 1.00 12.40 ? 369 THR A CG2 1 ATOM 2247 N N . ALA A 1 288 ? 20.933 33.454 69.601 1.00 9.36 ? 370 ALA A N 1 ATOM 2248 C CA . ALA A 1 288 ? 21.658 32.627 70.563 1.00 9.94 ? 370 ALA A CA 1 ATOM 2249 C C . ALA A 1 288 ? 21.377 31.139 70.425 1.00 11.05 ? 370 ALA A C 1 ATOM 2250 O O . ALA A 1 288 ? 22.272 30.313 70.623 1.00 11.02 ? 370 ALA A O 1 ATOM 2251 C CB . ALA A 1 288 ? 21.358 33.082 71.983 1.00 11.63 ? 370 ALA A CB 1 ATOM 2252 N N . SER A 1 289 ? 20.134 30.794 70.104 1.00 9.26 ? 371 SER A N 1 ATOM 2253 C CA . SER A 1 289 ? 19.729 29.390 70.074 1.00 7.23 ? 371 SER A CA 1 ATOM 2254 C C . SER A 1 289 ? 18.817 29.075 68.896 1.00 7.17 ? 371 SER A C 1 ATOM 2255 O O . SER A 1 289 ? 18.368 29.975 68.183 1.00 8.58 ? 371 SER A O 1 ATOM 2256 C CB . SER A 1 289 ? 19.034 29.016 71.384 1.00 14.65 ? 371 SER A CB 1 ATOM 2257 O OG . SER A 1 289 ? 17.809 29.709 71.513 1.00 22.75 ? 371 SER A OG 1 ATOM 2258 N N . ARG A 1 290 ? 18.542 27.790 68.702 1.00 6.25 ? 372 ARG A N 1 ATOM 2259 C CA . ARG A 1 290 ? 17.718 27.337 67.587 1.00 6.45 ? 372 ARG A CA 1 ATOM 2260 C C . ARG A 1 290 ? 16.244 27.495 67.929 1.00 7.54 ? 372 ARG A C 1 ATOM 2261 O O . ARG A 1 290 ? 15.529 26.514 68.168 1.00 7.98 ? 372 ARG A O 1 ATOM 2262 C CB . ARG A 1 290 ? 18.055 25.886 67.242 1.00 6.27 ? 372 ARG A CB 1 ATOM 2263 C CG . ARG A 1 290 ? 19.497 25.718 66.757 1.00 5.95 ? 372 ARG A CG 1 ATOM 2264 C CD . ARG A 1 290 ? 19.958 24.261 66.759 1.00 8.69 ? 372 ARG A CD 1 ATOM 2265 N NE . ARG A 1 290 ? 21.263 24.136 66.106 1.00 5.46 ? 372 ARG A NE 1 ATOM 2266 C CZ . ARG A 1 290 ? 21.843 22.982 65.796 1.00 8.07 ? 372 ARG A CZ 1 ATOM 2267 N NH1 . ARG A 1 290 ? 21.243 21.834 66.087 1.00 9.20 ? 372 ARG A NH1 1 ATOM 2268 N NH2 . ARG A 1 290 ? 23.023 22.975 65.189 1.00 6.37 ? 372 ARG A NH2 1 ATOM 2269 N N . SER A 1 291 ? 15.800 28.744 67.979 1.00 6.85 ? 373 SER A N 1 ATOM 2270 C CA . SER A 1 291 ? 14.415 29.038 68.312 1.00 6.97 ? 373 SER A CA 1 ATOM 2271 C C . SER A 1 291 ? 13.879 30.093 67.357 1.00 8.30 ? 373 SER A C 1 ATOM 2272 O O . SER A 1 291 ? 14.601 31.008 66.943 1.00 8.14 ? 373 SER A O 1 ATOM 2273 C CB . SER A 1 291 ? 14.281 29.491 69.768 1.00 12.24 ? 373 SER A CB 1 ATOM 2274 O OG . SER A 1 291 ? 14.959 30.705 69.991 1.00 18.92 ? 373 SER A OG 1 ATOM 2275 N N . GLY A 1 292 ? 12.615 29.943 66.985 1.00 5.51 ? 374 GLY A N 1 ATOM 2276 C CA . GLY A 1 292 ? 11.993 30.843 66.039 1.00 5.80 ? 374 GLY A CA 1 ATOM 2277 C C . GLY A 1 292 ? 12.468 30.589 64.623 1.00 6.47 ? 374 GLY A C 1 ATOM 2278 O O . GLY A 1 292 ? 13.491 29.933 64.399 1.00 7.32 ? 374 GLY A O 1 ATOM 2279 N N . TYR A 1 293 ? 11.705 31.092 63.660 1.00 4.96 ? 375 TYR A N 1 ATOM 2280 C CA . TYR A 1 293 ? 12.136 31.072 62.272 1.00 4.89 ? 375 TYR A CA 1 ATOM 2281 C C . TYR A 1 293 ? 11.412 32.135 61.474 1.00 6.11 ? 375 TYR A C 1 ATOM 2282 O O . TYR A 1 293 ? 10.200 32.307 61.610 1.00 6.44 ? 375 TYR A O 1 ATOM 2283 C CB . TYR A 1 293 ? 11.938 29.695 61.621 1.00 5.75 ? 375 TYR A CB 1 ATOM 2284 C CG . TYR A 1 293 ? 12.924 29.493 60.500 1.00 6.54 ? 375 TYR A CG 1 ATOM 2285 C CD1 . TYR A 1 293 ? 14.190 28.980 60.755 1.00 5.83 ? 375 TYR A CD1 1 ATOM 2286 C CD2 . TYR A 1 293 ? 12.615 29.869 59.198 1.00 5.75 ? 375 TYR A CD2 1 ATOM 2287 C CE1 . TYR A 1 293 ? 15.111 28.824 59.743 1.00 6.77 ? 375 TYR A CE1 1 ATOM 2288 C CE2 . TYR A 1 293 ? 13.531 29.713 58.177 1.00 5.67 ? 375 TYR A CE2 1 ATOM 2289 C CZ . TYR A 1 293 ? 14.775 29.188 58.458 1.00 5.69 ? 375 TYR A CZ 1 ATOM 2290 O OH . TYR A 1 293 ? 15.693 29.032 57.446 1.00 8.54 ? 375 TYR A OH 1 ATOM 2291 N N . GLU A 1 294 ? 12.164 32.849 60.643 1.00 5.65 ? 376 GLU A N 1 ATOM 2292 C CA . GLU A 1 294 ? 11.594 33.907 59.826 1.00 5.33 ? 376 GLU A CA 1 ATOM 2293 C C . GLU A 1 294 ? 12.202 33.913 58.434 1.00 6.05 ? 376 GLU A C 1 ATOM 2294 O O . GLU A 1 294 ? 13.336 33.468 58.235 1.00 6.04 ? 376 GLU A O 1 ATOM 2295 C CB . GLU A 1 294 ? 11.803 35.275 60.486 1.00 8.23 ? 376 GLU A CB 1 ATOM 2296 C CG . GLU A 1 294 ? 13.262 35.657 60.703 1.00 9.28 ? 376 GLU A CG 1 ATOM 2297 C CD . GLU A 1 294 ? 13.409 37.025 61.342 1.00 12.58 ? 376 GLU A CD 1 ATOM 2298 O OE1 . GLU A 1 294 ? 12.372 37.662 61.633 1.00 10.43 ? 376 GLU A OE1 1 ATOM 2299 O OE2 . GLU A 1 294 ? 14.559 37.458 61.554 1.00 9.74 ? 376 GLU A OE2 1 ATOM 2300 N N . MET A 1 295 ? 11.431 34.420 57.479 1.00 8.09 ? 377 MET A N 1 ATOM 2301 C CA . MET A 1 295 ? 11.916 34.668 56.129 1.00 8.15 ? 377 MET A CA 1 ATOM 2302 C C . MET A 1 295 ? 12.012 36.172 55.935 1.00 8.10 ? 377 MET A C 1 ATOM 2303 O O . MET A 1 295 ? 11.114 36.911 56.339 1.00 7.93 ? 377 MET A O 1 ATOM 2304 C CB . MET A 1 295 ? 10.954 34.085 55.092 1.00 6.77 ? 377 MET A CB 1 ATOM 2305 C CG . MET A 1 295 ? 10.810 32.567 55.144 1.00 5.56 ? 377 MET A CG 1 ATOM 2306 S SD . MET A 1 295 ? 12.380 31.715 54.923 1.00 7.84 ? 377 MET A SD 1 ATOM 2307 C CE . MET A 1 295 ? 12.857 32.287 53.294 1.00 10.11 ? 377 MET A CE 1 ATOM 2308 N N . LEU A 1 296 ? 13.099 36.620 55.314 1.00 8.32 ? 378 LEU A N 1 ATOM 2309 C CA . LEU A 1 296 ? 13.309 38.042 55.050 1.00 9.83 ? 378 LEU A CA 1 ATOM 2310 C C . LEU A 1 296 ? 13.629 38.275 53.578 1.00 9.43 ? 378 LEU A C 1 ATOM 2311 O O . LEU A 1 296 ? 14.496 37.605 53.010 1.00 7.75 ? 378 LEU A O 1 ATOM 2312 C CB . LEU A 1 296 ? 14.447 38.579 55.921 1.00 6.24 ? 378 LEU A CB 1 ATOM 2313 C CG . LEU A 1 296 ? 14.214 38.529 57.432 1.00 10.19 ? 378 LEU A CG 1 ATOM 2314 C CD1 . LEU A 1 296 ? 15.494 38.811 58.199 1.00 10.14 ? 378 LEU A CD1 1 ATOM 2315 C CD2 . LEU A 1 296 ? 13.123 39.515 57.828 1.00 10.86 ? 378 LEU A CD2 1 ATOM 2316 N N . LYS A 1 297 ? 12.925 39.221 52.965 1.00 5.42 ? 379 LYS A N 1 ATOM 2317 C CA . LYS A 1 297 ? 13.177 39.592 51.578 1.00 7.78 ? 379 LYS A CA 1 ATOM 2318 C C . LYS A 1 297 ? 14.310 40.603 51.582 1.00 8.73 ? 379 LYS A C 1 ATOM 2319 O O . LYS A 1 297 ? 14.149 41.712 52.075 1.00 9.99 ? 379 LYS A O 1 ATOM 2320 C CB . LYS A 1 297 ? 11.924 40.218 50.961 1.00 6.18 ? 379 LYS A CB 1 ATOM 2321 C CG . LYS A 1 297 ? 12.046 40.534 49.475 1.00 8.37 ? 379 LYS A CG 1 ATOM 2322 C CD . LYS A 1 297 ? 10.780 41.201 48.944 1.00 10.34 ? 379 LYS A CD 1 ATOM 2323 C CE . LYS A 1 297 ? 10.883 41.477 47.449 1.00 12.51 ? 379 LYS A CE 1 ATOM 2324 N NZ . LYS A 1 297 ? 9.671 42.179 46.924 1.00 11.37 ? 379 LYS A NZ 1 ATOM 2325 N N . VAL A 1 298 ? 15.463 40.208 51.050 1.00 6.45 ? 380 VAL A N 1 ATOM 2326 C CA . VAL A 1 298 ? 16.662 41.037 51.096 1.00 8.42 ? 380 VAL A CA 1 ATOM 2327 C C . VAL A 1 298 ? 17.223 41.145 49.680 1.00 8.80 ? 380 VAL A C 1 ATOM 2328 O O . VAL A 1 298 ? 17.967 40.272 49.240 1.00 8.87 ? 380 VAL A O 1 ATOM 2329 C CB . VAL A 1 298 ? 17.724 40.428 52.038 1.00 8.39 ? 380 VAL A CB 1 ATOM 2330 C CG1 . VAL A 1 298 ? 18.950 41.330 52.128 1.00 9.14 ? 380 VAL A CG1 1 ATOM 2331 C CG2 . VAL A 1 298 ? 17.151 40.203 53.430 1.00 7.91 ? 380 VAL A CG2 1 ATOM 2332 N N . PRO A 1 299 ? 16.841 42.208 48.950 1.00 12.23 ? 381 PRO A N 1 ATOM 2333 C CA . PRO A 1 299 ? 17.232 42.331 47.539 1.00 12.69 ? 381 PRO A CA 1 ATOM 2334 C C . PRO A 1 299 ? 18.739 42.245 47.314 1.00 10.55 ? 381 PRO A C 1 ATOM 2335 O O . PRO A 1 299 ? 19.512 42.932 47.991 1.00 10.96 ? 381 PRO A O 1 ATOM 2336 C CB . PRO A 1 299 ? 16.697 43.712 47.150 1.00 15.94 ? 381 PRO A CB 1 ATOM 2337 C CG . PRO A 1 299 ? 15.517 43.907 48.051 1.00 11.86 ? 381 PRO A CG 1 ATOM 2338 C CD . PRO A 1 299 ? 15.924 43.287 49.363 1.00 10.32 ? 381 PRO A CD 1 ATOM 2339 N N . ASN A 1 300 ? 19.140 41.376 46.389 1.00 10.89 ? 382 ASN A N 1 ATOM 2340 C CA . ASN A 1 300 ? 20.545 41.197 46.044 1.00 9.85 ? 382 ASN A CA 1 ATOM 2341 C C . ASN A 1 300 ? 21.435 40.840 47.233 1.00 8.70 ? 382 ASN A C 1 ATOM 2342 O O . ASN A 1 300 ? 22.598 41.239 47.285 1.00 10.47 ? 382 ASN A O 1 ATOM 2343 C CB . ASN A 1 300 ? 21.075 42.452 45.339 1.00 10.00 ? 382 ASN A CB 1 ATOM 2344 C CG . ASN A 1 300 ? 20.311 42.769 44.068 1.00 20.38 ? 382 ASN A CG 1 ATOM 2345 O OD1 . ASN A 1 300 ? 20.148 41.913 43.204 1.00 24.10 ? 382 ASN A OD1 1 ATOM 2346 N ND2 . ASN A 1 300 ? 19.831 43.999 43.954 1.00 25.44 ? 382 ASN A ND2 1 ATOM 2347 N N . ALA A 1 301 ? 20.889 40.081 48.181 1.00 10.10 ? 383 ALA A N 1 ATOM 2348 C CA . ALA A 1 301 ? 21.637 39.685 49.373 1.00 7.39 ? 383 ALA A CA 1 ATOM 2349 C C . ALA A 1 301 ? 22.969 39.026 49.026 1.00 6.98 ? 383 ALA A C 1 ATOM 2350 O O . ALA A 1 301 ? 23.959 39.206 49.728 1.00 7.77 ? 383 ALA A O 1 ATOM 2351 C CB . ALA A 1 301 ? 20.796 38.753 50.250 1.00 8.88 ? 383 ALA A CB 1 ATOM 2352 N N . LEU A 1 302 ? 22.994 38.261 47.940 1.00 8.30 ? 384 LEU A N 1 ATOM 2353 C CA . LEU A 1 302 ? 24.210 37.545 47.571 1.00 7.76 ? 384 LEU A CA 1 ATOM 2354 C C . LEU A 1 302 ? 25.372 38.492 47.273 1.00 9.05 ? 384 LEU A C 1 ATOM 2355 O O . LEU A 1 302 ? 26.507 38.220 47.654 1.00 9.64 ? 384 LEU A O 1 ATOM 2356 C CB . LEU A 1 302 ? 23.958 36.620 46.374 1.00 8.34 ? 384 LEU A CB 1 ATOM 2357 C CG . LEU A 1 302 ? 25.202 35.901 45.843 1.00 8.24 ? 384 LEU A CG 1 ATOM 2358 C CD1 . LEU A 1 302 ? 25.825 35.011 46.914 1.00 12.30 ? 384 LEU A CD1 1 ATOM 2359 C CD2 . LEU A 1 302 ? 24.879 35.097 44.592 1.00 14.95 ? 384 LEU A CD2 1 ATOM 2360 N N . THR A 1 303 ? 25.076 39.616 46.624 1.00 11.33 ? 385 THR A N 1 ATOM 2361 C CA . THR A 1 303 ? 26.123 40.465 46.053 1.00 12.56 ? 385 THR A CA 1 ATOM 2362 C C . THR A 1 303 ? 26.253 41.855 46.680 1.00 11.77 ? 385 THR A C 1 ATOM 2363 O O . THR A 1 303 ? 27.226 42.563 46.410 1.00 15.54 ? 385 THR A O 1 ATOM 2364 C CB . THR A 1 303 ? 25.903 40.648 44.544 1.00 12.52 ? 385 THR A CB 1 ATOM 2365 O OG1 . THR A 1 303 ? 24.608 41.217 44.320 1.00 11.34 ? 385 THR A OG1 1 ATOM 2366 C CG2 . THR A 1 303 ? 25.994 39.308 43.826 1.00 14.80 ? 385 THR A CG2 1 ATOM 2367 N N . ASP A 1 304 ? 25.278 42.242 47.503 1.00 10.88 ? 386 ASP A N 1 ATOM 2368 C CA . ASP A 1 304 ? 25.218 43.591 48.073 1.00 9.83 ? 386 ASP A CA 1 ATOM 2369 C C . ASP A 1 304 ? 25.558 43.546 49.561 1.00 9.31 ? 386 ASP A C 1 ATOM 2370 O O . ASP A 1 304 ? 24.743 43.103 50.371 1.00 13.37 ? 386 ASP A O 1 ATOM 2371 C CB . ASP A 1 304 ? 23.810 44.176 47.867 1.00 9.48 ? 386 ASP A CB 1 ATOM 2372 C CG . ASP A 1 304 ? 23.673 45.616 48.354 1.00 14.81 ? 386 ASP A CG 1 ATOM 2373 O OD1 . ASP A 1 304 ? 24.612 46.158 48.979 1.00 11.80 ? 386 ASP A OD1 1 ATOM 2374 O OD2 . ASP A 1 304 ? 22.597 46.209 48.111 1.00 15.39 ? 386 ASP A OD2 1 ATOM 2375 N N . ASP A 1 305 ? 26.750 44.015 49.928 1.00 11.22 ? 387 ASP A N 1 ATOM 2376 C CA . ASP A 1 305 ? 27.171 43.945 51.328 1.00 11.04 ? 387 ASP A CA 1 ATOM 2377 C C . ASP A 1 305 ? 26.511 44.984 52.241 1.00 9.23 ? 387 ASP A C 1 ATOM 2378 O O . ASP A 1 305 ? 26.852 45.080 53.419 1.00 10.42 ? 387 ASP A O 1 ATOM 2379 C CB . ASP A 1 305 ? 28.706 43.950 51.471 1.00 10.93 ? 387 ASP A CB 1 ATOM 2380 C CG . ASP A 1 305 ? 29.349 45.276 51.073 1.00 18.59 ? 387 ASP A CG 1 ATOM 2381 O OD1 . ASP A 1 305 ? 28.631 46.263 50.815 1.00 14.76 ? 387 ASP A OD1 1 ATOM 2382 O OD2 . ASP A 1 305 ? 30.599 45.326 51.039 1.00 14.37 ? 387 ASP A OD2 1 ATOM 2383 N N . ARG A 1 306 ? 25.558 45.745 51.701 1.00 10.68 ? 388 ARG A N 1 ATOM 2384 C CA . ARG A 1 306 ? 24.788 46.699 52.502 1.00 12.40 ? 388 ARG A CA 1 ATOM 2385 C C . ARG A 1 306 ? 23.302 46.335 52.579 1.00 14.65 ? 388 ARG A C 1 ATOM 2386 O O . ARG A 1 306 ? 22.525 47.029 53.240 1.00 11.76 ? 388 ARG A O 1 ATOM 2387 C CB . ARG A 1 306 ? 24.917 48.115 51.924 1.00 14.44 ? 388 ARG A CB 1 ATOM 2388 C CG . ARG A 1 306 ? 26.329 48.523 51.548 1.00 15.64 ? 388 ARG A CG 1 ATOM 2389 C CD . ARG A 1 306 ? 27.206 48.666 52.778 1.00 14.52 ? 388 ARG A CD 1 ATOM 2390 N NE . ARG A 1 306 ? 28.588 48.950 52.404 1.00 19.35 ? 388 ARG A NE 1 ATOM 2391 C CZ . ARG A 1 306 ? 29.122 50.167 52.378 1.00 22.61 ? 388 ARG A CZ 1 ATOM 2392 N NH1 . ARG A 1 306 ? 28.397 51.224 52.720 1.00 21.83 ? 388 ARG A NH1 1 ATOM 2393 N NH2 . ARG A 1 306 ? 30.388 50.325 52.017 1.00 26.85 ? 388 ARG A NH2 1 ATOM 2394 N N . SER A 1 307 ? 22.911 45.250 51.911 1.00 12.41 ? 389 SER A N 1 ATOM 2395 C CA . SER A 1 307 ? 21.492 44.924 51.724 1.00 9.63 ? 389 SER A CA 1 ATOM 2396 C C . SER A 1 307 ? 20.710 44.636 53.013 1.00 11.84 ? 389 SER A C 1 ATOM 2397 O O . SER A 1 307 ? 21.177 43.916 53.899 1.00 11.72 ? 389 SER A O 1 ATOM 2398 C CB . SER A 1 307 ? 21.342 43.759 50.743 1.00 7.54 ? 389 SER A CB 1 ATOM 2399 O OG . SER A 1 307 ? 22.158 42.673 51.141 1.00 8.68 ? 389 SER A OG 1 ATOM 2400 N N . LYS A 1 308 ? 19.505 45.195 53.092 1.00 9.89 ? 390 LYS A N 1 ATOM 2401 C CA . LYS A 1 308 ? 18.645 45.069 54.269 1.00 14.02 ? 390 LYS A CA 1 ATOM 2402 C C . LYS A 1 308 ? 17.257 44.541 53.883 1.00 8.31 ? 390 LYS A C 1 ATOM 2403 O O . LYS A 1 308 ? 16.897 44.552 52.708 1.00 10.63 ? 390 LYS A O 1 ATOM 2404 C CB . LYS A 1 308 ? 18.530 46.428 54.969 1.00 17.46 ? 390 LYS A CB 1 ATOM 2405 C CG . LYS A 1 308 ? 19.821 46.909 55.621 1.00 18.85 ? 390 LYS A CG 1 ATOM 2406 C CD . LYS A 1 308 ? 20.311 45.910 56.658 1.00 14.43 ? 390 LYS A CD 1 ATOM 2407 C CE . LYS A 1 308 ? 21.533 46.429 57.405 1.00 27.06 ? 390 LYS A CE 1 ATOM 2408 N NZ . LYS A 1 308 ? 21.193 47.631 58.214 1.00 24.34 ? 390 LYS A NZ 1 ATOM 2409 N N . PRO A 1 309 ? 16.465 44.076 54.868 1.00 10.04 ? 391 PRO A N 1 ATOM 2410 C CA . PRO A 1 309 ? 15.151 43.534 54.500 1.00 10.23 ? 391 PRO A CA 1 ATOM 2411 C C . PRO A 1 309 ? 14.151 44.613 54.086 1.00 12.17 ? 391 PRO A C 1 ATOM 2412 O O . PRO A 1 309 ? 14.189 45.725 54.623 1.00 11.57 ? 391 PRO A O 1 ATOM 2413 C CB . PRO A 1 309 ? 14.667 42.863 55.797 1.00 10.97 ? 391 PRO A CB 1 ATOM 2414 C CG . PRO A 1 309 ? 15.889 42.681 56.638 1.00 9.36 ? 391 PRO A CG 1 ATOM 2415 C CD . PRO A 1 309 ? 16.765 43.855 56.293 1.00 11.24 ? 391 PRO A CD 1 ATOM 2416 N N . ILE A 1 310 ? 13.268 44.282 53.148 1.00 7.72 ? 392 ILE A N 1 ATOM 2417 C CA . ILE A 1 310 ? 12.180 45.181 52.761 1.00 8.84 ? 392 ILE A CA 1 ATOM 2418 C C . ILE A 1 310 ? 10.806 44.543 52.987 1.00 12.08 ? 392 ILE A C 1 ATOM 2419 O O . ILE A 1 310 ? 9.768 45.181 52.784 1.00 11.84 ? 392 ILE A O 1 ATOM 2420 C CB . ILE A 1 310 ? 12.305 45.659 51.296 1.00 10.30 ? 392 ILE A CB 1 ATOM 2421 C CG1 . ILE A 1 310 ? 12.083 44.502 50.316 1.00 11.81 ? 392 ILE A CG1 1 ATOM 2422 C CG2 . ILE A 1 310 ? 13.657 46.344 51.065 1.00 12.40 ? 392 ILE A CG2 1 ATOM 2423 C CD1 . ILE A 1 310 ? 11.943 44.947 48.865 1.00 12.12 ? 392 ILE A CD1 1 ATOM 2424 N N . GLN A 1 311 ? 10.811 43.283 53.414 1.00 9.04 ? 393 GLN A N 1 ATOM 2425 C CA . GLN A 1 311 ? 9.579 42.541 53.674 1.00 7.97 ? 393 GLN A CA 1 ATOM 2426 C C . GLN A 1 311 ? 9.985 41.282 54.430 1.00 9.54 ? 393 GLN A C 1 ATOM 2427 O O . GLN A 1 311 ? 11.140 40.861 54.353 1.00 8.37 ? 393 GLN A O 1 ATOM 2428 C CB . GLN A 1 311 ? 8.891 42.167 52.356 1.00 11.19 ? 393 GLN A CB 1 ATOM 2429 C CG . GLN A 1 311 ? 7.425 41.737 52.493 1.00 7.79 ? 393 GLN A CG 1 ATOM 2430 C CD . GLN A 1 311 ? 6.849 41.174 51.200 1.00 11.25 ? 393 GLN A CD 1 ATOM 2431 O OE1 . GLN A 1 311 ? 7.217 41.594 50.097 1.00 10.44 ? 393 GLN A OE1 1 ATOM 2432 N NE2 . GLN A 1 311 ? 5.945 40.211 51.330 1.00 6.74 ? 393 GLN A NE2 1 ATOM 2433 N N . GLY A 1 312 ? 9.058 40.685 55.173 1.00 8.63 ? 394 GLY A N 1 ATOM 2434 C CA . GLY A 1 312 ? 9.367 39.458 55.888 1.00 7.77 ? 394 GLY A CA 1 ATOM 2435 C C . GLY A 1 312 ? 8.142 38.622 56.214 1.00 9.52 ? 394 GLY A C 1 ATOM 2436 O O . GLY A 1 312 ? 7.011 39.022 55.941 1.00 8.78 ? 394 GLY A O 1 ATOM 2437 N N . GLN A 1 313 ? 8.367 37.449 56.799 1.00 7.35 ? 395 GLN A N 1 ATOM 2438 C CA . GLN A 1 313 ? 7.264 36.613 57.270 1.00 6.67 ? 395 GLN A CA 1 ATOM 2439 C C . GLN A 1 313 ? 7.751 35.738 58.413 1.00 9.51 ? 395 GLN A C 1 ATOM 2440 O O . GLN A 1 313 ? 8.777 35.062 58.300 1.00 8.27 ? 395 GLN A O 1 ATOM 2441 C CB . GLN A 1 313 ? 6.687 35.755 56.135 1.00 7.33 ? 395 GLN A CB 1 ATOM 2442 C CG . GLN A 1 313 ? 5.415 34.992 56.528 1.00 5.80 ? 395 GLN A CG 1 ATOM 2443 C CD . GLN A 1 313 ? 4.748 34.304 55.351 1.00 8.67 ? 395 GLN A CD 1 ATOM 2444 O OE1 . GLN A 1 313 ? 4.740 34.826 54.237 1.00 9.07 ? 395 GLN A OE1 1 ATOM 2445 N NE2 . GLN A 1 313 ? 4.174 33.122 55.597 1.00 6.14 ? 395 GLN A NE2 1 ATOM 2446 N N . THR A 1 314 ? 7.031 35.765 59.530 1.00 9.25 ? 396 THR A N 1 ATOM 2447 C CA . THR A 1 314 ? 7.379 34.887 60.641 1.00 9.74 ? 396 THR A CA 1 ATOM 2448 C C . THR A 1 314 ? 6.812 33.505 60.343 1.00 8.79 ? 396 THR A C 1 ATOM 2449 O O . THR A 1 314 ? 5.664 33.384 59.914 1.00 9.78 ? 396 THR A O 1 ATOM 2450 C CB . THR A 1 314 ? 6.853 35.415 61.989 1.00 14.24 ? 396 THR A CB 1 ATOM 2451 O OG1 . THR A 1 314 ? 7.541 36.628 62.327 1.00 13.47 ? 396 THR A OG1 1 ATOM 2452 C CG2 . THR A 1 314 ? 7.099 34.388 63.097 1.00 10.39 ? 396 THR A CG2 1 ATOM 2453 N N . ILE A 1 315 ? 7.628 32.473 60.547 1.00 7.17 ? 397 ILE A N 1 ATOM 2454 C CA . ILE A 1 315 ? 7.211 31.092 60.307 1.00 5.13 ? 397 ILE A CA 1 ATOM 2455 C C . ILE A 1 315 ? 6.996 30.376 61.639 1.00 5.89 ? 397 ILE A C 1 ATOM 2456 O O . ILE A 1 315 ? 6.007 29.654 61.823 1.00 5.88 ? 397 ILE A O 1 ATOM 2457 C CB . ILE A 1 315 ? 8.283 30.317 59.505 1.00 5.94 ? 397 ILE A CB 1 ATOM 2458 C CG1 . ILE A 1 315 ? 8.759 31.128 58.287 1.00 5.03 ? 397 ILE A CG1 1 ATOM 2459 C CG2 . ILE A 1 315 ? 7.757 28.946 59.097 1.00 6.50 ? 397 ILE A CG2 1 ATOM 2460 C CD1 . ILE A 1 315 ? 7.651 31.490 57.293 1.00 8.55 ? 397 ILE A CD1 1 ATOM 2461 N N . VAL A 1 316 ? 7.943 30.565 62.556 1.00 5.40 ? 398 VAL A N 1 ATOM 2462 C CA . VAL A 1 316 ? 7.867 29.978 63.894 1.00 5.89 ? 398 VAL A CA 1 ATOM 2463 C C . VAL A 1 316 ? 8.213 31.063 64.913 1.00 7.39 ? 398 VAL A C 1 ATOM 2464 O O . VAL A 1 316 ? 9.209 31.770 64.749 1.00 7.26 ? 398 VAL A O 1 ATOM 2465 C CB . VAL A 1 316 ? 8.843 28.790 64.043 1.00 5.40 ? 398 VAL A CB 1 ATOM 2466 C CG1 . VAL A 1 316 ? 8.733 28.182 65.432 1.00 6.89 ? 398 VAL A CG1 1 ATOM 2467 C CG2 . VAL A 1 316 ? 8.566 27.725 62.981 1.00 8.15 ? 398 VAL A CG2 1 ATOM 2468 N N . LEU A 1 317 ? 7.381 31.219 65.942 1.00 5.60 ? 399 LEU A N 1 ATOM 2469 C CA . LEU A 1 317 ? 7.630 32.235 66.969 1.00 9.01 ? 399 LEU A CA 1 ATOM 2470 C C . LEU A 1 317 ? 8.932 31.955 67.704 1.00 8.97 ? 399 LEU A C 1 ATOM 2471 O O . LEU A 1 317 ? 9.331 30.801 67.851 1.00 7.62 ? 399 LEU A O 1 ATOM 2472 C CB . LEU A 1 317 ? 6.486 32.281 67.985 1.00 10.69 ? 399 LEU A CB 1 ATOM 2473 C CG . LEU A 1 317 ? 5.112 32.702 67.460 1.00 10.84 ? 399 LEU A CG 1 ATOM 2474 C CD1 . LEU A 1 317 ? 4.064 32.639 68.565 1.00 13.63 ? 399 LEU A CD1 1 ATOM 2475 C CD2 . LEU A 1 317 ? 5.170 34.093 66.846 1.00 12.14 ? 399 LEU A CD2 1 ATOM 2476 N N . ASN A 1 318 ? 9.585 33.010 68.187 1.00 8.29 ? 400 ASN A N 1 ATOM 2477 C CA . ASN A 1 318 ? 10.833 32.843 68.925 1.00 9.96 ? 400 ASN A CA 1 ATOM 2478 C C . ASN A 1 318 ? 10.668 31.958 70.160 1.00 11.67 ? 400 ASN A C 1 ATOM 2479 O O . ASN A 1 318 ? 11.605 31.290 70.584 1.00 13.61 ? 400 ASN A O 1 ATOM 2480 C CB . ASN A 1 318 ? 11.415 34.198 69.324 1.00 12.63 ? 400 ASN A CB 1 ATOM 2481 C CG . ASN A 1 318 ? 12.872 34.100 69.745 1.00 17.63 ? 400 ASN A CG 1 ATOM 2482 O OD1 . ASN A 1 318 ? 13.619 33.254 69.249 1.00 18.05 ? 400 ASN A OD1 1 ATOM 2483 N ND2 . ASN A 1 318 ? 13.278 34.955 70.671 1.00 27.10 ? 400 ASN A ND2 1 ATOM 2484 N N . ALA A 1 319 ? 9.464 31.946 70.721 1.00 10.33 ? 401 ALA A N 1 ATOM 2485 C CA . ALA A 1 319 ? 9.159 31.114 71.884 1.00 11.56 ? 401 ALA A CA 1 ATOM 2486 C C . ALA A 1 319 ? 9.175 29.614 71.587 1.00 16.56 ? 401 ALA A C 1 ATOM 2487 O O . ALA A 1 319 ? 9.178 28.797 72.511 1.00 14.71 ? 401 ALA A O 1 ATOM 2488 C CB . ALA A 1 319 ? 7.815 31.508 72.466 1.00 14.59 ? 401 ALA A CB 1 ATOM 2489 N N . ASP A 1 320 ? 9.165 29.248 70.307 1.00 8.70 ? 402 ASP A N 1 ATOM 2490 C CA . ASP A 1 320 ? 9.109 27.836 69.925 1.00 7.21 ? 402 ASP A CA 1 ATOM 2491 C C . ASP A 1 320 ? 10.425 27.351 69.317 1.00 9.70 ? 402 ASP A C 1 ATOM 2492 O O . ASP A 1 320 ? 11.112 28.100 68.622 1.00 8.94 ? 402 ASP A O 1 ATOM 2493 C CB . ASP A 1 320 ? 7.953 27.594 68.952 1.00 7.85 ? 402 ASP A CB 1 ATOM 2494 C CG . ASP A 1 320 ? 6.598 27.748 69.612 1.00 14.10 ? 402 ASP A CG 1 ATOM 2495 O OD1 . ASP A 1 320 ? 6.352 27.057 70.623 1.00 15.20 ? 402 ASP A OD1 1 ATOM 2496 O OD2 . ASP A 1 320 ? 5.786 28.569 69.133 1.00 9.85 ? 402 ASP A OD2 1 ATOM 2497 N N . TRP A 1 321 ? 10.767 26.091 69.570 1.00 8.19 ? 403 TRP A N 1 ATOM 2498 C CA . TRP A 1 321 ? 12.032 25.542 69.086 1.00 7.61 ? 403 TRP A CA 1 ATOM 2499 C C . TRP A 1 321 ? 11.993 25.305 67.584 1.00 9.64 ? 403 TRP A C 1 ATOM 2500 O O . TRP A 1 321 ? 10.993 24.815 67.049 1.00 8.74 ? 403 TRP A O 1 ATOM 2501 C CB . TRP A 1 321 ? 12.364 24.231 69.807 1.00 8.89 ? 403 TRP A CB 1 ATOM 2502 C CG . TRP A 1 321 ? 12.482 24.398 71.284 1.00 9.78 ? 403 TRP A CG 1 ATOM 2503 C CD1 . TRP A 1 321 ? 11.684 23.839 72.248 1.00 11.92 ? 403 TRP A CD1 1 ATOM 2504 C CD2 . TRP A 1 321 ? 13.444 25.199 71.975 1.00 9.72 ? 403 TRP A CD2 1 ATOM 2505 N NE1 . TRP A 1 321 ? 12.102 24.241 73.494 1.00 11.94 ? 403 TRP A NE1 1 ATOM 2506 C CE2 . TRP A 1 321 ? 13.178 25.078 73.354 1.00 10.90 ? 403 TRP A CE2 1 ATOM 2507 C CE3 . TRP A 1 321 ? 14.506 26.012 71.560 1.00 12.68 ? 403 TRP A CE3 1 ATOM 2508 C CZ2 . TRP A 1 321 ? 13.938 25.736 74.320 1.00 13.54 ? 403 TRP A CZ2 1 ATOM 2509 C CZ3 . TRP A 1 321 ? 15.259 26.664 72.522 1.00 16.03 ? 403 TRP A CZ3 1 ATOM 2510 C CH2 . TRP A 1 321 ? 14.969 26.523 73.884 1.00 13.81 ? 403 TRP A CH2 1 ATOM 2511 N N . SER A 1 322 ? 13.079 25.665 66.904 1.00 5.71 ? 404 SER A N 1 ATOM 2512 C CA . SER A 1 322 ? 13.230 25.313 65.498 1.00 2.71 ? 404 SER A CA 1 ATOM 2513 C C . SER A 1 322 ? 14.394 24.337 65.349 1.00 5.99 ? 404 SER A C 1 ATOM 2514 O O . SER A 1 322 ? 14.508 23.379 66.119 1.00 6.94 ? 404 SER A O 1 ATOM 2515 C CB . SER A 1 322 ? 13.404 26.555 64.617 1.00 5.86 ? 404 SER A CB 1 ATOM 2516 O OG . SER A 1 322 ? 14.465 27.378 65.058 1.00 5.99 ? 404 SER A OG 1 ATOM 2517 N N . GLY A 1 323 ? 15.260 24.575 64.370 1.00 6.00 ? 405 GLY A N 1 ATOM 2518 C CA . GLY A 1 323 ? 16.338 23.645 64.075 1.00 5.58 ? 405 GLY A CA 1 ATOM 2519 C C . GLY A 1 323 ? 16.816 23.801 62.646 1.00 5.59 ? 405 GLY A C 1 ATOM 2520 O O . GLY A 1 323 ? 16.826 24.910 62.120 1.00 7.65 ? 405 GLY A O 1 ATOM 2521 N N . TYR A 1 324 ? 17.218 22.695 62.023 1.00 6.52 ? 406 TYR A N 1 ATOM 2522 C CA . TYR A 1 324 ? 17.687 22.719 60.638 1.00 5.61 ? 406 TYR A CA 1 ATOM 2523 C C . TYR A 1 324 ? 16.606 23.238 59.690 1.00 6.18 ? 406 TYR A C 1 ATOM 2524 O O . TYR A 1 324 ? 15.408 23.075 59.940 1.00 6.41 ? 406 TYR A O 1 ATOM 2525 C CB . TYR A 1 324 ? 18.106 21.313 60.192 1.00 6.11 ? 406 TYR A CB 1 ATOM 2526 C CG . TYR A 1 324 ? 19.484 20.881 60.641 1.00 6.80 ? 406 TYR A CG 1 ATOM 2527 C CD1 . TYR A 1 324 ? 20.139 21.525 61.687 1.00 9.17 ? 406 TYR A CD1 1 ATOM 2528 C CD2 . TYR A 1 324 ? 20.139 19.837 59.999 1.00 5.11 ? 406 TYR A CD2 1 ATOM 2529 C CE1 . TYR A 1 324 ? 21.406 21.126 62.088 1.00 7.86 ? 406 TYR A CE1 1 ATOM 2530 C CE2 . TYR A 1 324 ? 21.404 19.435 60.388 1.00 6.99 ? 406 TYR A CE2 1 ATOM 2531 C CZ . TYR A 1 324 ? 22.031 20.084 61.429 1.00 7.25 ? 406 TYR A CZ 1 ATOM 2532 O OH . TYR A 1 324 ? 23.287 19.676 61.815 1.00 8.60 ? 406 TYR A OH 1 ATOM 2533 N N . SER A 1 325 ? 17.029 23.874 58.603 1.00 4.64 ? 407 SER A N 1 ATOM 2534 C CA . SER A 1 325 ? 16.107 24.267 57.545 1.00 3.96 ? 407 SER A CA 1 ATOM 2535 C C . SER A 1 325 ? 16.807 24.073 56.206 1.00 5.76 ? 407 SER A C 1 ATOM 2536 O O . SER A 1 325 ? 18.038 24.121 56.132 1.00 6.26 ? 407 SER A O 1 ATOM 2537 C CB . SER A 1 325 ? 15.638 25.713 57.716 1.00 5.72 ? 407 SER A CB 1 ATOM 2538 O OG . SER A 1 325 ? 16.737 26.610 57.777 1.00 5.78 ? 407 SER A OG 1 ATOM 2539 N N . GLY A 1 326 ? 16.035 23.834 55.153 1.00 3.49 ? 408 GLY A N 1 ATOM 2540 C CA . GLY A 1 326 ? 16.630 23.567 53.854 1.00 5.19 ? 408 GLY A CA 1 ATOM 2541 C C . GLY A 1 326 ? 15.654 23.779 52.718 1.00 5.85 ? 408 GLY A C 1 ATOM 2542 O O . GLY A 1 326 ? 14.444 23.911 52.935 1.00 5.22 ? 408 GLY A O 1 ATOM 2543 N N . SER A 1 327 ? 16.188 23.804 51.501 1.00 5.34 ? 409 SER A N 1 ATOM 2544 C CA . SER A 1 327 ? 15.407 24.104 50.307 1.00 6.55 ? 409 SER A CA 1 ATOM 2545 C C . SER A 1 327 ? 15.041 22.845 49.529 1.00 6.58 ? 409 SER A C 1 ATOM 2546 O O . SER A 1 327 ? 15.760 21.849 49.564 1.00 6.78 ? 409 SER A O 1 ATOM 2547 C CB . SER A 1 327 ? 16.207 25.043 49.403 1.00 7.20 ? 409 SER A CB 1 ATOM 2548 O OG . SER A 1 327 ? 17.503 24.508 49.156 1.00 7.03 ? 409 SER A OG 1 ATOM 2549 N N . PHE A 1 328 ? 13.908 22.904 48.835 1.00 6.26 ? 410 PHE A N 1 ATOM 2550 C CA . PHE A 1 328 ? 13.522 21.898 47.853 1.00 7.25 ? 410 PHE A CA 1 ATOM 2551 C C . PHE A 1 328 ? 12.506 22.555 46.934 1.00 6.28 ? 410 PHE A C 1 ATOM 2552 O O . PHE A 1 328 ? 11.904 23.566 47.297 1.00 6.68 ? 410 PHE A O 1 ATOM 2553 C CB . PHE A 1 328 ? 12.897 20.665 48.523 1.00 6.59 ? 410 PHE A CB 1 ATOM 2554 C CG . PHE A 1 328 ? 11.547 20.922 49.143 1.00 6.50 ? 410 PHE A CG 1 ATOM 2555 C CD1 . PHE A 1 328 ? 11.449 21.476 50.412 1.00 7.38 ? 410 PHE A CD1 1 ATOM 2556 C CD2 . PHE A 1 328 ? 10.380 20.591 48.463 1.00 7.32 ? 410 PHE A CD2 1 ATOM 2557 C CE1 . PHE A 1 328 ? 10.207 21.712 50.990 1.00 8.89 ? 410 PHE A CE1 1 ATOM 2558 C CE2 . PHE A 1 328 ? 9.135 20.824 49.029 1.00 8.63 ? 410 PHE A CE2 1 ATOM 2559 C CZ . PHE A 1 328 ? 9.048 21.378 50.299 1.00 6.55 ? 410 PHE A CZ 1 ATOM 2560 N N . MET A 1 329 ? 12.320 22.002 45.740 1.00 5.94 ? 411 MET A N 1 ATOM 2561 C CA . MET A 1 329 ? 11.240 22.463 44.873 1.00 5.33 ? 411 MET A CA 1 ATOM 2562 C C . MET A 1 329 ? 10.608 21.296 44.135 1.00 6.77 ? 411 MET A C 1 ATOM 2563 O O . MET A 1 329 ? 11.242 20.255 43.947 1.00 7.85 ? 411 MET A O 1 ATOM 2564 C CB . MET A 1 329 ? 11.741 23.520 43.879 1.00 6.56 ? 411 MET A CB 1 ATOM 2565 C CG . MET A 1 329 ? 12.175 24.826 44.536 1.00 6.80 ? 411 MET A CG 1 ATOM 2566 S SD . MET A 1 329 ? 12.365 26.192 43.379 1.00 7.72 ? 411 MET A SD 1 ATOM 2567 C CE . MET A 1 329 ? 13.714 25.580 42.373 1.00 8.43 ? 411 MET A CE 1 ATOM 2568 N N . ASP A 1 330 ? 9.354 21.462 43.723 1.00 6.81 ? 412 ASP A N 1 ATOM 2569 C CA . ASP A 1 330 ? 8.714 20.449 42.899 1.00 7.39 ? 412 ASP A CA 1 ATOM 2570 C C . ASP A 1 330 ? 9.053 20.737 41.445 1.00 7.85 ? 412 ASP A C 1 ATOM 2571 O O . ASP A 1 330 ? 8.359 21.495 40.774 1.00 8.71 ? 412 ASP A O 1 ATOM 2572 C CB . ASP A 1 330 ? 7.198 20.445 43.107 1.00 6.63 ? 412 ASP A CB 1 ATOM 2573 C CG . ASP A 1 330 ? 6.513 19.313 42.369 1.00 11.13 ? 412 ASP A CG 1 ATOM 2574 O OD1 . ASP A 1 330 ? 7.203 18.553 41.653 1.00 8.38 ? 412 ASP A OD1 1 ATOM 2575 O OD2 . ASP A 1 330 ? 5.278 19.184 42.502 1.00 8.49 ? 412 ASP A OD2 1 ATOM 2576 N N . TYR A 1 331 ? 10.119 20.114 40.958 1.00 7.16 ? 413 TYR A N 1 ATOM 2577 C CA . TYR A 1 331 ? 10.596 20.370 39.607 1.00 7.88 ? 413 TYR A CA 1 ATOM 2578 C C . TYR A 1 331 ? 9.657 19.850 38.521 1.00 11.47 ? 413 TYR A C 1 ATOM 2579 O O . TYR A 1 331 ? 9.848 20.142 37.339 1.00 13.21 ? 413 TYR A O 1 ATOM 2580 C CB . TYR A 1 331 ? 12.019 19.820 39.449 1.00 8.01 ? 413 TYR A CB 1 ATOM 2581 C CG . TYR A 1 331 ? 12.980 20.553 40.351 1.00 7.66 ? 413 TYR A CG 1 ATOM 2582 C CD1 . TYR A 1 331 ? 13.528 21.769 39.962 1.00 6.72 ? 413 TYR A CD1 1 ATOM 2583 C CD2 . TYR A 1 331 ? 13.303 20.058 41.612 1.00 6.53 ? 413 TYR A CD2 1 ATOM 2584 C CE1 . TYR A 1 331 ? 14.381 22.460 40.786 1.00 6.88 ? 413 TYR A CE1 1 ATOM 2585 C CE2 . TYR A 1 331 ? 14.160 20.747 42.448 1.00 8.98 ? 413 TYR A CE2 1 ATOM 2586 C CZ . TYR A 1 331 ? 14.701 21.948 42.024 1.00 8.36 ? 413 TYR A CZ 1 ATOM 2587 O OH . TYR A 1 331 ? 15.556 22.653 42.845 1.00 7.91 ? 413 TYR A OH 1 ATOM 2588 N N . TRP A 1 332 ? 8.629 19.109 38.927 1.00 8.20 ? 414 TRP A N 1 ATOM 2589 C CA . TRP A 1 332 ? 7.716 18.479 37.980 1.00 9.40 ? 414 TRP A CA 1 ATOM 2590 C C . TRP A 1 332 ? 6.319 19.093 38.017 1.00 12.05 ? 414 TRP A C 1 ATOM 2591 O O . TRP A 1 332 ? 5.379 18.576 37.411 1.00 15.26 ? 414 TRP A O 1 ATOM 2592 C CB . TRP A 1 332 ? 7.698 16.961 38.205 1.00 7.47 ? 414 TRP A CB 1 ATOM 2593 C CG . TRP A 1 332 ? 9.068 16.385 37.963 1.00 7.34 ? 414 TRP A CG 1 ATOM 2594 C CD1 . TRP A 1 332 ? 9.559 15.910 36.778 1.00 10.03 ? 414 TRP A CD1 1 ATOM 2595 C CD2 . TRP A 1 332 ? 10.143 16.287 38.909 1.00 7.58 ? 414 TRP A CD2 1 ATOM 2596 N NE1 . TRP A 1 332 ? 10.860 15.502 36.934 1.00 10.79 ? 414 TRP A NE1 1 ATOM 2597 C CE2 . TRP A 1 332 ? 11.245 15.721 38.232 1.00 8.81 ? 414 TRP A CE2 1 ATOM 2598 C CE3 . TRP A 1 332 ? 10.275 16.607 40.266 1.00 9.18 ? 414 TRP A CE3 1 ATOM 2599 C CZ2 . TRP A 1 332 ? 12.467 15.475 38.863 1.00 8.56 ? 414 TRP A CZ2 1 ATOM 2600 C CZ3 . TRP A 1 332 ? 11.485 16.365 40.891 1.00 9.04 ? 414 TRP A CZ3 1 ATOM 2601 C CH2 . TRP A 1 332 ? 12.568 15.803 40.189 1.00 9.08 ? 414 TRP A CH2 1 ATOM 2602 N N . ALA A 1 333 ? 6.194 20.218 38.714 1.00 7.48 ? 415 ALA A N 1 ATOM 2603 C CA . ALA A 1 333 ? 4.925 20.936 38.770 1.00 7.85 ? 415 ALA A CA 1 ATOM 2604 C C . ALA A 1 333 ? 4.609 21.624 37.439 1.00 14.33 ? 415 ALA A C 1 ATOM 2605 O O . ALA A 1 333 ? 5.503 21.911 36.644 1.00 16.01 ? 415 ALA A O 1 ATOM 2606 C CB . ALA A 1 333 ? 4.940 21.954 39.902 1.00 8.68 ? 415 ALA A CB 1 ATOM 2607 N N . GLU A 1 334 ? 3.332 21.902 37.208 1.00 13.60 ? 416 GLU A N 1 ATOM 2608 C CA . GLU A 1 334 ? 2.912 22.619 36.009 1.00 19.32 ? 416 GLU A CA 1 ATOM 2609 C C . GLU A 1 334 ? 3.249 24.100 36.132 1.00 19.28 ? 416 GLU A C 1 ATOM 2610 O O . GLU A 1 334 ? 3.500 24.594 37.228 1.00 16.36 ? 416 GLU A O 1 ATOM 2611 C CB . GLU A 1 334 ? 1.406 22.453 35.797 1.00 25.93 ? 416 GLU A CB 1 ATOM 2612 C CG . GLU A 1 334 ? 0.966 21.021 35.553 1.00 31.59 ? 416 GLU A CG 1 ATOM 2613 C CD . GLU A 1 334 ? 1.521 20.468 34.261 1.00 35.25 ? 416 GLU A CD 1 ATOM 2614 O OE1 . GLU A 1 334 ? 0.978 20.805 33.188 1.00 43.70 ? 416 GLU A OE1 1 ATOM 2615 O OE2 . GLU A 1 334 ? 2.509 19.707 34.316 1.00 46.01 ? 416 GLU A OE2 1 ATOM 2616 N N . GLY A 1 335 ? 3.258 24.815 35.011 1.00 19.54 ? 417 GLY A N 1 ATOM 2617 C CA . GLY A 1 335 ? 3.483 26.250 35.059 1.00 18.10 ? 417 GLY A CA 1 ATOM 2618 C C . GLY A 1 335 ? 4.777 26.698 34.411 1.00 15.93 ? 417 GLY A C 1 ATOM 2619 O O . GLY A 1 335 ? 5.511 25.890 33.846 1.00 20.32 ? 417 GLY A O 1 ATOM 2620 N N A ASP A 1 336 ? 5.064 27.992 34.509 0.47 15.13 ? 418 ASP A N 1 ATOM 2621 N N B ASP A 1 336 ? 5.069 27.991 34.500 0.53 15.12 ? 418 ASP A N 1 ATOM 2622 C CA A ASP A 1 336 ? 6.198 28.578 33.801 0.47 16.53 ? 418 ASP A CA 1 ATOM 2623 C CA B ASP A 1 336 ? 6.219 28.547 33.793 0.53 16.51 ? 418 ASP A CA 1 ATOM 2624 C C A ASP A 1 336 ? 7.391 28.875 34.704 0.47 15.37 ? 418 ASP A C 1 ATOM 2625 C C B ASP A 1 336 ? 7.392 28.889 34.706 0.53 15.36 ? 418 ASP A C 1 ATOM 2626 O O A ASP A 1 336 ? 8.434 29.331 34.232 0.47 13.97 ? 418 ASP A O 1 ATOM 2627 O O B ASP A 1 336 ? 8.413 29.400 34.245 0.53 13.95 ? 418 ASP A O 1 ATOM 2628 C CB A ASP A 1 336 ? 5.769 29.861 33.086 0.47 16.65 ? 418 ASP A CB 1 ATOM 2629 C CB B ASP A 1 336 ? 5.805 29.771 32.965 0.53 16.61 ? 418 ASP A CB 1 ATOM 2630 C CG A ASP A 1 336 ? 4.697 29.619 32.046 0.47 22.93 ? 418 ASP A CG 1 ATOM 2631 C CG B ASP A 1 336 ? 5.516 30.999 33.818 0.53 21.78 ? 418 ASP A CG 1 ATOM 2632 O OD1 A ASP A 1 336 ? 4.661 28.509 31.472 0.47 24.10 ? 418 ASP A OD1 1 ATOM 2633 O OD1 B ASP A 1 336 ? 5.387 30.879 35.056 0.53 18.37 ? 418 ASP A OD1 1 ATOM 2634 O OD2 A ASP A 1 336 ? 3.890 30.542 31.804 0.47 25.39 ? 418 ASP A OD2 1 ATOM 2635 O OD2 B ASP A 1 336 ? 5.405 32.099 33.236 0.53 25.56 ? 418 ASP A OD2 1 ATOM 2636 N N . CYS A 1 337 ? 7.239 28.618 35.998 1.00 11.08 ? 419 CYS A N 1 ATOM 2637 C CA . CYS A 1 337 ? 8.299 28.907 36.957 1.00 8.05 ? 419 CYS A CA 1 ATOM 2638 C C . CYS A 1 337 ? 8.348 27.844 38.048 1.00 10.70 ? 419 CYS A C 1 ATOM 2639 O O . CYS A 1 337 ? 7.367 27.129 38.273 1.00 10.18 ? 419 CYS A O 1 ATOM 2640 C CB . CYS A 1 337 ? 8.101 30.294 37.574 1.00 10.65 ? 419 CYS A CB 1 ATOM 2641 S SG . CYS A 1 337 ? 6.496 30.553 38.376 1.00 13.37 ? 419 CYS A SG 1 ATOM 2642 N N . TYR A 1 338 ? 9.500 27.736 38.704 1.00 9.83 ? 420 TYR A N 1 ATOM 2643 C CA . TYR A 1 338 ? 9.671 26.833 39.841 1.00 7.21 ? 420 TYR A CA 1 ATOM 2644 C C . TYR A 1 338 ? 9.287 27.560 41.121 1.00 9.31 ? 420 TYR A C 1 ATOM 2645 O O . TYR A 1 338 ? 9.805 28.644 41.408 1.00 6.97 ? 420 TYR A O 1 ATOM 2646 C CB . TYR A 1 338 ? 11.130 26.387 39.953 1.00 8.24 ? 420 TYR A CB 1 ATOM 2647 C CG . TYR A 1 338 ? 11.630 25.501 38.830 1.00 10.29 ? 420 TYR A CG 1 ATOM 2648 C CD1 . TYR A 1 338 ? 10.837 24.491 38.301 1.00 9.83 ? 420 TYR A CD1 1 ATOM 2649 C CD2 . TYR A 1 338 ? 12.907 25.676 38.305 1.00 10.96 ? 420 TYR A CD2 1 ATOM 2650 C CE1 . TYR A 1 338 ? 11.305 23.674 37.280 1.00 9.04 ? 420 TYR A CE1 1 ATOM 2651 C CE2 . TYR A 1 338 ? 13.381 24.866 37.285 1.00 11.51 ? 420 TYR A CE2 1 ATOM 2652 C CZ . TYR A 1 338 ? 12.577 23.873 36.775 1.00 11.39 ? 420 TYR A CZ 1 ATOM 2653 O OH . TYR A 1 338 ? 13.052 23.069 35.756 1.00 10.53 ? 420 TYR A OH 1 ATOM 2654 N N . ARG A 1 339 ? 8.395 26.954 41.899 1.00 8.54 ? 421 ARG A N 1 ATOM 2655 C CA . ARG A 1 339 ? 7.944 27.544 43.155 1.00 6.79 ? 421 ARG A CA 1 ATOM 2656 C C . ARG A 1 339 ? 8.891 27.173 44.290 1.00 5.93 ? 421 ARG A C 1 ATOM 2657 O O . ARG A 1 339 ? 9.008 26.004 44.660 1.00 7.54 ? 421 ARG A O 1 ATOM 2658 C CB . ARG A 1 339 ? 6.525 27.071 43.464 1.00 7.90 ? 421 ARG A CB 1 ATOM 2659 C CG . ARG A 1 339 ? 5.921 27.623 44.743 1.00 8.53 ? 421 ARG A CG 1 ATOM 2660 C CD . ARG A 1 339 ? 4.560 26.985 45.003 1.00 9.77 ? 421 ARG A CD 1 ATOM 2661 N NE . ARG A 1 339 ? 3.612 27.293 43.935 1.00 8.57 ? 421 ARG A NE 1 ATOM 2662 C CZ . ARG A 1 339 ? 2.362 27.702 44.130 1.00 15.42 ? 421 ARG A CZ 1 ATOM 2663 N NH1 . ARG A 1 339 ? 1.887 27.843 45.361 1.00 8.55 ? 421 ARG A NH1 1 ATOM 2664 N NH2 . ARG A 1 339 ? 1.582 27.965 43.087 1.00 12.16 ? 421 ARG A NH2 1 ATOM 2665 N N . ALA A 1 340 ? 9.570 28.176 44.833 1.00 6.87 ? 422 ALA A N 1 ATOM 2666 C CA . ALA A 1 340 ? 10.491 27.976 45.942 1.00 8.66 ? 422 ALA A CA 1 ATOM 2667 C C . ALA A 1 340 ? 9.781 27.365 47.147 1.00 6.04 ? 422 ALA A C 1 ATOM 2668 O O . ALA A 1 340 ? 8.694 27.806 47.526 1.00 6.92 ? 422 ALA A O 1 ATOM 2669 C CB . ALA A 1 340 ? 11.126 29.296 46.331 1.00 7.76 ? 422 ALA A CB 1 ATOM 2670 N N . CYS A 1 341 ? 10.400 26.352 47.748 1.00 6.01 ? 423 CYS A N 1 ATOM 2671 C CA . CYS A 1 341 ? 9.863 25.758 48.972 1.00 6.92 ? 423 CYS A CA 1 ATOM 2672 C C . CYS A 1 341 ? 10.965 25.568 50.009 1.00 7.13 ? 423 CYS A C 1 ATOM 2673 O O . CYS A 1 341 ? 12.155 25.587 49.681 1.00 5.67 ? 423 CYS A O 1 ATOM 2674 C CB . CYS A 1 341 ? 9.207 24.405 48.690 1.00 10.19 ? 423 CYS A CB 1 ATOM 2675 S SG . CYS A 1 341 ? 7.874 24.413 47.484 1.00 8.67 ? 423 CYS A SG 1 ATOM 2676 N N . PHE A 1 342 ? 10.568 25.387 51.265 1.00 3.78 ? 424 PHE A N 1 ATOM 2677 C CA . PHE A 1 342 ? 11.529 25.053 52.312 1.00 4.81 ? 424 PHE A CA 1 ATOM 2678 C C . PHE A 1 342 ? 10.850 24.299 53.447 1.00 2.97 ? 424 PHE A C 1 ATOM 2679 O O . PHE A 1 342 ? 9.623 24.284 53.541 1.00 5.12 ? 424 PHE A O 1 ATOM 2680 C CB . PHE A 1 342 ? 12.235 26.307 52.840 1.00 4.31 ? 424 PHE A CB 1 ATOM 2681 C CG . PHE A 1 342 ? 11.341 27.245 53.619 1.00 8.08 ? 424 PHE A CG 1 ATOM 2682 C CD1 . PHE A 1 342 ? 10.634 28.250 52.974 1.00 8.19 ? 424 PHE A CD1 1 ATOM 2683 C CD2 . PHE A 1 342 ? 11.238 27.139 55.003 1.00 4.56 ? 424 PHE A CD2 1 ATOM 2684 C CE1 . PHE A 1 342 ? 9.821 29.123 53.694 1.00 6.71 ? 424 PHE A CE1 1 ATOM 2685 C CE2 . PHE A 1 342 ? 10.428 28.004 55.728 1.00 6.22 ? 424 PHE A CE2 1 ATOM 2686 C CZ . PHE A 1 342 ? 9.720 28.997 55.073 1.00 7.26 ? 424 PHE A CZ 1 ATOM 2687 N N . TYR A 1 343 ? 11.655 23.658 54.288 1.00 5.26 ? 425 TYR A N 1 ATOM 2688 C CA . TYR A 1 343 ? 11.153 23.008 55.495 1.00 6.32 ? 425 TYR A CA 1 ATOM 2689 C C . TYR A 1 343 ? 11.901 23.599 56.681 1.00 4.82 ? 425 TYR A C 1 ATOM 2690 O O . TYR A 1 343 ? 13.012 24.124 56.532 1.00 4.78 ? 425 TYR A O 1 ATOM 2691 C CB . TYR A 1 343 ? 11.390 21.489 55.444 1.00 4.32 ? 425 TYR A CB 1 ATOM 2692 C CG . TYR A 1 343 ? 12.861 21.145 55.446 1.00 5.29 ? 425 TYR A CG 1 ATOM 2693 C CD1 . TYR A 1 343 ? 13.560 20.992 56.640 1.00 4.70 ? 425 TYR A CD1 1 ATOM 2694 C CD2 . TYR A 1 343 ? 13.560 21.008 54.252 1.00 5.91 ? 425 TYR A CD2 1 ATOM 2695 C CE1 . TYR A 1 343 ? 14.914 20.717 56.643 1.00 4.65 ? 425 TYR A CE1 1 ATOM 2696 C CE2 . TYR A 1 343 ? 14.907 20.723 54.246 1.00 4.81 ? 425 TYR A CE2 1 ATOM 2697 C CZ . TYR A 1 343 ? 15.578 20.579 55.444 1.00 5.21 ? 425 TYR A CZ 1 ATOM 2698 O OH . TYR A 1 343 ? 16.925 20.298 55.439 1.00 5.55 ? 425 TYR A OH 1 ATOM 2699 N N . VAL A 1 344 ? 11.297 23.506 57.860 1.00 4.22 ? 426 VAL A N 1 ATOM 2700 C CA . VAL A 1 344 ? 11.994 23.813 59.098 1.00 4.72 ? 426 VAL A CA 1 ATOM 2701 C C . VAL A 1 344 ? 11.839 22.608 60.007 1.00 4.64 ? 426 VAL A C 1 ATOM 2702 O O . VAL A 1 344 ? 10.723 22.126 60.226 1.00 4.57 ? 426 VAL A O 1 ATOM 2703 C CB . VAL A 1 344 ? 11.407 25.042 59.813 1.00 5.78 ? 426 VAL A CB 1 ATOM 2704 C CG1 . VAL A 1 344 ? 12.244 25.383 61.048 1.00 5.60 ? 426 VAL A CG1 1 ATOM 2705 C CG2 . VAL A 1 344 ? 11.336 26.239 58.869 1.00 6.41 ? 426 VAL A CG2 1 ATOM 2706 N N . GLU A 1 345 ? 12.964 22.114 60.509 1.00 3.98 ? 427 GLU A N 1 ATOM 2707 C CA . GLU A 1 345 ? 12.975 21.061 61.518 1.00 5.95 ? 427 GLU A CA 1 ATOM 2708 C C . GLU A 1 345 ? 12.620 21.681 62.857 1.00 6.98 ? 427 GLU A C 1 ATOM 2709 O O . GLU A 1 345 ? 13.232 22.664 63.268 1.00 4.92 ? 427 GLU A O 1 ATOM 2710 C CB . GLU A 1 345 ? 14.375 20.453 61.610 1.00 5.82 ? 427 GLU A CB 1 ATOM 2711 C CG . GLU A 1 345 ? 14.548 19.419 62.713 1.00 4.38 ? 427 GLU A CG 1 ATOM 2712 C CD . GLU A 1 345 ? 15.999 18.993 62.870 1.00 5.89 ? 427 GLU A CD 1 ATOM 2713 O OE1 . GLU A 1 345 ? 16.886 19.863 62.769 1.00 7.90 ? 427 GLU A OE1 1 ATOM 2714 O OE2 . GLU A 1 345 ? 16.255 17.792 63.095 1.00 5.08 ? 427 GLU A OE2 1 ATOM 2715 N N . LEU A 1 346 ? 11.638 21.109 63.542 1.00 4.30 ? 428 LEU A N 1 ATOM 2716 C CA . LEU A 1 346 ? 11.241 21.614 64.850 1.00 3.62 ? 428 LEU A CA 1 ATOM 2717 C C . LEU A 1 346 ? 11.709 20.624 65.913 1.00 4.09 ? 428 LEU A C 1 ATOM 2718 O O . LEU A 1 346 ? 11.031 19.632 66.192 1.00 4.65 ? 428 LEU A O 1 ATOM 2719 C CB . LEU A 1 346 ? 9.720 21.803 64.896 1.00 3.97 ? 428 LEU A CB 1 ATOM 2720 C CG . LEU A 1 346 ? 9.147 22.591 63.710 1.00 5.56 ? 428 LEU A CG 1 ATOM 2721 C CD1 . LEU A 1 346 ? 7.619 22.582 63.713 1.00 5.98 ? 428 LEU A CD1 1 ATOM 2722 C CD2 . LEU A 1 346 ? 9.676 24.025 63.710 1.00 7.36 ? 428 LEU A CD2 1 ATOM 2723 N N . ILE A 1 347 ? 12.881 20.886 66.487 1.00 4.24 ? 429 ILE A N 1 ATOM 2724 C CA . ILE A 1 347 ? 13.510 19.943 67.412 1.00 4.25 ? 429 ILE A CA 1 ATOM 2725 C C . ILE A 1 347 ? 12.864 19.960 68.795 1.00 6.24 ? 429 ILE A C 1 ATOM 2726 O O . ILE A 1 347 ? 12.663 21.025 69.381 1.00 5.83 ? 429 ILE A O 1 ATOM 2727 C CB . ILE A 1 347 ? 15.009 20.235 67.556 1.00 4.47 ? 429 ILE A CB 1 ATOM 2728 C CG1 . ILE A 1 347 ? 15.693 20.173 66.186 1.00 5.19 ? 429 ILE A CG1 1 ATOM 2729 C CG2 . ILE A 1 347 ? 15.655 19.266 68.539 1.00 6.98 ? 429 ILE A CG2 1 ATOM 2730 C CD1 . ILE A 1 347 ? 17.144 20.686 66.183 1.00 5.40 ? 429 ILE A CD1 1 ATOM 2731 N N . ARG A 1 348 ? 12.544 18.774 69.307 1.00 2.65 ? 430 ARG A N 1 ATOM 2732 C CA . ARG A 1 348 ? 11.996 18.636 70.655 1.00 4.47 ? 430 ARG A CA 1 ATOM 2733 C C . ARG A 1 348 ? 12.893 17.710 71.450 1.00 7.19 ? 430 ARG A C 1 ATOM 2734 O O . ARG A 1 348 ? 13.543 16.826 70.884 1.00 5.90 ? 430 ARG A O 1 ATOM 2735 C CB . ARG A 1 348 ? 10.570 18.079 70.630 1.00 5.60 ? 430 ARG A CB 1 ATOM 2736 C CG . ARG A 1 348 ? 9.564 18.925 69.859 1.00 7.67 ? 430 ARG A CG 1 ATOM 2737 C CD . ARG A 1 348 ? 9.560 20.389 70.318 1.00 5.65 ? 430 ARG A CD 1 ATOM 2738 N NE . ARG A 1 348 ? 9.267 20.564 71.744 1.00 6.86 ? 430 ARG A NE 1 ATOM 2739 C CZ . ARG A 1 348 ? 8.043 20.673 72.259 1.00 7.53 ? 430 ARG A CZ 1 ATOM 2740 N NH1 . ARG A 1 348 ? 6.971 20.609 71.475 1.00 7.36 ? 430 ARG A NH1 1 ATOM 2741 N NH2 . ARG A 1 348 ? 7.889 20.851 73.567 1.00 6.97 ? 430 ARG A NH2 1 ATOM 2742 N N . GLY A 1 349 ? 12.938 17.905 72.762 1.00 4.98 ? 431 GLY A N 1 ATOM 2743 C CA . GLY A 1 349 ? 13.778 17.070 73.601 1.00 6.19 ? 431 GLY A CA 1 ATOM 2744 C C . GLY A 1 349 ? 15.153 17.672 73.827 1.00 7.75 ? 431 GLY A C 1 ATOM 2745 O O . GLY A 1 349 ? 15.312 18.894 73.888 1.00 7.07 ? 431 GLY A O 1 ATOM 2746 N N . ARG A 1 350 ? 16.160 16.815 73.955 1.00 6.50 ? 432 ARG A N 1 ATOM 2747 C CA . ARG A 1 350 ? 17.491 17.284 74.339 1.00 7.94 ? 432 ARG A CA 1 ATOM 2748 C C . ARG A 1 350 ? 18.213 18.001 73.200 1.00 6.25 ? 432 ARG A C 1 ATOM 2749 O O . ARG A 1 350 ? 17.992 17.687 72.030 1.00 6.90 ? 432 ARG A O 1 ATOM 2750 C CB . ARG A 1 350 ? 18.313 16.122 74.899 1.00 7.05 ? 432 ARG A CB 1 ATOM 2751 C CG . ARG A 1 350 ? 17.744 15.649 76.228 1.00 8.38 ? 432 ARG A CG 1 ATOM 2752 C CD . ARG A 1 350 ? 18.551 14.563 76.923 1.00 8.19 ? 432 ARG A CD 1 ATOM 2753 N NE . ARG A 1 350 ? 18.076 14.453 78.303 1.00 11.09 ? 432 ARG A NE 1 ATOM 2754 C CZ . ARG A 1 350 ? 18.818 14.087 79.339 1.00 14.64 ? 432 ARG A CZ 1 ATOM 2755 N NH1 . ARG A 1 350 ? 20.090 13.759 79.169 1.00 14.83 ? 432 ARG A NH1 1 ATOM 2756 N NH2 . ARG A 1 350 ? 18.281 14.050 80.552 1.00 14.19 ? 432 ARG A NH2 1 ATOM 2757 N N . PRO A 1 351 ? 19.091 18.966 73.534 1.00 7.03 ? 433 PRO A N 1 ATOM 2758 C CA . PRO A 1 351 ? 19.526 19.351 74.883 1.00 7.58 ? 433 PRO A CA 1 ATOM 2759 C C . PRO A 1 351 ? 18.630 20.385 75.565 1.00 9.58 ? 433 PRO A C 1 ATOM 2760 O O . PRO A 1 351 ? 18.725 20.550 76.782 1.00 11.59 ? 433 PRO A O 1 ATOM 2761 C CB . PRO A 1 351 ? 20.902 19.961 74.622 1.00 9.45 ? 433 PRO A CB 1 ATOM 2762 C CG . PRO A 1 351 ? 20.740 20.617 73.281 1.00 10.72 ? 433 PRO A CG 1 ATOM 2763 C CD . PRO A 1 351 ? 19.837 19.699 72.491 1.00 9.33 ? 433 PRO A CD 1 ATOM 2764 N N . LYS A 1 352 ? 17.775 21.068 74.807 1.00 8.06 ? 434 LYS A N 1 ATOM 2765 C CA . LYS A 1 352 ? 17.006 22.182 75.360 1.00 9.36 ? 434 LYS A CA 1 ATOM 2766 C C . LYS A 1 352 ? 15.898 21.756 76.328 1.00 13.21 ? 434 LYS A C 1 ATOM 2767 O O . LYS A 1 352 ? 15.549 22.496 77.251 1.00 11.02 ? 434 LYS A O 1 ATOM 2768 C CB . LYS A 1 352 ? 16.425 23.051 74.240 1.00 7.60 ? 434 LYS A CB 1 ATOM 2769 C CG . LYS A 1 352 ? 17.472 23.856 73.481 1.00 10.63 ? 434 LYS A CG 1 ATOM 2770 C CD . LYS A 1 352 ? 18.175 24.827 74.427 1.00 13.77 ? 434 LYS A CD 1 ATOM 2771 C CE . LYS A 1 352 ? 19.125 25.764 73.689 1.00 14.77 ? 434 LYS A CE 1 ATOM 2772 N NZ . LYS A 1 352 ? 20.411 25.085 73.339 1.00 23.46 ? 434 LYS A NZ 1 ATOM 2773 N N . GLU A 1 353 ? 15.331 20.576 76.108 1.00 8.15 ? 435 GLU A N 1 ATOM 2774 C CA . GLU A 1 353 ? 14.263 20.083 76.971 1.00 7.68 ? 435 GLU A CA 1 ATOM 2775 C C . GLU A 1 353 ? 14.698 18.755 77.571 1.00 11.69 ? 435 GLU A C 1 ATOM 2776 O O . GLU A 1 353 ? 14.406 17.689 77.026 1.00 11.26 ? 435 GLU A O 1 ATOM 2777 C CB . GLU A 1 353 ? 12.960 19.939 76.176 1.00 8.43 ? 435 GLU A CB 1 ATOM 2778 C CG . GLU A 1 353 ? 12.532 21.241 75.482 1.00 9.69 ? 435 GLU A CG 1 ATOM 2779 C CD . GLU A 1 353 ? 11.327 21.071 74.577 1.00 9.91 ? 435 GLU A CD 1 ATOM 2780 O OE1 . GLU A 1 353 ? 11.454 20.400 73.529 1.00 9.52 ? 435 GLU A OE1 1 ATOM 2781 O OE2 . GLU A 1 353 ? 10.252 21.619 74.903 1.00 10.02 ? 435 GLU A OE2 1 ATOM 2782 N N . ASP A 1 354 ? 15.408 18.820 78.694 1.00 9.45 ? 436 ASP A N 1 ATOM 2783 C CA . ASP A 1 354 ? 16.100 17.637 79.197 1.00 12.41 ? 436 ASP A CA 1 ATOM 2784 C C . ASP A 1 354 ? 15.327 16.819 80.230 1.00 13.22 ? 436 ASP A C 1 ATOM 2785 O O . ASP A 1 354 ? 15.877 15.899 80.833 1.00 13.41 ? 436 ASP A O 1 ATOM 2786 C CB . ASP A 1 354 ? 17.499 17.995 79.719 1.00 13.07 ? 436 ASP A CB 1 ATOM 2787 C CG . ASP A 1 354 ? 17.468 18.902 80.936 1.00 23.16 ? 436 ASP A CG 1 ATOM 2788 O OD1 . ASP A 1 354 ? 16.376 19.164 81.482 1.00 19.73 ? 436 ASP A OD1 1 ATOM 2789 O OD2 . ASP A 1 354 ? 18.559 19.346 81.354 1.00 30.84 ? 436 ASP A OD2 1 ATOM 2790 N N . LYS A 1 355 ? 14.055 17.140 80.434 1.00 11.90 ? 437 LYS A N 1 ATOM 2791 C CA . LYS A 1 355 ? 13.242 16.309 81.312 1.00 13.70 ? 437 LYS A CA 1 ATOM 2792 C C . LYS A 1 355 ? 12.894 14.985 80.627 1.00 14.86 ? 437 LYS A C 1 ATOM 2793 O O . LYS A 1 355 ? 12.581 14.000 81.294 1.00 11.47 ? 437 LYS A O 1 ATOM 2794 C CB . LYS A 1 355 ? 12.007 17.066 81.808 1.00 17.05 ? 437 LYS A CB 1 ATOM 2795 C CG . LYS A 1 355 ? 12.372 18.211 82.759 1.00 19.36 ? 437 LYS A CG 1 ATOM 2796 C CD . LYS A 1 355 ? 11.151 18.935 83.312 1.00 31.98 ? 437 LYS A CD 1 ATOM 2797 C CE . LYS A 1 355 ? 11.555 19.971 84.364 1.00 34.78 ? 437 LYS A CE 1 ATOM 2798 N NZ . LYS A 1 355 ? 12.389 21.074 83.799 1.00 42.83 ? 437 LYS A NZ 1 ATOM 2799 N N . VAL A 1 356 ? 12.971 14.965 79.296 1.00 10.68 ? 438 VAL A N 1 ATOM 2800 C CA . VAL A 1 356 ? 12.933 13.705 78.552 1.00 7.40 ? 438 VAL A CA 1 ATOM 2801 C C . VAL A 1 356 ? 14.352 13.300 78.181 1.00 9.27 ? 438 VAL A C 1 ATOM 2802 O O . VAL A 1 356 ? 15.262 14.130 78.194 1.00 10.29 ? 438 VAL A O 1 ATOM 2803 C CB . VAL A 1 356 ? 12.080 13.792 77.269 1.00 7.78 ? 438 VAL A CB 1 ATOM 2804 C CG1 . VAL A 1 356 ? 10.634 14.129 77.608 1.00 10.33 ? 438 VAL A CG1 1 ATOM 2805 C CG2 . VAL A 1 356 ? 12.661 14.809 76.298 1.00 8.27 ? 438 VAL A CG2 1 ATOM 2806 N N . TRP A 1 357 ? 14.538 12.026 77.848 1.00 5.48 ? 439 TRP A N 1 ATOM 2807 C CA . TRP A 1 357 ? 15.866 11.504 77.560 1.00 7.15 ? 439 TRP A CA 1 ATOM 2808 C C . TRP A 1 357 ? 16.123 11.361 76.070 1.00 8.19 ? 439 TRP A C 1 ATOM 2809 O O . TRP A 1 357 ? 17.192 10.907 75.663 1.00 8.47 ? 439 TRP A O 1 ATOM 2810 C CB . TRP A 1 357 ? 16.065 10.159 78.259 1.00 9.08 ? 439 TRP A CB 1 ATOM 2811 C CG . TRP A 1 357 ? 16.148 10.318 79.739 1.00 13.36 ? 439 TRP A CG 1 ATOM 2812 C CD1 . TRP A 1 357 ? 15.107 10.329 80.624 1.00 20.99 ? 439 TRP A CD1 1 ATOM 2813 C CD2 . TRP A 1 357 ? 17.335 10.522 80.512 1.00 13.34 ? 439 TRP A CD2 1 ATOM 2814 N NE1 . TRP A 1 357 ? 15.577 10.518 81.902 1.00 26.62 ? 439 TRP A NE1 1 ATOM 2815 C CE2 . TRP A 1 357 ? 16.942 10.641 81.859 1.00 20.56 ? 439 TRP A CE2 1 ATOM 2816 C CE3 . TRP A 1 357 ? 18.694 10.610 80.196 1.00 15.22 ? 439 TRP A CE3 1 ATOM 2817 C CZ2 . TRP A 1 357 ? 17.860 10.842 82.888 1.00 24.62 ? 439 TRP A CZ2 1 ATOM 2818 C CZ3 . TRP A 1 357 ? 19.603 10.812 81.220 1.00 24.36 ? 439 TRP A CZ3 1 ATOM 2819 C CH2 . TRP A 1 357 ? 19.183 10.923 82.547 1.00 20.18 ? 439 TRP A CH2 1 ATOM 2820 N N . TRP A 1 358 ? 15.142 11.753 75.264 1.00 8.05 ? 440 TRP A N 1 ATOM 2821 C CA . TRP A 1 358 ? 15.262 11.631 73.812 1.00 5.49 ? 440 TRP A CA 1 ATOM 2822 C C . TRP A 1 358 ? 15.443 12.974 73.102 1.00 7.72 ? 440 TRP A C 1 ATOM 2823 O O . TRP A 1 358 ? 15.276 14.035 73.701 1.00 6.77 ? 440 TRP A O 1 ATOM 2824 C CB . TRP A 1 358 ? 14.056 10.884 73.226 1.00 6.08 ? 440 TRP A CB 1 ATOM 2825 C CG . TRP A 1 358 ? 12.699 11.377 73.696 1.00 5.51 ? 440 TRP A CG 1 ATOM 2826 C CD1 . TRP A 1 358 ? 11.914 10.815 74.668 1.00 6.93 ? 440 TRP A CD1 1 ATOM 2827 C CD2 . TRP A 1 358 ? 11.965 12.503 73.189 1.00 6.29 ? 440 TRP A CD2 1 ATOM 2828 N NE1 . TRP A 1 358 ? 10.741 11.530 74.804 1.00 7.44 ? 440 TRP A NE1 1 ATOM 2829 C CE2 . TRP A 1 358 ? 10.752 12.572 73.912 1.00 10.45 ? 440 TRP A CE2 1 ATOM 2830 C CE3 . TRP A 1 358 ? 12.222 13.468 72.207 1.00 5.29 ? 440 TRP A CE3 1 ATOM 2831 C CZ2 . TRP A 1 358 ? 9.798 13.568 73.678 1.00 6.46 ? 440 TRP A CZ2 1 ATOM 2832 C CZ3 . TRP A 1 358 ? 11.274 14.450 71.973 1.00 5.70 ? 440 TRP A CZ3 1 ATOM 2833 C CH2 . TRP A 1 358 ? 10.074 14.493 72.703 1.00 6.60 ? 440 TRP A CH2 1 ATOM 2834 N N . THR A 1 359 ? 15.804 12.898 71.823 1.00 3.78 ? 441 THR A N 1 ATOM 2835 C CA . THR A 1 359 ? 15.804 14.050 70.928 1.00 4.85 ? 441 THR A CA 1 ATOM 2836 C C . THR A 1 359 ? 15.097 13.614 69.658 1.00 3.47 ? 441 THR A C 1 ATOM 2837 O O . THR A 1 359 ? 15.448 12.590 69.078 1.00 5.23 ? 441 THR A O 1 ATOM 2838 C CB . THR A 1 359 ? 17.229 14.483 70.555 1.00 4.88 ? 441 THR A CB 1 ATOM 2839 O OG1 . THR A 1 359 ? 17.909 14.976 71.719 1.00 6.50 ? 441 THR A OG1 1 ATOM 2840 C CG2 . THR A 1 359 ? 17.197 15.588 69.485 1.00 4.02 ? 441 THR A CG2 1 ATOM 2841 N N . SER A 1 360 ? 14.093 14.370 69.232 1.00 3.74 ? 442 SER A N 1 ATOM 2842 C CA . SER A 1 360 ? 13.450 14.090 67.955 1.00 4.85 ? 442 SER A CA 1 ATOM 2843 C C . SER A 1 360 ? 13.025 15.413 67.345 1.00 6.12 ? 442 SER A C 1 ATOM 2844 O O . SER A 1 360 ? 13.524 16.469 67.740 1.00 6.86 ? 442 SER A O 1 ATOM 2845 C CB . SER A 1 360 ? 12.254 13.144 68.127 1.00 4.57 ? 442 SER A CB 1 ATOM 2846 O OG . SER A 1 360 ? 11.874 12.562 66.885 1.00 6.04 ? 442 SER A OG 1 ATOM 2847 N N . ASN A 1 361 ? 12.117 15.363 66.380 1.00 4.62 ? 443 ASN A N 1 ATOM 2848 C CA . ASN A 1 361 ? 11.650 16.580 65.739 1.00 4.04 ? 443 ASN A CA 1 ATOM 2849 C C . ASN A 1 361 ? 10.346 16.330 65.011 1.00 4.02 ? 443 ASN A C 1 ATOM 2850 O O . ASN A 1 361 ? 9.954 15.176 64.792 1.00 5.71 ? 443 ASN A O 1 ATOM 2851 C CB . ASN A 1 361 ? 12.679 17.047 64.708 1.00 3.33 ? 443 ASN A CB 1 ATOM 2852 C CG . ASN A 1 361 ? 12.748 16.113 63.509 1.00 4.98 ? 443 ASN A CG 1 ATOM 2853 O OD1 . ASN A 1 361 ? 13.332 15.033 63.592 1.00 5.39 ? 443 ASN A OD1 1 ATOM 2854 N ND2 . ASN A 1 361 ? 12.127 16.510 62.398 1.00 4.49 ? 443 ASN A ND2 1 ATOM 2855 N N . SER A 1 362 ? 9.673 17.411 64.626 1.00 4.08 ? 444 SER A N 1 ATOM 2856 C CA . SER A 1 362 ? 8.638 17.311 63.605 1.00 5.00 ? 444 SER A CA 1 ATOM 2857 C C . SER A 1 362 ? 9.016 18.242 62.459 1.00 6.41 ? 444 SER A C 1 ATOM 2858 O O . SER A 1 362 ? 10.075 18.874 62.487 1.00 5.52 ? 444 SER A O 1 ATOM 2859 C CB . SER A 1 362 ? 7.250 17.637 64.159 1.00 4.18 ? 444 SER A CB 1 ATOM 2860 O OG . SER A 1 362 ? 7.099 19.023 64.421 1.00 5.97 ? 444 SER A OG 1 ATOM 2861 N N . ILE A 1 363 ? 8.166 18.318 61.443 1.00 4.11 ? 445 ILE A N 1 ATOM 2862 C CA . ILE A 1 363 ? 8.488 19.078 60.245 1.00 4.36 ? 445 ILE A CA 1 ATOM 2863 C C . ILE A 1 363 ? 7.376 20.071 59.951 1.00 4.72 ? 445 ILE A C 1 ATOM 2864 O O . ILE A 1 363 ? 6.195 19.739 60.083 1.00 4.57 ? 445 ILE A O 1 ATOM 2865 C CB . ILE A 1 363 ? 8.636 18.132 59.025 1.00 5.15 ? 445 ILE A CB 1 ATOM 2866 C CG1 . ILE A 1 363 ? 9.814 17.168 59.213 1.00 7.07 ? 445 ILE A CG1 1 ATOM 2867 C CG2 . ILE A 1 363 ? 8.780 18.924 57.711 1.00 5.46 ? 445 ILE A CG2 1 ATOM 2868 C CD1 . ILE A 1 363 ? 9.839 16.033 58.172 1.00 5.35 ? 445 ILE A CD1 1 ATOM 2869 N N . VAL A 1 364 ? 7.745 21.294 59.583 1.00 4.24 ? 446 VAL A N 1 ATOM 2870 C CA . VAL A 1 364 ? 6.805 22.185 58.908 1.00 4.86 ? 446 VAL A CA 1 ATOM 2871 C C . VAL A 1 364 ? 7.452 22.632 57.599 1.00 5.30 ? 446 VAL A C 1 ATOM 2872 O O . VAL A 1 364 ? 8.679 22.751 57.518 1.00 5.23 ? 446 VAL A O 1 ATOM 2873 C CB . VAL A 1 364 ? 6.395 23.391 59.788 1.00 4.66 ? 446 VAL A CB 1 ATOM 2874 C CG1 . VAL A 1 364 ? 7.601 24.271 60.117 1.00 6.72 ? 446 VAL A CG1 1 ATOM 2875 C CG2 . VAL A 1 364 ? 5.290 24.207 59.104 1.00 6.32 ? 446 VAL A CG2 1 ATOM 2876 N N A SER A 1 365 ? 6.638 22.849 56.571 0.50 4.86 ? 447 SER A N 1 ATOM 2877 N N B SER A 1 365 ? 6.697 22.852 56.538 0.50 4.86 ? 447 SER A N 1 ATOM 2878 C CA A SER A 1 365 ? 7.156 23.182 55.247 0.50 5.70 ? 447 SER A CA 1 ATOM 2879 C CA B SER A 1 365 ? 7.230 23.337 55.283 0.50 5.71 ? 447 SER A CA 1 ATOM 2880 C C A SER A 1 365 ? 6.265 24.218 54.583 0.50 6.20 ? 447 SER A C 1 ATOM 2881 C C B SER A 1 365 ? 6.277 24.293 54.665 0.50 6.20 ? 447 SER A C 1 ATOM 2882 O O A SER A 1 365 ? 5.040 24.168 54.722 0.50 6.02 ? 447 SER A O 1 ATOM 2883 O O B SER A 1 365 ? 5.112 24.084 54.706 0.50 6.01 ? 447 SER A O 1 ATOM 2884 C CB A SER A 1 365 ? 7.212 21.925 54.372 0.50 5.61 ? 447 SER A CB 1 ATOM 2885 C CB B SER A 1 365 ? 7.445 22.251 54.209 0.50 5.63 ? 447 SER A CB 1 ATOM 2886 O OG A SER A 1 365 ? 7.811 22.210 53.123 0.50 14.04 ? 447 SER A OG 1 ATOM 2887 O OG B SER A 1 365 ? 6.417 21.419 54.248 0.50 13.97 ? 447 SER A OG 1 ATOM 2888 N N . MET A 1 366 ? 6.888 25.153 53.865 1.00 6.37 ? 448 MET A N 1 ATOM 2889 C CA . MET A 1 366 ? 6.173 26.211 53.153 1.00 5.55 ? 448 MET A CA 1 ATOM 2890 C C . MET A 1 366 ? 6.646 26.309 51.706 1.00 6.08 ? 448 MET A C 1 ATOM 2891 O O . MET A 1 366 ? 7.774 25.926 51.387 1.00 6.62 ? 448 MET A O 1 ATOM 2892 C CB . MET A 1 366 ? 6.429 27.565 53.824 1.00 3.81 ? 448 MET A CB 1 ATOM 2893 C CG . MET A 1 366 ? 6.459 27.523 55.344 1.00 9.76 ? 448 MET A CG 1 ATOM 2894 S SD . MET A 1 366 ? 4.814 27.605 56.063 1.00 14.68 ? 448 MET A SD 1 ATOM 2895 C CE . MET A 1 366 ? 4.435 29.337 55.768 1.00 10.62 ? 448 MET A CE 1 ATOM 2896 N N . CYS A 1 367 ? 5.791 26.841 50.835 1.00 6.62 ? 449 CYS A N 1 ATOM 2897 C CA . CYS A 1 367 ? 6.193 27.165 49.465 1.00 7.97 ? 449 CYS A CA 1 ATOM 2898 C C . CYS A 1 367 ? 5.791 28.610 49.191 1.00 8.00 ? 449 CYS A C 1 ATOM 2899 O O . CYS A 1 367 ? 4.981 29.174 49.920 1.00 8.21 ? 449 CYS A O 1 ATOM 2900 C CB . CYS A 1 367 ? 5.526 26.231 48.455 1.00 9.21 ? 449 CYS A CB 1 ATOM 2901 S SG . CYS A 1 367 ? 6.117 24.507 48.521 1.00 9.43 ? 449 CYS A SG 1 ATOM 2902 N N . SER A 1 368 ? 6.345 29.215 48.145 1.00 7.56 ? 450 SER A N 1 ATOM 2903 C CA . SER A 1 368 ? 6.064 30.627 47.892 1.00 7.04 ? 450 SER A CA 1 ATOM 2904 C C . SER A 1 368 ? 4.723 30.836 47.194 1.00 6.43 ? 450 SER A C 1 ATOM 2905 O O . SER A 1 368 ? 4.221 29.949 46.498 1.00 8.30 ? 450 SER A O 1 ATOM 2906 C CB . SER A 1 368 ? 7.189 31.273 47.079 1.00 6.25 ? 450 SER A CB 1 ATOM 2907 O OG . SER A 1 368 ? 7.269 30.712 45.781 1.00 8.98 ? 450 SER A OG 1 ATOM 2908 N N . SER A 1 369 ? 4.149 32.019 47.403 1.00 7.97 ? 451 SER A N 1 ATOM 2909 C CA . SER A 1 369 ? 2.941 32.454 46.708 1.00 7.61 ? 451 SER A CA 1 ATOM 2910 C C . SER A 1 369 ? 3.226 33.790 46.023 1.00 8.88 ? 451 SER A C 1 ATOM 2911 O O . SER A 1 369 ? 4.034 34.579 46.517 1.00 8.36 ? 451 SER A O 1 ATOM 2912 C CB . SER A 1 369 ? 1.802 32.637 47.718 1.00 8.71 ? 451 SER A CB 1 ATOM 2913 O OG . SER A 1 369 ? 0.638 33.172 47.106 1.00 9.47 ? 451 SER A OG 1 ATOM 2914 N N . THR A 1 370 ? 2.571 34.048 44.894 1.00 7.25 ? 452 THR A N 1 ATOM 2915 C CA . THR A 1 370 ? 2.651 35.364 44.257 1.00 9.01 ? 452 THR A CA 1 ATOM 2916 C C . THR A 1 370 ? 1.646 36.337 44.876 1.00 12.84 ? 452 THR A C 1 ATOM 2917 O O . THR A 1 370 ? 1.659 37.534 44.575 1.00 10.08 ? 452 THR A O 1 ATOM 2918 C CB . THR A 1 370 ? 2.420 35.291 42.737 1.00 10.03 ? 452 THR A CB 1 ATOM 2919 O OG1 . THR A 1 370 ? 1.122 34.751 42.475 1.00 11.18 ? 452 THR A OG1 1 ATOM 2920 C CG2 . THR A 1 370 ? 3.473 34.409 42.075 1.00 11.29 ? 452 THR A CG2 1 ATOM 2921 N N . GLU A 1 371 ? 0.773 35.820 45.736 1.00 9.02 ? 453 GLU A N 1 ATOM 2922 C CA . GLU A 1 371 ? -0.100 36.669 46.540 1.00 9.68 ? 453 GLU A CA 1 ATOM 2923 C C . GLU A 1 371 ? 0.662 37.167 47.765 1.00 8.51 ? 453 GLU A C 1 ATOM 2924 O O . GLU A 1 371 ? 1.719 36.636 48.108 1.00 9.82 ? 453 GLU A O 1 ATOM 2925 C CB . GLU A 1 371 ? -1.341 35.895 46.997 1.00 9.92 ? 453 GLU A CB 1 ATOM 2926 C CG . GLU A 1 371 ? -2.138 35.262 45.866 1.00 13.46 ? 453 GLU A CG 1 ATOM 2927 C CD . GLU A 1 371 ? -2.742 36.286 44.918 1.00 18.10 ? 453 GLU A CD 1 ATOM 2928 O OE1 . GLU A 1 371 ? -3.095 37.392 45.374 1.00 22.60 ? 453 GLU A OE1 1 ATOM 2929 O OE2 . GLU A 1 371 ? -2.873 35.971 43.718 1.00 28.42 ? 453 GLU A OE2 1 ATOM 2930 N N . PHE A 1 372 ? 0.125 38.188 48.420 1.00 7.68 ? 454 PHE A N 1 ATOM 2931 C CA . PHE A 1 372 ? 0.672 38.640 49.695 1.00 9.72 ? 454 PHE A CA 1 ATOM 2932 C C . PHE A 1 372 ? -0.210 38.097 50.815 1.00 12.92 ? 454 PHE A C 1 ATOM 2933 O O . PHE A 1 372 ? -1.129 38.773 51.289 1.00 11.07 ? 454 PHE A O 1 ATOM 2934 C CB . PHE A 1 372 ? 0.747 40.168 49.742 1.00 12.61 ? 454 PHE A CB 1 ATOM 2935 C CG . PHE A 1 372 ? 1.756 40.754 48.790 1.00 9.27 ? 454 PHE A CG 1 ATOM 2936 C CD1 . PHE A 1 372 ? 1.445 40.931 47.448 1.00 13.87 ? 454 PHE A CD1 1 ATOM 2937 C CD2 . PHE A 1 372 ? 3.016 41.131 49.239 1.00 12.12 ? 454 PHE A CD2 1 ATOM 2938 C CE1 . PHE A 1 372 ? 2.371 41.469 46.569 1.00 14.67 ? 454 PHE A CE1 1 ATOM 2939 C CE2 . PHE A 1 372 ? 3.947 41.674 48.368 1.00 11.08 ? 454 PHE A CE2 1 ATOM 2940 C CZ . PHE A 1 372 ? 3.624 41.843 47.032 1.00 13.11 ? 454 PHE A CZ 1 ATOM 2941 N N . LEU A 1 373 ? 0.068 36.861 51.222 1.00 8.58 ? 455 LEU A N 1 ATOM 2942 C CA . LEU A 1 373 ? -0.805 36.137 52.145 1.00 8.19 ? 455 LEU A CA 1 ATOM 2943 C C . LEU A 1 373 ? -0.578 36.511 53.606 1.00 10.13 ? 455 LEU A C 1 ATOM 2944 O O . LEU A 1 373 ? 0.538 36.841 54.010 1.00 10.34 ? 455 LEU A O 1 ATOM 2945 C CB . LEU A 1 373 ? -0.615 34.626 51.973 1.00 7.90 ? 455 LEU A CB 1 ATOM 2946 C CG . LEU A 1 373 ? -0.914 34.045 50.592 1.00 7.85 ? 455 LEU A CG 1 ATOM 2947 C CD1 . LEU A 1 373 ? -0.606 32.554 50.553 1.00 9.80 ? 455 LEU A CD1 1 ATOM 2948 C CD2 . LEU A 1 373 ? -2.372 34.293 50.223 1.00 7.62 ? 455 LEU A CD2 1 ATOM 2949 N N . GLY A 1 374 ? -1.644 36.449 54.400 1.00 9.72 ? 456 GLY A N 1 ATOM 2950 C CA . GLY A 1 374 ? -1.522 36.628 55.835 1.00 8.21 ? 456 GLY A CA 1 ATOM 2951 C C . GLY A 1 374 ? -0.638 35.552 56.443 1.00 8.11 ? 456 GLY A C 1 ATOM 2952 O O . GLY A 1 374 ? -0.546 34.442 55.915 1.00 9.04 ? 456 GLY A O 1 ATOM 2953 N N . GLN A 1 375 ? 0.013 35.870 57.554 1.00 7.90 ? 457 GLN A N 1 ATOM 2954 C CA . GLN A 1 375 ? 0.931 34.917 58.171 1.00 7.58 ? 457 GLN A CA 1 ATOM 2955 C C . GLN A 1 375 ? 0.384 34.310 59.465 1.00 7.56 ? 457 GLN A C 1 ATOM 2956 O O . GLN A 1 375 ? -0.295 34.979 60.249 1.00 8.18 ? 457 GLN A O 1 ATOM 2957 C CB . GLN A 1 375 ? 2.283 35.587 58.443 1.00 7.31 ? 457 GLN A CB 1 ATOM 2958 C CG . GLN A 1 375 ? 2.201 36.725 59.459 1.00 8.70 ? 457 GLN A CG 1 ATOM 2959 C CD . GLN A 1 375 ? 3.544 37.370 59.735 1.00 16.24 ? 457 GLN A CD 1 ATOM 2960 O OE1 . GLN A 1 375 ? 4.575 36.912 59.252 1.00 18.59 ? 457 GLN A OE1 1 ATOM 2961 N NE2 . GLN A 1 375 ? 3.537 38.440 60.519 1.00 19.67 ? 457 GLN A NE2 1 ATOM 2962 N N . TRP A 1 376 ? 0.672 33.029 59.671 1.00 6.62 ? 458 TRP A N 1 ATOM 2963 C CA . TRP A 1 376 ? 0.457 32.390 60.965 1.00 6.72 ? 458 TRP A CA 1 ATOM 2964 C C . TRP A 1 376 ? 1.824 31.996 61.485 1.00 9.98 ? 458 TRP A C 1 ATOM 2965 O O . TRP A 1 376 ? 2.840 32.321 60.869 1.00 14.74 ? 458 TRP A O 1 ATOM 2966 C CB . TRP A 1 376 ? -0.391 31.132 60.815 1.00 6.71 ? 458 TRP A CB 1 ATOM 2967 C CG . TRP A 1 376 ? -1.294 30.861 61.989 1.00 7.59 ? 458 TRP A CG 1 ATOM 2968 C CD1 . TRP A 1 376 ? -1.461 31.637 63.102 1.00 8.19 ? 458 TRP A CD1 1 ATOM 2969 C CD2 . TRP A 1 376 ? -2.164 29.737 62.149 1.00 7.66 ? 458 TRP A CD2 1 ATOM 2970 N NE1 . TRP A 1 376 ? -2.391 31.062 63.943 1.00 6.17 ? 458 TRP A NE1 1 ATOM 2971 C CE2 . TRP A 1 376 ? -2.837 29.896 63.376 1.00 7.84 ? 458 TRP A CE2 1 ATOM 2972 C CE3 . TRP A 1 376 ? -2.444 28.613 61.366 1.00 5.61 ? 458 TRP A CE3 1 ATOM 2973 C CZ2 . TRP A 1 376 ? -3.772 28.968 63.841 1.00 9.67 ? 458 TRP A CZ2 1 ATOM 2974 C CZ3 . TRP A 1 376 ? -3.377 27.695 61.828 1.00 6.25 ? 458 TRP A CZ3 1 ATOM 2975 C CH2 . TRP A 1 376 ? -4.028 27.879 63.051 1.00 5.30 ? 458 TRP A CH2 1 ATOM 2976 N N . ASN A 1 377 ? 1.853 31.306 62.620 1.00 8.53 ? 459 ASN A N 1 ATOM 2977 C CA . ASN A 1 377 ? 3.093 30.729 63.126 1.00 6.10 ? 459 ASN A CA 1 ATOM 2978 C C . ASN A 1 377 ? 2.842 29.253 63.351 1.00 8.30 ? 459 ASN A C 1 ATOM 2979 O O . ASN A 1 377 ? 1.700 28.854 63.596 1.00 7.34 ? 459 ASN A O 1 ATOM 2980 C CB . ASN A 1 377 ? 3.527 31.409 64.420 1.00 6.59 ? 459 ASN A CB 1 ATOM 2981 C CG . ASN A 1 377 ? 2.573 31.137 65.566 1.00 8.98 ? 459 ASN A CG 1 ATOM 2982 O OD1 . ASN A 1 377 ? 2.734 30.160 66.300 1.00 8.30 ? 459 ASN A OD1 1 ATOM 2983 N ND2 . ASN A 1 377 ? 1.566 31.995 65.721 1.00 9.12 ? 459 ASN A ND2 1 ATOM 2984 N N . TRP A 1 378 ? 3.892 28.438 63.264 1.00 6.41 ? 460 TRP A N 1 ATOM 2985 C CA . TRP A 1 378 ? 3.708 26.992 63.169 1.00 5.69 ? 460 TRP A CA 1 ATOM 2986 C C . TRP A 1 378 ? 4.597 26.211 64.127 1.00 5.28 ? 460 TRP A C 1 ATOM 2987 O O . TRP A 1 378 ? 5.673 25.755 63.741 1.00 9.26 ? 460 TRP A O 1 ATOM 2988 C CB . TRP A 1 378 ? 3.972 26.537 61.729 1.00 5.48 ? 460 TRP A CB 1 ATOM 2989 C CG . TRP A 1 378 ? 3.019 27.140 60.722 1.00 5.47 ? 460 TRP A CG 1 ATOM 2990 C CD1 . TRP A 1 378 ? 3.199 28.291 60.000 1.00 6.95 ? 460 TRP A CD1 1 ATOM 2991 C CD2 . TRP A 1 378 ? 1.737 26.628 60.344 1.00 5.19 ? 460 TRP A CD2 1 ATOM 2992 N NE1 . TRP A 1 378 ? 2.105 28.519 59.194 1.00 7.27 ? 460 TRP A NE1 1 ATOM 2993 C CE2 . TRP A 1 378 ? 1.197 27.510 59.384 1.00 5.70 ? 460 TRP A CE2 1 ATOM 2994 C CE3 . TRP A 1 378 ? 0.995 25.503 60.718 1.00 5.16 ? 460 TRP A CE3 1 ATOM 2995 C CZ2 . TRP A 1 378 ? -0.048 27.298 58.793 1.00 6.34 ? 460 TRP A CZ2 1 ATOM 2996 C CZ3 . TRP A 1 378 ? -0.238 25.293 60.131 1.00 6.19 ? 460 TRP A CZ3 1 ATOM 2997 C CH2 . TRP A 1 378 ? -0.751 26.187 59.183 1.00 7.15 ? 460 TRP A CH2 1 ATOM 2998 N N . PRO A 1 379 ? 4.141 26.048 65.381 1.00 4.55 ? 461 PRO A N 1 ATOM 2999 C CA . PRO A 1 379 ? 4.914 25.349 66.413 1.00 6.31 ? 461 PRO A CA 1 ATOM 3000 C C . PRO A 1 379 ? 4.850 23.843 66.212 1.00 3.81 ? 461 PRO A C 1 ATOM 3001 O O . PRO A 1 379 ? 3.957 23.350 65.521 1.00 6.08 ? 461 PRO A O 1 ATOM 3002 C CB . PRO A 1 379 ? 4.172 25.698 67.714 1.00 8.46 ? 461 PRO A CB 1 ATOM 3003 C CG . PRO A 1 379 ? 3.089 26.681 67.340 1.00 11.91 ? 461 PRO A CG 1 ATOM 3004 C CD . PRO A 1 379 ? 2.825 26.473 65.880 1.00 7.24 ? 461 PRO A CD 1 ATOM 3005 N N . ASP A 1 380 ? 5.780 23.119 66.820 1.00 4.08 ? 462 ASP A N 1 ATOM 3006 C CA . ASP A 1 380 ? 5.696 21.665 66.828 1.00 3.47 ? 462 ASP A CA 1 ATOM 3007 C C . ASP A 1 380 ? 4.364 21.225 67.423 1.00 5.40 ? 462 ASP A C 1 ATOM 3008 O O . ASP A 1 380 ? 3.658 20.382 66.849 1.00 7.14 ? 462 ASP A O 1 ATOM 3009 C CB . ASP A 1 380 ? 6.853 21.073 67.627 1.00 4.37 ? 462 ASP A CB 1 ATOM 3010 C CG . ASP A 1 380 ? 6.647 19.616 67.927 1.00 6.10 ? 462 ASP A CG 1 ATOM 3011 O OD1 . ASP A 1 380 ? 6.789 18.802 66.993 1.00 8.12 ? 462 ASP A OD1 1 ATOM 3012 O OD2 . ASP A 1 380 ? 6.337 19.285 69.090 1.00 6.75 ? 462 ASP A OD2 1 ATOM 3013 N N . GLY A 1 381 ? 4.018 21.799 68.572 1.00 4.12 ? 463 GLY A N 1 ATOM 3014 C CA . GLY A 1 381 ? 2.700 21.597 69.150 1.00 6.88 ? 463 GLY A CA 1 ATOM 3015 C C . GLY A 1 381 ? 2.590 20.535 70.226 1.00 7.63 ? 463 GLY A C 1 ATOM 3016 O O . GLY A 1 381 ? 1.522 20.338 70.808 1.00 7.37 ? 463 GLY A O 1 ATOM 3017 N N . ALA A 1 382 ? 3.685 19.839 70.505 1.00 6.17 ? 464 ALA A N 1 ATOM 3018 C CA . ALA A 1 382 ? 3.640 18.809 71.536 1.00 5.15 ? 464 ALA A CA 1 ATOM 3019 C C . ALA A 1 382 ? 3.875 19.413 72.913 1.00 6.74 ? 464 ALA A C 1 ATOM 3020 O O . ALA A 1 382 ? 4.584 20.410 73.056 1.00 7.19 ? 464 ALA A O 1 ATOM 3021 C CB . ALA A 1 382 ? 4.649 17.712 71.252 1.00 5.50 ? 464 ALA A CB 1 ATOM 3022 N N . LYS A 1 383 ? 3.263 18.812 73.926 1.00 8.74 ? 465 LYS A N 1 ATOM 3023 C CA . LYS A 1 383 ? 3.486 19.227 75.303 1.00 11.43 ? 465 LYS A CA 1 ATOM 3024 C C . LYS A 1 383 ? 4.437 18.231 75.951 1.00 8.21 ? 465 LYS A C 1 ATOM 3025 O O . LYS A 1 383 ? 4.079 17.072 76.152 1.00 8.52 ? 465 LYS A O 1 ATOM 3026 C CB . LYS A 1 383 ? 2.157 19.285 76.060 1.00 10.62 ? 465 LYS A CB 1 ATOM 3027 C CG . LYS A 1 383 ? 1.165 20.282 75.464 1.00 16.13 ? 465 LYS A CG 1 ATOM 3028 C CD . LYS A 1 383 ? -0.230 20.161 76.082 1.00 26.55 ? 465 LYS A CD 1 ATOM 3029 C CE . LYS A 1 383 ? -0.277 20.715 77.496 1.00 29.41 ? 465 LYS A CE 1 ATOM 3030 N NZ . LYS A 1 383 ? -0.143 22.199 77.490 1.00 43.25 ? 465 LYS A NZ 1 ATOM 3031 N N . ILE A 1 384 ? 5.652 18.689 76.256 1.00 8.70 ? 466 ILE A N 1 ATOM 3032 C CA . ILE A 1 384 ? 6.713 17.838 76.795 1.00 10.46 ? 466 ILE A CA 1 ATOM 3033 C C . ILE A 1 384 ? 6.289 17.097 78.066 1.00 12.60 ? 466 ILE A C 1 ATOM 3034 O O . ILE A 1 384 ? 6.671 15.942 78.279 1.00 10.21 ? 466 ILE A O 1 ATOM 3035 C CB . ILE A 1 384 ? 7.997 18.673 77.068 1.00 21.13 ? 466 ILE A CB 1 ATOM 3036 C CG1 . ILE A 1 384 ? 8.891 18.704 75.832 1.00 20.41 ? 466 ILE A CG1 1 ATOM 3037 C CG2 . ILE A 1 384 ? 8.782 18.121 78.255 1.00 35.44 ? 466 ILE A CG2 1 ATOM 3038 C CD1 . ILE A 1 384 ? 9.476 17.344 75.451 1.00 16.06 ? 466 ILE A CD1 1 ATOM 3039 N N . GLU A 1 385 ? 5.481 17.759 78.890 1.00 13.76 ? 467 GLU A N 1 ATOM 3040 C CA . GLU A 1 385 ? 5.008 17.189 80.151 1.00 14.49 ? 467 GLU A CA 1 ATOM 3041 C C . GLU A 1 385 ? 4.271 15.864 79.960 1.00 12.22 ? 467 GLU A C 1 ATOM 3042 O O . GLU A 1 385 ? 4.247 15.026 80.862 1.00 11.91 ? 467 GLU A O 1 ATOM 3043 C CB . GLU A 1 385 ? 4.089 18.183 80.871 1.00 17.35 ? 467 GLU A CB 1 ATOM 3044 C CG . GLU A 1 385 ? 2.717 18.332 80.216 1.00 26.62 ? 467 GLU A CG 1 ATOM 3045 C CD . GLU A 1 385 ? 2.073 19.672 80.494 1.00 48.74 ? 467 GLU A CD 1 ATOM 3046 O OE1 . GLU A 1 385 ? 1.199 19.739 81.386 1.00 48.52 ? 467 GLU A OE1 1 ATOM 3047 O OE2 . GLU A 1 385 ? 2.439 20.655 79.813 1.00 47.23 ? 467 GLU A OE2 1 ATOM 3048 N N . TYR A 1 386 ? 3.667 15.677 78.789 1.00 8.51 ? 468 TYR A N 1 ATOM 3049 C CA . TYR A 1 386 ? 2.909 14.462 78.508 1.00 8.91 ? 468 TYR A CA 1 ATOM 3050 C C . TYR A 1 386 ? 3.822 13.245 78.425 1.00 10.69 ? 468 TYR A C 1 ATOM 3051 O O . TYR A 1 386 ? 3.379 12.111 78.606 1.00 8.85 ? 468 TYR A O 1 ATOM 3052 C CB . TYR A 1 386 ? 2.133 14.608 77.195 1.00 7.74 ? 468 TYR A CB 1 ATOM 3053 C CG . TYR A 1 386 ? 0.898 15.488 77.273 1.00 8.62 ? 468 TYR A CG 1 ATOM 3054 C CD1 . TYR A 1 386 ? 0.324 15.823 78.495 1.00 11.90 ? 468 TYR A CD1 1 ATOM 3055 C CD2 . TYR A 1 386 ? 0.299 15.968 76.115 1.00 6.12 ? 468 TYR A CD2 1 ATOM 3056 C CE1 . TYR A 1 386 ? -0.811 16.623 78.555 1.00 12.20 ? 468 TYR A CE1 1 ATOM 3057 C CE2 . TYR A 1 386 ? -0.828 16.761 76.163 1.00 8.19 ? 468 TYR A CE2 1 ATOM 3058 C CZ . TYR A 1 386 ? -1.381 17.084 77.384 1.00 10.53 ? 468 TYR A CZ 1 ATOM 3059 O OH . TYR A 1 386 ? -2.507 17.877 77.427 1.00 10.52 ? 468 TYR A OH 1 ATOM 3060 N N . PHE A 1 387 ? 5.099 13.484 78.149 1.00 8.77 ? 469 PHE A N 1 ATOM 3061 C CA . PHE A 1 387 ? 6.052 12.400 77.947 1.00 10.27 ? 469 PHE A CA 1 ATOM 3062 C C . PHE A 1 387 ? 6.744 11.973 79.237 1.00 16.53 ? 469 PHE A C 1 ATOM 3063 O O . PHE A 1 387 ? 7.585 11.077 79.220 1.00 15.91 ? 469 PHE A O 1 ATOM 3064 C CB . PHE A 1 387 ? 7.117 12.812 76.926 1.00 7.93 ? 469 PHE A CB 1 ATOM 3065 C CG . PHE A 1 387 ? 6.625 12.837 75.507 1.00 8.92 ? 469 PHE A CG 1 ATOM 3066 C CD1 . PHE A 1 387 ? 6.039 13.980 74.983 1.00 8.14 ? 469 PHE A CD1 1 ATOM 3067 C CD2 . PHE A 1 387 ? 6.763 11.721 74.691 1.00 8.92 ? 469 PHE A CD2 1 ATOM 3068 C CE1 . PHE A 1 387 ? 5.592 14.010 73.669 1.00 8.60 ? 469 PHE A CE1 1 ATOM 3069 C CE2 . PHE A 1 387 ? 6.319 11.746 73.375 1.00 6.82 ? 469 PHE A CE2 1 ATOM 3070 C CZ . PHE A 1 387 ? 5.734 12.895 72.868 1.00 9.67 ? 469 PHE A CZ 1 ATOM 3071 N N . LEU A 1 388 ? 6.391 12.610 80.348 1.00 12.49 ? 470 LEU A N 1 ATOM 3072 C CA . LEU A 1 388 ? 7.075 12.361 81.618 1.00 16.13 ? 470 LEU A CA 1 ATOM 3073 C C . LEU A 1 388 ? 6.419 11.257 82.439 1.00 23.16 ? 470 LEU A C 1 ATOM 3074 O O . LEU A 1 388 ? 5.273 10.873 82.198 1.00 18.09 ? 470 LEU A O 1 ATOM 3075 C CB . LEU A 1 388 ? 7.161 13.650 82.436 1.00 13.78 ? 470 LEU A CB 1 ATOM 3076 C CG . LEU A 1 388 ? 7.905 14.804 81.763 1.00 16.41 ? 470 LEU A CG 1 ATOM 3077 C CD1 . LEU A 1 388 ? 8.059 15.991 82.712 1.00 19.83 ? 470 LEU A CD1 1 ATOM 3078 C CD2 . LEU A 1 388 ? 9.267 14.347 81.234 1.00 12.67 ? 470 LEU A CD2 1 ATOM 3079 O OXT . LEU A 1 388 ? 7.031 10.717 83.363 1.00 28.35 ? 470 LEU A OXT 1 HETATM 3080 C C1 . NAG B 2 . ? 16.616 17.603 28.716 1.00 36.09 ? 501 NAG A C1 1 HETATM 3081 C C2 . NAG B 2 . ? 15.454 16.842 28.069 1.00 31.90 ? 501 NAG A C2 1 HETATM 3082 C C3 . NAG B 2 . ? 15.956 15.626 27.299 1.00 41.05 ? 501 NAG A C3 1 HETATM 3083 C C4 . NAG B 2 . ? 17.054 16.045 26.332 1.00 38.86 ? 501 NAG A C4 1 HETATM 3084 C C5 . NAG B 2 . ? 18.158 16.753 27.111 1.00 42.88 ? 501 NAG A C5 1 HETATM 3085 C C6 . NAG B 2 . ? 19.342 17.130 26.218 1.00 40.92 ? 501 NAG A C6 1 HETATM 3086 C C7 . NAG B 2 . ? 13.164 16.716 28.873 1.00 37.61 ? 501 NAG A C7 1 HETATM 3087 C C8 . NAG B 2 . ? 12.229 16.438 30.014 1.00 28.69 ? 501 NAG A C8 1 HETATM 3088 N N2 . NAG B 2 . ? 14.457 16.445 29.054 1.00 35.17 ? 501 NAG A N2 1 HETATM 3089 O O3 . NAG B 2 . ? 14.892 15.029 26.595 1.00 41.21 ? 501 NAG A O3 1 HETATM 3090 O O4 . NAG B 2 . ? 17.565 14.911 25.666 1.00 51.67 ? 501 NAG A O4 1 HETATM 3091 O O5 . NAG B 2 . ? 17.617 17.896 27.753 1.00 39.26 ? 501 NAG A O5 1 HETATM 3092 O O6 . NAG B 2 . ? 18.922 17.963 25.162 1.00 48.65 ? 501 NAG A O6 1 HETATM 3093 O O7 . NAG B 2 . ? 12.727 17.177 27.821 1.00 44.58 ? 501 NAG A O7 1 HETATM 3094 C C1 . NAG C 2 . ? 18.291 6.921 80.270 1.00 21.74 ? 502 NAG A C1 1 HETATM 3095 C C2 . NAG C 2 . ? 17.468 6.630 81.532 1.00 22.20 ? 502 NAG A C2 1 HETATM 3096 C C3 . NAG C 2 . ? 18.184 7.162 82.772 1.00 32.22 ? 502 NAG A C3 1 HETATM 3097 C C4 . NAG C 2 . ? 19.581 6.557 82.824 1.00 32.71 ? 502 NAG A C4 1 HETATM 3098 C C5 . NAG C 2 . ? 20.301 6.886 81.518 1.00 35.61 ? 502 NAG A C5 1 HETATM 3099 C C6 . NAG C 2 . ? 21.735 6.366 81.490 1.00 32.43 ? 502 NAG A C6 1 HETATM 3100 C C7 . NAG C 2 . ? 15.055 6.404 81.606 1.00 28.24 ? 502 NAG A C7 1 HETATM 3101 C C8 . NAG C 2 . ? 13.717 7.061 81.456 1.00 31.92 ? 502 NAG A C8 1 HETATM 3102 N N2 . NAG C 2 . ? 16.127 7.175 81.438 1.00 24.48 ? 502 NAG A N2 1 HETATM 3103 O O3 . NAG C 2 . ? 17.450 6.872 83.941 1.00 34.41 ? 502 NAG A O3 1 HETATM 3104 O O4 . NAG C 2 . ? 20.301 7.062 83.926 1.00 47.69 ? 502 NAG A O4 1 HETATM 3105 O O5 . NAG C 2 . ? 19.576 6.350 80.426 1.00 26.64 ? 502 NAG A O5 1 HETATM 3106 O O6 . NAG C 2 . ? 22.492 7.161 80.605 1.00 47.21 ? 502 NAG A O6 1 HETATM 3107 O O7 . NAG C 2 . ? 15.128 5.207 81.873 1.00 34.54 ? 502 NAG A O7 1 HETATM 3108 C C1 . NAG D 2 . ? 39.778 1.366 58.308 1.00 10.19 ? 503 NAG A C1 1 HETATM 3109 C C2 . NAG D 2 . ? 40.720 0.806 59.385 1.00 12.77 ? 503 NAG A C2 1 HETATM 3110 C C3 . NAG D 2 . ? 41.693 -0.225 58.813 1.00 11.04 ? 503 NAG A C3 1 HETATM 3111 C C4 . NAG D 2 . ? 40.983 -1.260 57.949 1.00 11.45 ? 503 NAG A C4 1 HETATM 3112 C C5 . NAG D 2 . ? 40.101 -0.538 56.929 1.00 11.86 ? 503 NAG A C5 1 HETATM 3113 C C6 . NAG D 2 . ? 39.325 -1.493 56.021 1.00 8.57 ? 503 NAG A C6 1 HETATM 3114 C C7 . NAG D 2 . ? 41.456 2.166 61.289 1.00 18.76 ? 503 NAG A C7 1 HETATM 3115 C C8 . NAG D 2 . ? 42.376 3.265 61.741 1.00 19.41 ? 503 NAG A C8 1 HETATM 3116 N N2 . NAG D 2 . ? 41.493 1.877 59.990 1.00 13.16 ? 503 NAG A N2 1 HETATM 3117 O O3 . NAG D 2 . ? 42.379 -0.862 59.867 1.00 12.86 ? 503 NAG A O3 1 HETATM 3118 O O4 . NAG D 2 . ? 41.958 -2.052 57.297 1.00 12.02 ? 503 NAG A O4 1 HETATM 3119 O O5 . NAG D 2 . ? 39.181 0.292 57.606 1.00 10.37 ? 503 NAG A O5 1 HETATM 3120 O O6 . NAG D 2 . ? 38.521 -2.356 56.795 1.00 9.99 ? 503 NAG A O6 1 HETATM 3121 O O7 . NAG D 2 . ? 40.723 1.596 62.101 1.00 19.49 ? 503 NAG A O7 1 HETATM 3122 C C1 . NAG E 2 . ? 41.751 -3.458 57.548 1.00 12.03 ? 504 NAG A C1 1 HETATM 3123 C C2 . NAG E 2 . ? 42.314 -4.305 56.408 1.00 8.88 ? 504 NAG A C2 1 HETATM 3124 C C3 . NAG E 2 . ? 41.923 -5.762 56.646 1.00 9.78 ? 504 NAG A C3 1 HETATM 3125 C C4 . NAG E 2 . ? 42.372 -6.210 58.037 1.00 8.89 ? 504 NAG A C4 1 HETATM 3126 C C5 . NAG E 2 . ? 41.852 -5.220 59.085 1.00 12.30 ? 504 NAG A C5 1 HETATM 3127 C C6 . NAG E 2 . ? 42.304 -5.551 60.504 1.00 18.83 ? 504 NAG A C6 1 HETATM 3128 C C7 . NAG E 2 . ? 42.532 -3.091 54.299 1.00 15.81 ? 504 NAG A C7 1 HETATM 3129 C C8 . NAG E 2 . ? 41.958 -2.823 52.937 1.00 13.97 ? 504 NAG A C8 1 HETATM 3130 N N2 . NAG E 2 . ? 41.809 -3.847 55.125 1.00 10.67 ? 504 NAG A N2 1 HETATM 3131 O O3 . NAG E 2 . ? 42.423 -6.601 55.625 1.00 10.55 ? 504 NAG A O3 1 HETATM 3132 O O4 . NAG E 2 . ? 41.853 -7.495 58.302 1.00 8.73 ? 504 NAG A O4 1 HETATM 3133 O O5 . NAG E 2 . ? 42.283 -3.909 58.770 1.00 12.69 ? 504 NAG A O5 1 HETATM 3134 O O6 . NAG E 2 . ? 43.710 -5.495 60.565 1.00 22.06 ? 504 NAG A O6 1 HETATM 3135 O O7 . NAG E 2 . ? 43.625 -2.619 54.612 1.00 14.34 ? 504 NAG A O7 1 HETATM 3136 C C1 . BMA F 3 . ? 42.878 -8.458 58.596 1.00 10.75 ? 505 BMA A C1 1 HETATM 3137 C C2 . BMA F 3 . ? 42.170 -9.597 59.333 1.00 13.59 ? 505 BMA A C2 1 HETATM 3138 C C3 . BMA F 3 . ? 43.080 -10.788 59.546 1.00 12.81 ? 505 BMA A C3 1 HETATM 3139 C C4 . BMA F 3 . ? 43.865 -11.144 58.275 1.00 14.89 ? 505 BMA A C4 1 HETATM 3140 C C5 . BMA F 3 . ? 44.545 -9.901 57.672 1.00 11.63 ? 505 BMA A C5 1 HETATM 3141 C C6 . BMA F 3 . ? 45.178 -10.224 56.336 1.00 10.96 ? 505 BMA A C6 1 HETATM 3142 O O2 . BMA F 3 . ? 41.103 -10.092 58.530 1.00 11.49 ? 505 BMA A O2 1 HETATM 3143 O O3 . BMA F 3 . ? 42.290 -11.903 59.961 1.00 13.17 ? 505 BMA A O3 1 HETATM 3144 O O4 . BMA F 3 . ? 44.862 -12.118 58.578 1.00 15.32 ? 505 BMA A O4 1 HETATM 3145 O O5 . BMA F 3 . ? 43.538 -8.899 57.433 1.00 10.61 ? 505 BMA A O5 1 HETATM 3146 O O6 . BMA F 3 . ? 46.034 -9.157 55.896 1.00 14.88 ? 505 BMA A O6 1 HETATM 3147 C C1 . MAN G 4 . ? 42.936 -12.596 61.039 1.00 11.37 ? 506 MAN A C1 1 HETATM 3148 C C2 . MAN G 4 . ? 42.222 -13.913 61.284 1.00 16.72 ? 506 MAN A C2 1 HETATM 3149 C C3 . MAN G 4 . ? 40.797 -13.595 61.745 1.00 13.75 ? 506 MAN A C3 1 HETATM 3150 C C4 . MAN G 4 . ? 40.869 -12.803 63.046 1.00 15.81 ? 506 MAN A C4 1 HETATM 3151 C C5 . MAN G 4 . ? 41.693 -11.541 62.791 1.00 17.29 ? 506 MAN A C5 1 HETATM 3152 C C6 . MAN G 4 . ? 41.880 -10.746 64.079 1.00 20.03 ? 506 MAN A C6 1 HETATM 3153 O O2 . MAN G 4 . ? 43.021 -14.534 62.266 1.00 13.85 ? 506 MAN A O2 1 HETATM 3154 O O3 . MAN G 4 . ? 39.986 -14.746 61.883 1.00 11.70 ? 506 MAN A O3 1 HETATM 3155 O O4 . MAN G 4 . ? 39.566 -12.477 63.494 1.00 12.38 ? 506 MAN A O4 1 HETATM 3156 O O5 . MAN G 4 . ? 42.972 -11.876 62.260 1.00 13.69 ? 506 MAN A O5 1 HETATM 3157 O O6 . MAN G 4 . ? 42.299 -9.443 63.745 1.00 27.90 ? 506 MAN A O6 1 HETATM 3158 C C1 . MAN H 4 . ? 42.645 -15.883 62.588 1.00 12.94 ? 507 MAN A C1 1 HETATM 3159 C C2 . MAN H 4 . ? 43.585 -16.340 63.695 1.00 16.02 ? 507 MAN A C2 1 HETATM 3160 C C3 . MAN H 4 . ? 45.000 -16.443 63.140 1.00 18.92 ? 507 MAN A C3 1 HETATM 3161 C C4 . MAN H 4 . ? 44.990 -17.420 61.974 1.00 18.66 ? 507 MAN A C4 1 HETATM 3162 C C5 . MAN H 4 . ? 43.981 -16.955 60.925 1.00 15.47 ? 507 MAN A C5 1 HETATM 3163 C C6 . MAN H 4 . ? 43.923 -17.939 59.761 1.00 15.12 ? 507 MAN A C6 1 HETATM 3164 O O2 . MAN H 4 . ? 43.144 -17.584 64.184 1.00 15.58 ? 507 MAN A O2 1 HETATM 3165 O O3 . MAN H 4 . ? 45.878 -16.887 64.149 1.00 17.04 ? 507 MAN A O3 1 HETATM 3166 O O4 . MAN H 4 . ? 46.278 -17.497 61.402 1.00 19.46 ? 507 MAN A O4 1 HETATM 3167 O O5 . MAN H 4 . ? 42.691 -16.798 61.508 1.00 14.48 ? 507 MAN A O5 1 HETATM 3168 O O6 . MAN H 4 . ? 43.738 -19.249 60.251 1.00 17.78 ? 507 MAN A O6 1 HETATM 3169 C C1 . MAN I 4 . ? 42.570 -17.448 65.495 1.00 15.51 ? 508 MAN A C1 1 HETATM 3170 C C2 . MAN I 4 . ? 42.345 -18.870 65.983 1.00 15.09 ? 508 MAN A C2 1 HETATM 3171 C C3 . MAN I 4 . ? 41.299 -19.506 65.079 1.00 13.78 ? 508 MAN A C3 1 HETATM 3172 C C4 . MAN I 4 . ? 40.009 -18.708 65.184 1.00 16.75 ? 508 MAN A C4 1 HETATM 3173 C C5 . MAN I 4 . ? 40.291 -17.273 64.755 1.00 17.40 ? 508 MAN A C5 1 HETATM 3174 C C6 . MAN I 4 . ? 39.048 -16.395 64.877 1.00 16.09 ? 508 MAN A C6 1 HETATM 3175 O O2 . MAN I 4 . ? 41.923 -18.887 67.331 1.00 15.29 ? 508 MAN A O2 1 HETATM 3176 O O3 . MAN I 4 . ? 41.055 -20.823 65.491 1.00 17.54 ? 508 MAN A O3 1 HETATM 3177 O O4 . MAN I 4 . ? 39.026 -19.282 64.345 1.00 11.99 ? 508 MAN A O4 1 HETATM 3178 O O5 . MAN I 4 . ? 41.348 -16.721 65.531 1.00 15.58 ? 508 MAN A O5 1 HETATM 3179 O O6 . MAN I 4 . ? 38.595 -16.387 66.215 1.00 15.63 ? 508 MAN A O6 1 HETATM 3180 C C1 . MAN J 4 . ? 47.308 -9.238 56.557 1.00 13.91 ? 509 MAN A C1 1 HETATM 3181 C C2 . MAN J 4 . ? 48.136 -8.004 56.213 1.00 17.24 ? 509 MAN A C2 1 HETATM 3182 C C3 . MAN J 4 . ? 48.437 -7.959 54.720 1.00 17.41 ? 509 MAN A C3 1 HETATM 3183 C C4 . MAN J 4 . ? 49.080 -9.274 54.288 1.00 18.08 ? 509 MAN A C4 1 HETATM 3184 C C5 . MAN J 4 . ? 48.210 -10.441 54.751 1.00 13.43 ? 509 MAN A C5 1 HETATM 3185 C C6 . MAN J 4 . ? 48.816 -11.797 54.432 1.00 24.12 ? 509 MAN A C6 1 HETATM 3186 O O2 . MAN J 4 . ? 49.351 -8.048 56.927 1.00 22.09 ? 509 MAN A O2 1 HETATM 3187 O O3 . MAN J 4 . ? 49.292 -6.861 54.464 1.00 20.94 ? 509 MAN A O3 1 HETATM 3188 O O4 . MAN J 4 . ? 49.220 -9.283 52.886 1.00 18.87 ? 509 MAN A O4 1 HETATM 3189 O O5 . MAN J 4 . ? 48.041 -10.379 56.150 1.00 13.63 ? 509 MAN A O5 1 HETATM 3190 O O6 . MAN J 4 . ? 50.161 -11.759 54.862 1.00 23.63 ? 509 MAN A O6 1 HETATM 3191 C C1 . MAN K 4 . ? 50.783 -13.053 54.753 1.00 35.36 ? 510 MAN A C1 1 HETATM 3192 C C2 . MAN K 4 . ? 52.200 -12.942 55.288 1.00 40.96 ? 510 MAN A C2 1 HETATM 3193 C C3 . MAN K 4 . ? 52.907 -11.844 54.508 1.00 34.18 ? 510 MAN A C3 1 HETATM 3194 C C4 . MAN K 4 . ? 52.892 -12.189 53.023 1.00 40.45 ? 510 MAN A C4 1 HETATM 3195 C C5 . MAN K 4 . ? 51.478 -12.525 52.557 1.00 32.96 ? 510 MAN A C5 1 HETATM 3196 C C6 . MAN K 4 . ? 51.440 -13.049 51.127 1.00 41.34 ? 510 MAN A C6 1 HETATM 3197 O O2 . MAN K 4 . ? 52.867 -14.172 55.095 1.00 38.35 ? 510 MAN A O2 1 HETATM 3198 O O3 . MAN K 4 . ? 54.235 -11.709 54.955 1.00 41.46 ? 510 MAN A O3 1 HETATM 3199 O O4 . MAN K 4 . ? 53.341 -11.074 52.292 1.00 39.23 ? 510 MAN A O4 1 HETATM 3200 O O5 . MAN K 4 . ? 50.882 -13.485 53.412 1.00 31.52 ? 510 MAN A O5 1 HETATM 3201 O O6 . MAN K 4 . ? 52.572 -12.586 50.426 1.00 62.87 ? 510 MAN A O6 1 HETATM 3202 C C1 . MAN L 4 . ? 48.639 -5.899 53.608 1.00 20.88 ? 511 MAN A C1 1 HETATM 3203 C C2 . MAN L 4 . ? 49.662 -4.870 53.123 1.00 22.11 ? 511 MAN A C2 1 HETATM 3204 C C3 . MAN L 4 . ? 50.159 -4.052 54.307 1.00 25.99 ? 511 MAN A C3 1 HETATM 3205 C C4 . MAN L 4 . ? 48.963 -3.407 54.994 1.00 27.39 ? 511 MAN A C4 1 HETATM 3206 C C5 . MAN L 4 . ? 47.949 -4.477 55.386 1.00 16.50 ? 511 MAN A C5 1 HETATM 3207 C C6 . MAN L 4 . ? 46.718 -3.840 56.024 1.00 18.38 ? 511 MAN A C6 1 HETATM 3208 O O2 . MAN L 4 . ? 49.073 -4.015 52.164 1.00 27.28 ? 511 MAN A O2 1 HETATM 3209 O O3 . MAN L 4 . ? 51.049 -3.055 53.864 1.00 33.49 ? 511 MAN A O3 1 HETATM 3210 O O4 . MAN L 4 . ? 49.375 -2.703 56.145 1.00 28.97 ? 511 MAN A O4 1 HETATM 3211 O O5 . MAN L 4 . ? 47.568 -5.218 54.239 1.00 21.45 ? 511 MAN A O5 1 HETATM 3212 O O6 . MAN L 4 . ? 45.922 -4.836 56.626 1.00 17.29 ? 511 MAN A O6 1 HETATM 3213 CA CA . CA M 5 . ? 28.813 29.330 62.047 1.00 19.24 ? 512 CA A CA 1 HETATM 3214 O O . HOH N 6 . ? 15.970 21.947 45.351 1.00 8.31 ? 601 HOH A O 1 HETATM 3215 O O . HOH N 6 . ? 4.443 17.576 66.783 1.00 4.59 ? 602 HOH A O 1 HETATM 3216 O O . HOH N 6 . ? 19.716 31.046 61.623 1.00 5.71 ? 603 HOH A O 1 HETATM 3217 O O . HOH N 6 . ? 15.798 17.847 43.470 1.00 7.28 ? 604 HOH A O 1 HETATM 3218 O O . HOH N 6 . ? 17.100 12.314 67.052 1.00 4.80 ? 605 HOH A O 1 HETATM 3219 O O . HOH N 6 . ? 0.555 13.874 60.403 1.00 6.00 ? 606 HOH A O 1 HETATM 3220 O O . HOH N 6 . ? 15.309 19.200 50.729 1.00 3.76 ? 607 HOH A O 1 HETATM 3221 O O . HOH N 6 . ? 21.279 13.955 65.216 1.00 7.86 ? 608 HOH A O 1 HETATM 3222 O O . HOH N 6 . ? 5.100 19.540 62.730 1.00 3.75 ? 609 HOH A O 1 HETATM 3223 O O . HOH N 6 . ? 28.018 18.381 55.891 1.00 6.91 ? 610 HOH A O 1 HETATM 3224 O O . HOH N 6 . ? 21.866 38.745 63.512 1.00 8.62 ? 611 HOH A O 1 HETATM 3225 O O . HOH N 6 . ? 8.998 14.500 61.486 1.00 9.18 ? 612 HOH A O 1 HETATM 3226 O O . HOH N 6 . ? 32.747 2.688 56.323 1.00 8.92 ? 613 HOH A O 1 HETATM 3227 O O . HOH N 6 . ? 0.610 18.633 53.081 1.00 6.42 ? 614 HOH A O 1 HETATM 3228 O O . HOH N 6 . ? 25.632 3.783 53.535 1.00 6.19 ? 615 HOH A O 1 HETATM 3229 O O . HOH N 6 . ? 11.473 14.126 60.651 1.00 4.82 ? 616 HOH A O 1 HETATM 3230 O O . HOH N 6 . ? 10.339 11.735 47.073 1.00 7.86 ? 617 HOH A O 1 HETATM 3231 O O . HOH N 6 . ? 5.637 32.218 44.243 1.00 9.50 ? 618 HOH A O 1 HETATM 3232 O O . HOH N 6 . ? 18.625 20.997 49.513 1.00 7.46 ? 619 HOH A O 1 HETATM 3233 O O . HOH N 6 . ? 0.735 31.992 55.012 1.00 6.26 ? 620 HOH A O 1 HETATM 3234 O O . HOH N 6 . ? 30.984 29.587 63.318 1.00 9.70 ? 621 HOH A O 1 HETATM 3235 O O . HOH N 6 . ? 28.363 3.230 54.394 1.00 5.60 ? 622 HOH A O 1 HETATM 3236 O O . HOH N 6 . ? 19.638 13.616 67.513 1.00 6.66 ? 623 HOH A O 1 HETATM 3237 O O . HOH N 6 . ? 12.087 1.509 60.611 1.00 7.39 ? 624 HOH A O 1 HETATM 3238 O O . HOH N 6 . ? -1.022 12.556 72.104 1.00 6.43 ? 625 HOH A O 1 HETATM 3239 O O . HOH N 6 . ? 17.999 18.742 57.443 1.00 5.32 ? 626 HOH A O 1 HETATM 3240 O O . HOH N 6 . ? 14.265 15.426 43.794 1.00 7.62 ? 627 HOH A O 1 HETATM 3241 O O . HOH N 6 . ? 1.104 30.855 57.602 1.00 6.29 ? 628 HOH A O 1 HETATM 3242 O O . HOH N 6 . ? 30.901 34.196 63.407 1.00 8.95 ? 629 HOH A O 1 HETATM 3243 O O . HOH N 6 . ? 27.023 19.575 52.024 1.00 6.57 ? 630 HOH A O 1 HETATM 3244 O O . HOH N 6 . ? 5.452 29.222 66.529 1.00 6.13 ? 631 HOH A O 1 HETATM 3245 O O . HOH N 6 . ? 20.563 1.304 60.879 1.00 3.81 ? 632 HOH A O 1 HETATM 3246 O O . HOH N 6 . ? 12.349 17.777 44.591 1.00 6.87 ? 633 HOH A O 1 HETATM 3247 O O . HOH N 6 . ? 5.961 3.335 70.417 1.00 10.43 ? 634 HOH A O 1 HETATM 3248 O O . HOH N 6 . ? 9.660 12.797 63.638 1.00 8.90 ? 635 HOH A O 1 HETATM 3249 O O . HOH N 6 . ? 19.773 13.682 56.387 1.00 6.19 ? 636 HOH A O 1 HETATM 3250 O O . HOH N 6 . ? 27.816 38.703 55.087 1.00 9.24 ? 637 HOH A O 1 HETATM 3251 O O . HOH N 6 . ? 17.703 22.351 69.875 1.00 8.55 ? 638 HOH A O 1 HETATM 3252 O O . HOH N 6 . ? 27.812 30.779 63.696 1.00 10.42 ? 639 HOH A O 1 HETATM 3253 O O . HOH N 6 . ? 20.662 16.184 68.112 1.00 5.40 ? 640 HOH A O 1 HETATM 3254 O O . HOH N 6 . ? 7.515 40.705 47.456 1.00 12.81 ? 641 HOH A O 1 HETATM 3255 O O . HOH N 6 . ? 19.742 21.007 68.478 1.00 8.28 ? 642 HOH A O 1 HETATM 3256 O O . HOH N 6 . ? 19.721 32.369 55.025 1.00 7.74 ? 643 HOH A O 1 HETATM 3257 O O . HOH N 6 . ? 30.509 1.698 57.647 1.00 6.73 ? 644 HOH A O 1 HETATM 3258 O O . HOH N 6 . ? 3.320 37.079 54.472 1.00 8.11 ? 645 HOH A O 1 HETATM 3259 O O . HOH N 6 . ? 20.849 37.533 46.053 1.00 9.50 ? 646 HOH A O 1 HETATM 3260 O O . HOH N 6 . ? 12.302 10.244 78.216 1.00 10.44 ? 647 HOH A O 1 HETATM 3261 O O . HOH N 6 . ? 35.454 9.324 58.004 1.00 8.32 ? 648 HOH A O 1 HETATM 3262 O O . HOH N 6 . ? 14.978 4.166 78.539 1.00 11.66 ? 649 HOH A O 1 HETATM 3263 O O . HOH N 6 . ? 16.676 20.651 71.875 1.00 6.45 ? 650 HOH A O 1 HETATM 3264 O O . HOH N 6 . ? 7.210 24.258 41.380 1.00 9.48 ? 651 HOH A O 1 HETATM 3265 O O . HOH N 6 . ? 17.931 26.514 60.248 1.00 6.37 ? 652 HOH A O 1 HETATM 3266 O O . HOH N 6 . ? -0.638 29.498 54.165 1.00 8.86 ? 653 HOH A O 1 HETATM 3267 O O . HOH N 6 . ? 4.995 39.309 54.069 1.00 10.02 ? 654 HOH A O 1 HETATM 3268 O O . HOH N 6 . ? 21.409 10.651 37.647 1.00 10.38 ? 655 HOH A O 1 HETATM 3269 O O . HOH N 6 . ? 25.691 16.856 58.935 1.00 14.39 ? 656 HOH A O 1 HETATM 3270 O O . HOH N 6 . ? 6.138 16.138 41.699 1.00 9.87 ? 657 HOH A O 1 HETATM 3271 O O . HOH N 6 . ? 23.833 3.870 60.566 1.00 6.85 ? 658 HOH A O 1 HETATM 3272 O O . HOH N 6 . ? 19.678 27.493 49.592 1.00 11.44 ? 659 HOH A O 1 HETATM 3273 O O . HOH N 6 . ? 23.985 18.371 33.075 1.00 11.88 ? 660 HOH A O 1 HETATM 3274 O O . HOH N 6 . ? 44.926 -6.856 54.917 1.00 14.75 ? 661 HOH A O 1 HETATM 3275 O O . HOH N 6 . ? 16.371 17.139 40.886 1.00 8.68 ? 662 HOH A O 1 HETATM 3276 O O . HOH N 6 . ? 19.656 11.721 74.497 1.00 9.41 ? 663 HOH A O 1 HETATM 3277 O O . HOH N 6 . ? 9.317 30.919 43.934 1.00 10.24 ? 664 HOH A O 1 HETATM 3278 O O . HOH N 6 . ? 18.018 15.542 35.610 1.00 9.23 ? 665 HOH A O 1 HETATM 3279 O O . HOH N 6 . ? 21.210 37.358 43.304 1.00 15.30 ? 666 HOH A O 1 HETATM 3280 O O . HOH N 6 . ? 22.891 10.008 39.933 1.00 11.06 ? 667 HOH A O 1 HETATM 3281 O O . HOH N 6 . ? 14.078 3.165 61.798 1.00 8.59 ? 668 HOH A O 1 HETATM 3282 O O . HOH N 6 . ? 37.522 24.295 54.846 1.00 12.04 ? 669 HOH A O 1 HETATM 3283 O O . HOH N 6 . ? 18.958 29.068 59.839 1.00 6.95 ? 670 HOH A O 1 HETATM 3284 O O . HOH N 6 . ? 39.450 22.781 48.709 1.00 15.87 ? 671 HOH A O 1 HETATM 3285 O O . HOH N 6 . ? 6.305 6.625 69.912 1.00 7.76 ? 672 HOH A O 1 HETATM 3286 O O . HOH N 6 . ? 32.141 43.738 52.588 1.00 14.27 ? 673 HOH A O 1 HETATM 3287 O O . HOH N 6 . ? 40.463 18.983 58.349 1.00 13.13 ? 674 HOH A O 1 HETATM 3288 O O . HOH N 6 . ? 10.807 1.243 69.663 1.00 9.18 ? 675 HOH A O 1 HETATM 3289 O O . HOH N 6 . ? 30.815 7.842 63.483 1.00 12.07 ? 676 HOH A O 1 HETATM 3290 O O . HOH N 6 . ? 7.604 34.373 70.707 1.00 13.85 ? 677 HOH A O 1 HETATM 3291 O O . HOH N 6 . ? 37.456 0.952 61.218 1.00 10.82 ? 678 HOH A O 1 HETATM 3292 O O . HOH N 6 . ? 37.296 13.615 38.837 1.00 18.91 ? 679 HOH A O 1 HETATM 3293 O O . HOH N 6 . ? 7.807 23.640 43.989 1.00 9.68 ? 680 HOH A O 1 HETATM 3294 O O . HOH N 6 . ? 14.170 21.267 71.919 1.00 11.85 ? 681 HOH A O 1 HETATM 3295 O O . HOH N 6 . ? 34.861 16.553 61.950 1.00 12.14 ? 682 HOH A O 1 HETATM 3296 O O . HOH N 6 . ? 20.151 5.450 67.159 1.00 10.52 ? 683 HOH A O 1 HETATM 3297 O O . HOH N 6 . ? 27.488 29.882 58.315 1.00 8.69 ? 684 HOH A O 1 HETATM 3298 O O . HOH N 6 . ? 6.256 21.561 75.910 1.00 13.15 ? 685 HOH A O 1 HETATM 3299 O O . HOH N 6 . ? 15.088 32.774 38.894 1.00 13.15 ? 686 HOH A O 1 HETATM 3300 O O . HOH N 6 . ? 4.507 25.174 41.305 1.00 14.68 ? 687 HOH A O 1 HETATM 3301 O O . HOH N 6 . ? 23.258 25.113 55.385 1.00 7.29 ? 688 HOH A O 1 HETATM 3302 O O . HOH N 6 . ? 22.745 19.520 64.969 1.00 13.04 ? 689 HOH A O 1 HETATM 3303 O O . HOH N 6 . ? 36.668 5.822 47.390 1.00 10.77 ? 690 HOH A O 1 HETATM 3304 O O . HOH N 6 . ? -3.539 18.693 74.948 1.00 12.63 ? 691 HOH A O 1 HETATM 3305 O O . HOH N 6 . ? 11.563 21.122 35.210 1.00 19.20 ? 692 HOH A O 1 HETATM 3306 O O . HOH N 6 . ? 10.440 31.089 34.582 1.00 13.53 ? 693 HOH A O 1 HETATM 3307 O O . HOH N 6 . ? 21.174 12.155 76.583 1.00 11.95 ? 694 HOH A O 1 HETATM 3308 O O . HOH N 6 . ? 15.683 23.698 68.494 1.00 8.69 ? 695 HOH A O 1 HETATM 3309 O O . HOH N 6 . ? 9.672 11.502 66.045 1.00 10.41 ? 696 HOH A O 1 HETATM 3310 O O . HOH N 6 . ? 23.555 47.340 62.314 1.00 13.07 ? 697 HOH A O 1 HETATM 3311 O O . HOH N 6 . ? 19.451 18.359 69.440 1.00 7.71 ? 698 HOH A O 1 HETATM 3312 O O . HOH N 6 . ? 16.829 2.962 61.294 1.00 11.20 ? 699 HOH A O 1 HETATM 3313 O O . HOH N 6 . ? 17.281 0.656 50.975 1.00 13.86 ? 700 HOH A O 1 HETATM 3314 O O . HOH N 6 . ? 0.023 11.757 53.923 1.00 10.67 ? 701 HOH A O 1 HETATM 3315 O O . HOH N 6 . ? 24.580 22.375 61.939 1.00 14.16 ? 702 HOH A O 1 HETATM 3316 O O . HOH N 6 . ? 8.265 24.210 67.968 1.00 8.08 ? 703 HOH A O 1 HETATM 3317 O O . HOH N 6 . ? 38.010 22.234 51.039 1.00 11.18 ? 704 HOH A O 1 HETATM 3318 O O . HOH N 6 . ? 37.698 2.746 63.270 1.00 14.20 ? 705 HOH A O 1 HETATM 3319 O O . HOH N 6 . ? 35.000 22.892 54.508 1.00 10.14 ? 706 HOH A O 1 HETATM 3320 O O . HOH N 6 . ? 24.177 34.659 56.089 1.00 7.11 ? 707 HOH A O 1 HETATM 3321 O O . HOH N 6 . ? 18.685 29.634 57.106 1.00 11.61 ? 708 HOH A O 1 HETATM 3322 O O . HOH N 6 . ? 12.455 35.174 39.516 1.00 14.14 ? 709 HOH A O 1 HETATM 3323 O O . HOH N 6 . ? 27.878 42.295 64.389 1.00 15.09 ? 710 HOH A O 1 HETATM 3324 O O . HOH N 6 . ? 39.901 3.224 54.933 1.00 11.21 ? 711 HOH A O 1 HETATM 3325 O O . HOH N 6 . ? 1.643 29.823 68.825 1.00 13.13 ? 712 HOH A O 1 HETATM 3326 O O . HOH N 6 . ? 19.193 4.402 71.231 1.00 18.05 ? 713 HOH A O 1 HETATM 3327 O O . HOH N 6 . ? 29.418 19.175 53.494 1.00 10.14 ? 714 HOH A O 1 HETATM 3328 O O . HOH N 6 . ? 22.862 26.463 66.321 1.00 11.51 ? 715 HOH A O 1 HETATM 3329 O O . HOH N 6 . ? 5.431 23.071 45.279 1.00 10.61 ? 716 HOH A O 1 HETATM 3330 O O . HOH N 6 . ? 11.721 7.907 47.958 1.00 12.15 ? 717 HOH A O 1 HETATM 3331 O O . HOH N 6 . ? 4.029 32.081 58.317 1.00 10.77 ? 718 HOH A O 1 HETATM 3332 O O . HOH N 6 . ? 41.181 29.639 55.615 1.00 18.65 ? 719 HOH A O 1 HETATM 3333 O O . HOH N 6 . ? 31.978 16.814 62.495 1.00 17.11 ? 720 HOH A O 1 HETATM 3334 O O . HOH N 6 . ? 15.945 18.059 38.203 1.00 13.14 ? 721 HOH A O 1 HETATM 3335 O O . HOH N 6 . ? 31.643 -1.223 43.589 1.00 12.52 ? 722 HOH A O 1 HETATM 3336 O O . HOH N 6 . ? -1.891 24.228 52.098 1.00 10.86 ? 723 HOH A O 1 HETATM 3337 O O . HOH N 6 . ? 34.547 34.073 64.265 1.00 20.48 ? 724 HOH A O 1 HETATM 3338 O O . HOH N 6 . ? 38.897 27.548 48.311 1.00 23.02 ? 725 HOH A O 1 HETATM 3339 O O . HOH N 6 . ? 28.561 44.681 47.837 1.00 20.35 ? 726 HOH A O 1 HETATM 3340 O O . HOH N 6 . ? 28.121 18.338 58.714 1.00 11.89 ? 727 HOH A O 1 HETATM 3341 O O . HOH N 6 . ? 30.382 19.154 61.941 1.00 15.77 ? 728 HOH A O 1 HETATM 3342 O O . HOH N 6 . ? 26.776 41.206 68.207 1.00 13.33 ? 729 HOH A O 1 HETATM 3343 O O . HOH N 6 . ? 29.104 28.078 38.706 1.00 17.32 ? 730 HOH A O 1 HETATM 3344 O O . HOH N 6 . ? 34.932 39.621 52.454 1.00 16.88 ? 731 HOH A O 1 HETATM 3345 O O . HOH N 6 . ? 25.726 18.621 63.935 1.00 15.68 ? 732 HOH A O 1 HETATM 3346 O O . HOH N 6 . ? 20.295 26.134 70.214 1.00 12.98 ? 733 HOH A O 1 HETATM 3347 O O . HOH N 6 . ? 38.986 19.215 49.156 1.00 15.96 ? 734 HOH A O 1 HETATM 3348 O O . HOH N 6 . ? 35.602 29.953 58.517 1.00 15.49 ? 735 HOH A O 1 HETATM 3349 O O . HOH N 6 . ? 3.506 11.650 49.481 1.00 12.10 ? 736 HOH A O 1 HETATM 3350 O O . HOH N 6 . ? 8.701 35.627 67.733 1.00 12.19 ? 737 HOH A O 1 HETATM 3351 O O . HOH N 6 . ? 38.338 27.082 51.216 1.00 22.57 ? 738 HOH A O 1 HETATM 3352 O O . HOH N 6 . ? 27.550 19.799 61.583 1.00 17.21 ? 739 HOH A O 1 HETATM 3353 O O . HOH N 6 . ? 1.195 38.901 62.359 1.00 15.59 ? 740 HOH A O 1 HETATM 3354 O O . HOH N 6 . ? 38.550 24.623 52.292 1.00 17.52 ? 741 HOH A O 1 HETATM 3355 O O . HOH N 6 . ? 8.250 43.823 49.002 1.00 19.80 ? 742 HOH A O 1 HETATM 3356 O O . HOH N 6 . ? 36.054 9.168 44.738 1.00 15.61 ? 743 HOH A O 1 HETATM 3357 O O . HOH N 6 . ? 24.039 37.295 55.051 1.00 11.54 ? 744 HOH A O 1 HETATM 3358 O O . HOH N 6 . ? 26.459 7.538 34.319 1.00 17.56 ? 745 HOH A O 1 HETATM 3359 O O . HOH N 6 . ? 6.311 4.930 52.645 1.00 15.57 ? 746 HOH A O 1 HETATM 3360 O O . HOH N 6 . ? 4.621 20.410 79.074 1.00 21.04 ? 747 HOH A O 1 HETATM 3361 O O . HOH N 6 . ? 7.050 41.473 43.917 1.00 16.64 ? 748 HOH A O 1 HETATM 3362 O O . HOH N 6 . ? 5.943 34.418 39.152 1.00 14.25 ? 749 HOH A O 1 HETATM 3363 O O . HOH N 6 . ? 23.618 48.564 55.409 1.00 16.35 ? 750 HOH A O 1 HETATM 3364 O O . HOH N 6 . ? 13.566 8.006 76.635 1.00 13.21 ? 751 HOH A O 1 HETATM 3365 O O . HOH N 6 . ? 1.264 22.426 39.805 1.00 16.24 ? 752 HOH A O 1 HETATM 3366 O O . HOH N 6 . ? 39.714 34.860 50.452 1.00 20.76 ? 753 HOH A O 1 HETATM 3367 O O . HOH N 6 . ? 15.575 -3.713 43.157 1.00 14.73 ? 754 HOH A O 1 HETATM 3368 O O . HOH N 6 . ? 33.326 41.685 51.325 1.00 15.41 ? 755 HOH A O 1 HETATM 3369 O O . HOH N 6 . ? 35.132 6.470 45.103 1.00 15.57 ? 756 HOH A O 1 HETATM 3370 O O . HOH N 6 . ? 11.625 14.735 34.082 1.00 12.23 ? 757 HOH A O 1 HETATM 3371 O O . HOH N 6 . ? 30.783 45.251 59.718 0.50 20.41 ? 758 HOH A O 1 HETATM 3372 O O . HOH N 6 . ? 22.490 39.904 42.996 1.00 22.28 ? 759 HOH A O 1 HETATM 3373 O O . HOH N 6 . ? 11.472 7.609 45.156 1.00 16.05 ? 760 HOH A O 1 HETATM 3374 O O . HOH N 6 . ? 4.414 9.369 80.040 1.00 16.07 ? 761 HOH A O 1 HETATM 3375 O O . HOH N 6 . ? -2.128 39.486 47.281 1.00 18.21 ? 762 HOH A O 1 HETATM 3376 O O . HOH N 6 . ? 24.880 20.917 64.712 1.00 20.60 ? 763 HOH A O 1 HETATM 3377 O O . HOH N 6 . ? 19.971 23.487 70.978 1.00 15.31 ? 764 HOH A O 1 HETATM 3378 O O . HOH N 6 . ? 3.672 0.970 71.018 1.00 17.60 ? 765 HOH A O 1 HETATM 3379 O O . HOH N 6 . ? 18.068 6.305 34.496 1.00 18.52 ? 766 HOH A O 1 HETATM 3380 O O . HOH N 6 . ? 27.679 17.741 30.883 1.00 22.25 ? 767 HOH A O 1 HETATM 3381 O O . HOH N 6 . ? 21.936 51.554 61.301 1.00 17.32 ? 768 HOH A O 1 HETATM 3382 O O . HOH N 6 . ? -0.559 16.589 60.120 1.00 14.70 ? 769 HOH A O 1 HETATM 3383 O O . HOH N 6 . ? 31.158 5.301 39.693 1.00 15.16 ? 770 HOH A O 1 HETATM 3384 O O . HOH N 6 . ? 34.071 6.643 65.900 1.00 16.71 ? 771 HOH A O 1 HETATM 3385 O O . HOH N 6 . ? 44.840 -1.032 56.591 1.00 21.04 ? 772 HOH A O 1 HETATM 3386 O O . HOH N 6 . ? 2.768 14.388 46.742 1.00 14.21 ? 773 HOH A O 1 HETATM 3387 O O . HOH N 6 . ? 5.191 23.623 70.348 1.00 13.40 ? 774 HOH A O 1 HETATM 3388 O O . HOH N 6 . ? 31.152 27.354 37.236 1.00 16.75 ? 775 HOH A O 1 HETATM 3389 O O . HOH N 6 . ? 29.567 41.606 45.328 1.00 19.72 ? 776 HOH A O 1 HETATM 3390 O O . HOH N 6 . ? 18.084 36.804 69.935 1.00 18.45 ? 777 HOH A O 1 HETATM 3391 O O . HOH N 6 . ? 10.024 1.196 58.514 1.00 12.65 ? 778 HOH A O 1 HETATM 3392 O O . HOH N 6 . ? 42.070 21.525 60.053 1.00 20.37 ? 779 HOH A O 1 HETATM 3393 O O . HOH N 6 . ? 17.437 3.549 47.942 1.00 17.80 ? 780 HOH A O 1 HETATM 3394 O O . HOH N 6 . ? 23.241 -2.638 41.905 1.00 17.75 ? 781 HOH A O 1 HETATM 3395 O O . HOH N 6 . ? 13.854 5.565 41.911 1.00 16.07 ? 782 HOH A O 1 HETATM 3396 O O . HOH N 6 . ? 1.212 7.175 55.625 1.00 20.35 ? 783 HOH A O 1 HETATM 3397 O O . HOH N 6 . ? 32.976 26.349 33.788 1.00 22.70 ? 784 HOH A O 1 HETATM 3398 O O . HOH N 6 . ? 28.072 36.797 69.022 1.00 18.80 ? 785 HOH A O 1 HETATM 3399 O O . HOH N 6 . ? 24.093 14.285 60.791 1.00 22.19 ? 786 HOH A O 1 HETATM 3400 O O . HOH N 6 . ? 10.460 33.210 36.738 1.00 21.28 ? 787 HOH A O 1 HETATM 3401 O O . HOH N 6 . ? 3.737 28.998 70.593 1.00 20.38 ? 788 HOH A O 1 HETATM 3402 O O . HOH N 6 . ? 8.026 24.749 70.756 1.00 17.49 ? 789 HOH A O 1 HETATM 3403 O O . HOH N 6 . ? 29.835 6.857 65.695 1.00 16.86 ? 790 HOH A O 1 HETATM 3404 O O . HOH N 6 . ? -0.863 40.441 53.605 1.00 15.88 ? 791 HOH A O 1 HETATM 3405 O O . HOH N 6 . ? 9.926 38.876 45.567 1.00 13.11 ? 792 HOH A O 1 HETATM 3406 O O . HOH N 6 . ? 4.185 21.190 43.633 1.00 18.36 ? 793 HOH A O 1 HETATM 3407 O O . HOH N 6 . ? 28.823 47.901 48.857 1.00 24.98 ? 794 HOH A O 1 HETATM 3408 O O . HOH N 6 . ? 31.935 47.621 51.625 1.00 19.69 ? 795 HOH A O 1 HETATM 3409 O O . HOH N 6 . ? 37.079 6.828 64.952 1.00 14.43 ? 796 HOH A O 1 HETATM 3410 O O . HOH N 6 . ? 42.213 18.565 60.919 1.00 23.97 ? 797 HOH A O 1 HETATM 3411 O O . HOH N 6 . ? 14.929 -1.358 41.945 1.00 19.39 ? 798 HOH A O 1 HETATM 3412 O O . HOH N 6 . ? 40.210 34.140 56.122 1.00 22.44 ? 799 HOH A O 1 HETATM 3413 O O . HOH N 6 . ? 14.774 40.603 47.556 1.00 16.66 ? 800 HOH A O 1 HETATM 3414 O O . HOH N 6 . ? 41.264 23.207 53.444 1.00 24.23 ? 801 HOH A O 1 HETATM 3415 O O . HOH N 6 . ? 40.005 16.692 48.366 1.00 20.77 ? 802 HOH A O 1 HETATM 3416 O O . HOH N 6 . ? 24.641 12.767 61.916 1.00 16.48 ? 803 HOH A O 1 HETATM 3417 O O . HOH N 6 . ? 9.561 10.343 77.278 1.00 14.16 ? 804 HOH A O 1 HETATM 3418 O O . HOH N 6 . ? 32.201 43.728 57.400 1.00 24.68 ? 805 HOH A O 1 HETATM 3419 O O . HOH N 6 . ? 22.653 8.117 67.001 1.00 15.80 ? 806 HOH A O 1 HETATM 3420 O O . HOH N 6 . ? 37.959 8.082 48.642 1.00 16.48 ? 807 HOH A O 1 HETATM 3421 O O . HOH N 6 . ? 21.198 45.841 60.388 1.00 28.93 ? 808 HOH A O 1 HETATM 3422 O O . HOH N 6 . ? 16.372 41.384 40.147 1.00 19.93 ? 809 HOH A O 1 HETATM 3423 O O . HOH N 6 . ? 38.691 39.161 55.729 1.00 26.11 ? 810 HOH A O 1 HETATM 3424 O O . HOH N 6 . ? 16.394 5.751 47.180 1.00 17.36 ? 811 HOH A O 1 HETATM 3425 O O . HOH N 6 . ? 37.663 27.984 66.050 1.00 24.59 ? 812 HOH A O 1 HETATM 3426 O O . HOH N 6 . ? 10.672 37.397 40.316 1.00 21.81 ? 813 HOH A O 1 HETATM 3427 O O . HOH N 6 . ? 40.229 31.664 57.389 1.00 22.09 ? 814 HOH A O 1 HETATM 3428 O O . HOH N 6 . ? 22.959 19.234 45.462 1.00 15.43 ? 815 HOH A O 1 HETATM 3429 O O . HOH N 6 . ? 8.464 24.280 73.389 1.00 23.89 ? 816 HOH A O 1 HETATM 3430 O O . HOH N 6 . ? 22.135 22.034 70.059 1.00 25.38 ? 817 HOH A O 1 HETATM 3431 O O . HOH N 6 . ? 13.721 -0.179 81.588 1.00 20.26 ? 818 HOH A O 1 HETATM 3432 O O . HOH N 6 . ? 20.455 28.676 40.875 1.00 25.79 ? 819 HOH A O 1 HETATM 3433 O O . HOH N 6 . ? 3.630 30.660 43.421 1.00 18.63 ? 820 HOH A O 1 HETATM 3434 O O . HOH N 6 . ? 10.407 32.753 32.533 1.00 22.97 ? 821 HOH A O 1 HETATM 3435 O O . HOH N 6 . ? 36.470 25.851 37.326 1.00 41.41 ? 822 HOH A O 1 HETATM 3436 O O . HOH N 6 . ? 35.263 24.389 39.274 1.00 21.20 ? 823 HOH A O 1 HETATM 3437 O O . HOH N 6 . ? 32.282 2.369 43.511 1.00 17.50 ? 824 HOH A O 1 HETATM 3438 O O . HOH N 6 . ? 11.079 6.902 40.299 1.00 18.18 ? 825 HOH A O 1 HETATM 3439 O O . HOH N 6 . ? 13.540 -0.136 51.382 1.00 14.98 ? 826 HOH A O 1 HETATM 3440 O O . HOH N 6 . ? 31.852 16.724 65.034 1.00 25.54 ? 827 HOH A O 1 HETATM 3441 O O . HOH N 6 . ? 0.000 -0.000 70.191 0.25 23.96 ? 828 HOH A O 1 HETATM 3442 O O . HOH N 6 . ? 16.424 12.282 28.983 1.00 20.18 ? 829 HOH A O 1 HETATM 3443 O O . HOH N 6 . ? 3.857 19.354 45.616 1.00 20.37 ? 830 HOH A O 1 HETATM 3444 O O . HOH N 6 . ? 0.868 24.909 38.623 1.00 23.13 ? 831 HOH A O 1 HETATM 3445 O O . HOH N 6 . ? 25.756 0.241 70.358 1.00 25.82 ? 832 HOH A O 1 HETATM 3446 O O . HOH N 6 . ? 19.980 45.503 47.873 1.00 23.38 ? 833 HOH A O 1 HETATM 3447 O O . HOH N 6 . ? 38.385 17.456 64.265 1.00 20.37 ? 834 HOH A O 1 HETATM 3448 O O . HOH N 6 . ? 37.615 39.241 52.853 1.00 27.09 ? 835 HOH A O 1 HETATM 3449 O O . HOH N 6 . ? 42.251 14.839 58.374 1.00 25.15 ? 836 HOH A O 1 HETATM 3450 O O . HOH N 6 . ? -0.443 8.316 76.525 1.00 25.34 ? 837 HOH A O 1 HETATM 3451 O O . HOH N 6 . ? 0.916 34.553 63.913 1.00 23.85 ? 838 HOH A O 1 HETATM 3452 O O . HOH N 6 . ? 34.402 36.346 45.247 1.00 26.32 ? 839 HOH A O 1 HETATM 3453 O O . HOH N 6 . ? 26.978 22.879 64.470 1.00 26.41 ? 840 HOH A O 1 HETATM 3454 O O . HOH N 6 . ? 20.819 1.120 39.578 1.00 21.96 ? 841 HOH A O 1 HETATM 3455 O O . HOH N 6 . ? 34.218 33.875 44.677 1.00 21.45 ? 842 HOH A O 1 HETATM 3456 O O . HOH N 6 . ? 33.944 45.251 56.558 0.50 32.04 ? 843 HOH A O 1 HETATM 3457 O O . HOH N 6 . ? 18.601 0.100 38.045 1.00 27.40 ? 844 HOH A O 1 HETATM 3458 O O . HOH N 6 . ? 39.743 27.483 54.678 1.00 17.90 ? 845 HOH A O 1 HETATM 3459 O O . HOH N 6 . ? 24.481 43.907 44.098 1.00 22.62 ? 846 HOH A O 1 HETATM 3460 O O . HOH N 6 . ? 22.079 35.432 41.861 1.00 27.07 ? 847 HOH A O 1 HETATM 3461 O O . HOH N 6 . ? 24.382 18.116 30.499 1.00 24.09 ? 848 HOH A O 1 HETATM 3462 O O . HOH N 6 . ? 41.695 18.034 43.814 1.00 22.45 ? 849 HOH A O 1 HETATM 3463 O O . HOH N 6 . ? 41.019 16.210 60.518 1.00 21.88 ? 850 HOH A O 1 HETATM 3464 O O . HOH N 6 . ? 44.947 -1.223 52.780 1.00 30.21 ? 851 HOH A O 1 HETATM 3465 O O . HOH N 6 . ? 40.092 2.426 64.557 1.00 30.07 ? 852 HOH A O 1 HETATM 3466 O O . HOH N 6 . ? 21.857 32.412 42.681 1.00 22.88 ? 853 HOH A O 1 HETATM 3467 O O . HOH N 6 . ? 33.581 42.445 48.541 1.00 24.58 ? 854 HOH A O 1 HETATM 3468 O O . HOH N 6 . ? 39.099 -7.715 59.233 1.00 22.45 ? 855 HOH A O 1 HETATM 3469 O O . HOH N 6 . ? 29.912 8.948 67.714 1.00 26.18 ? 856 HOH A O 1 HETATM 3470 O O . HOH N 6 . ? 42.413 31.051 53.781 1.00 31.99 ? 857 HOH A O 1 HETATM 3471 O O . HOH N 6 . ? 20.826 39.490 69.871 1.00 25.08 ? 858 HOH A O 1 HETATM 3472 O O . HOH N 6 . ? 20.712 19.734 78.405 1.00 25.58 ? 859 HOH A O 1 HETATM 3473 O O . HOH N 6 . ? 3.187 12.630 82.079 1.00 23.20 ? 860 HOH A O 1 HETATM 3474 O O . HOH N 6 . ? 22.021 27.210 73.131 1.00 28.30 ? 861 HOH A O 1 HETATM 3475 O O . HOH N 6 . ? 46.813 -11.239 60.179 1.00 28.74 ? 862 HOH A O 1 HETATM 3476 O O . HOH N 6 . ? 9.472 35.163 72.590 1.00 25.35 ? 863 HOH A O 1 HETATM 3477 O O . HOH N 6 . ? 4.421 5.339 50.417 1.00 24.19 ? 864 HOH A O 1 HETATM 3478 O O . HOH N 6 . ? 24.593 31.097 71.968 1.00 19.87 ? 865 HOH A O 1 HETATM 3479 O O . HOH N 6 . ? 40.690 5.373 50.840 1.00 30.88 ? 866 HOH A O 1 HETATM 3480 O O . HOH N 6 . ? 29.764 31.514 44.125 1.00 28.61 ? 867 HOH A O 1 HETATM 3481 O O . HOH N 6 . ? 12.558 19.600 79.702 1.00 21.77 ? 868 HOH A O 1 HETATM 3482 O O . HOH N 6 . ? 3.806 32.631 39.068 1.00 23.60 ? 869 HOH A O 1 HETATM 3483 O O . HOH N 6 . ? 26.407 28.095 37.742 1.00 30.36 ? 870 HOH A O 1 HETATM 3484 O O . HOH N 6 . ? 9.768 22.552 77.054 1.00 20.77 ? 871 HOH A O 1 HETATM 3485 O O . HOH N 6 . ? 21.086 23.686 75.721 1.00 28.45 ? 872 HOH A O 1 HETATM 3486 O O . HOH N 6 . ? 12.829 19.297 31.712 1.00 20.92 ? 873 HOH A O 1 HETATM 3487 O O . HOH N 6 . ? 32.405 10.529 68.140 1.00 26.98 ? 874 HOH A O 1 HETATM 3488 O O . HOH N 6 . ? 31.381 33.869 43.756 1.00 27.25 ? 875 HOH A O 1 HETATM 3489 O O . HOH N 6 . ? 32.194 31.392 69.704 1.00 24.14 ? 876 HOH A O 1 HETATM 3490 O O . HOH N 6 . ? 11.594 11.432 81.435 1.00 29.07 ? 877 HOH A O 1 HETATM 3491 O O . HOH N 6 . ? 16.657 -2.973 45.620 1.00 18.44 ? 878 HOH A O 1 HETATM 3492 O O . HOH N 6 . ? 9.873 12.413 34.519 1.00 22.65 ? 879 HOH A O 1 HETATM 3493 O O . HOH N 6 . ? 40.772 27.803 51.444 1.00 30.49 ? 880 HOH A O 1 HETATM 3494 O O . HOH N 6 . ? 11.753 21.700 32.222 1.00 29.90 ? 881 HOH A O 1 HETATM 3495 O O . HOH N 6 . ? 2.872 29.441 35.925 1.00 37.34 ? 882 HOH A O 1 HETATM 3496 O O . HOH N 6 . ? -3.197 40.212 50.012 1.00 25.80 ? 883 HOH A O 1 HETATM 3497 O O . HOH N 6 . ? 21.798 21.509 29.220 1.00 29.68 ? 884 HOH A O 1 HETATM 3498 O O . HOH N 6 . ? 43.642 28.668 56.944 1.00 28.23 ? 885 HOH A O 1 HETATM 3499 O O . HOH N 6 . ? 38.597 11.157 63.146 1.00 23.58 ? 886 HOH A O 1 HETATM 3500 O O . HOH N 6 . ? 2.455 7.486 49.258 1.00 29.25 ? 887 HOH A O 1 HETATM 3501 O O . HOH N 6 . ? 26.824 12.876 68.839 1.00 24.56 ? 888 HOH A O 1 HETATM 3502 O O . HOH N 6 . ? 43.021 3.174 58.373 1.00 36.61 ? 889 HOH A O 1 HETATM 3503 O O . HOH N 6 . ? 18.505 31.529 41.999 1.00 24.80 ? 890 HOH A O 1 HETATM 3504 O O . HOH N 6 . ? -0.031 21.830 72.547 1.00 23.68 ? 891 HOH A O 1 HETATM 3505 O O . HOH N 6 . ? 40.866 21.655 63.491 1.00 28.97 ? 892 HOH A O 1 HETATM 3506 O O . HOH N 6 . ? 7.937 6.916 77.655 1.00 29.52 ? 893 HOH A O 1 HETATM 3507 O O . HOH N 6 . ? 12.626 4.896 38.719 1.00 26.94 ? 894 HOH A O 1 HETATM 3508 O O . HOH N 6 . ? 0.052 9.101 54.137 1.00 31.34 ? 895 HOH A O 1 HETATM 3509 O O . HOH N 6 . ? 39.862 -17.391 68.426 1.00 26.17 ? 896 HOH A O 1 HETATM 3510 O O . HOH N 6 . ? 36.951 43.114 56.739 1.00 26.70 ? 897 HOH A O 1 HETATM 3511 O O . HOH N 6 . ? 24.563 25.199 32.774 1.00 28.02 ? 898 HOH A O 1 HETATM 3512 O O . HOH N 6 . ? 28.389 14.798 66.838 1.00 25.16 ? 899 HOH A O 1 HETATM 3513 O O . HOH N 6 . ? 38.536 9.509 46.364 1.00 23.77 ? 900 HOH A O 1 HETATM 3514 O O . HOH N 6 . ? 6.340 39.002 61.478 1.00 28.13 ? 901 HOH A O 1 HETATM 3515 O O . HOH N 6 . ? 40.427 28.858 64.770 1.00 36.40 ? 902 HOH A O 1 HETATM 3516 O O . HOH N 6 . ? 22.884 2.662 37.671 1.00 26.37 ? 903 HOH A O 1 HETATM 3517 O O . HOH N 6 . ? 23.687 27.664 70.866 1.00 25.16 ? 904 HOH A O 1 HETATM 3518 O O . HOH N 6 . ? 14.161 45.764 45.379 1.00 29.20 ? 905 HOH A O 1 HETATM 3519 O O . HOH N 6 . ? 1.497 23.576 74.072 1.00 35.59 ? 906 HOH A O 1 HETATM 3520 O O . HOH N 6 . ? 36.878 11.364 66.200 1.00 35.77 ? 907 HOH A O 1 HETATM 3521 O O . HOH N 6 . ? 19.512 36.733 72.133 1.00 36.83 ? 908 HOH A O 1 HETATM 3522 O O . HOH N 6 . ? 6.512 24.856 37.024 1.00 32.49 ? 909 HOH A O 1 HETATM 3523 O O . HOH N 6 . ? 9.884 10.991 83.752 1.00 37.89 ? 910 HOH A O 1 HETATM 3524 O O . HOH N 6 . ? 34.481 4.030 66.814 1.00 32.54 ? 911 HOH A O 1 HETATM 3525 O O . HOH N 6 . ? 7.304 34.200 36.918 1.00 31.18 ? 912 HOH A O 1 HETATM 3526 O O . HOH N 6 . ? 33.363 4.616 41.084 1.00 26.39 ? 913 HOH A O 1 HETATM 3527 O O . HOH N 6 . ? 5.231 14.504 36.422 1.00 25.98 ? 914 HOH A O 1 HETATM 3528 O O . HOH N 6 . ? 22.083 44.911 64.918 1.00 26.02 ? 915 HOH A O 1 HETATM 3529 O O . HOH N 6 . ? 53.857 -16.509 55.234 1.00 41.47 ? 916 HOH A O 1 HETATM 3530 O O . HOH N 6 . ? 33.595 28.818 37.136 1.00 29.67 ? 917 HOH A O 1 HETATM 3531 O O . HOH N 6 . ? 40.928 36.422 53.044 1.00 32.27 ? 918 HOH A O 1 HETATM 3532 O O . HOH N 6 . ? 29.680 28.161 34.258 1.00 33.83 ? 919 HOH A O 1 HETATM 3533 O O . HOH N 6 . ? 36.077 18.441 64.149 1.00 32.42 ? 920 HOH A O 1 HETATM 3534 O O . HOH N 6 . ? 14.016 20.417 28.476 1.00 40.32 ? 921 HOH A O 1 HETATM 3535 O O . HOH N 6 . ? 40.876 -6.990 63.420 1.00 34.41 ? 922 HOH A O 1 HETATM 3536 O O . HOH N 6 . ? 21.232 9.077 77.713 1.00 24.61 ? 923 HOH A O 1 HETATM 3537 O O . HOH N 6 . ? 9.703 41.032 44.030 1.00 26.14 ? 924 HOH A O 1 HETATM 3538 O O . HOH N 6 . ? 38.696 22.467 42.171 1.00 28.96 ? 925 HOH A O 1 HETATM 3539 O O . HOH N 6 . ? 41.426 7.752 53.729 1.00 28.72 ? 926 HOH A O 1 HETATM 3540 O O . HOH N 6 . ? 47.055 -14.925 60.648 1.00 35.83 ? 927 HOH A O 1 HETATM 3541 O O . HOH N 6 . ? 5.194 33.678 72.060 1.00 33.38 ? 928 HOH A O 1 HETATM 3542 O O . HOH N 6 . ? 41.832 11.295 61.453 1.00 27.16 ? 929 HOH A O 1 HETATM 3543 O O . HOH N 6 . ? 29.317 29.613 65.884 1.00 25.79 ? 930 HOH A O 1 HETATM 3544 O O . HOH N 6 . ? 26.432 29.207 72.037 1.00 41.03 ? 931 HOH A O 1 HETATM 3545 O O . HOH N 6 . ? 17.832 9.778 27.900 1.00 40.99 ? 932 HOH A O 1 HETATM 3546 O O . HOH N 6 . ? 1.807 5.300 50.933 1.00 26.53 ? 933 HOH A O 1 HETATM 3547 O O . HOH N 6 . ? 10.246 21.077 79.587 1.00 28.76 ? 934 HOH A O 1 HETATM 3548 O O . HOH N 6 . ? 24.559 28.425 39.588 1.00 21.90 ? 935 HOH A O 1 HETATM 3549 O O . HOH N 6 . ? 49.875 -11.283 58.132 1.00 33.98 ? 936 HOH A O 1 HETATM 3550 O O . HOH N 6 . ? 42.873 0.897 52.560 1.00 33.91 ? 937 HOH A O 1 HETATM 3551 O O . HOH N 6 . ? 34.148 18.715 33.344 1.00 27.62 ? 938 HOH A O 1 HETATM 3552 O O . HOH N 6 . ? -3.134 32.055 66.510 1.00 26.86 ? 939 HOH A O 1 HETATM 3553 O O . HOH N 6 . ? 25.547 51.830 52.977 1.00 25.47 ? 940 HOH A O 1 HETATM 3554 O O . HOH N 6 . ? 36.274 9.094 41.924 1.00 24.92 ? 941 HOH A O 1 HETATM 3555 O O . HOH N 6 . ? 39.437 37.230 49.473 1.00 38.43 ? 942 HOH A O 1 HETATM 3556 O O . HOH N 6 . ? 9.397 28.931 31.586 1.00 31.33 ? 943 HOH A O 1 HETATM 3557 O O . HOH N 6 . ? 34.963 28.023 34.877 1.00 39.02 ? 944 HOH A O 1 HETATM 3558 O O . HOH N 6 . ? 9.311 8.375 75.731 1.00 24.89 ? 945 HOH A O 1 HETATM 3559 O O . HOH N 6 . ? 25.058 37.352 69.564 1.00 30.39 ? 946 HOH A O 1 HETATM 3560 O O . HOH N 6 . ? 1.377 12.858 44.485 1.00 27.23 ? 947 HOH A O 1 HETATM 3561 O O . HOH N 6 . ? 20.748 49.366 52.708 1.00 43.37 ? 948 HOH A O 1 HETATM 3562 O O . HOH N 6 . ? 42.090 4.963 55.232 1.00 31.48 ? 949 HOH A O 1 HETATM 3563 O O . HOH N 6 . ? 12.566 13.897 84.018 1.00 31.18 ? 950 HOH A O 1 HETATM 3564 O O . HOH N 6 . ? 31.696 44.626 48.576 1.00 37.58 ? 951 HOH A O 1 HETATM 3565 O O . HOH N 6 . ? 22.959 7.820 76.296 1.00 35.34 ? 952 HOH A O 1 HETATM 3566 O O . HOH N 6 . ? 22.130 1.011 53.081 1.00 20.25 ? 953 HOH A O 1 HETATM 3567 O O . HOH N 6 . ? 16.420 0.559 48.216 1.00 29.47 ? 954 HOH A O 1 HETATM 3568 O O . HOH N 6 . ? 30.036 38.981 45.360 1.00 26.76 ? 955 HOH A O 1 HETATM 3569 O O . HOH N 6 . ? -2.249 20.253 72.860 1.00 26.05 ? 956 HOH A O 1 HETATM 3570 O O . HOH N 6 . ? 3.852 31.913 36.303 1.00 31.87 ? 957 HOH A O 1 HETATM 3571 O O . HOH N 6 . ? 2.021 -0.625 69.064 1.00 31.08 ? 958 HOH A O 1 HETATM 3572 O O . HOH N 6 . ? 34.307 44.855 53.708 1.00 32.12 ? 959 HOH A O 1 HETATM 3573 O O . HOH N 6 . ? 12.718 5.340 44.493 1.00 26.24 ? 960 HOH A O 1 HETATM 3574 O O . HOH N 6 . ? 15.996 36.257 38.251 1.00 33.85 ? 961 HOH A O 1 HETATM 3575 O O . HOH N 6 . ? 14.020 -0.663 48.855 1.00 28.28 ? 962 HOH A O 1 HETATM 3576 O O . HOH N 6 . ? 44.714 -8.754 62.318 1.00 35.40 ? 963 HOH A O 1 HETATM 3577 O O . HOH N 6 . ? 44.728 -2.152 59.198 1.00 24.11 ? 964 HOH A O 1 HETATM 3578 O O . HOH N 6 . ? 40.644 9.300 45.155 1.00 37.31 ? 965 HOH A O 1 HETATM 3579 O O . HOH N 6 . ? 28.563 36.742 43.007 1.00 36.64 ? 966 HOH A O 1 HETATM 3580 O O . HOH N 6 . ? 8.870 -1.517 82.072 1.00 40.13 ? 967 HOH A O 1 HETATM 3581 O O . HOH N 6 . ? 35.918 10.276 35.862 1.00 45.67 ? 968 HOH A O 1 HETATM 3582 O O . HOH N 6 . ? 35.353 28.079 39.141 1.00 35.60 ? 969 HOH A O 1 HETATM 3583 O O . HOH N 6 . ? 38.653 9.252 65.229 1.00 31.91 ? 970 HOH A O 1 HETATM 3584 O O . HOH N 6 . ? 14.116 2.415 80.614 1.00 23.26 ? 971 HOH A O 1 HETATM 3585 O O . HOH N 6 . ? 15.833 21.553 79.623 1.00 40.02 ? 972 HOH A O 1 HETATM 3586 O O . HOH N 6 . ? 16.555 33.174 36.032 1.00 36.00 ? 973 HOH A O 1 HETATM 3587 O O . HOH N 6 . ? 24.301 19.294 73.366 1.00 31.61 ? 974 HOH A O 1 HETATM 3588 O O . HOH N 6 . ? 25.532 48.463 48.055 1.00 31.86 ? 975 HOH A O 1 HETATM 3589 O O . HOH N 6 . ? 23.679 51.388 50.724 1.00 40.48 ? 976 HOH A O 1 HETATM 3590 O O . HOH N 6 . ? 41.564 11.018 47.225 1.00 29.42 ? 977 HOH A O 1 HETATM 3591 O O . HOH N 6 . ? 32.347 37.230 69.987 1.00 36.10 ? 978 HOH A O 1 HETATM 3592 O O . HOH N 6 . ? 27.785 -0.105 39.458 1.00 34.70 ? 979 HOH A O 1 HETATM 3593 O O . HOH N 6 . ? 9.970 37.468 63.000 1.00 22.60 ? 980 HOH A O 1 HETATM 3594 O O . HOH N 6 . ? 19.489 6.868 30.990 1.00 35.57 ? 981 HOH A O 1 HETATM 3595 O O . HOH N 6 . ? 4.388 36.843 39.045 1.00 31.62 ? 982 HOH A O 1 HETATM 3596 O O . HOH N 6 . ? 8.151 7.755 42.127 1.00 26.07 ? 983 HOH A O 1 HETATM 3597 O O . HOH N 6 . ? 10.629 25.503 30.649 1.00 37.67 ? 984 HOH A O 1 HETATM 3598 O O . HOH N 6 . ? 30.948 22.005 66.218 1.00 36.72 ? 985 HOH A O 1 HETATM 3599 O O . HOH N 6 . ? 45.559 -14.718 58.413 1.00 36.08 ? 986 HOH A O 1 HETATM 3600 O O . HOH N 6 . ? 8.530 21.481 35.393 1.00 28.43 ? 987 HOH A O 1 HETATM 3601 O O . HOH N 6 . ? 42.215 9.621 49.185 1.00 32.01 ? 988 HOH A O 1 HETATM 3602 O O . HOH N 6 . ? 25.612 44.050 70.616 1.00 35.86 ? 989 HOH A O 1 HETATM 3603 O O . HOH N 6 . ? 41.334 26.013 63.772 1.00 28.96 ? 990 HOH A O 1 HETATM 3604 O O . HOH N 6 . ? 1.284 4.779 53.825 1.00 30.58 ? 991 HOH A O 1 HETATM 3605 O O . HOH N 6 . ? 27.973 25.787 30.978 1.00 30.77 ? 992 HOH A O 1 HETATM 3606 O O . HOH N 6 . ? 42.252 14.628 52.571 1.00 33.27 ? 993 HOH A O 1 HETATM 3607 O O . HOH N 6 . ? 17.233 5.030 44.885 1.00 23.97 ? 994 HOH A O 1 HETATM 3608 O O . HOH N 6 . ? -2.760 4.687 72.671 1.00 29.21 ? 995 HOH A O 1 HETATM 3609 O O . HOH N 6 . ? 29.586 29.986 68.679 1.00 25.71 ? 996 HOH A O 1 HETATM 3610 O O . HOH N 6 . ? 39.882 29.972 44.672 1.00 35.81 ? 997 HOH A O 1 HETATM 3611 O O . HOH N 6 . ? 43.037 10.953 51.068 1.00 33.56 ? 998 HOH A O 1 HETATM 3612 O O . HOH N 6 . ? 23.166 19.458 71.078 1.00 32.54 ? 999 HOH A O 1 HETATM 3613 O O . HOH N 6 . ? 29.429 31.003 39.311 1.00 31.39 ? 1000 HOH A O 1 HETATM 3614 O O . HOH N 6 . ? 34.802 24.871 32.069 1.00 33.40 ? 1001 HOH A O 1 HETATM 3615 O O . HOH N 6 . ? 12.944 5.981 78.146 1.00 25.81 ? 1002 HOH A O 1 HETATM 3616 O O . HOH N 6 . ? 41.264 26.686 47.114 1.00 41.40 ? 1003 HOH A O 1 HETATM 3617 O O . HOH N 6 . ? 16.549 15.462 83.798 1.00 39.84 ? 1004 HOH A O 1 HETATM 3618 O O . HOH N 6 . ? 11.376 24.738 76.587 1.00 26.52 ? 1005 HOH A O 1 HETATM 3619 O O . HOH N 6 . ? -1.541 6.488 74.946 1.00 36.83 ? 1006 HOH A O 1 HETATM 3620 O O . HOH N 6 . ? 16.679 45.634 43.475 1.00 34.51 ? 1007 HOH A O 1 HETATM 3621 O O . HOH N 6 . ? 10.416 38.791 60.033 1.00 30.02 ? 1008 HOH A O 1 HETATM 3622 O O . HOH N 6 . ? 3.546 34.743 62.154 1.00 21.02 ? 1009 HOH A O 1 HETATM 3623 O O . HOH N 6 . ? 42.894 7.383 61.176 1.00 32.33 ? 1010 HOH A O 1 HETATM 3624 O O . HOH N 6 . ? 41.999 14.005 62.437 1.00 40.98 ? 1011 HOH A O 1 HETATM 3625 O O . HOH N 6 . ? 26.675 36.459 41.243 1.00 39.89 ? 1012 HOH A O 1 HETATM 3626 O O . HOH N 6 . ? 5.626 5.706 46.887 1.00 28.86 ? 1013 HOH A O 1 HETATM 3627 O O . HOH N 6 . ? 0.225 39.806 43.851 1.00 24.17 ? 1014 HOH A O 1 HETATM 3628 O O . HOH N 6 . ? 37.091 21.677 35.761 1.00 27.76 ? 1015 HOH A O 1 HETATM 3629 O O . HOH N 6 . ? 23.337 16.144 68.046 1.00 37.07 ? 1016 HOH A O 1 HETATM 3630 O O . HOH N 6 . ? 18.786 33.847 39.968 1.00 34.43 ? 1017 HOH A O 1 HETATM 3631 O O . HOH N 6 . ? 11.455 3.334 81.385 1.00 36.37 ? 1018 HOH A O 1 HETATM 3632 O O . HOH N 6 . ? 13.564 35.971 37.036 1.00 39.75 ? 1019 HOH A O 1 HETATM 3633 O O . HOH N 6 . ? 41.041 20.542 50.294 1.00 33.96 ? 1020 HOH A O 1 HETATM 3634 O O . HOH N 6 . ? 45.249 -6.182 52.141 1.00 22.16 ? 1021 HOH A O 1 HETATM 3635 O O . HOH N 6 . ? 8.271 46.242 50.772 1.00 28.24 ? 1022 HOH A O 1 HETATM 3636 O O . HOH N 6 . ? 22.757 45.251 67.745 0.50 20.59 ? 1023 HOH A O 1 HETATM 3637 O O . HOH N 6 . ? 20.670 26.186 32.255 1.00 26.38 ? 1024 HOH A O 1 HETATM 3638 O O . HOH N 6 . ? 3.077 -2.282 70.482 1.00 30.67 ? 1025 HOH A O 1 HETATM 3639 O O . HOH N 6 . ? 12.821 43.631 45.549 1.00 20.92 ? 1026 HOH A O 1 HETATM 3640 O O . HOH N 6 . ? 23.477 17.145 63.776 1.00 25.76 ? 1027 HOH A O 1 HETATM 3641 O O . HOH N 6 . ? 24.260 29.533 41.485 1.00 35.52 ? 1028 HOH A O 1 HETATM 3642 O O . HOH N 6 . ? 31.510 14.555 66.908 1.00 32.75 ? 1029 HOH A O 1 HETATM 3643 O O . HOH N 6 . ? 45.174 -12.446 64.127 1.00 32.16 ? 1030 HOH A O 1 HETATM 3644 O O . HOH N 6 . ? 28.639 28.161 70.377 1.00 28.85 ? 1031 HOH A O 1 HETATM 3645 O O . HOH N 6 . ? 35.937 5.739 42.541 1.00 33.00 ? 1032 HOH A O 1 HETATM 3646 O O . HOH N 6 . ? 20.027 47.623 61.955 1.00 39.12 ? 1033 HOH A O 1 HETATM 3647 O O . HOH N 6 . ? 3.327 30.742 40.464 1.00 32.79 ? 1034 HOH A O 1 HETATM 3648 O O . HOH N 6 . ? 24.034 51.126 55.706 1.00 30.86 ? 1035 HOH A O 1 HETATM 3649 O O . HOH N 6 . ? -0.939 25.512 37.282 1.00 38.35 ? 1036 HOH A O 1 HETATM 3650 O O . HOH N 6 . ? 15.355 48.177 54.700 1.00 32.77 ? 1037 HOH A O 1 HETATM 3651 O O . HOH N 6 . ? 7.898 7.575 45.595 1.00 26.31 ? 1038 HOH A O 1 HETATM 3652 O O . HOH N 6 . ? 32.080 -0.776 40.936 1.00 32.31 ? 1039 HOH A O 1 HETATM 3653 O O . HOH N 6 . ? 39.571 9.593 42.467 1.00 35.99 ? 1040 HOH A O 1 HETATM 3654 O O . HOH N 6 . ? 34.633 2.466 40.018 1.00 31.85 ? 1041 HOH A O 1 HETATM 3655 O O . HOH N 6 . ? 41.571 30.039 50.788 1.00 30.75 ? 1042 HOH A O 1 HETATM 3656 O O . HOH N 6 . ? 36.684 13.687 64.999 1.00 35.32 ? 1043 HOH A O 1 HETATM 3657 O O . HOH N 6 . ? 11.202 -0.456 50.068 1.00 28.47 ? 1044 HOH A O 1 HETATM 3658 O O . HOH N 6 . ? 1.666 5.918 74.600 1.00 30.42 ? 1045 HOH A O 1 HETATM 3659 O O . HOH N 6 . ? 16.207 4.147 35.824 1.00 32.01 ? 1046 HOH A O 1 HETATM 3660 O O . HOH N 6 . ? 14.188 21.263 80.995 1.00 34.63 ? 1047 HOH A O 1 HETATM 3661 O O . HOH N 6 . ? 43.521 26.666 61.881 1.00 42.88 ? 1048 HOH A O 1 HETATM 3662 O O . HOH N 6 . ? 37.042 34.948 63.765 1.00 34.29 ? 1049 HOH A O 1 HETATM 3663 O O . HOH N 6 . ? 47.437 -0.445 56.245 1.00 31.33 ? 1050 HOH A O 1 HETATM 3664 O O . HOH N 6 . ? 25.250 27.409 35.485 1.00 35.96 ? 1051 HOH A O 1 HETATM 3665 O O . HOH N 6 . ? 15.983 35.267 71.392 1.00 37.27 ? 1052 HOH A O 1 HETATM 3666 O O . HOH N 6 . ? 24.881 15.043 69.624 1.00 31.73 ? 1053 HOH A O 1 HETATM 3667 O O . HOH N 6 . ? -4.667 3.293 71.866 1.00 37.23 ? 1054 HOH A O 1 HETATM 3668 O O . HOH N 6 . ? 39.918 31.363 49.265 1.00 30.34 ? 1055 HOH A O 1 HETATM 3669 O O . HOH N 6 . ? 41.728 17.228 56.402 1.00 36.65 ? 1056 HOH A O 1 HETATM 3670 O O . HOH N 6 . ? 9.251 38.237 65.343 1.00 34.29 ? 1057 HOH A O 1 HETATM 3671 O O . HOH N 6 . ? 7.123 23.024 77.616 1.00 32.74 ? 1058 HOH A O 1 HETATM 3672 O O . HOH N 6 . ? 28.276 17.520 64.374 1.00 38.59 ? 1059 HOH A O 1 HETATM 3673 O O . HOH N 6 . ? 46.752 -4.276 51.271 1.00 45.20 ? 1060 HOH A O 1 HETATM 3674 O O . HOH N 6 . ? 6.543 44.017 44.694 1.00 34.85 ? 1061 HOH A O 1 HETATM 3675 O O . HOH N 6 . ? 36.610 41.016 49.416 1.00 34.10 ? 1062 HOH A O 1 HETATM 3676 O O . HOH N 6 . ? 43.721 1.601 56.086 1.00 36.90 ? 1063 HOH A O 1 HETATM 3677 O O . HOH N 6 . ? 23.790 23.305 68.973 1.00 37.62 ? 1064 HOH A O 1 HETATM 3678 O O . HOH N 6 . ? 41.988 15.301 49.520 1.00 42.34 ? 1065 HOH A O 1 HETATM 3679 O O . HOH N 6 . ? 10.976 40.762 41.509 1.00 39.72 ? 1066 HOH A O 1 HETATM 3680 O O . HOH N 6 . ? 38.956 38.061 58.217 1.00 37.25 ? 1067 HOH A O 1 HETATM 3681 O O . HOH N 6 . ? 3.914 15.596 83.613 1.00 33.85 ? 1068 HOH A O 1 HETATM 3682 O O . HOH N 6 . ? 49.385 -15.635 51.729 1.00 32.18 ? 1069 HOH A O 1 HETATM 3683 O O . HOH N 6 . ? 2.033 41.430 62.243 1.00 36.88 ? 1070 HOH A O 1 HETATM 3684 O O . HOH N 6 . ? 19.310 19.787 28.170 1.00 37.11 ? 1071 HOH A O 1 HETATM 3685 O O . HOH N 6 . ? -3.609 21.632 71.287 1.00 39.94 ? 1072 HOH A O 1 HETATM 3686 O O . HOH N 6 . ? 6.801 38.942 38.824 1.00 36.68 ? 1073 HOH A O 1 HETATM 3687 O O . HOH N 6 . ? 24.126 50.353 48.719 1.00 37.96 ? 1074 HOH A O 1 HETATM 3688 O O . HOH N 6 . ? 23.694 13.097 76.892 1.00 37.26 ? 1075 HOH A O 1 HETATM 3689 O O . HOH N 6 . ? 22.415 46.033 44.742 1.00 35.86 ? 1076 HOH A O 1 HETATM 3690 O O . HOH N 6 . ? 39.178 25.931 66.482 1.00 37.94 ? 1077 HOH A O 1 HETATM 3691 O O . HOH N 6 . ? 3.889 31.591 72.145 1.00 37.86 ? 1078 HOH A O 1 HETATM 3692 O O . HOH N 6 . ? 38.764 39.642 49.949 1.00 46.32 ? 1079 HOH A O 1 HETATM 3693 O O . HOH N 6 . ? 21.892 13.590 81.592 1.00 33.14 ? 1080 HOH A O 1 HETATM 3694 O O . HOH N 6 . ? 31.520 19.011 31.314 1.00 34.63 ? 1081 HOH A O 1 HETATM 3695 O O . HOH N 6 . ? 37.793 28.989 68.742 1.00 41.57 ? 1082 HOH A O 1 HETATM 3696 O O . HOH N 6 . ? 6.059 22.322 32.621 1.00 39.08 ? 1083 HOH A O 1 HETATM 3697 O O . HOH N 6 . ? 2.644 26.424 71.405 1.00 40.21 ? 1084 HOH A O 1 HETATM 3698 O O . HOH N 6 . ? 41.513 5.742 59.386 1.00 32.16 ? 1085 HOH A O 1 HETATM 3699 O O . HOH N 6 . ? 36.254 42.422 52.747 1.00 42.52 ? 1086 HOH A O 1 HETATM 3700 O O . HOH N 6 . ? 43.975 -20.163 68.767 1.00 32.32 ? 1087 HOH A O 1 HETATM 3701 O O . HOH N 6 . ? 19.959 23.539 78.152 1.00 40.65 ? 1088 HOH A O 1 HETATM 3702 O O . HOH N 6 . ? 7.280 13.023 34.466 1.00 37.18 ? 1089 HOH A O 1 HETATM 3703 O O . HOH N 6 . ? -3.130 18.931 79.734 1.00 31.70 ? 1090 HOH A O 1 HETATM 3704 O O . HOH N 6 . ? 23.077 10.041 79.699 1.00 35.45 ? 1091 HOH A O 1 HETATM 3705 O O . HOH N 6 . ? 23.001 36.367 71.315 1.00 39.03 ? 1092 HOH A O 1 HETATM 3706 O O . HOH N 6 . ? 47.226 0.014 53.539 1.00 33.08 ? 1093 HOH A O 1 HETATM 3707 O O . HOH N 6 . ? 19.576 13.393 28.292 1.00 37.48 ? 1094 HOH A O 1 HETATM 3708 O O . HOH N 6 . ? 40.760 5.396 57.122 1.00 35.04 ? 1095 HOH A O 1 HETATM 3709 O O . HOH N 6 . ? 28.315 15.655 32.075 1.00 39.95 ? 1096 HOH A O 1 HETATM 3710 O O . HOH N 6 . ? 20.343 13.799 24.783 1.00 40.64 ? 1097 HOH A O 1 HETATM 3711 O O . HOH N 6 . ? 29.521 6.841 34.144 1.00 38.34 ? 1098 HOH A O 1 HETATM 3712 O O . HOH N 6 . ? 6.751 36.529 69.481 1.00 34.15 ? 1099 HOH A O 1 HETATM 3713 O O . HOH N 6 . ? 51.911 -8.432 52.141 1.00 35.79 ? 1100 HOH A O 1 HETATM 3714 O O . HOH N 6 . ? 18.907 46.551 45.582 1.00 39.15 ? 1101 HOH A O 1 HETATM 3715 O O . HOH N 6 . ? 44.913 -2.347 50.332 1.00 37.67 ? 1102 HOH A O 1 HETATM 3716 O O . HOH N 6 . ? 51.951 -7.190 56.145 1.00 36.21 ? 1103 HOH A O 1 HETATM 3717 O O . HOH N 6 . ? 34.646 35.000 67.299 1.00 38.76 ? 1104 HOH A O 1 HETATM 3718 O O . HOH N 6 . ? 45.644 -18.367 68.022 1.00 40.63 ? 1105 HOH A O 1 HETATM 3719 O O . HOH N 6 . ? 9.805 13.395 85.517 1.00 38.02 ? 1106 HOH A O 1 HETATM 3720 O O . HOH N 6 . ? 40.168 23.044 66.296 1.00 42.77 ? 1107 HOH A O 1 HETATM 3721 O O . HOH N 6 . ? 35.609 36.765 67.883 1.00 43.75 ? 1108 HOH A O 1 HETATM 3722 O O . HOH N 6 . ? 40.232 13.125 64.200 1.00 39.17 ? 1109 HOH A O 1 HETATM 3723 O O . HOH N 6 . ? 8.758 31.483 30.588 1.00 38.56 ? 1110 HOH A O 1 HETATM 3724 O O . HOH N 6 . ? 49.036 -6.996 59.364 1.00 39.50 ? 1111 HOH A O 1 HETATM 3725 O O . HOH N 6 . ? 21.066 5.609 70.432 1.00 44.23 ? 1112 HOH A O 1 HETATM 3726 O O . HOH N 6 . ? 31.229 33.592 70.814 1.00 39.90 ? 1113 HOH A O 1 HETATM 3727 O O . HOH N 6 . ? 41.116 33.704 48.573 1.00 46.03 ? 1114 HOH A O 1 HETATM 3728 O O . HOH N 6 . ? 42.425 33.918 54.016 1.00 42.74 ? 1115 HOH A O 1 HETATM 3729 O O . HOH N 6 . ? 38.182 5.048 66.465 1.00 43.53 ? 1116 HOH A O 1 HETATM 3730 O O . HOH N 6 . ? 41.206 40.411 55.628 1.00 44.43 ? 1117 HOH A O 1 HETATM 3731 O O . HOH N 6 . ? 31.043 31.823 37.286 1.00 41.99 ? 1118 HOH A O 1 HETATM 3732 O O . HOH N 6 . ? 23.336 6.217 69.795 1.00 40.78 ? 1119 HOH A O 1 HETATM 3733 O O . HOH N 6 . ? 39.750 13.606 39.663 1.00 44.31 ? 1120 HOH A O 1 HETATM 3734 O O . HOH N 6 . ? 33.622 39.895 69.341 1.00 45.73 ? 1121 HOH A O 1 HETATM 3735 O O . HOH N 6 . ? 36.776 37.404 59.308 1.00 42.83 ? 1122 HOH A O 1 HETATM 3736 O O . HOH N 6 . ? 30.698 1.785 40.888 1.00 40.97 ? 1123 HOH A O 1 HETATM 3737 O O . HOH N 6 . ? 26.709 13.368 31.049 1.00 45.47 ? 1124 HOH A O 1 HETATM 3738 O O . HOH N 6 . ? 44.133 18.553 52.683 1.00 47.69 ? 1125 HOH A O 1 HETATM 3739 O O . HOH N 6 . ? 24.926 14.654 30.406 1.00 47.07 ? 1126 HOH A O 1 HETATM 3740 O O . HOH N 6 . ? 21.649 48.553 49.369 1.00 39.79 ? 1127 HOH A O 1 HETATM 3741 O O . HOH N 6 . ? -2.481 8.243 78.402 1.00 35.85 ? 1128 HOH A O 1 HETATM 3742 O O . HOH N 6 . ? 53.125 -7.233 53.500 1.00 42.82 ? 1129 HOH A O 1 HETATM 3743 O O . HOH N 6 . ? 5.700 27.976 73.288 1.00 46.68 ? 1130 HOH A O 1 HETATM 3744 O O . HOH N 6 . ? 42.612 31.651 58.884 1.00 40.40 ? 1131 HOH A O 1 HETATM 3745 O O . HOH N 6 . ? 42.532 22.788 62.188 1.00 44.20 ? 1132 HOH A O 1 HETATM 3746 O O . HOH N 6 . ? 26.581 45.795 45.184 1.00 42.76 ? 1133 HOH A O 1 HETATM 3747 O O . HOH N 6 . ? 49.876 -0.707 52.197 1.00 44.08 ? 1134 HOH A O 1 HETATM 3748 O O . HOH N 6 . ? -4.734 30.074 67.606 1.00 38.61 ? 1135 HOH A O 1 HETATM 3749 O O . HOH N 6 . ? 19.709 10.164 86.175 1.00 42.67 ? 1136 HOH A O 1 HETATM 3750 O O . HOH N 6 . ? 20.834 25.375 34.383 1.00 32.35 ? 1137 HOH A O 1 HETATM 3751 O O . HOH N 6 . ? 23.697 14.864 62.557 1.00 34.50 ? 1138 HOH A O 1 HETATM 3752 O O . HOH N 6 . ? 22.832 25.762 34.642 1.00 32.18 ? 1139 HOH A O 1 HETATM 3753 O O . HOH N 6 . ? 16.952 33.446 72.372 1.00 36.67 ? 1140 HOH A O 1 HETATM 3754 O O . HOH N 6 . ? 30.023 19.396 64.435 1.00 27.79 ? 1141 HOH A O 1 HETATM 3755 O O . HOH N 6 . ? 22.793 9.857 84.226 1.00 34.15 ? 1142 HOH A O 1 HETATM 3756 O O . HOH N 6 . ? 22.481 7.850 85.019 1.00 40.53 ? 1143 HOH A O 1 HETATM 3757 O O . HOH N 6 . ? 47.900 -19.217 69.454 1.00 32.21 ? 1144 HOH A O 1 HETATM 3758 O O . HOH N 6 . ? 7.742 23.456 38.770 1.00 34.15 ? 1145 HOH A O 1 HETATM 3759 O O . HOH N 6 . ? 40.107 7.650 49.881 1.00 44.19 ? 1146 HOH A O 1 HETATM 3760 O O . HOH N 6 . ? 51.605 -15.849 56.490 1.00 42.85 ? 1147 HOH A O 1 HETATM 3761 O O . HOH N 6 . ? 13.902 -1.789 39.099 1.00 33.37 ? 1148 HOH A O 1 HETATM 3762 O O . HOH N 6 . ? 41.813 23.167 50.187 1.00 42.71 ? 1149 HOH A O 1 HETATM 3763 O O . HOH N 6 . ? 27.061 8.636 32.012 1.00 45.69 ? 1150 HOH A O 1 HETATM 3764 O O . HOH N 6 . ? 19.126 14.434 83.417 1.00 37.99 ? 1151 HOH A O 1 HETATM 3765 O O . HOH N 6 . ? 19.921 49.919 60.468 1.00 40.79 ? 1152 HOH A O 1 HETATM 3766 O O . HOH N 6 . ? 52.588 -18.204 54.034 1.00 43.45 ? 1153 HOH A O 1 HETATM 3767 O O . HOH N 6 . ? 24.089 1.571 71.824 1.00 34.54 ? 1154 HOH A O 1 HETATM 3768 O O . HOH N 6 . ? 10.188 44.435 44.966 1.00 43.54 ? 1155 HOH A O 1 HETATM 3769 O O . HOH N 6 . ? 16.718 49.144 57.123 1.00 42.97 ? 1156 HOH A O 1 HETATM 3770 O O . HOH N 6 . ? 40.823 24.151 45.835 1.00 38.23 ? 1157 HOH A O 1 HETATM 3771 O O . HOH N 6 . ? 44.243 28.072 59.270 1.00 42.03 ? 1158 HOH A O 1 HETATM 3772 O O . HOH N 6 . ? 31.244 34.452 41.047 1.00 42.19 ? 1159 HOH A O 1 HETATM 3773 O O . HOH N 6 . ? 33.035 8.845 35.001 1.00 41.45 ? 1160 HOH A O 1 HETATM 3774 O O . HOH N 6 . ? -1.652 41.377 45.452 1.00 45.04 ? 1161 HOH A O 1 HETATM 3775 O O . HOH N 6 . ? 18.180 12.841 86.332 1.00 43.19 ? 1162 HOH A O 1 HETATM 3776 O O . HOH N 6 . ? 4.152 23.199 72.877 1.00 44.54 ? 1163 HOH A O 1 HETATM 3777 O O . HOH N 6 . ? 35.650 2.048 65.535 1.00 42.90 ? 1164 HOH A O 1 HETATM 3778 O O . HOH N 6 . ? 38.256 36.123 61.641 1.00 45.86 ? 1165 HOH A O 1 HETATM 3779 O O . HOH N 6 . ? 9.489 12.435 31.416 1.00 45.58 ? 1166 HOH A O 1 HETATM 3780 O O . HOH N 6 . ? 6.187 41.594 41.177 1.00 43.54 ? 1167 HOH A O 1 HETATM 3781 O O . HOH N 6 . ? 9.734 47.109 46.373 1.00 39.79 ? 1168 HOH A O 1 HETATM 3782 O O . HOH N 6 . ? 3.874 9.114 83.758 1.00 38.87 ? 1169 HOH A O 1 HETATM 3783 O O . HOH N 6 . ? 14.051 10.961 84.358 1.00 41.10 ? 1170 HOH A O 1 HETATM 3784 O O . HOH N 6 . ? 44.230 7.891 48.056 1.00 49.06 ? 1171 HOH A O 1 HETATM 3785 O O . HOH N 6 . ? 34.648 14.791 66.626 1.00 39.30 ? 1172 HOH A O 1 HETATM 3786 O O . HOH N 6 . ? 31.885 4.565 36.917 1.00 43.75 ? 1173 HOH A O 1 HETATM 3787 O O . HOH N 6 . ? 43.340 21.740 54.774 1.00 44.56 ? 1174 HOH A O 1 HETATM 3788 O O . HOH N 6 . ? 3.380 7.544 43.653 1.00 45.25 ? 1175 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 . ARG A 1 ? 0.5537 0.5331 0.4831 0.0023 -0.0013 -0.0020 83 ARG A N 2 C CA . ARG A 1 ? 0.3698 0.3493 0.3016 0.0022 0.0000 -0.0002 83 ARG A CA 3 C C . ARG A 1 ? 0.3873 0.3662 0.3176 0.0021 0.0028 0.0005 83 ARG A C 4 O O . ARG A 1 ? 0.3706 0.3494 0.2995 0.0020 0.0044 -0.0007 83 ARG A O 5 C CB . ARG A 1 ? 0.4366 0.4170 0.3729 0.0019 0.0002 -0.0007 83 ARG A CB 6 C CG . ARG A 1 ? 0.5089 0.4899 0.4477 0.0020 -0.0022 -0.0004 83 ARG A CG 7 C CD . ARG A 1 ? 0.4715 0.4533 0.4143 0.0017 -0.0015 -0.0005 83 ARG A CD 8 N NE . ARG A 1 ? 0.6361 0.6184 0.5814 0.0018 -0.0035 -0.0001 83 ARG A NE 9 C CZ . ARG A 1 ? 0.5450 0.5279 0.4936 0.0015 -0.0033 -0.0001 83 ARG A CZ 10 N NH1 . ARG A 1 ? 0.5292 0.5123 0.4791 0.0012 -0.0012 -0.0005 83 ARG A NH1 11 N NH2 . ARG A 1 ? 0.5069 0.4902 0.4575 0.0016 -0.0051 0.0003 83 ARG A NH2 12 N N . ASN A 2 ? 0.3176 0.2963 0.2484 0.0021 0.0034 0.0025 84 ASN A N 13 C CA . ASN A 2 ? 0.2978 0.2758 0.2277 0.0019 0.0061 0.0033 84 ASN A CA 14 C C . ASN A 2 ? 0.2439 0.2225 0.1781 0.0015 0.0075 0.0040 84 ASN A C 15 O O . ASN A 2 ? 0.2545 0.2337 0.1915 0.0015 0.0063 0.0044 84 ASN A O 16 C CB . ASN A 2 ? 0.3528 0.3298 0.2793 0.0021 0.0059 0.0050 84 ASN A CB 17 C CG . ASN A 2 ? 0.5051 0.4814 0.4268 0.0025 0.0048 0.0044 84 ASN A CG 18 O OD1 . ASN A 2 ? 0.5095 0.4854 0.4288 0.0024 0.0064 0.0034 84 ASN A OD1 19 N ND2 . ASN A 2 ? 0.5259 0.5021 0.4463 0.0029 0.0022 0.0049 84 ASN A ND2 20 N N . PHE A 3 ? 0.1777 0.1560 0.1124 0.0012 0.0102 0.0040 85 PHE A N 21 C CA . PHE A 3 ? 0.1744 0.1531 0.1130 0.0008 0.0116 0.0047 85 PHE A CA 22 C C . PHE A 3 ? 0.2200 0.1982 0.1586 0.0009 0.0110 0.0067 85 PHE A C 23 O O . PHE A 3 ? 0.2074 0.1846 0.1427 0.0012 0.0109 0.0077 85 PHE A O 24 C CB . PHE A 3 ? 0.1708 0.1491 0.1097 0.0005 0.0145 0.0044 85 PHE A CB 25 C CG . PHE A 3 ? 0.2425 0.2214 0.1825 0.0004 0.0154 0.0025 85 PHE A CG 26 C CD1 . PHE A 3 ? 0.1623 0.1422 0.1055 0.0003 0.0145 0.0015 85 PHE A CD1 27 C CD2 . PHE A 3 ? 0.2057 0.1841 0.1435 0.0004 0.0172 0.0018 85 PHE A CD2 28 C CE1 . PHE A 3 ? 0.2038 0.1842 0.1483 0.0002 0.0153 -0.0002 85 PHE A CE1 29 C CE2 . PHE A 3 ? 0.2007 0.1796 0.1398 0.0003 0.0181 -0.0001 85 PHE A CE2 30 C CZ . PHE A 3 ? 0.1892 0.1691 0.1317 0.0002 0.0171 -0.0010 85 PHE A CZ 31 N N . ASN A 4 ? 0.1856 0.1644 0.1278 0.0007 0.0107 0.0072 86 ASN A N 32 C CA . ASN A 4 ? 0.1697 0.1480 0.1123 0.0008 0.0103 0.0089 86 ASN A CA 33 C C . ASN A 4 ? 0.1657 0.1431 0.1084 0.0005 0.0128 0.0099 86 ASN A C 34 O O . ASN A 4 ? 0.1742 0.1519 0.1190 0.0001 0.0147 0.0092 86 ASN A O 35 C CB . ASN A 4 ? 0.1489 0.1281 0.0954 0.0007 0.0093 0.0090 86 ASN A CB 36 C CG . ASN A 4 ? 0.1979 0.1765 0.1451 0.0008 0.0090 0.0108 86 ASN A CG 37 O OD1 . ASN A 4 ? 0.2126 0.1913 0.1625 0.0005 0.0102 0.0112 86 ASN A OD1 38 N ND2 . ASN A 4 ? 0.1340 0.1120 0.0786 0.0013 0.0074 0.0118 86 ASN A ND2 39 N N . ASN A 5 ? 0.1592 0.1356 0.0998 0.0007 0.0127 0.0116 87 ASN A N 40 C CA . ASN A 5 ? 0.1493 0.1247 0.0903 0.0004 0.0149 0.0127 87 ASN A CA 41 C C . ASN A 5 ? 0.1353 0.1105 0.0788 0.0003 0.0144 0.0141 87 ASN A C 42 O O . ASN A 5 ? 0.1816 0.1568 0.1247 0.0007 0.0123 0.0147 87 ASN A O 43 C CB . ASN A 5 ? 0.1932 0.1672 0.1296 0.0006 0.0156 0.0137 87 ASN A CB 44 C CG . ASN A 5 ? 0.3067 0.2807 0.2403 0.0007 0.0162 0.0123 87 ASN A CG 45 O OD1 . ASN A 5 ? 0.2427 0.2174 0.1783 0.0003 0.0176 0.0109 87 ASN A OD1 46 N ND2 . ASN A 5 ? 0.3400 0.3135 0.2692 0.0011 0.0149 0.0125 87 ASN A ND2 47 N N . LEU A 6 ? 0.1515 0.1265 0.0977 -0.0001 0.0163 0.0144 88 LEU A N 48 C CA . LEU A 6 ? 0.1413 0.1159 0.0900 -0.0002 0.0161 0.0156 88 LEU A CA 49 C C . LEU A 6 ? 0.1868 0.1598 0.1332 0.0000 0.0163 0.0176 88 LEU A C 50 O O . LEU A 6 ? 0.2412 0.2133 0.1882 -0.0004 0.0184 0.0183 88 LEU A O 51 C CB . LEU A 6 ? 0.1284 0.1034 0.0812 -0.0008 0.0179 0.0150 88 LEU A CB 52 C CG . LEU A 6 ? 0.1507 0.1272 0.1060 -0.0010 0.0177 0.0132 88 LEU A CG 53 C CD1 . LEU A 6 ? 0.1656 0.1425 0.1247 -0.0016 0.0197 0.0126 88 LEU A CD1 54 C CD2 . LEU A 6 ? 0.1464 0.1238 0.1031 -0.0008 0.0155 0.0130 88 LEU A CD2 55 N N . THR A 7 ? 0.1845 0.1572 0.1283 0.0005 0.0143 0.0185 89 THR A N 56 C CA . THR A 7 ? 0.1894 0.1605 0.1301 0.0008 0.0143 0.0204 89 THR A CA 57 C C . THR A 7 ? 0.2562 0.2267 0.1989 0.0009 0.0134 0.0221 89 THR A C 58 O O . THR A 7 ? 0.2366 0.2056 0.1772 0.0011 0.0135 0.0239 89 THR A O 59 C CB . THR A 7 ? 0.1620 0.1330 0.0982 0.0013 0.0124 0.0206 89 THR A CB 60 O OG1 . THR A 7 ? 0.2327 0.2046 0.1699 0.0018 0.0098 0.0203 89 THR A OG1 61 C CG2 . THR A 7 ? 0.1884 0.1598 0.1225 0.0012 0.0133 0.0189 89 THR A CG2 62 N N . LYS A 8 ? 0.1599 0.1313 0.1062 0.0009 0.0125 0.0214 90 LYS A N 63 C CA . LYS A 8 ? 0.1820 0.1528 0.1304 0.0011 0.0115 0.0228 90 LYS A CA 64 C C . LYS A 8 ? 0.2135 0.1841 0.1659 0.0005 0.0132 0.0227 90 LYS A C 65 O O . LYS A 8 ? 0.1873 0.1586 0.1417 0.0001 0.0147 0.0213 90 LYS A O 66 C CB . LYS A 8 ? 0.1718 0.1436 0.1211 0.0015 0.0090 0.0223 90 LYS A CB 67 C CG . LYS A 8 ? 0.1863 0.1586 0.1320 0.0021 0.0071 0.0221 90 LYS A CG 68 C CD . LYS A 8 ? 0.2227 0.1962 0.1700 0.0025 0.0048 0.0213 90 LYS A CD 69 C CE . LYS A 8 ? 0.2409 0.2146 0.1847 0.0030 0.0028 0.0211 90 LYS A CE 70 N NZ . LYS A 8 ? 0.2413 0.2163 0.1869 0.0034 0.0006 0.0202 90 LYS A NZ 71 N N . GLY A 9 ? 0.1526 0.1220 0.1065 0.0007 0.0130 0.0241 91 GLY A N 72 C CA . GLY A 9 ? 0.1554 0.1246 0.1134 0.0002 0.0143 0.0239 91 GLY A CA 73 C C . GLY A 9 ? 0.1814 0.1516 0.1422 0.0004 0.0128 0.0231 91 GLY A C 74 O O . GLY A 9 ? 0.1550 0.1259 0.1146 0.0009 0.0107 0.0230 91 GLY A O 75 N N . LEU A 10 ? 0.1456 0.1158 0.1102 0.0001 0.0138 0.0226 92 LEU A N 76 C CA . LEU A 10 ? 0.1529 0.1238 0.1202 0.0003 0.0126 0.0220 92 LEU A CA 77 C C . LEU A 10 ? 0.1931 0.1629 0.1604 0.0009 0.0110 0.0235 92 LEU A C 78 O O . LEU A 10 ? 0.1324 0.1006 0.0994 0.0010 0.0115 0.0251 92 LEU A O 79 C CB . LEU A 10 ? 0.1114 0.0825 0.0827 -0.0003 0.0142 0.0210 92 LEU A CB 80 C CG . LEU A 10 ? 0.1594 0.1315 0.1316 -0.0009 0.0157 0.0193 92 LEU A CG 81 C CD1 . LEU A 10 ? 0.1167 0.0890 0.0931 -0.0014 0.0168 0.0184 92 LEU A CD1 82 C CD2 . LEU A 10 ? 0.1526 0.1264 0.1234 -0.0008 0.0146 0.0181 92 LEU A CD2 83 N N . CYS A 11 ? 0.1352 0.1056 0.1032 0.0014 0.0092 0.0232 93 CYS A N 84 C CA . CYS A 11 ? 0.1567 0.1261 0.1258 0.0020 0.0078 0.0245 93 CYS A CA 85 C C . CYS A 11 ? 0.1443 0.1128 0.1171 0.0018 0.0092 0.0245 93 CYS A C 86 O O . CYS A 11 ? 0.1408 0.1100 0.1158 0.0012 0.0108 0.0231 93 CYS A O 87 C CB . CYS A 11 ? 0.1355 0.1060 0.1052 0.0025 0.0059 0.0238 93 CYS A CB 88 S SG . CYS A 11 ? 0.1705 0.1423 0.1365 0.0029 0.0040 0.0236 93 CYS A SG 89 N N . THR A 12 ? 0.1421 0.1091 0.1159 0.0022 0.0086 0.0260 94 THR A N 90 C CA . THR A 12 ? 0.1350 0.1011 0.1127 0.0022 0.0098 0.0259 94 THR A CA 91 C C . THR A 12 ? 0.1519 0.1190 0.1327 0.0023 0.0095 0.0244 94 THR A C 92 O O . THR A 12 ? 0.1456 0.1132 0.1265 0.0030 0.0078 0.0246 94 THR A O 93 C CB . THR A 12 ? 0.1803 0.1444 0.1583 0.0027 0.0090 0.0278 94 THR A CB 94 O OG1 . THR A 12 ? 0.1769 0.1399 0.1519 0.0025 0.0095 0.0293 94 THR A OG1 95 C CG2 . THR A 12 ? 0.1694 0.1327 0.1520 0.0027 0.0102 0.0275 94 THR A CG2 96 N N . ILE A 13 ? 0.1272 0.0948 0.1108 0.0017 0.0113 0.0231 95 ILE A N 97 C CA . ILE A 13 ? 0.1106 0.0792 0.0970 0.0017 0.0113 0.0215 95 ILE A CA 98 C C . ILE A 13 ? 0.1140 0.0817 0.1045 0.0020 0.0117 0.0216 95 ILE A C 99 O O . ILE A 13 ? 0.1241 0.0911 0.1169 0.0014 0.0133 0.0212 95 ILE A O 100 C CB . ILE A 13 ? 0.0832 0.0529 0.0704 0.0008 0.0129 0.0198 95 ILE A CB 101 C CG1 . ILE A 13 ? 0.1188 0.0896 0.1025 0.0005 0.0126 0.0195 95 ILE A CG1 102 C CG2 . ILE A 13 ? 0.1238 0.0944 0.1135 0.0007 0.0129 0.0182 95 ILE A CG2 103 C CD1 . ILE A 13 ? 0.1150 0.0865 0.0994 -0.0004 0.0143 0.0181 95 ILE A CD1 104 N N . ASN A 14 ? 0.1013 0.0690 0.0930 0.0028 0.0103 0.0220 96 ASN A N 105 C CA . ASN A 14 ? 0.1105 0.0775 0.1063 0.0031 0.0107 0.0219 96 ASN A CA 106 C C . ASN A 14 ? 0.1252 0.0933 0.1239 0.0031 0.0110 0.0202 96 ASN A C 107 O O . ASN A 14 ? 0.1284 0.0961 0.1309 0.0032 0.0117 0.0194 96 ASN A O 108 C CB . ASN A 14 ? 0.1077 0.0735 0.1034 0.0041 0.0090 0.0237 96 ASN A CB 109 C CG . ASN A 14 ? 0.1207 0.0849 0.1144 0.0041 0.0092 0.0254 96 ASN A CG 110 O OD1 . ASN A 14 ? 0.1400 0.1036 0.1344 0.0034 0.0109 0.0252 96 ASN A OD1 111 N ND2 . ASN A 14 ? 0.1318 0.0952 0.1228 0.0048 0.0073 0.0270 96 ASN A ND2 112 N N . SER A 15 ? 0.1104 0.0797 0.1073 0.0030 0.0105 0.0194 97 SER A N 113 C CA . SER A 15 ? 0.0996 0.0701 0.0985 0.0028 0.0109 0.0177 97 SER A CA 114 C C . SER A 15 ? 0.1214 0.0939 0.1174 0.0025 0.0101 0.0168 97 SER A C 115 O O . SER A 15 ? 0.0962 0.0683 0.0887 0.0025 0.0096 0.0179 97 SER A O 116 C CB . SER A 15 ? 0.1009 0.0718 0.1029 0.0037 0.0100 0.0176 97 SER A CB 117 O OG . SER A 15 ? 0.1289 0.1002 0.1295 0.0045 0.0081 0.0189 97 SER A OG 118 N N . TRP A 16 ? 0.0875 0.0618 0.0846 0.0022 0.0100 0.0149 98 TRP A N 119 C CA . TRP A 16 ? 0.0897 0.0658 0.0845 0.0019 0.0092 0.0141 98 TRP A CA 120 C C . TRP A 16 ? 0.0924 0.0699 0.0884 0.0025 0.0080 0.0135 98 TRP A C 121 O O . TRP A 16 ? 0.1116 0.0894 0.1107 0.0026 0.0085 0.0127 98 TRP A O 122 C CB . TRP A 16 ? 0.0774 0.0544 0.0720 0.0010 0.0103 0.0122 98 TRP A CB 123 C CG . TRP A 16 ? 0.0913 0.0671 0.0854 0.0004 0.0116 0.0126 98 TRP A CG 124 C CD1 . TRP A 16 ? 0.1305 0.1049 0.1269 0.0001 0.0129 0.0124 98 TRP A CD1 125 C CD2 . TRP A 16 ? 0.0873 0.0629 0.0785 0.0001 0.0118 0.0132 98 TRP A CD2 126 N NE1 . TRP A 16 ? 0.1022 0.0758 0.0976 -0.0005 0.0139 0.0130 98 TRP A NE1 127 C CE2 . TRP A 16 ? 0.1271 0.1013 0.1192 -0.0005 0.0133 0.0134 98 TRP A CE2 128 C CE3 . TRP A 16 ? 0.1298 0.1062 0.1178 0.0001 0.0109 0.0135 98 TRP A CE3 129 C CZ2 . TRP A 16 ? 0.1317 0.1055 0.1218 -0.0009 0.0141 0.0140 98 TRP A CZ2 130 C CZ3 . TRP A 16 ? 0.1057 0.0816 0.0915 -0.0003 0.0117 0.0140 98 TRP A CZ3 131 C CH2 . TRP A 16 ? 0.0946 0.0693 0.0815 -0.0008 0.0133 0.0142 98 TRP A CH2 132 N N . HIS A 17 ? 0.0809 0.0593 0.0748 0.0027 0.0066 0.0140 99 HIS A N 133 C CA . HIS A 17 ? 0.0659 0.0458 0.0612 0.0031 0.0055 0.0135 99 HIS A CA 134 C C . HIS A 17 ? 0.0712 0.0528 0.0651 0.0025 0.0054 0.0122 99 HIS A C 135 O O . HIS A 17 ? 0.0566 0.0382 0.0478 0.0020 0.0056 0.0120 99 HIS A O 136 C CB . HIS A 17 ? 0.0741 0.0537 0.0688 0.0040 0.0036 0.0151 99 HIS A CB 137 C CG . HIS A 17 ? 0.0787 0.0583 0.0695 0.0039 0.0026 0.0156 99 HIS A CG 138 N ND1 . HIS A 17 ? 0.0945 0.0757 0.0843 0.0036 0.0018 0.0147 99 HIS A ND1 139 C CD2 . HIS A 17 ? 0.0892 0.0673 0.0767 0.0040 0.0023 0.0170 99 HIS A CD2 140 C CE1 . HIS A 17 ? 0.1253 0.1060 0.1115 0.0036 0.0010 0.0153 99 HIS A CE1 141 N NE2 . HIS A 17 ? 0.1087 0.0876 0.0933 0.0038 0.0013 0.0167 99 HIS A NE2 142 N N . ILE A 18 ? 0.0686 0.0515 0.0645 0.0026 0.0053 0.0113 100 ILE A N 143 C CA . ILE A 18 ? 0.0851 0.0696 0.0799 0.0021 0.0052 0.0102 100 ILE A CA 144 C C . ILE A 18 ? 0.0850 0.0698 0.0774 0.0023 0.0037 0.0109 100 ILE A C 145 O O . ILE A 18 ? 0.1194 0.1039 0.1121 0.0029 0.0023 0.0119 100 ILE A O 146 C CB . ILE A 18 ? 0.0799 0.0655 0.0773 0.0022 0.0055 0.0093 100 ILE A CB 147 C CG1 . ILE A 18 ? 0.0991 0.0861 0.0951 0.0017 0.0056 0.0083 100 ILE A CG1 148 C CG2 . ILE A 18 ? 0.0749 0.0609 0.0746 0.0030 0.0043 0.0101 100 ILE A CG2 149 C CD1 . ILE A 18 ? 0.0851 0.0719 0.0795 0.0010 0.0067 0.0073 100 ILE A CD1 150 N N . TYR A 19 ? 0.0514 0.0367 0.0415 0.0017 0.0039 0.0103 101 TYR A N 151 C CA . TYR A 19 ? 0.0748 0.0603 0.0625 0.0017 0.0026 0.0106 101 TYR A CA 152 C C . TYR A 19 ? 0.0794 0.0664 0.0674 0.0014 0.0023 0.0097 101 TYR A C 153 O O . TYR A 19 ? 0.0989 0.0865 0.0871 0.0017 0.0010 0.0099 101 TYR A O 154 C CB . TYR A 19 ? 0.0863 0.0709 0.0712 0.0014 0.0032 0.0108 101 TYR A CB 155 C CG . TYR A 19 ? 0.0908 0.0756 0.0729 0.0014 0.0023 0.0109 101 TYR A CG 156 C CD1 . TYR A 19 ? 0.1298 0.1138 0.1103 0.0019 0.0009 0.0120 101 TYR A CD1 157 C CD2 . TYR A 19 ? 0.1038 0.0893 0.0848 0.0008 0.0027 0.0099 101 TYR A CD2 158 C CE1 . TYR A 19 ? 0.1489 0.1329 0.1265 0.0019 0.0001 0.0118 101 TYR A CE1 159 C CE2 . TYR A 19 ? 0.1234 0.1089 0.1020 0.0008 0.0020 0.0099 101 TYR A CE2 160 C CZ . TYR A 19 ? 0.1466 0.1314 0.1235 0.0013 0.0007 0.0108 101 TYR A CZ 161 O OH . TYR A 19 ? 0.1503 0.1351 0.1247 0.0013 0.0000 0.0105 101 TYR A OH 162 N N . GLY A 20 ? 0.0622 0.0498 0.0503 0.0009 0.0034 0.0087 102 GLY A N 163 C CA . GLY A 20 ? 0.0739 0.0628 0.0623 0.0006 0.0032 0.0079 102 GLY A CA 164 C C . GLY A 20 ? 0.0896 0.0790 0.0787 0.0002 0.0045 0.0069 102 GLY A C 165 O O . GLY A 20 ? 0.1117 0.1005 0.1007 0.0000 0.0054 0.0066 102 GLY A O 166 N N . LYS A 21 ? 0.0617 0.0520 0.0516 0.0001 0.0045 0.0065 103 LYS A N 167 C CA . LYS A 21 ? 0.0477 0.0384 0.0377 -0.0003 0.0055 0.0057 103 LYS A CA 168 C C . LYS A 21 ? 0.1045 0.0962 0.0946 -0.0004 0.0052 0.0056 103 LYS A C 169 O O . LYS A 21 ? 0.0591 0.0512 0.0508 -0.0001 0.0047 0.0060 103 LYS A O 170 C CB . LYS A 21 ? 0.0798 0.0703 0.0717 -0.0001 0.0065 0.0054 103 LYS A CB 171 C CG . LYS A 21 ? 0.0621 0.0527 0.0534 -0.0004 0.0077 0.0044 103 LYS A CG 172 C CD . LYS A 21 ? 0.0837 0.0740 0.0770 -0.0002 0.0088 0.0040 103 LYS A CD 173 C CE . LYS A 21 ? 0.0689 0.0590 0.0611 -0.0005 0.0099 0.0027 103 LYS A CE 174 N NZ . LYS A 21 ? 0.0605 0.0512 0.0508 -0.0008 0.0100 0.0023 103 LYS A NZ 175 N N . ASP A 22 ? 0.0765 0.0685 0.0651 -0.0008 0.0055 0.0051 104 ASP A N 176 C CA . ASP A 22 ? 0.0662 0.0589 0.0549 -0.0009 0.0052 0.0052 104 ASP A CA 177 C C . ASP A 22 ? 0.0687 0.0618 0.0577 -0.0010 0.0062 0.0049 104 ASP A C 178 O O . ASP A 22 ? 0.0900 0.0836 0.0794 -0.0011 0.0061 0.0052 104 ASP A O 179 C CB . ASP A 22 ? 0.0677 0.0605 0.0548 -0.0011 0.0044 0.0051 104 ASP A CB 180 C CG . ASP A 22 ? 0.0788 0.0716 0.0645 -0.0014 0.0048 0.0045 104 ASP A CG 181 O OD1 . ASP A 22 ? 0.0819 0.0744 0.0675 -0.0015 0.0056 0.0040 104 ASP A OD1 182 O OD2 . ASP A 22 ? 0.0914 0.0843 0.0762 -0.0016 0.0043 0.0044 104 ASP A OD2 183 N N . ASN A 23 ? 0.0560 0.0487 0.0445 -0.0011 0.0072 0.0043 105 ASN A N 184 C CA . ASN A 23 ? 0.0407 0.0335 0.0288 -0.0012 0.0083 0.0039 105 ASN A CA 185 C C . ASN A 23 ? 0.0917 0.0849 0.0781 -0.0014 0.0080 0.0041 105 ASN A C 186 O O . ASN A 23 ? 0.0698 0.0631 0.0563 -0.0014 0.0087 0.0044 105 ASN A O 187 C CB . ASN A 23 ? 0.0749 0.0680 0.0654 -0.0009 0.0090 0.0043 105 ASN A CB 188 C CG . ASN A 23 ? 0.0963 0.0890 0.0887 -0.0006 0.0093 0.0042 105 ASN A CG 189 O OD1 . ASN A 23 ? 0.0997 0.0919 0.0918 -0.0006 0.0101 0.0035 105 ASN A OD1 190 N ND2 . ASN A 23 ? 0.0920 0.0849 0.0865 -0.0003 0.0084 0.0049 105 ASN A ND2 191 N N . ALA A 24 ? 0.0655 0.0586 0.0505 -0.0016 0.0071 0.0040 106 ALA A N 192 C CA . ALA A 24 ? 0.0799 0.0733 0.0638 -0.0018 0.0065 0.0043 106 ALA A CA 193 C C . ALA A 24 ? 0.0965 0.0898 0.0787 -0.0019 0.0072 0.0042 106 ALA A C 194 O O . ALA A 24 ? 0.0748 0.0682 0.0566 -0.0019 0.0072 0.0048 106 ALA A O 195 C CB . ALA A 24 ? 0.0621 0.0556 0.0453 -0.0019 0.0055 0.0041 106 ALA A CB 196 N N . VAL A 25 ? 0.0758 0.0687 0.0567 -0.0019 0.0077 0.0033 107 VAL A N 197 C CA . VAL A 25 ? 0.0699 0.0625 0.0484 -0.0020 0.0081 0.0030 107 VAL A CA 198 C C . VAL A 25 ? 0.0859 0.0785 0.0646 -0.0019 0.0096 0.0034 107 VAL A C 199 O O . VAL A 25 ? 0.0769 0.0693 0.0540 -0.0019 0.0100 0.0040 107 VAL A O 200 C CB . VAL A 25 ? 0.0735 0.0658 0.0505 -0.0021 0.0081 0.0018 107 VAL A CB 201 C CG1 . VAL A 25 ? 0.0750 0.0670 0.0490 -0.0022 0.0082 0.0014 107 VAL A CG1 202 C CG2 . VAL A 25 ? 0.0956 0.0882 0.0732 -0.0023 0.0068 0.0015 107 VAL A CG2 203 N N . ARG A 26 ? 0.0591 0.0516 0.0398 -0.0018 0.0105 0.0032 108 ARG A N 204 C CA . ARG A 26 ? 0.0580 0.0505 0.0398 -0.0016 0.0121 0.0036 108 ARG A CA 205 C C . ARG A 26 ? 0.0904 0.0833 0.0732 -0.0017 0.0119 0.0048 108 ARG A C 206 O O . ARG A 26 ? 0.0975 0.0902 0.0794 -0.0017 0.0130 0.0053 108 ARG A O 207 C CB . ARG A 26 ? 0.0852 0.0779 0.0702 -0.0014 0.0127 0.0033 108 ARG A CB 208 C CG . ARG A 26 ? 0.0621 0.0542 0.0467 -0.0013 0.0134 0.0022 108 ARG A CG 209 C CD . ARG A 26 ? 0.0673 0.0595 0.0554 -0.0010 0.0136 0.0022 108 ARG A CD 210 N NE . ARG A 26 ? 0.0845 0.0771 0.0752 -0.0008 0.0146 0.0028 108 ARG A NE 211 C CZ . ARG A 26 ? 0.1024 0.0949 0.0939 -0.0007 0.0165 0.0023 108 ARG A CZ 212 N NH1 . ARG A 26 ? 0.1114 0.1031 0.1007 -0.0008 0.0175 0.0012 108 ARG A NH1 213 N NH2 . ARG A 26 ? 0.0863 0.0792 0.0807 -0.0005 0.0174 0.0029 108 ARG A NH2 214 N N . ILE A 27 ? 0.0628 0.0562 0.0476 -0.0017 0.0106 0.0052 109 ILE A N 215 C CA . ILE A 27 ? 0.0692 0.0630 0.0556 -0.0017 0.0103 0.0062 109 ILE A CA 216 C C . ILE A 27 ? 0.0876 0.0812 0.0717 -0.0019 0.0099 0.0067 109 ILE A C 217 O O . ILE A 27 ? 0.0980 0.0915 0.0824 -0.0020 0.0106 0.0076 109 ILE A O 218 C CB . ILE A 27 ? 0.0704 0.0646 0.0591 -0.0016 0.0089 0.0063 109 ILE A CB 219 C CG1 . ILE A 27 ? 0.0713 0.0657 0.0626 -0.0014 0.0093 0.0061 109 ILE A CG1 220 C CG2 . ILE A 27 ? 0.0860 0.0805 0.0762 -0.0017 0.0083 0.0071 109 ILE A CG2 221 C CD1 . ILE A 27 ? 0.0534 0.0480 0.0462 -0.0012 0.0078 0.0062 109 ILE A CD1 222 N N . GLY A 28 ? 0.0848 0.0781 0.0667 -0.0019 0.0089 0.0063 110 GLY A N 223 C CA . GLY A 28 ? 0.0788 0.0719 0.0587 -0.0020 0.0082 0.0068 110 GLY A CA 224 C C . GLY A 28 ? 0.0878 0.0804 0.0651 -0.0020 0.0093 0.0071 110 GLY A C 225 O O . GLY A 28 ? 0.1004 0.0926 0.0761 -0.0020 0.0088 0.0078 110 GLY A O 226 N N . GLU A 29 ? 0.0753 0.0675 0.0519 -0.0020 0.0108 0.0066 111 GLU A N 227 C CA . GLU A 29 ? 0.0734 0.0655 0.0480 -0.0019 0.0117 0.0068 111 GLU A CA 228 C C . GLU A 29 ? 0.1122 0.1044 0.0881 -0.0020 0.0123 0.0082 111 GLU A C 229 O O . GLU A 29 ? 0.0920 0.0840 0.0661 -0.0020 0.0124 0.0087 111 GLU A O 230 C CB . GLU A 29 ? 0.0984 0.0903 0.0729 -0.0019 0.0133 0.0059 111 GLU A CB 231 C CG . GLU A 29 ? 0.1047 0.0964 0.0768 -0.0018 0.0141 0.0057 111 GLU A CG 232 C CD . GLU A 29 ? 0.1170 0.1087 0.0903 -0.0019 0.0156 0.0068 111 GLU A CD 233 O OE1 . GLU A 29 ? 0.1092 0.1012 0.0858 -0.0019 0.0166 0.0072 111 GLU A OE1 234 O OE2 . GLU A 29 ? 0.1602 0.1518 0.1314 -0.0019 0.0158 0.0073 111 GLU A OE2 235 N N . SER A 30 ? 0.0903 0.0825 0.0692 -0.0021 0.0127 0.0087 112 SER A N 236 C CA . SER A 30 ? 0.0757 0.0680 0.0566 -0.0022 0.0134 0.0100 112 SER A CA 237 C C . SER A 30 ? 0.1802 0.1729 0.1644 -0.0023 0.0123 0.0103 112 SER A C 238 O O . SER A 30 ? 0.2936 0.2867 0.2813 -0.0024 0.0130 0.0107 112 SER A O 239 C CB . SER A 30 ? 0.1438 0.1361 0.1261 -0.0023 0.0155 0.0100 112 SER A CB 240 O OG . SER A 30 ? 0.3340 0.3263 0.3184 -0.0025 0.0161 0.0112 112 SER A OG 241 N N A SER A 31 ? 0.0939 0.0867 0.0775 -0.0022 0.0105 0.0100 113 SER A N 242 N N B SER A 31 ? 0.0934 0.0863 0.0771 -0.0022 0.0105 0.0100 113 SER A N 243 C CA A SER A 31 ? 0.0788 0.0720 0.0652 -0.0023 0.0092 0.0102 113 SER A CA 244 C CA B SER A 31 ? 0.0780 0.0713 0.0645 -0.0023 0.0091 0.0101 113 SER A CA 245 C C A SER A 31 ? 0.0932 0.0863 0.0779 -0.0022 0.0076 0.0099 113 SER A C 246 C C B SER A 31 ? 0.0930 0.0862 0.0777 -0.0022 0.0075 0.0099 113 SER A C 247 O O A SER A 31 ? 0.0951 0.0880 0.0771 -0.0021 0.0073 0.0096 113 SER A O 248 O O B SER A 31 ? 0.0952 0.0880 0.0770 -0.0021 0.0074 0.0096 113 SER A O 249 C CB A SER A 31 ? 0.0752 0.0691 0.0645 -0.0022 0.0088 0.0095 113 SER A CB 250 C CB B SER A 31 ? 0.0828 0.0768 0.0715 -0.0022 0.0086 0.0092 113 SER A CB 251 O OG A SER A 31 ? 0.1075 0.1016 0.0955 -0.0021 0.0083 0.0086 113 SER A OG 252 O OG B SER A 31 ? 0.0666 0.0609 0.0580 -0.0022 0.0097 0.0094 113 SER A OG 253 N N . ASP A 32 ? 0.0707 0.0640 0.0573 -0.0022 0.0064 0.0100 114 ASP A N 254 C CA . ASP A 32 ? 0.0611 0.0544 0.0467 -0.0021 0.0051 0.0099 114 ASP A CA 255 C C . ASP A 32 ? 0.0986 0.0922 0.0839 -0.0020 0.0041 0.0087 114 ASP A C 256 O O . ASP A 32 ? 0.0833 0.0772 0.0701 -0.0020 0.0032 0.0083 114 ASP A O 257 C CB . ASP A 32 ? 0.0653 0.0583 0.0529 -0.0022 0.0045 0.0105 114 ASP A CB 258 C CG . ASP A 32 ? 0.1317 0.1242 0.1193 -0.0023 0.0055 0.0119 114 ASP A CG 259 O OD1 . ASP A 32 ? 0.1328 0.1247 0.1175 -0.0022 0.0062 0.0124 114 ASP A OD1 260 O OD2 . ASP A 32 ? 0.1220 0.1144 0.1123 -0.0024 0.0057 0.0124 114 ASP A OD2 261 N N . VAL A 33 ? 0.0712 0.0648 0.0547 -0.0020 0.0045 0.0082 115 VAL A N 262 C CA . VAL A 33 ? 0.0787 0.0726 0.0619 -0.0020 0.0039 0.0072 115 VAL A CA 263 C C . VAL A 33 ? 0.0763 0.0702 0.0581 -0.0019 0.0030 0.0068 115 VAL A C 264 O O . VAL A 33 ? 0.0677 0.0613 0.0476 -0.0019 0.0031 0.0070 115 VAL A O 265 C CB . VAL A 33 ? 0.0684 0.0623 0.0510 -0.0020 0.0048 0.0067 115 VAL A CB 266 C CG1 . VAL A 33 ? 0.0850 0.0790 0.0672 -0.0020 0.0043 0.0057 115 VAL A CG1 267 C CG2 . VAL A 33 ? 0.0752 0.0693 0.0600 -0.0019 0.0055 0.0069 115 VAL A CG2 268 N N . LEU A 34 ? 0.0481 0.0422 0.0307 -0.0019 0.0022 0.0063 116 LEU A N 269 C CA . LEU A 34 ? 0.0433 0.0376 0.0253 -0.0019 0.0014 0.0059 116 LEU A CA 270 C C . LEU A 34 ? 0.0707 0.0650 0.0514 -0.0019 0.0016 0.0052 116 LEU A C 271 O O . LEU A 34 ? 0.0835 0.0778 0.0643 -0.0020 0.0021 0.0047 116 LEU A O 272 C CB . LEU A 34 ? 0.0529 0.0474 0.0363 -0.0018 0.0008 0.0054 116 LEU A CB 273 C CG . LEU A 34 ? 0.0568 0.0511 0.0416 -0.0018 0.0005 0.0059 116 LEU A CG 274 C CD1 . LEU A 34 ? 0.0586 0.0531 0.0445 -0.0017 0.0002 0.0052 116 LEU A CD1 275 C CD2 . LEU A 34 ? 0.0386 0.0329 0.0235 -0.0016 -0.0002 0.0064 116 LEU A CD2 276 N N . VAL A 35 ? 0.0405 0.0349 0.0201 -0.0019 0.0009 0.0050 117 VAL A N 277 C CA . VAL A 35 ? 0.0639 0.0584 0.0428 -0.0020 0.0007 0.0041 117 VAL A CA 278 C C . VAL A 35 ? 0.0814 0.0762 0.0619 -0.0021 0.0005 0.0034 117 VAL A C 279 O O . VAL A 35 ? 0.0867 0.0819 0.0685 -0.0020 0.0000 0.0035 117 VAL A O 280 C CB . VAL A 35 ? 0.0562 0.0507 0.0337 -0.0019 -0.0003 0.0041 117 VAL A CB 281 C CG1 . VAL A 35 ? 0.0479 0.0428 0.0253 -0.0021 -0.0007 0.0028 117 VAL A CG1 282 C CG2 . VAL A 35 ? 0.0717 0.0656 0.0468 -0.0018 0.0001 0.0048 117 VAL A CG2 283 N N . THR A 36 ? 0.0720 0.0668 0.0528 -0.0023 0.0011 0.0027 118 THR A N 284 C CA . THR A 36 ? 0.0401 0.0351 0.0222 -0.0024 0.0012 0.0021 118 THR A CA 285 C C . THR A 36 ? 0.0630 0.0581 0.0453 -0.0027 0.0013 0.0012 118 THR A C 286 O O . THR A 36 ? 0.0902 0.0851 0.0713 -0.0028 0.0012 0.0008 118 THR A O 287 C CB . THR A 36 ? 0.0720 0.0667 0.0546 -0.0024 0.0020 0.0024 118 THR A CB 288 O OG1 . THR A 36 ? 0.0972 0.0915 0.0792 -0.0025 0.0027 0.0024 118 THR A OG1 289 C CG2 . THR A 36 ? 0.0599 0.0546 0.0427 -0.0022 0.0018 0.0031 118 THR A CG2 290 N N . ARG A 37 ? 0.0523 0.0475 0.0361 -0.0029 0.0015 0.0007 119 ARG A N 291 C CA . ARG A 37 ? 0.0512 0.0463 0.0356 -0.0032 0.0020 -0.0001 119 ARG A CA 292 C C . ARG A 37 ? 0.0660 0.0609 0.0518 -0.0033 0.0027 -0.0001 119 ARG A C 293 O O . ARG A 37 ? 0.0653 0.0603 0.0512 -0.0031 0.0027 0.0004 119 ARG A O 294 C CB . ARG A 37 ? 0.0574 0.0528 0.0421 -0.0034 0.0012 -0.0010 119 ARG A CB 295 C CG . ARG A 37 ? 0.0741 0.0692 0.0573 -0.0035 0.0012 -0.0015 119 ARG A CG 296 C CD . ARG A 37 ? 0.0784 0.0737 0.0627 -0.0038 0.0008 -0.0029 119 ARG A CD 297 N NE . ARG A 37 ? 0.0748 0.0697 0.0611 -0.0041 0.0018 -0.0032 119 ARG A NE 298 C CZ . ARG A 37 ? 0.1028 0.0981 0.0912 -0.0045 0.0017 -0.0041 119 ARG A CZ 299 N NH1 . ARG A 37 ? 0.0807 0.0767 0.0697 -0.0046 0.0003 -0.0050 119 ARG A NH1 300 N NH2 . ARG A 37 ? 0.0954 0.0902 0.0855 -0.0048 0.0029 -0.0042 119 ARG A NH2 301 N N . GLU A 38 ? 0.0678 0.0624 0.0545 -0.0036 0.0034 -0.0006 120 GLU A N 302 C CA . GLU A 38 ? 0.0536 0.0479 0.0413 -0.0037 0.0044 -0.0005 120 GLU A CA 303 C C . GLU A 38 ? 0.0640 0.0577 0.0504 -0.0035 0.0049 0.0005 120 GLU A C 304 O O . GLU A 38 ? 0.0826 0.0763 0.0691 -0.0034 0.0050 0.0007 120 GLU A O 305 C CB . GLU A 38 ? 0.0782 0.0733 0.0677 -0.0039 0.0041 -0.0010 120 GLU A CB 306 C CG . GLU A 38 ? 0.0745 0.0702 0.0658 -0.0042 0.0035 -0.0020 120 GLU A CG 307 C CD . GLU A 38 ? 0.0920 0.0884 0.0826 -0.0040 0.0019 -0.0022 120 GLU A CD 308 O OE1 . GLU A 38 ? 0.0832 0.0797 0.0727 -0.0036 0.0014 -0.0015 120 GLU A OE1 309 O OE2 . GLU A 38 ? 0.0670 0.0636 0.0579 -0.0041 0.0012 -0.0030 120 GLU A OE2 310 N N . PRO A 39 ? 0.0692 0.0623 0.0546 -0.0033 0.0050 0.0010 121 PRO A N 311 C CA . PRO A 39 ? 0.0538 0.0464 0.0382 -0.0030 0.0052 0.0018 121 PRO A CA 312 C C . PRO A 39 ? 0.0574 0.0491 0.0416 -0.0030 0.0061 0.0022 121 PRO A C 313 O O . PRO A 39 ? 0.0811 0.0726 0.0664 -0.0033 0.0068 0.0019 121 PRO A O 314 C CB . PRO A 39 ? 0.0507 0.0431 0.0346 -0.0028 0.0051 0.0021 121 PRO A CB 315 C CG . PRO A 39 ? 0.0785 0.0707 0.0632 -0.0031 0.0055 0.0015 121 PRO A CG 316 C CD . PRO A 39 ? 0.0751 0.0679 0.0605 -0.0034 0.0052 0.0006 121 PRO A CD 317 N N . TYR A 40 ? 0.0642 0.0554 0.0472 -0.0027 0.0060 0.0029 122 TYR A N 318 C CA . TYR A 40 ? 0.0705 0.0607 0.0527 -0.0026 0.0068 0.0035 122 TYR A CA 319 C C . TYR A 40 ? 0.0771 0.0669 0.0578 -0.0022 0.0061 0.0043 122 TYR A C 320 O O . TYR A 40 ? 0.0721 0.0624 0.0527 -0.0020 0.0052 0.0042 122 TYR A O 321 C CB . TYR A 40 ? 0.0727 0.0626 0.0550 -0.0029 0.0078 0.0034 122 TYR A CB 322 C CG . TYR A 40 ? 0.0724 0.0628 0.0544 -0.0029 0.0076 0.0029 122 TYR A CG 323 C CD1 . TYR A 40 ? 0.0742 0.0658 0.0579 -0.0031 0.0072 0.0020 122 TYR A CD1 324 C CD2 . TYR A 40 ? 0.0681 0.0579 0.0484 -0.0027 0.0080 0.0032 122 TYR A CD2 325 C CE1 . TYR A 40 ? 0.0759 0.0679 0.0599 -0.0030 0.0072 0.0016 122 TYR A CE1 326 C CE2 . TYR A 40 ? 0.0702 0.0604 0.0504 -0.0027 0.0080 0.0026 122 TYR A CE2 327 C CZ . TYR A 40 ? 0.0828 0.0742 0.0651 -0.0028 0.0077 0.0018 122 TYR A CZ 328 O OH . TYR A 40 ? 0.0795 0.0713 0.0623 -0.0028 0.0077 0.0012 122 TYR A OH 329 N N . VAL A 41 ? 0.0794 0.0680 0.0587 -0.0020 0.0065 0.0050 123 VAL A N 330 C CA . VAL A 41 ? 0.0689 0.0571 0.0467 -0.0016 0.0057 0.0057 123 VAL A CA 331 C C . VAL A 41 ? 0.0616 0.0489 0.0372 -0.0015 0.0062 0.0060 123 VAL A C 332 O O . VAL A 41 ? 0.0825 0.0692 0.0580 -0.0017 0.0075 0.0061 123 VAL A O 333 C CB . VAL A 41 ? 0.0873 0.0748 0.0654 -0.0012 0.0055 0.0065 123 VAL A CB 334 C CG1 . VAL A 41 ? 0.0805 0.0677 0.0573 -0.0007 0.0042 0.0071 123 VAL A CG1 335 C CG2 . VAL A 41 ? 0.0790 0.0672 0.0592 -0.0014 0.0054 0.0061 123 VAL A CG2 336 N N . SER A 42 ? 0.0683 0.0555 0.0422 -0.0012 0.0053 0.0059 124 SER A N 337 C CA . SER A 42 ? 0.0974 0.0839 0.0692 -0.0011 0.0057 0.0060 124 SER A CA 338 C C . SER A 42 ? 0.1309 0.1172 0.1009 -0.0006 0.0042 0.0063 124 SER A C 339 O O . SER A 42 ? 0.0865 0.0731 0.0567 -0.0005 0.0030 0.0059 124 SER A O 340 C CB . SER A 42 ? 0.0973 0.0842 0.0692 -0.0014 0.0065 0.0050 124 SER A CB 341 O OG . SER A 42 ? 0.1000 0.0864 0.0704 -0.0013 0.0074 0.0050 124 SER A OG 342 N N . CYS A 43 ? 0.0888 0.0743 0.0569 -0.0003 0.0042 0.0068 125 CYS A N 343 C CA . CYS A 43 ? 0.0952 0.0804 0.0615 0.0002 0.0026 0.0070 125 CYS A CA 344 C C . CYS A 43 ? 0.1234 0.1084 0.0876 0.0002 0.0026 0.0062 125 CYS A C 345 O O . CYS A 43 ? 0.1049 0.0898 0.0685 0.0000 0.0041 0.0059 125 CYS A O 346 C CB . CYS A 43 ? 0.1127 0.0970 0.0780 0.0005 0.0023 0.0083 125 CYS A CB 347 S SG . CYS A 43 ? 0.1350 0.1191 0.1025 0.0006 0.0021 0.0093 125 CYS A SG 348 N N . ASP A 44 ? 0.1002 0.0854 0.0635 0.0005 0.0010 0.0057 126 ASP A N 349 C CA . ASP A 44 ? 0.1114 0.0962 0.0722 0.0006 0.0005 0.0049 126 ASP A CA 350 C C . ASP A 44 ? 0.1385 0.1227 0.0974 0.0011 -0.0007 0.0058 126 ASP A C 351 O O . ASP A 44 ? 0.1292 0.1133 0.0890 0.0013 -0.0013 0.0069 126 ASP A O 352 C CB . ASP A 44 ? 0.1135 0.0986 0.0747 0.0006 -0.0008 0.0038 126 ASP A CB 353 C CG . ASP A 44 ? 0.1585 0.1442 0.1212 0.0002 0.0003 0.0029 126 ASP A CG 354 O OD1 . ASP A 44 ? 0.1573 0.1431 0.1211 -0.0001 0.0019 0.0031 126 ASP A OD1 355 O OD2 . ASP A 44 ? 0.1677 0.1535 0.1306 0.0002 -0.0006 0.0019 126 ASP A OD2 356 N N . PRO A 45 ? 0.1372 0.1209 0.0933 0.0013 -0.0011 0.0053 127 PRO A N 357 C CA . PRO A 45 ? 0.1140 0.0971 0.0681 0.0018 -0.0025 0.0062 127 PRO A CA 358 C C . PRO A 45 ? 0.1599 0.1433 0.1151 0.0021 -0.0049 0.0063 127 PRO A C 359 O O . PRO A 45 ? 0.1756 0.1586 0.1300 0.0026 -0.0061 0.0073 127 PRO A O 360 C CB . PRO A 45 ? 0.1401 0.1228 0.0910 0.0019 -0.0025 0.0053 127 PRO A CB 361 C CG . PRO A 45 ? 0.1073 0.0900 0.0584 0.0014 -0.0002 0.0046 127 PRO A CG 362 C CD . PRO A 45 ? 0.1299 0.1135 0.0844 0.0011 0.0000 0.0042 127 PRO A CD 363 N N . ASP A 46 ? 0.1295 0.1135 0.0867 0.0020 -0.0057 0.0054 128 ASP A N 364 C CA . ASP A 46 ? 0.1888 0.1731 0.1474 0.0023 -0.0081 0.0054 128 ASP A CA 365 C C . ASP A 46 ? 0.1866 0.1714 0.1484 0.0021 -0.0081 0.0058 128 ASP A C 366 O O . ASP A 46 ? 0.1734 0.1585 0.1369 0.0023 -0.0100 0.0059 128 ASP A O 367 C CB . ASP A 46 ? 0.2254 0.2098 0.1832 0.0022 -0.0096 0.0039 128 ASP A CB 368 C CG . ASP A 46 ? 0.3259 0.3107 0.2847 0.0018 -0.0086 0.0026 128 ASP A CG 369 O OD1 . ASP A 46 ? 0.2553 0.2401 0.2146 0.0014 -0.0065 0.0029 128 ASP A OD1 370 O OD2 . ASP A 46 ? 0.5183 0.5031 0.4774 0.0017 -0.0100 0.0014 128 ASP A OD2 371 N N . GLU A 47 ? 0.1254 0.1104 0.0882 0.0017 -0.0060 0.0060 129 GLU A N 372 C CA . GLU A 47 ? 0.1377 0.1235 0.1040 0.0014 -0.0057 0.0061 129 GLU A CA 373 C C . GLU A 47 ? 0.1386 0.1244 0.1054 0.0011 -0.0035 0.0065 129 GLU A C 374 O O . GLU A 47 ? 0.1495 0.1349 0.1147 0.0009 -0.0021 0.0062 129 GLU A O 375 C CB . GLU A 47 ? 0.1442 0.1313 0.1128 0.0011 -0.0060 0.0048 129 GLU A CB 376 C CG . GLU A 47 ? 0.2919 0.2803 0.2647 0.0008 -0.0055 0.0049 129 GLU A CG 377 C CD . GLU A 47 ? 0.3238 0.3131 0.2984 0.0004 -0.0056 0.0038 129 GLU A CD 378 O OE1 . GLU A 47 ? 0.2258 0.2147 0.1987 0.0004 -0.0058 0.0029 129 GLU A OE1 379 O OE2 . GLU A 47 ? 0.2507 0.2409 0.2283 0.0002 -0.0052 0.0039 129 GLU A OE2 380 N N . CYS A 48 ? 0.1288 0.1152 0.0985 0.0010 -0.0031 0.0071 130 CYS A N 381 C CA . CYS A 48 ? 0.0907 0.0773 0.0615 0.0006 -0.0012 0.0072 130 CYS A CA 382 C C . CYS A 48 ? 0.0785 0.0665 0.0524 0.0003 -0.0010 0.0065 130 CYS A C 383 O O . CYS A 48 ? 0.0834 0.0722 0.0594 0.0004 -0.0020 0.0065 130 CYS A O 384 C CB . CYS A 48 ? 0.1165 0.1024 0.0877 0.0008 -0.0007 0.0084 130 CYS A CB 385 S SG . CYS A 48 ? 0.1673 0.1515 0.1350 0.0012 -0.0006 0.0094 130 CYS A SG 386 N N . ARG A 49 ? 0.0888 0.0771 0.0631 -0.0002 0.0003 0.0060 131 ARG A N 387 C CA . ARG A 49 ? 0.0543 0.0438 0.0309 -0.0005 0.0004 0.0054 131 ARG A CA 388 C C . ARG A 49 ? 0.0783 0.0681 0.0559 -0.0008 0.0017 0.0053 131 ARG A C 389 O O . ARG A 49 ? 0.0745 0.0636 0.0512 -0.0009 0.0027 0.0054 131 ARG A O 390 C CB . ARG A 49 ? 0.0726 0.0624 0.0488 -0.0006 0.0002 0.0045 131 ARG A CB 391 C CG . ARG A 49 ? 0.0761 0.0659 0.0518 -0.0003 -0.0013 0.0042 131 ARG A CG 392 C CD . ARG A 49 ? 0.1154 0.1052 0.0904 -0.0005 -0.0014 0.0032 131 ARG A CD 393 N NE . ARG A 49 ? 0.1199 0.1105 0.0970 -0.0007 -0.0012 0.0028 131 ARG A NE 394 C CZ . ARG A 49 ? 0.1510 0.1422 0.1302 -0.0008 -0.0021 0.0026 131 ARG A CZ 395 N NH1 . ARG A 49 ? 0.1461 0.1373 0.1257 -0.0006 -0.0033 0.0028 131 ARG A NH1 396 N NH2 . ARG A 49 ? 0.1137 0.1055 0.0947 -0.0010 -0.0018 0.0024 131 ARG A NH2 397 N N . PHE A 50 ? 0.0898 0.0804 0.0693 -0.0010 0.0017 0.0051 132 PHE A N 398 C CA . PHE A 50 ? 0.0791 0.0701 0.0595 -0.0013 0.0026 0.0048 132 PHE A CA 399 C C . PHE A 50 ? 0.0733 0.0648 0.0537 -0.0015 0.0028 0.0041 132 PHE A C 400 O O . PHE A 50 ? 0.0870 0.0787 0.0674 -0.0015 0.0021 0.0038 132 PHE A O 401 C CB . PHE A 50 ? 0.0491 0.0408 0.0311 -0.0013 0.0026 0.0048 132 PHE A CB 402 C CG . PHE A 50 ? 0.0895 0.0808 0.0721 -0.0011 0.0029 0.0053 132 PHE A CG 403 C CD1 . PHE A 50 ? 0.1047 0.0950 0.0865 -0.0009 0.0030 0.0058 132 PHE A CD1 404 C CD2 . PHE A 50 ? 0.1029 0.0945 0.0868 -0.0011 0.0031 0.0052 132 PHE A CD2 405 C CE1 . PHE A 50 ? 0.1330 0.1229 0.1157 -0.0007 0.0032 0.0063 132 PHE A CE1 406 C CE2 . PHE A 50 ? 0.0650 0.0563 0.0499 -0.0009 0.0034 0.0056 132 PHE A CE2 407 C CZ . PHE A 50 ? 0.0964 0.0869 0.0809 -0.0007 0.0034 0.0061 132 PHE A CZ 408 N N . TYR A 51 ? 0.0581 0.0496 0.0387 -0.0018 0.0036 0.0037 133 TYR A N 409 C CA . TYR A 51 ? 0.0666 0.0587 0.0478 -0.0020 0.0037 0.0031 133 TYR A CA 410 C C . TYR A 51 ? 0.0446 0.0373 0.0270 -0.0022 0.0039 0.0028 133 TYR A C 411 O O . TYR A 51 ? 0.0768 0.0692 0.0593 -0.0023 0.0043 0.0029 133 TYR A O 412 C CB . TYR A 51 ? 0.0584 0.0499 0.0389 -0.0021 0.0046 0.0029 133 TYR A CB 413 C CG . TYR A 51 ? 0.0777 0.0686 0.0564 -0.0018 0.0044 0.0030 133 TYR A CG 414 C CD1 . TYR A 51 ? 0.0737 0.0638 0.0509 -0.0016 0.0041 0.0037 133 TYR A CD1 415 C CD2 . TYR A 51 ? 0.0990 0.0900 0.0775 -0.0018 0.0045 0.0023 133 TYR A CD2 416 C CE1 . TYR A 51 ? 0.0770 0.0664 0.0523 -0.0013 0.0037 0.0037 133 TYR A CE1 417 C CE2 . TYR A 51 ? 0.1119 0.1022 0.0885 -0.0016 0.0043 0.0022 133 TYR A CE2 418 C CZ . TYR A 51 ? 0.1066 0.0962 0.0814 -0.0013 0.0038 0.0029 133 TYR A CZ 419 O OH . TYR A 51 ? 0.1116 0.1004 0.0841 -0.0011 0.0034 0.0027 133 TYR A OH 420 N N . ALA A 52 ? 0.0716 0.0649 0.0548 -0.0023 0.0035 0.0023 134 ALA A N 421 C CA . ALA A 52 ? 0.0573 0.0512 0.0415 -0.0025 0.0034 0.0019 134 ALA A CA 422 C C . ALA A 52 ? 0.0706 0.0652 0.0557 -0.0025 0.0029 0.0016 134 ALA A C 423 O O . ALA A 52 ? 0.0661 0.0607 0.0513 -0.0023 0.0026 0.0016 134 ALA A O 424 C CB . ALA A 52 ? 0.0421 0.0361 0.0259 -0.0025 0.0031 0.0022 134 ALA A CB 425 N N . LEU A 53 ? 0.0436 0.0386 0.0296 -0.0027 0.0026 0.0011 135 LEU A N 426 C CA . LEU A 53 ? 0.0732 0.0689 0.0602 -0.0026 0.0018 0.0009 135 LEU A CA 427 C C . LEU A 53 ? 0.0780 0.0738 0.0643 -0.0024 0.0009 0.0014 135 LEU A C 428 O O . LEU A 53 ? 0.0815 0.0773 0.0670 -0.0025 0.0007 0.0014 135 LEU A O 429 C CB . LEU A 53 ? 0.0748 0.0711 0.0635 -0.0028 0.0017 0.0002 135 LEU A CB 430 C CG . LEU A 53 ? 0.1039 0.1001 0.0939 -0.0030 0.0028 -0.0003 135 LEU A CG 431 C CD1 . LEU A 53 ? 0.0944 0.0912 0.0865 -0.0033 0.0027 -0.0011 135 LEU A CD1 432 C CD2 . LEU A 53 ? 0.0648 0.0610 0.0553 -0.0028 0.0030 -0.0004 135 LEU A CD2 433 N N . SER A 54 ? 0.0522 0.0479 0.0384 -0.0021 0.0005 0.0019 136 SER A N 434 C CA . SER A 54 ? 0.0614 0.0571 0.0470 -0.0020 -0.0001 0.0026 136 SER A CA 435 C C . SER A 54 ? 0.0757 0.0719 0.0618 -0.0019 -0.0010 0.0024 136 SER A C 436 O O . SER A 54 ? 0.0638 0.0604 0.0514 -0.0019 -0.0013 0.0018 136 SER A O 437 C CB . SER A 54 ? 0.0779 0.0733 0.0639 -0.0018 -0.0003 0.0031 136 SER A CB 438 O OG . SER A 54 ? 0.0696 0.0649 0.0551 -0.0017 -0.0008 0.0039 136 SER A OG 439 N N . GLN A 55 ? 0.0591 0.0550 0.0438 -0.0018 -0.0016 0.0030 137 GLN A N 440 C CA . GLN A 55 ? 0.0748 0.0710 0.0595 -0.0016 -0.0028 0.0031 137 GLN A CA 441 C C . GLN A 55 ? 0.0868 0.0828 0.0717 -0.0013 -0.0034 0.0042 137 GLN A C 442 O O . GLN A 55 ? 0.0832 0.0793 0.0678 -0.0011 -0.0045 0.0046 137 GLN A O 443 C CB . GLN A 55 ? 0.0553 0.0514 0.0379 -0.0017 -0.0030 0.0030 137 GLN A CB 444 C CG . GLN A 55 ? 0.0555 0.0519 0.0383 -0.0021 -0.0027 0.0018 137 GLN A CG 445 C CD . GLN A 55 ? 0.0831 0.0802 0.0676 -0.0021 -0.0038 0.0010 137 GLN A CD 446 O OE1 . GLN A 55 ? 0.0803 0.0778 0.0662 -0.0018 -0.0047 0.0012 137 GLN A OE1 447 N NE2 . GLN A 55 ? 0.0706 0.0678 0.0552 -0.0024 -0.0037 0.0000 137 GLN A NE2 448 N N . GLY A 56 ? 0.0707 0.0663 0.0561 -0.0013 -0.0027 0.0046 138 GLY A N 449 C CA . GLY A 56 ? 0.0567 0.0520 0.0428 -0.0010 -0.0032 0.0055 138 GLY A CA 450 C C . GLY A 56 ? 0.0467 0.0414 0.0309 -0.0009 -0.0033 0.0067 138 GLY A C 451 O O . GLY A 56 ? 0.0795 0.0739 0.0639 -0.0006 -0.0041 0.0076 138 GLY A O 452 N N . THR A 57 ? 0.0589 0.0534 0.0413 -0.0011 -0.0025 0.0068 139 THR A N 453 C CA . THR A 57 ? 0.0602 0.0541 0.0405 -0.0011 -0.0022 0.0079 139 THR A CA 454 C C . THR A 57 ? 0.0633 0.0570 0.0427 -0.0014 -0.0008 0.0077 139 THR A C 455 O O . THR A 57 ? 0.0585 0.0527 0.0385 -0.0015 -0.0005 0.0067 139 THR A O 456 C CB . THR A 57 ? 0.0706 0.0643 0.0486 -0.0009 -0.0031 0.0079 139 THR A CB 457 O OG1 . THR A 57 ? 0.0915 0.0845 0.0669 -0.0009 -0.0025 0.0090 139 THR A OG1 458 C CG2 . THR A 57 ? 0.0961 0.0904 0.0736 -0.0011 -0.0031 0.0065 139 THR A CG2 459 N N . THR A 58 ? 0.0638 0.0570 0.0423 -0.0014 0.0000 0.0086 140 THR A N 460 C CA . THR A 58 ? 0.0746 0.0677 0.0524 -0.0016 0.0013 0.0084 140 THR A CA 461 C C . THR A 58 ? 0.0792 0.0721 0.0541 -0.0016 0.0015 0.0080 140 THR A C 462 O O . THR A 58 ? 0.0908 0.0834 0.0639 -0.0014 0.0006 0.0082 140 THR A O 463 C CB . THR A 58 ? 0.0894 0.0822 0.0680 -0.0017 0.0024 0.0094 140 THR A CB 464 O OG1 . THR A 58 ? 0.0742 0.0662 0.0508 -0.0016 0.0027 0.0106 140 THR A OG1 465 C CG2 . THR A 58 ? 0.0700 0.0629 0.0515 -0.0017 0.0021 0.0096 140 THR A CG2 466 N N . ILE A 59 ? 0.0646 0.0575 0.0390 -0.0017 0.0027 0.0075 141 ILE A N 467 C CA . ILE A 59 ? 0.0841 0.0767 0.0558 -0.0018 0.0030 0.0068 141 ILE A CA 468 C C . ILE A 59 ? 0.0956 0.0878 0.0653 -0.0016 0.0034 0.0077 141 ILE A C 469 O O . ILE A 59 ? 0.1186 0.1109 0.0861 -0.0014 0.0027 0.0074 141 ILE A O 470 C CB . ILE A 59 ? 0.1190 0.1116 0.0911 -0.0019 0.0043 0.0060 141 ILE A CB 471 C CG1 . ILE A 59 ? 0.1905 0.1837 0.1653 -0.0020 0.0040 0.0054 141 ILE A CG1 472 C CG2 . ILE A 59 ? 0.1242 0.1165 0.0938 -0.0019 0.0044 0.0050 141 ILE A CG2 473 C CD1 . ILE A 59 ? 0.2287 0.2218 0.2042 -0.0021 0.0051 0.0047 141 ILE A CD1 474 N N . ARG A 60 ? 0.1059 0.0981 0.0766 -0.0016 0.0045 0.0088 142 ARG A N 475 C CA . ARG A 60 ? 0.1209 0.1129 0.0902 -0.0015 0.0051 0.0097 142 ARG A CA 476 C C . ARG A 60 ? 0.1205 0.1122 0.0891 -0.0013 0.0038 0.0109 142 ARG A C 477 O O . ARG A 60 ? 0.1063 0.0978 0.0732 -0.0012 0.0039 0.0117 142 ARG A O 478 C CB . ARG A 60 ? 0.1385 0.1303 0.1094 -0.0017 0.0068 0.0105 142 ARG A CB 479 C CG . ARG A 60 ? 0.1687 0.1607 0.1395 -0.0018 0.0083 0.0096 142 ARG A CG 480 C CD . ARG A 60 ? 0.1628 0.1548 0.1306 -0.0017 0.0085 0.0091 142 ARG A CD 481 N NE . ARG A 60 ? 0.1453 0.1371 0.1131 -0.0018 0.0103 0.0085 142 ARG A NE 482 C CZ . ARG A 60 ? 0.2138 0.2055 0.1790 -0.0017 0.0110 0.0080 142 ARG A CZ 483 N NH1 . ARG A 60 ? 0.1850 0.1766 0.1473 -0.0015 0.0098 0.0079 142 ARG A NH1 484 N NH2 . ARG A 60 ? 0.1622 0.1537 0.1277 -0.0018 0.0128 0.0074 142 ARG A NH2 485 N N . GLY A 61 ? 0.0770 0.0686 0.0471 -0.0012 0.0026 0.0109 143 GLY A N 486 C CA . GLY A 61 ? 0.0947 0.0859 0.0645 -0.0009 0.0013 0.0119 143 GLY A CA 487 C C . GLY A 61 ? 0.1040 0.0954 0.0714 -0.0006 -0.0001 0.0115 143 GLY A C 488 O O . GLY A 61 ? 0.1010 0.0928 0.0676 -0.0007 -0.0005 0.0101 143 GLY A O 489 N N . LYS A 62 ? 0.0772 0.0683 0.0436 -0.0002 -0.0009 0.0127 144 LYS A N 490 C CA . LYS A 62 ? 0.0825 0.0737 0.0466 0.0001 -0.0024 0.0124 144 LYS A CA 491 C C . LYS A 62 ? 0.0823 0.0737 0.0473 0.0002 -0.0043 0.0113 144 LYS A C 492 O O . LYS A 62 ? 0.0946 0.0863 0.0580 0.0003 -0.0056 0.0104 144 LYS A O 493 C CB . LYS A 62 ? 0.0700 0.0608 0.0330 0.0006 -0.0029 0.0142 144 LYS A CB 494 C CG . LYS A 62 ? 0.1287 0.1195 0.0902 0.0004 -0.0011 0.0152 144 LYS A CG 495 C CD . LYS A 62 ? 0.1554 0.1456 0.1159 0.0007 -0.0017 0.0172 144 LYS A CD 496 C CE . LYS A 62 ? 0.1909 0.1809 0.1499 0.0002 0.0001 0.0182 144 LYS A CE 497 N NZ . LYS A 62 ? 0.1985 0.1878 0.1564 0.0003 -0.0005 0.0203 144 LYS A NZ 498 N N . HIS A 63 ? 0.0763 0.0676 0.0439 -0.0001 -0.0046 0.0114 145 HIS A N 499 C CA . HIS A 63 ? 0.0738 0.0660 0.0437 -0.0001 -0.0060 0.0102 145 HIS A CA 500 C C . HIS A 63 ? 0.0878 0.0808 0.0580 -0.0004 -0.0055 0.0084 145 HIS A C 501 O O . HIS A 63 ? 0.1021 0.0959 0.0744 -0.0005 -0.0064 0.0072 145 HIS A O 502 C CB . HIS A 63 ? 0.0742 0.0668 0.0481 0.0000 -0.0061 0.0104 145 HIS A CB 503 C CG . HIS A 63 ? 0.0943 0.0862 0.0686 0.0004 -0.0069 0.0120 145 HIS A CG 504 N ND1 . HIS A 63 ? 0.0859 0.0769 0.0603 0.0004 -0.0059 0.0135 145 HIS A ND1 505 C CD2 . HIS A 63 ? 0.1020 0.0940 0.0770 0.0009 -0.0088 0.0125 145 HIS A CD2 506 C CE1 . HIS A 63 ? 0.1041 0.0945 0.0791 0.0009 -0.0069 0.0148 145 HIS A CE1 507 N NE2 . HIS A 63 ? 0.0982 0.0892 0.0735 0.0012 -0.0088 0.0142 145 HIS A NE2 508 N N . SER A 64 ? 0.0805 0.0730 0.0488 -0.0007 -0.0040 0.0081 146 SER A N 509 C CA . SER A 64 ? 0.0983 0.0913 0.0668 -0.0010 -0.0035 0.0065 146 SER A CA 510 C C . SER A 64 ? 0.0850 0.0781 0.0515 -0.0010 -0.0049 0.0055 146 SER A C 511 O O . SER A 64 ? 0.0876 0.0813 0.0550 -0.0012 -0.0050 0.0040 146 SER A O 512 C CB . SER A 64 ? 0.0777 0.0702 0.0450 -0.0013 -0.0015 0.0064 146 SER A CB 513 O OG . SER A 64 ? 0.1175 0.1098 0.0822 -0.0011 -0.0010 0.0067 146 SER A OG 514 N N . ASN A 65 ? 0.0948 0.0873 0.0586 -0.0006 -0.0060 0.0064 147 ASN A N 515 C CA . ASN A 65 ? 0.1386 0.1314 0.1008 -0.0005 -0.0077 0.0054 147 ASN A CA 516 C C . ASN A 65 ? 0.1381 0.1319 0.1034 -0.0005 -0.0095 0.0045 147 ASN A C 517 O O . ASN A 65 ? 0.1353 0.1294 0.1028 -0.0002 -0.0105 0.0054 147 ASN A O 518 C CB . ASN A 65 ? 0.1328 0.1255 0.0931 0.0001 -0.0083 0.0067 147 ASN A CB 519 C CG . ASN A 65 ? 0.1909 0.1839 0.1488 0.0003 -0.0097 0.0058 147 ASN A CG 520 O OD1 . ASN A 65 ? 0.1357 0.1291 0.0940 0.0000 -0.0108 0.0041 147 ASN A OD1 521 N ND2 . ASN A 65 ? 0.2484 0.2413 0.2038 0.0007 -0.0098 0.0068 147 ASN A ND2 522 N N . GLY A 66 ? 0.0915 0.0859 0.0576 -0.0008 -0.0098 0.0028 148 GLY A N 523 C CA . GLY A 66 ? 0.1273 0.1228 0.0971 -0.0009 -0.0112 0.0017 148 GLY A CA 524 C C . GLY A 66 ? 0.1377 0.1338 0.1113 -0.0013 -0.0098 0.0010 148 GLY A C 525 O O . GLY A 66 ? 0.1079 0.1050 0.0850 -0.0014 -0.0106 0.0002 148 GLY A O 526 N N . THR A 67 ? 0.0829 0.0786 0.0561 -0.0015 -0.0078 0.0013 149 THR A N 527 C CA . THR A 67 ? 0.1138 0.1099 0.0901 -0.0018 -0.0065 0.0009 149 THR A CA 528 C C . THR A 67 ? 0.1103 0.1068 0.0880 -0.0023 -0.0062 -0.0007 149 THR A C 529 O O . THR A 67 ? 0.1044 0.1011 0.0842 -0.0025 -0.0050 -0.0010 149 THR A O 530 C CB . THR A 67 ? 0.0801 0.0757 0.0559 -0.0018 -0.0047 0.0018 149 THR A CB 531 O OG1 . THR A 67 ? 0.0845 0.0793 0.0571 -0.0019 -0.0040 0.0019 149 THR A OG1 532 C CG2 . THR A 67 ? 0.0938 0.0893 0.0701 -0.0015 -0.0049 0.0032 149 THR A CG2 533 N N . ILE A 68 ? 0.0799 0.0764 0.0564 -0.0024 -0.0073 -0.0018 150 ILE A N 534 C CA . ILE A 68 ? 0.0727 0.0696 0.0514 -0.0028 -0.0072 -0.0034 150 ILE A CA 535 C C . ILE A 68 ? 0.0980 0.0960 0.0808 -0.0029 -0.0078 -0.0037 150 ILE A C 536 O O . ILE A 68 ? 0.1091 0.1074 0.0946 -0.0033 -0.0071 -0.0046 150 ILE A O 537 C CB . ILE A 68 ? 0.1431 0.1399 0.1199 -0.0029 -0.0085 -0.0047 150 ILE A CB 538 C CG1 . ILE A 68 ? 0.1479 0.1448 0.1270 -0.0035 -0.0079 -0.0064 150 ILE A CG1 539 C CG2 . ILE A 68 ? 0.1382 0.1356 0.1150 -0.0026 -0.0110 -0.0048 150 ILE A CG2 540 C CD1 . ILE A 68 ? 0.2111 0.2078 0.1884 -0.0037 -0.0091 -0.0080 150 ILE A CD1 541 N N . HIS A 69 ? 0.1525 0.1509 0.1359 -0.0025 -0.0090 -0.0029 151 HIS A N 542 C CA . HIS A 69 ? 0.1709 0.1703 0.1584 -0.0025 -0.0096 -0.0032 151 HIS A CA 543 C C . HIS A 69 ? 0.1592 0.1586 0.1489 -0.0027 -0.0077 -0.0029 151 HIS A C 544 O O . HIS A 69 ? 0.1421 0.1410 0.1304 -0.0025 -0.0066 -0.0019 151 HIS A O 545 C CB . HIS A 69 ? 0.1932 0.1929 0.1808 -0.0019 -0.0114 -0.0023 151 HIS A CB 546 C CG . HIS A 69 ? 0.2198 0.2197 0.2056 -0.0017 -0.0137 -0.0027 151 HIS A CG 547 N ND1 . HIS A 69 ? 0.2729 0.2735 0.2603 -0.0020 -0.0148 -0.0043 151 HIS A ND1 548 C CD2 . HIS A 69 ? 0.2703 0.2695 0.2527 -0.0012 -0.0150 -0.0017 151 HIS A CD2 549 C CE1 . HIS A 69 ? 0.2341 0.2345 0.2189 -0.0017 -0.0170 -0.0043 151 HIS A CE1 550 N NE2 . HIS A 69 ? 0.3314 0.3309 0.3129 -0.0012 -0.0171 -0.0027 151 HIS A NE2 551 N N . ASP A 70 ? 0.1045 0.1047 0.0977 -0.0030 -0.0074 -0.0039 152 ASP A N 552 C CA . ASP A 70 ? 0.0954 0.0955 0.0904 -0.0032 -0.0054 -0.0038 152 ASP A CA 553 C C . ASP A 70 ? 0.1005 0.1009 0.0971 -0.0029 -0.0052 -0.0031 152 ASP A C 554 O O . ASP A 70 ? 0.0896 0.0895 0.0857 -0.0029 -0.0037 -0.0026 152 ASP A O 555 C CB . ASP A 70 ? 0.1171 0.1177 0.1153 -0.0037 -0.0048 -0.0050 152 ASP A CB 556 C CG . ASP A 70 ? 0.1692 0.1692 0.1661 -0.0042 -0.0045 -0.0057 152 ASP A CG 557 O OD1 . ASP A 70 ? 0.1434 0.1425 0.1377 -0.0042 -0.0034 -0.0052 152 ASP A OD1 558 O OD2 . ASP A 70 ? 0.1772 0.1778 0.1761 -0.0045 -0.0053 -0.0069 152 ASP A OD2 559 N N . ARG A 71 ? 0.0730 0.0741 0.0715 -0.0026 -0.0067 -0.0032 153 ARG A N 560 C CA . ARG A 71 ? 0.0789 0.0804 0.0800 -0.0023 -0.0063 -0.0029 153 ARG A CA 561 C C . ARG A 71 ? 0.1938 0.1954 0.1944 -0.0016 -0.0079 -0.0020 153 ARG A C 562 O O . ARG A 71 ? 0.3267 0.3289 0.3284 -0.0014 -0.0098 -0.0022 153 ARG A O 563 C CB . ARG A 71 ? 0.0717 0.0743 0.0772 -0.0025 -0.0061 -0.0040 153 ARG A CB 564 C CG . ARG A 71 ? 0.0888 0.0913 0.0951 -0.0031 -0.0043 -0.0047 153 ARG A CG 565 C CD . ARG A 71 ? 0.0710 0.0745 0.0822 -0.0034 -0.0039 -0.0058 153 ARG A CD 566 N NE . ARG A 71 ? 0.1278 0.1324 0.1412 -0.0034 -0.0061 -0.0065 153 ARG A NE 567 C CZ . ARG A 71 ? 0.1435 0.1482 0.1566 -0.0038 -0.0070 -0.0073 153 ARG A CZ 568 N NH1 . ARG A 71 ? 0.0927 0.0965 0.1036 -0.0042 -0.0056 -0.0074 153 ARG A NH1 569 N NH2 . ARG A 71 ? 0.1387 0.1443 0.1537 -0.0037 -0.0093 -0.0080 153 ARG A NH2 570 N N . SER A 72 ? 0.1403 0.1411 0.1393 -0.0014 -0.0072 -0.0010 154 SER A N 571 C CA . SER A 72 ? 0.0927 0.0933 0.0915 -0.0008 -0.0085 0.0000 154 SER A CA 572 C C . SER A 72 ? 0.1042 0.1046 0.1043 -0.0007 -0.0072 0.0003 154 SER A C 573 O O . SER A 72 ? 0.0746 0.0747 0.0745 -0.0010 -0.0055 -0.0002 154 SER A O 574 C CB . SER A 72 ? 0.1107 0.1104 0.1055 -0.0007 -0.0090 0.0011 154 SER A CB 575 O OG . SER A 72 ? 0.1013 0.1002 0.0945 -0.0008 -0.0075 0.0017 154 SER A OG 576 N N . GLN A 73 ? 0.0625 0.0628 0.0636 -0.0001 -0.0082 0.0010 155 GLN A N 577 C CA . GLN A 73 ? 0.0675 0.0674 0.0699 0.0000 -0.0072 0.0011 155 GLN A CA 578 C C . GLN A 73 ? 0.0933 0.0921 0.0927 -0.0001 -0.0064 0.0019 155 GLN A C 579 O O . GLN A 73 ? 0.0861 0.0844 0.0862 0.0000 -0.0057 0.0020 155 GLN A O 580 C CB . GLN A 73 ? 0.0723 0.0723 0.0771 0.0007 -0.0086 0.0017 155 GLN A CB 581 C CG . GLN A 73 ? 0.0747 0.0758 0.0834 0.0009 -0.0095 0.0009 155 GLN A CG 582 C CD . GLN A 73 ? 0.1103 0.1120 0.1187 0.0011 -0.0117 0.0012 155 GLN A CD 583 O OE1 . GLN A 73 ? 0.0968 0.0981 0.1017 0.0008 -0.0121 0.0015 155 GLN A OE1 584 N NE2 . GLN A 73 ? 0.0922 0.0946 0.1042 0.0016 -0.0132 0.0012 155 GLN A NE2 585 N N . TYR A 74 ? 0.0743 0.0727 0.0706 -0.0003 -0.0064 0.0024 156 TYR A N 586 C CA . TYR A 74 ? 0.0425 0.0400 0.0364 -0.0004 -0.0058 0.0033 156 TYR A CA 587 C C . TYR A 74 ? 0.0726 0.0699 0.0651 -0.0008 -0.0043 0.0027 156 TYR A C 588 O O . TYR A 74 ? 0.0707 0.0674 0.0614 -0.0009 -0.0038 0.0033 156 TYR A O 589 C CB . TYR A 74 ? 0.0529 0.0499 0.0443 -0.0002 -0.0067 0.0044 156 TYR A CB 590 C CG . TYR A 74 ? 0.0811 0.0784 0.0738 0.0002 -0.0084 0.0049 156 TYR A CG 591 C CD1 . TYR A 74 ? 0.0809 0.0780 0.0761 0.0006 -0.0088 0.0052 156 TYR A CD1 592 C CD2 . TYR A 74 ? 0.1199 0.1176 0.1115 0.0003 -0.0097 0.0048 156 TYR A CD2 593 C CE1 . TYR A 74 ? 0.0609 0.0583 0.0577 0.0012 -0.0104 0.0057 156 TYR A CE1 594 C CE2 . TYR A 74 ? 0.1041 0.1019 0.0969 0.0008 -0.0115 0.0052 156 TYR A CE2 595 C CZ . TYR A 74 ? 0.1060 0.1037 0.1015 0.0013 -0.0119 0.0058 156 TYR A CZ 596 O OH . TYR A 74 ? 0.1248 0.1227 0.1219 0.0018 -0.0138 0.0063 156 TYR A OH 597 N N . ARG A 75 ? 0.0614 0.0593 0.0551 -0.0011 -0.0038 0.0017 157 ARG A N 598 C CA . ARG A 75 ? 0.0417 0.0393 0.0341 -0.0014 -0.0025 0.0013 157 ARG A CA 599 C C . ARG A 75 ? 0.0589 0.0562 0.0520 -0.0015 -0.0014 0.0009 157 ARG A C 600 O O . ARG A 75 ? 0.0854 0.0829 0.0806 -0.0013 -0.0014 0.0005 157 ARG A O 601 C CB . ARG A 75 ? 0.0608 0.0589 0.0538 -0.0018 -0.0023 0.0004 157 ARG A CB 602 C CG . ARG A 75 ? 0.0635 0.0618 0.0555 -0.0018 -0.0034 0.0005 157 ARG A CG 603 C CD . ARG A 75 ? 0.0657 0.0641 0.0575 -0.0022 -0.0028 -0.0003 157 ARG A CD 604 N NE . ARG A 75 ? 0.0701 0.0678 0.0597 -0.0024 -0.0018 0.0000 157 ARG A NE 605 C CZ . ARG A 75 ? 0.0756 0.0731 0.0647 -0.0027 -0.0013 -0.0005 157 ARG A CZ 606 N NH1 . ARG A 75 ? 0.0629 0.0597 0.0502 -0.0028 -0.0004 -0.0002 157 ARG A NH1 607 N NH2 . ARG A 75 ? 0.0669 0.0650 0.0577 -0.0030 -0.0017 -0.0014 157 ARG A NH2 608 N N . ALA A 76 ? 0.0488 0.0455 0.0402 -0.0016 -0.0005 0.0010 158 ALA A N 609 C CA . ALA A 76 ? 0.0552 0.0515 0.0465 -0.0017 0.0004 0.0006 158 ALA A CA 610 C C . ALA A 76 ? 0.0798 0.0757 0.0693 -0.0019 0.0012 0.0007 158 ALA A C 611 O O . ALA A 76 ? 0.0669 0.0626 0.0551 -0.0020 0.0010 0.0012 158 ALA A O 612 C CB . ALA A 76 ? 0.0982 0.0941 0.0894 -0.0014 -0.0001 0.0010 158 ALA A CB 613 N N . LEU A 77 ? 0.0703 0.0658 0.0594 -0.0020 0.0022 0.0002 159 LEU A N 614 C CA . LEU A 77 ? 0.0495 0.0443 0.0367 -0.0021 0.0028 0.0005 159 LEU A CA 615 C C . LEU A 77 ? 0.0610 0.0554 0.0470 -0.0019 0.0023 0.0009 159 LEU A C 616 O O . LEU A 77 ? 0.0817 0.0759 0.0680 -0.0017 0.0021 0.0006 159 LEU A O 617 C CB . LEU A 77 ? 0.0698 0.0642 0.0567 -0.0022 0.0041 0.0000 159 LEU A CB 618 C CG . LEU A 77 ? 0.0644 0.0579 0.0489 -0.0022 0.0046 0.0004 159 LEU A CG 619 C CD1 . LEU A 77 ? 0.0604 0.0538 0.0447 -0.0024 0.0047 0.0009 159 LEU A CD1 620 C CD2 . LEU A 77 ? 0.0618 0.0547 0.0455 -0.0022 0.0059 0.0001 159 LEU A CD2 621 N N . ILE A 78 ? 0.0668 0.0610 0.0519 -0.0019 0.0020 0.0015 160 ILE A N 622 C CA . ILE A 78 ? 0.0679 0.0618 0.0524 -0.0018 0.0015 0.0019 160 ILE A CA 623 C C . ILE A 78 ? 0.0771 0.0704 0.0601 -0.0018 0.0018 0.0022 160 ILE A C 624 O O . ILE A 78 ? 0.0844 0.0776 0.0671 -0.0019 0.0024 0.0023 160 ILE A O 625 C CB . ILE A 78 ? 0.0682 0.0624 0.0533 -0.0018 0.0009 0.0025 160 ILE A CB 626 C CG1 . ILE A 78 ? 0.0596 0.0540 0.0443 -0.0019 0.0012 0.0028 160 ILE A CG1 627 C CG2 . ILE A 78 ? 0.0544 0.0489 0.0408 -0.0017 0.0004 0.0025 160 ILE A CG2 628 C CD1 . ILE A 78 ? 0.0526 0.0470 0.0373 -0.0019 0.0010 0.0035 160 ILE A CD1 629 N N . SER A 79 ? 0.0543 0.0473 0.0368 -0.0016 0.0013 0.0023 161 SER A N 630 C CA . SER A 79 ? 0.0788 0.0713 0.0602 -0.0015 0.0013 0.0027 161 SER A CA 631 C C . SER A 79 ? 0.0805 0.0732 0.0627 -0.0014 0.0004 0.0031 161 SER A C 632 O O . SER A 79 ? 0.0916 0.0845 0.0749 -0.0014 -0.0001 0.0029 161 SER A O 633 C CB . SER A 79 ? 0.0896 0.0813 0.0691 -0.0014 0.0014 0.0025 161 SER A CB 634 O OG . SER A 79 ? 0.1085 0.1001 0.0879 -0.0012 0.0007 0.0019 161 SER A OG 635 N N . TRP A 80 ? 0.0748 0.0673 0.0568 -0.0013 0.0003 0.0036 162 TRP A N 636 C CA . TRP A 80 ? 0.0938 0.0866 0.0772 -0.0012 -0.0004 0.0040 162 TRP A CA 637 C C . TRP A 80 ? 0.0782 0.0706 0.0612 -0.0009 -0.0007 0.0044 162 TRP A C 638 O O . TRP A 80 ? 0.0941 0.0860 0.0758 -0.0009 -0.0002 0.0046 162 TRP A O 639 C CB . TRP A 80 ? 0.0830 0.0764 0.0678 -0.0014 0.0001 0.0043 162 TRP A CB 640 C CG . TRP A 80 ? 0.0625 0.0559 0.0470 -0.0014 0.0009 0.0045 162 TRP A CG 641 C CD1 . TRP A 80 ? 0.0512 0.0446 0.0364 -0.0013 0.0012 0.0049 162 TRP A CD1 642 C CD2 . TRP A 80 ? 0.0590 0.0523 0.0427 -0.0016 0.0016 0.0043 162 TRP A CD2 643 N NE1 . TRP A 80 ? 0.0688 0.0621 0.0535 -0.0014 0.0020 0.0049 162 TRP A NE1 644 C CE2 . TRP A 80 ? 0.0765 0.0697 0.0603 -0.0016 0.0022 0.0044 162 TRP A CE2 645 C CE3 . TRP A 80 ? 0.0604 0.0539 0.0438 -0.0017 0.0017 0.0038 162 TRP A CE3 646 C CZ2 . TRP A 80 ? 0.0539 0.0471 0.0373 -0.0018 0.0028 0.0041 162 TRP A CZ2 647 C CZ3 . TRP A 80 ? 0.0433 0.0368 0.0264 -0.0019 0.0022 0.0035 162 TRP A CZ3 648 C CH2 . TRP A 80 ? 0.0677 0.0611 0.0508 -0.0019 0.0027 0.0036 162 TRP A CH2 649 N N . PRO A 81 ? 0.0865 0.0792 0.0709 -0.0008 -0.0016 0.0046 163 PRO A N 650 C CA . PRO A 81 ? 0.0953 0.0877 0.0796 -0.0005 -0.0022 0.0050 163 PRO A CA 651 C C . PRO A 81 ? 0.0901 0.0823 0.0746 -0.0004 -0.0013 0.0056 163 PRO A C 652 O O . PRO A 81 ? 0.0793 0.0719 0.0650 -0.0006 -0.0004 0.0056 163 PRO A O 653 C CB . PRO A 81 ? 0.1061 0.0991 0.0929 -0.0004 -0.0032 0.0051 163 PRO A CB 654 C CG . PRO A 81 ? 0.1131 0.1062 0.1002 -0.0007 -0.0035 0.0045 163 PRO A CG 655 C CD . PRO A 81 ? 0.0898 0.0831 0.0762 -0.0009 -0.0022 0.0044 163 PRO A CD 656 N N . LEU A 82 ? 0.0941 0.0855 0.0774 -0.0001 -0.0016 0.0060 164 LEU A N 657 C CA . LEU A 82 ? 0.0746 0.0656 0.0582 0.0000 -0.0008 0.0066 164 LEU A CA 658 C C . LEU A 82 ? 0.0704 0.0622 0.0567 0.0001 -0.0004 0.0067 164 LEU A C 659 O O . LEU A 82 ? 0.0833 0.0755 0.0714 0.0003 -0.0012 0.0068 164 LEU A O 660 C CB . LEU A 82 ? 0.1092 0.0993 0.0916 0.0005 -0.0015 0.0072 164 LEU A CB 661 C CG . LEU A 82 ? 0.1944 0.1837 0.1767 0.0006 -0.0006 0.0079 164 LEU A CG 662 C CD1 . LEU A 82 ? 0.2225 0.2113 0.2029 0.0003 0.0006 0.0077 164 LEU A CD1 663 C CD2 . LEU A 82 ? 0.1360 0.1246 0.1181 0.0012 -0.0016 0.0088 164 LEU A CD2 664 N N . SER A 83 ? 0.0749 0.0667 0.0615 -0.0002 0.0009 0.0065 165 SER A N 665 C CA . SER A 83 ? 0.0765 0.0687 0.0651 -0.0002 0.0016 0.0065 165 SER A CA 666 C C . SER A 83 ? 0.0769 0.0700 0.0669 -0.0004 0.0018 0.0063 165 SER A C 667 O O . SER A 83 ? 0.0816 0.0750 0.0730 -0.0004 0.0027 0.0063 165 SER A O 668 C CB . SER A 83 ? 0.0750 0.0670 0.0653 0.0003 0.0013 0.0071 165 SER A CB 669 O OG . SER A 83 ? 0.0815 0.0725 0.0707 0.0005 0.0016 0.0074 165 SER A OG 670 N N . SER A 84 ? 0.0751 0.0685 0.0647 -0.0005 0.0010 0.0062 166 SER A N 671 C CA . SER A 84 ? 0.0853 0.0793 0.0757 -0.0008 0.0014 0.0061 166 SER A CA 672 C C . SER A 84 ? 0.0748 0.0687 0.0636 -0.0011 0.0023 0.0058 166 SER A C 673 O O . SER A 84 ? 0.0896 0.0831 0.0768 -0.0011 0.0024 0.0055 166 SER A O 674 C CB . SER A 84 ? 0.1298 0.1240 0.1205 -0.0008 0.0003 0.0059 166 SER A CB 675 O OG . SER A 84 ? 0.2166 0.2111 0.2095 -0.0007 -0.0006 0.0061 166 SER A OG 676 N N . PRO A 85 ? 0.0846 0.0788 0.0737 -0.0013 0.0029 0.0058 167 PRO A N 677 C CA . PRO A 85 ? 0.0988 0.0929 0.0861 -0.0015 0.0033 0.0055 167 PRO A CA 678 C C . PRO A 85 ? 0.0695 0.0637 0.0563 -0.0016 0.0026 0.0055 167 PRO A C 679 O O . PRO A 85 ? 0.0871 0.0814 0.0750 -0.0016 0.0019 0.0056 167 PRO A O 680 C CB . PRO A 85 ? 0.1291 0.1233 0.1166 -0.0016 0.0043 0.0058 167 PRO A CB 681 C CG . PRO A 85 ? 0.1177 0.1123 0.1075 -0.0015 0.0042 0.0063 167 PRO A CG 682 C CD . PRO A 85 ? 0.0775 0.0721 0.0685 -0.0013 0.0033 0.0062 167 PRO A CD 683 N N . PRO A 86 ? 0.0600 0.0541 0.0455 -0.0017 0.0026 0.0051 168 PRO A N 684 C CA . PRO A 86 ? 0.0585 0.0527 0.0438 -0.0018 0.0019 0.0050 168 PRO A CA 685 C C . PRO A 86 ? 0.1039 0.0983 0.0897 -0.0018 0.0019 0.0055 168 PRO A C 686 O O . PRO A 86 ? 0.1182 0.1125 0.1030 -0.0019 0.0022 0.0056 168 PRO A O 687 C CB . PRO A 86 ? 0.0823 0.0765 0.0665 -0.0019 0.0020 0.0045 168 PRO A CB 688 C CG . PRO A 86 ? 0.0976 0.0917 0.0812 -0.0019 0.0027 0.0044 168 PRO A CG 689 C CD . PRO A 86 ? 0.0676 0.0616 0.0519 -0.0018 0.0032 0.0047 168 PRO A CD 690 N N . THR A 87 ? 0.0934 0.0878 0.0807 -0.0018 0.0016 0.0058 169 THR A N 691 C CA . THR A 87 ? 0.0867 0.0811 0.0747 -0.0019 0.0018 0.0065 169 THR A CA 692 C C . THR A 87 ? 0.0752 0.0695 0.0637 -0.0019 0.0010 0.0064 169 THR A C 693 O O . THR A 87 ? 0.0719 0.0662 0.0604 -0.0018 0.0004 0.0057 169 THR A O 694 C CB . THR A 87 ? 0.0910 0.0856 0.0811 -0.0019 0.0020 0.0069 169 THR A CB 695 O OG1 . THR A 87 ? 0.1471 0.1416 0.1386 -0.0019 0.0011 0.0066 169 THR A OG1 696 C CG2 . THR A 87 ? 0.1128 0.1075 0.1030 -0.0019 0.0027 0.0068 169 THR A CG2 697 N N . VAL A 88 ? 0.0653 0.0594 0.0542 -0.0019 0.0011 0.0071 170 VAL A N 698 C CA . VAL A 88 ? 0.0801 0.0740 0.0699 -0.0019 0.0004 0.0071 170 VAL A CA 699 C C . VAL A 88 ? 0.0865 0.0804 0.0782 -0.0019 -0.0001 0.0066 170 VAL A C 700 O O . VAL A 88 ? 0.1258 0.1196 0.1180 -0.0019 -0.0008 0.0060 170 VAL A O 701 C CB . VAL A 88 ? 0.0946 0.0882 0.0846 -0.0019 0.0007 0.0082 170 VAL A CB 702 C CG1 . VAL A 88 ? 0.0983 0.0915 0.0898 -0.0018 0.0000 0.0083 170 VAL A CG1 703 C CG2 . VAL A 88 ? 0.0813 0.0748 0.0689 -0.0018 0.0010 0.0086 170 VAL A CG2 704 N N . TYR A 89 ? 0.0889 0.0830 0.0817 -0.0020 0.0001 0.0067 171 TYR A N 705 C CA . TYR A 89 ? 0.1041 0.0981 0.0991 -0.0021 -0.0006 0.0063 171 TYR A CA 706 C C . TYR A 89 ? 0.1417 0.1359 0.1361 -0.0020 -0.0013 0.0054 171 TYR A C 707 O O . TYR A 89 ? 0.1929 0.1870 0.1885 -0.0020 -0.0022 0.0048 171 TYR A O 708 C CB . TYR A 89 ? 0.1016 0.0958 0.0989 -0.0023 -0.0001 0.0070 171 TYR A CB 709 C CG . TYR A 89 ? 0.0888 0.0827 0.0860 -0.0024 0.0009 0.0082 171 TYR A CG 710 C CD1 . TYR A 89 ? 0.0857 0.0791 0.0831 -0.0024 0.0007 0.0086 171 TYR A CD1 711 C CD2 . TYR A 89 ? 0.1083 0.1023 0.1050 -0.0025 0.0021 0.0089 171 TYR A CD2 712 C CE1 . TYR A 89 ? 0.0698 0.0627 0.0666 -0.0024 0.0015 0.0099 171 TYR A CE1 713 C CE2 . TYR A 89 ? 0.0758 0.0694 0.0717 -0.0025 0.0031 0.0100 171 TYR A CE2 714 C CZ . TYR A 89 ? 0.0812 0.0742 0.0770 -0.0025 0.0027 0.0106 171 TYR A CZ 715 O OH . TYR A 89 ? 0.0952 0.0876 0.0899 -0.0025 0.0036 0.0119 171 TYR A OH 716 N N . ASN A 90 ? 0.1261 0.1204 0.1185 -0.0019 -0.0010 0.0052 172 ASN A N 717 C CA . ASN A 90 ? 0.1343 0.1285 0.1259 -0.0017 -0.0016 0.0046 172 ASN A CA 718 C C . ASN A 90 ? 0.1600 0.1539 0.1493 -0.0016 -0.0015 0.0041 172 ASN A C 719 O O . ASN A 90 ? 0.2735 0.2672 0.2616 -0.0015 -0.0018 0.0037 172 ASN A O 720 C CB . ASN A 90 ? 0.1553 0.1497 0.1471 -0.0016 -0.0013 0.0050 172 ASN A CB 721 C CG . ASN A 90 ? 0.2419 0.2364 0.2323 -0.0016 -0.0003 0.0053 172 ASN A CG 722 O OD1 . ASN A 90 ? 0.2732 0.2676 0.2627 -0.0017 0.0002 0.0054 172 ASN A OD1 723 N ND2 . ASN A 90 ? 0.1596 0.1541 0.1498 -0.0014 -0.0001 0.0054 172 ASN A ND2 724 N N . SER A 91 ? 0.1127 0.1067 0.1015 -0.0017 -0.0010 0.0042 173 SER A N 725 C CA . SER A 91 ? 0.0832 0.0770 0.0704 -0.0016 -0.0007 0.0037 173 SER A CA 726 C C . SER A 91 ? 0.1627 0.1563 0.1499 -0.0015 -0.0011 0.0029 173 SER A C 727 O O . SER A 91 ? 0.1847 0.1783 0.1734 -0.0016 -0.0014 0.0029 173 SER A O 728 C CB . SER A 91 ? 0.0838 0.0779 0.0707 -0.0017 -0.0002 0.0040 173 SER A CB 729 O OG . SER A 91 ? 0.1497 0.1439 0.1361 -0.0017 0.0004 0.0045 173 SER A OG 730 N N . ARG A 92 ? 0.0748 0.0680 0.0606 -0.0015 -0.0009 0.0023 174 ARG A N 731 C CA . ARG A 92 ? 0.0790 0.0720 0.0646 -0.0014 -0.0010 0.0014 174 ARG A CA 732 C C . ARG A 92 ? 0.0969 0.0901 0.0823 -0.0014 -0.0002 0.0012 174 ARG A C 733 O O . ARG A 92 ? 0.1094 0.1025 0.0937 -0.0015 0.0004 0.0013 174 ARG A O 734 C CB . ARG A 92 ? 0.1111 0.1035 0.0950 -0.0013 -0.0013 0.0009 174 ARG A CB 735 C CG . ARG A 92 ? 0.1684 0.1603 0.1514 -0.0012 -0.0011 -0.0001 174 ARG A CG 736 C CD . ARG A 92 ? 0.2466 0.2378 0.2275 -0.0010 -0.0018 -0.0006 174 ARG A CD 737 N NE . ARG A 92 ? 0.2306 0.2214 0.2092 -0.0010 -0.0012 -0.0002 174 ARG A NE 738 C CZ . ARG A 92 ? 0.2971 0.2874 0.2740 -0.0008 -0.0020 0.0001 174 ARG A CZ 739 N NH1 . ARG A 92 ? 0.2343 0.2246 0.2118 -0.0007 -0.0034 -0.0003 174 ARG A NH1 740 N NH2 . ARG A 92 ? 0.2280 0.2178 0.2028 -0.0007 -0.0015 0.0007 174 ARG A NH2 741 N N . VAL A 93 ? 0.0765 0.0698 0.0632 -0.0014 -0.0003 0.0008 175 VAL A N 742 C CA . VAL A 93 ? 0.0642 0.0577 0.0513 -0.0014 0.0004 0.0005 175 VAL A CA 743 C C . VAL A 93 ? 0.0952 0.0883 0.0813 -0.0013 0.0011 -0.0005 175 VAL A C 744 O O . VAL A 93 ? 0.1168 0.1096 0.1028 -0.0012 0.0010 -0.0012 175 VAL A O 745 C CB . VAL A 93 ? 0.0932 0.0871 0.0826 -0.0012 0.0000 0.0004 175 VAL A CB 746 C CG1 . VAL A 93 ? 0.0912 0.0855 0.0815 -0.0012 0.0005 0.0000 175 VAL A CG1 747 C CG2 . VAL A 93 ? 0.0811 0.0752 0.0710 -0.0013 -0.0006 0.0015 175 VAL A CG2 748 N N . GLU A 94 ? 0.0746 0.0678 0.0599 -0.0014 0.0020 -0.0004 176 GLU A N 749 C CA . GLU A 94 ? 0.0793 0.0720 0.0633 -0.0014 0.0031 -0.0011 176 GLU A CA 750 C C . GLU A 94 ? 0.1220 0.1152 0.1081 -0.0014 0.0038 -0.0019 176 GLU A C 751 O O . GLU A 94 ? 0.1259 0.1186 0.1115 -0.0013 0.0045 -0.0028 176 GLU A O 752 C CB . GLU A 94 ? 0.0768 0.0692 0.0592 -0.0016 0.0039 -0.0006 176 GLU A CB 753 C CG . GLU A 94 ? 0.1027 0.0947 0.0835 -0.0015 0.0032 0.0002 176 GLU A CG 754 C CD . GLU A 94 ? 0.2611 0.2523 0.2400 -0.0013 0.0026 -0.0001 176 GLU A CD 755 O OE1 . GLU A 94 ? 0.3024 0.2931 0.2802 -0.0012 0.0031 -0.0009 176 GLU A OE1 756 O OE2 . GLU A 94 ? 0.2332 0.2244 0.2117 -0.0012 0.0017 0.0004 176 GLU A OE2 757 N N . CYS A 95 ? 0.0790 0.0730 0.0672 -0.0014 0.0035 -0.0016 177 CYS A N 758 C CA . CYS A 95 ? 0.0642 0.0588 0.0550 -0.0014 0.0039 -0.0022 177 CYS A CA 759 C C . CYS A 95 ? 0.0873 0.0827 0.0799 -0.0014 0.0030 -0.0017 177 CYS A C 760 O O . CYS A 95 ? 0.0811 0.0766 0.0727 -0.0015 0.0024 -0.0009 177 CYS A O 761 C CB . CYS A 95 ? 0.1040 0.0985 0.0949 -0.0015 0.0055 -0.0029 177 CYS A CB 762 S SG . CYS A 95 ? 0.1442 0.1384 0.1331 -0.0019 0.0065 -0.0023 177 CYS A SG 763 N N . ILE A 96 ? 0.0860 0.0820 0.0814 -0.0012 0.0028 -0.0021 178 ILE A N 764 C CA . ILE A 96 ? 0.0686 0.0654 0.0656 -0.0012 0.0016 -0.0016 178 ILE A CA 765 C C . ILE A 96 ? 0.0752 0.0728 0.0738 -0.0014 0.0020 -0.0020 178 ILE A C 766 O O . ILE A 96 ? 0.0840 0.0818 0.0843 -0.0014 0.0031 -0.0028 178 ILE A O 767 C CB . ILE A 96 ? 0.0450 0.0420 0.0445 -0.0008 0.0007 -0.0016 178 ILE A CB 768 C CG1 . ILE A 96 ? 0.0880 0.0842 0.0866 -0.0006 0.0004 -0.0014 178 ILE A CG1 769 C CG2 . ILE A 96 ? 0.0690 0.0666 0.0697 -0.0006 -0.0007 -0.0009 178 ILE A CG2 770 C CD1 . ILE A 96 ? 0.1385 0.1343 0.1350 -0.0007 -0.0003 -0.0003 178 ILE A CD1 771 N N . GLY A 97 ? 0.0673 0.0652 0.0653 -0.0015 0.0013 -0.0015 179 GLY A N 772 C CA . GLY A 97 ? 0.0490 0.0476 0.0487 -0.0018 0.0015 -0.0020 179 GLY A CA 773 C C . GLY A 97 ? 0.1022 0.1008 0.1003 -0.0021 0.0011 -0.0016 179 GLY A C 774 O O . GLY A 97 ? 0.0707 0.0687 0.0663 -0.0021 0.0007 -0.0009 179 GLY A O 775 N N . TRP A 98 ? 0.0703 0.0695 0.0701 -0.0024 0.0012 -0.0022 180 TRP A N 776 C CA . TRP A 98 ? 0.0395 0.0386 0.0381 -0.0027 0.0007 -0.0021 180 TRP A CA 777 C C . TRP A 98 ? 0.0657 0.0646 0.0646 -0.0032 0.0022 -0.0026 180 TRP A C 778 O O . TRP A 98 ? 0.0905 0.0895 0.0894 -0.0035 0.0019 -0.0028 180 TRP A O 779 C CB . TRP A 98 ? 0.0289 0.0289 0.0292 -0.0026 -0.0010 -0.0024 180 TRP A CB 780 C CG . TRP A 98 ? 0.0616 0.0626 0.0658 -0.0025 -0.0013 -0.0031 180 TRP A CG 781 C CD1 . TRP A 98 ? 0.0719 0.0735 0.0777 -0.0020 -0.0025 -0.0029 180 TRP A CD1 782 C CD2 . TRP A 98 ? 0.0724 0.0740 0.0797 -0.0028 -0.0003 -0.0041 180 TRP A CD2 783 N NE1 . TRP A 98 ? 0.0532 0.0557 0.0631 -0.0020 -0.0024 -0.0038 180 TRP A NE1 784 C CE2 . TRP A 98 ? 0.0496 0.0523 0.0606 -0.0025 -0.0010 -0.0045 180 TRP A CE2 785 C CE3 . TRP A 98 ? 0.0637 0.0651 0.0714 -0.0034 0.0012 -0.0045 180 TRP A CE3 786 C CZ2 . TRP A 98 ? 0.0784 0.0819 0.0936 -0.0028 -0.0001 -0.0055 180 TRP A CZ2 787 C CZ3 . TRP A 98 ? 0.0664 0.0686 0.0780 -0.0037 0.0021 -0.0054 180 TRP A CZ3 788 C CH2 . TRP A 98 ? 0.0782 0.0814 0.0935 -0.0034 0.0015 -0.0059 180 TRP A CH2 789 N N . SER A 99 ? 0.0868 0.0853 0.0859 -0.0033 0.0038 -0.0027 181 SER A N 790 C CA . SER A 99 ? 0.0786 0.0765 0.0775 -0.0037 0.0054 -0.0027 181 SER A CA 791 C C . SER A 99 ? 0.0893 0.0862 0.0863 -0.0035 0.0068 -0.0023 181 SER A C 792 O O . SER A 99 ? 0.0954 0.0925 0.0931 -0.0033 0.0070 -0.0026 181 SER A O 793 C CB . SER A 99 ? 0.0806 0.0792 0.0831 -0.0041 0.0061 -0.0036 181 SER A CB 794 O OG . SER A 99 ? 0.0754 0.0732 0.0777 -0.0045 0.0078 -0.0035 181 SER A OG 795 N N . SER A 100 ? 0.0501 0.0460 0.0447 -0.0037 0.0076 -0.0018 182 SER A N 796 C CA . SER A 100 ? 0.0667 0.0616 0.0588 -0.0034 0.0085 -0.0013 182 SER A CA 797 C C . SER A 100 ? 0.0862 0.0799 0.0764 -0.0036 0.0099 -0.0008 182 SER A C 798 O O . SER A 100 ? 0.0713 0.0648 0.0620 -0.0039 0.0102 -0.0006 182 SER A O 799 C CB . SER A 100 ? 0.0830 0.0776 0.0729 -0.0031 0.0072 -0.0008 182 SER A CB 800 O OG . SER A 100 ? 0.1080 0.1020 0.0960 -0.0031 0.0069 -0.0002 182 SER A OG 801 N N . THR A 101 ? 0.0654 0.0582 0.0534 -0.0034 0.0107 -0.0005 183 THR A N 802 C CA . THR A 101 ? 0.0732 0.0646 0.0583 -0.0034 0.0116 0.0003 183 THR A CA 803 C C . THR A 101 ? 0.0676 0.0584 0.0498 -0.0030 0.0113 0.0004 183 THR A C 804 O O . THR A 101 ? 0.0962 0.0875 0.0790 -0.0028 0.0108 -0.0003 183 THR A O 805 C CB . THR A 101 ? 0.0735 0.0643 0.0592 -0.0038 0.0138 0.0004 183 THR A CB 806 O OG1 . THR A 101 ? 0.0827 0.0720 0.0655 -0.0037 0.0144 0.0015 183 THR A OG1 807 C CG2 . THR A 101 ? 0.0996 0.0904 0.0854 -0.0037 0.0150 -0.0003 183 THR A CG2 808 N N . SER A 102 ? 0.0789 0.0685 0.0582 -0.0028 0.0114 0.0013 184 SER A N 809 C CA . SER A 102 ? 0.1179 0.1068 0.0942 -0.0024 0.0108 0.0013 184 SER A CA 810 C C . SER A 102 ? 0.1081 0.0954 0.0811 -0.0023 0.0114 0.0024 184 SER A C 811 O O . SER A 102 ? 0.1021 0.0891 0.0754 -0.0024 0.0114 0.0032 184 SER A O 812 C CB . SER A 102 ? 0.0859 0.0754 0.0625 -0.0022 0.0088 0.0013 184 SER A CB 813 O OG . SER A 102 ? 0.0982 0.0872 0.0727 -0.0019 0.0081 0.0011 184 SER A OG 814 N N . CYS A 103 ? 0.1104 0.0971 0.0810 -0.0020 0.0115 0.0022 185 CYS A N 815 C CA . CYS A 103 ? 0.0940 0.0799 0.0625 -0.0017 0.0111 0.0032 185 CYS A CA 816 C C . CYS A 103 ? 0.1058 0.0913 0.0715 -0.0013 0.0104 0.0028 185 CYS A C 817 O O . CYS A 103 ? 0.1006 0.0861 0.0660 -0.0013 0.0110 0.0017 185 CYS A O 818 C CB . CYS A 103 ? 0.0909 0.0762 0.0598 -0.0019 0.0128 0.0038 185 CYS A CB 819 S SG . CYS A 103 ? 0.1277 0.1131 0.0977 -0.0022 0.0152 0.0029 185 CYS A SG 820 N N . HIS A 104 ? 0.1054 0.0904 0.0692 -0.0009 0.0092 0.0035 186 HIS A N 821 C CA . HIS A 104 ? 0.1189 0.1034 0.0798 -0.0005 0.0085 0.0032 186 HIS A CA 822 C C . HIS A 104 ? 0.1099 0.0935 0.0687 -0.0005 0.0097 0.0038 186 HIS A C 823 O O . HIS A 104 ? 0.1204 0.1037 0.0795 -0.0005 0.0101 0.0049 186 HIS A O 824 C CB . HIS A 104 ? 0.0979 0.0824 0.0580 -0.0002 0.0062 0.0036 186 HIS A CB 825 C CG . HIS A 104 ? 0.1228 0.1070 0.0807 0.0001 0.0050 0.0027 186 HIS A CG 826 N ND1 . HIS A 104 ? 0.1513 0.1349 0.1062 0.0004 0.0050 0.0026 186 HIS A ND1 827 C CD2 . HIS A 104 ? 0.1189 0.1035 0.0772 0.0002 0.0036 0.0018 186 HIS A CD2 828 C CE1 . HIS A 104 ? 0.1146 0.0981 0.0682 0.0005 0.0037 0.0016 186 HIS A CE1 829 N NE2 . HIS A 104 ? 0.1146 0.0987 0.0704 0.0004 0.0028 0.0010 186 HIS A NE2 830 N N . ASP A 105 ? 0.1268 0.1100 0.0835 -0.0004 0.0103 0.0030 187 ASP A N 831 C CA . ASP A 105 ? 0.1086 0.0910 0.0630 -0.0003 0.0116 0.0035 187 ASP A CA 832 C C . ASP A 105 ? 0.1770 0.1587 0.1277 0.0001 0.0102 0.0040 187 ASP A C 833 O O . ASP A 105 ? 0.1485 0.1293 0.0966 0.0002 0.0111 0.0045 187 ASP A O 834 C CB . ASP A 105 ? 0.0949 0.0771 0.0491 -0.0005 0.0136 0.0024 187 ASP A CB 835 C CG . ASP A 105 ? 0.1128 0.0952 0.0656 -0.0003 0.0129 0.0009 187 ASP A CG 836 O OD1 . ASP A 105 ? 0.1383 0.1206 0.0893 0.0001 0.0109 0.0007 187 ASP A OD1 837 O OD2 . ASP A 105 ? 0.1735 0.1561 0.1272 -0.0004 0.0143 -0.0003 187 ASP A OD2 838 N N . GLY A 106 ? 0.1154 0.0974 0.0660 0.0004 0.0080 0.0039 188 GLY A N 839 C CA . GLY A 106 ? 0.1138 0.0952 0.0612 0.0008 0.0063 0.0042 188 GLY A CA 840 C C . GLY A 106 ? 0.1723 0.1539 0.1184 0.0010 0.0052 0.0026 188 GLY A C 841 O O . GLY A 106 ? 0.1782 0.1597 0.1229 0.0013 0.0031 0.0025 188 GLY A O 842 N N . LYS A 107 ? 0.1459 0.1277 0.0925 0.0008 0.0066 0.0013 189 LYS A N 843 C CA . LYS A 107 ? 0.1148 0.0967 0.0605 0.0009 0.0058 -0.0005 189 LYS A CA 844 C C . LYS A 107 ? 0.1464 0.1290 0.0953 0.0007 0.0053 -0.0014 189 LYS A C 845 O O . LYS A 107 ? 0.1550 0.1378 0.1042 0.0008 0.0033 -0.0020 189 LYS A O 846 C CB . LYS A 107 ? 0.1574 0.1388 0.1013 0.0008 0.0077 -0.0015 189 LYS A CB 847 C CG . LYS A 107 ? 0.1673 0.1479 0.1073 0.0010 0.0082 -0.0008 189 LYS A CG 848 C CD . LYS A 107 ? 0.2268 0.2070 0.1651 0.0010 0.0101 -0.0020 189 LYS A CD 849 C CE . LYS A 107 ? 0.2916 0.2708 0.2256 0.0012 0.0106 -0.0014 189 LYS A CE 850 N NZ . LYS A 107 ? 0.3606 0.3394 0.2926 0.0013 0.0124 -0.0028 189 LYS A NZ 851 N N . SER A 108 ? 0.1339 0.1169 0.0854 0.0004 0.0070 -0.0014 190 SER A N 852 C CA . SER A 108 ? 0.1227 0.1063 0.0771 0.0001 0.0067 -0.0020 190 SER A CA 853 C C . SER A 108 ? 0.1419 0.1261 0.0992 -0.0002 0.0078 -0.0011 190 SER A C 854 O O . SER A 108 ? 0.1287 0.1127 0.0858 -0.0003 0.0090 -0.0001 190 SER A O 855 C CB . SER A 108 ? 0.1617 0.1452 0.1165 0.0001 0.0077 -0.0038 190 SER A CB 856 O OG . SER A 108 ? 0.2205 0.2037 0.1732 0.0003 0.0063 -0.0050 190 SER A OG 857 N N . ARG A 109 ? 0.1259 0.1106 0.0856 -0.0004 0.0074 -0.0014 191 ARG A N 858 C CA . ARG A 109 ? 0.1179 0.1032 0.0802 -0.0007 0.0082 -0.0007 191 ARG A CA 859 C C . ARG A 109 ? 0.0988 0.0843 0.0630 -0.0010 0.0100 -0.0016 191 ARG A C 860 O O . ARG A 109 ? 0.1115 0.0973 0.0764 -0.0010 0.0099 -0.0029 191 ARG A O 861 C CB . ARG A 109 ? 0.0942 0.0800 0.0580 -0.0008 0.0066 -0.0003 191 ARG A CB 862 C CG . ARG A 109 ? 0.1057 0.0925 0.0730 -0.0011 0.0071 0.0002 191 ARG A CG 863 C CD . ARG A 109 ? 0.1022 0.0897 0.0710 -0.0011 0.0055 0.0009 191 ARG A CD 864 N NE . ARG A 109 ? 0.0811 0.0678 0.0479 -0.0009 0.0050 0.0020 191 ARG A NE 865 C CZ . ARG A 109 ? 0.1034 0.0901 0.0710 -0.0010 0.0058 0.0029 191 ARG A CZ 866 N NH1 . ARG A 109 ? 0.0829 0.0699 0.0522 -0.0014 0.0072 0.0028 191 ARG A NH1 867 N NH2 . ARG A 109 ? 0.0941 0.0804 0.0608 -0.0007 0.0051 0.0039 191 ARG A NH2 868 N N . MET A 110 ? 0.0900 0.0758 0.0558 -0.0013 0.0116 -0.0010 192 MET A N 869 C CA . MET A 110 ? 0.1081 0.0946 0.0769 -0.0016 0.0131 -0.0018 192 MET A CA 870 C C . MET A 110 ? 0.0812 0.0690 0.0536 -0.0018 0.0120 -0.0013 192 MET A C 871 O O . MET A 110 ? 0.0958 0.0835 0.0680 -0.0019 0.0118 -0.0002 192 MET A O 872 C CB . MET A 110 ? 0.1039 0.0901 0.0730 -0.0018 0.0153 -0.0015 192 MET A CB 873 C CG . MET A 110 ? 0.1203 0.1074 0.0932 -0.0022 0.0169 -0.0023 192 MET A CG 874 S SD . MET A 110 ? 0.1100 0.0969 0.0841 -0.0025 0.0195 -0.0019 192 MET A SD 875 C CE . MET A 110 ? 0.1500 0.1367 0.1244 -0.0028 0.0190 -0.0003 192 MET A CE 876 N N . SER A 111 ? 0.1008 0.0900 0.0766 -0.0018 0.0114 -0.0021 193 SER A N 877 C CA . SER A 111 ? 0.0946 0.0850 0.0737 -0.0020 0.0105 -0.0017 193 SER A CA 878 C C . SER A 111 ? 0.0765 0.0678 0.0592 -0.0022 0.0114 -0.0025 193 SER A C 879 O O . SER A 111 ? 0.1174 0.1089 0.1009 -0.0020 0.0118 -0.0035 193 SER A O 880 C CB . SER A 111 ? 0.0990 0.0899 0.0786 -0.0018 0.0085 -0.0016 193 SER A CB 881 O OG . SER A 111 ? 0.1005 0.0907 0.0775 -0.0017 0.0076 -0.0009 193 SER A OG 882 N N . ILE A 112 ? 0.0752 0.0673 0.0603 -0.0025 0.0116 -0.0022 194 ILE A N 883 C CA . ILE A 112 ? 0.0740 0.0672 0.0629 -0.0027 0.0122 -0.0029 194 ILE A CA 884 C C . ILE A 112 ? 0.0759 0.0703 0.0673 -0.0027 0.0105 -0.0027 194 ILE A C 885 O O . ILE A 112 ? 0.0655 0.0598 0.0562 -0.0029 0.0099 -0.0021 194 ILE A O 886 C CB . ILE A 112 ? 0.0834 0.0763 0.0731 -0.0031 0.0143 -0.0029 194 ILE A CB 887 C CG1 . ILE A 112 ? 0.0935 0.0850 0.0800 -0.0030 0.0161 -0.0029 194 ILE A CG1 888 C CG2 . ILE A 112 ? 0.0998 0.0941 0.0943 -0.0032 0.0148 -0.0038 194 ILE A CG2 889 C CD1 . ILE A 112 ? 0.1057 0.0968 0.0930 -0.0034 0.0186 -0.0027 194 ILE A CD1 890 N N . CYS A 113 ? 0.0638 0.0591 0.0578 -0.0025 0.0096 -0.0033 195 CYS A N 891 C CA . CYS A 113 ? 0.0996 0.0959 0.0958 -0.0025 0.0080 -0.0031 195 CYS A CA 892 C C . CYS A 113 ? 0.0880 0.0854 0.0883 -0.0025 0.0081 -0.0039 195 CYS A C 893 O O . CYS A 113 ? 0.0796 0.0771 0.0814 -0.0023 0.0089 -0.0046 195 CYS A O 894 C CB . CYS A 113 ? 0.1240 0.1203 0.1194 -0.0021 0.0063 -0.0028 195 CYS A CB 895 S SG . CYS A 113 ? 0.1708 0.1662 0.1626 -0.0021 0.0056 -0.0019 195 CYS A SG 896 N N . ILE A 114 ? 0.0784 0.0767 0.0806 -0.0028 0.0074 -0.0039 196 ILE A N 897 C CA . ILE A 114 ? 0.0652 0.0647 0.0717 -0.0028 0.0070 -0.0046 196 ILE A CA 898 C C . ILE A 114 ? 0.0596 0.0598 0.0669 -0.0024 0.0046 -0.0043 196 ILE A C 899 O O . ILE A 114 ? 0.0810 0.0810 0.0863 -0.0025 0.0034 -0.0037 196 ILE A O 900 C CB . ILE A 114 ? 0.0392 0.0391 0.0476 -0.0033 0.0077 -0.0049 196 ILE A CB 901 C CG1 . ILE A 114 ? 0.0688 0.0678 0.0763 -0.0036 0.0103 -0.0049 196 ILE A CG1 902 C CG2 . ILE A 114 ? 0.0362 0.0376 0.0495 -0.0033 0.0070 -0.0057 196 ILE A CG2 903 C CD1 . ILE A 114 ? 0.0974 0.0964 0.1058 -0.0042 0.0112 -0.0049 196 ILE A CD1 904 N N . SER A 115 ? 0.0564 0.0574 0.0668 -0.0021 0.0040 -0.0047 197 SER A N 905 C CA . SER A 115 ? 0.0687 0.0702 0.0801 -0.0017 0.0017 -0.0043 197 SER A CA 906 C C . SER A 115 ? 0.0999 0.1028 0.1162 -0.0015 0.0010 -0.0051 197 SER A C 907 O O . SER A 115 ? 0.0881 0.0914 0.1073 -0.0017 0.0026 -0.0059 197 SER A O 908 C CB . SER A 115 ? 0.0848 0.0857 0.0948 -0.0012 0.0010 -0.0038 197 SER A CB 909 O OG . SER A 115 ? 0.0758 0.0769 0.0886 -0.0009 0.0016 -0.0044 197 SER A OG 910 N N . GLY A 116 ? 0.0604 0.0639 0.0778 -0.0012 -0.0012 -0.0047 198 GLY A N 911 C CA . GLY A 116 ? 0.0616 0.0663 0.0838 -0.0009 -0.0023 -0.0053 198 GLY A CA 912 C C . GLY A 116 ? 0.0693 0.0748 0.0923 -0.0011 -0.0043 -0.0054 198 GLY A C 913 O O . GLY A 116 ? 0.0786 0.0837 0.0983 -0.0014 -0.0046 -0.0051 198 GLY A O 914 N N . PRO A 117 ? 0.0655 0.0723 0.0929 -0.0007 -0.0058 -0.0059 199 PRO A N 915 C CA . PRO A 117 ? 0.0674 0.0751 0.0960 -0.0009 -0.0078 -0.0062 199 PRO A CA 916 C C . PRO A 117 ? 0.0959 0.1042 0.1266 -0.0017 -0.0063 -0.0073 199 PRO A C 917 O O . PRO A 117 ? 0.0758 0.0838 0.1074 -0.0020 -0.0037 -0.0077 199 PRO A O 918 C CB . PRO A 117 ? 0.0783 0.0872 0.1116 -0.0002 -0.0097 -0.0064 199 PRO A CB 919 C CG . PRO A 117 ? 0.0831 0.0922 0.1198 -0.0001 -0.0076 -0.0068 199 PRO A CG 920 C CD . PRO A 117 ? 0.0761 0.0836 0.1081 -0.0002 -0.0056 -0.0062 199 PRO A CD 921 N N . ASN A 118 ? 0.0794 0.0883 0.1107 -0.0020 -0.0078 -0.0079 200 ASN A N 922 C CA . ASN A 118 ? 0.0867 0.0960 0.1202 -0.0028 -0.0064 -0.0089 200 ASN A CA 923 C C . ASN A 118 ? 0.0599 0.0703 0.0993 -0.0030 -0.0047 -0.0098 200 ASN A C 924 O O . ASN A 118 ? 0.0840 0.0940 0.1241 -0.0036 -0.0021 -0.0103 200 ASN A O 925 C CB . ASN A 118 ? 0.1164 0.1263 0.1504 -0.0030 -0.0088 -0.0096 200 ASN A CB 926 C CG . ASN A 118 ? 0.1341 0.1429 0.1621 -0.0030 -0.0099 -0.0089 200 ASN A CG 927 O OD1 . ASN A 118 ? 0.1219 0.1295 0.1457 -0.0029 -0.0088 -0.0079 200 ASN A OD1 928 N ND2 . ASN A 118 ? 0.1604 0.1697 0.1882 -0.0031 -0.0122 -0.0095 200 ASN A ND2 929 N N . ASN A 119 ? 0.0794 0.0909 0.1230 -0.0024 -0.0059 -0.0101 201 ASN A N 930 C CA . ASN A 119 ? 0.0822 0.0949 0.1321 -0.0025 -0.0043 -0.0111 201 ASN A CA 931 C C . ASN A 119 ? 0.0969 0.1091 0.1473 -0.0022 -0.0019 -0.0109 201 ASN A C 932 O O . ASN A 119 ? 0.0994 0.1126 0.1552 -0.0022 -0.0006 -0.0117 201 ASN A O 933 C CB . ASN A 119 ? 0.1012 0.1158 0.1568 -0.0021 -0.0072 -0.0118 201 ASN A CB 934 C CG . ASN A 119 ? 0.1645 0.1790 0.2195 -0.0011 -0.0095 -0.0109 201 ASN A CG 935 O OD1 . ASN A 119 ? 0.1057 0.1189 0.1565 -0.0007 -0.0089 -0.0099 201 ASN A OD1 936 N ND2 . ASN A 119 ? 0.1266 0.1425 0.1860 -0.0007 -0.0123 -0.0113 201 ASN A ND2 937 N N . ASN A 120 ? 0.1047 0.1154 0.1497 -0.0019 -0.0014 -0.0099 202 ASN A N 938 C CA . ASN A 120 ? 0.0744 0.0845 0.1196 -0.0015 0.0005 -0.0098 202 ASN A CA 939 C C . ASN A 120 ? 0.0692 0.0776 0.1081 -0.0016 0.0019 -0.0090 202 ASN A C 940 O O . ASN A 120 ? 0.0767 0.0843 0.1140 -0.0011 0.0020 -0.0086 202 ASN A O 941 C CB . ASN A 120 ? 0.0643 0.0751 0.1120 -0.0006 -0.0017 -0.0096 202 ASN A CB 942 C CG . ASN A 120 ? 0.0562 0.0681 0.1102 -0.0003 -0.0004 -0.0106 202 ASN A CG 943 O OD1 . ASN A 120 ? 0.0803 0.0921 0.1359 -0.0007 0.0026 -0.0114 202 ASN A OD1 944 N ND2 . ASN A 120 ? 0.1038 0.1164 0.1612 0.0005 -0.0026 -0.0105 202 ASN A ND2 945 N N . ALA A 121 ? 0.0631 0.0707 0.0986 -0.0022 0.0028 -0.0088 203 ALA A N 946 C CA . ALA A 121 ? 0.0386 0.0446 0.0683 -0.0023 0.0039 -0.0080 203 ALA A CA 947 C C . ALA A 121 ? 0.0930 0.0982 0.1221 -0.0024 0.0069 -0.0083 203 ALA A C 948 O O . ALA A 121 ? 0.0870 0.0928 0.1199 -0.0026 0.0087 -0.0092 203 ALA A O 949 C CB . ALA A 121 ? 0.0654 0.0708 0.0920 -0.0029 0.0038 -0.0076 203 ALA A CB 950 N N . SER A 122 ? 0.0735 0.0773 0.0979 -0.0022 0.0074 -0.0077 204 SER A N 951 C CA . SER A 122 ? 0.0929 0.0958 0.1158 -0.0023 0.0100 -0.0080 204 SER A CA 952 C C . SER A 122 ? 0.0953 0.0966 0.1123 -0.0024 0.0104 -0.0072 204 SER A C 953 O O . SER A 122 ? 0.0819 0.0829 0.0964 -0.0022 0.0085 -0.0065 204 SER A O 954 C CB . SER A 122 ? 0.0753 0.0783 0.1001 -0.0017 0.0103 -0.0086 204 SER A CB 955 O OG . SER A 122 ? 0.0966 0.0992 0.1197 -0.0012 0.0082 -0.0080 204 SER A OG 956 N N . ALA A 123 ? 0.0793 0.0796 0.0942 -0.0027 0.0128 -0.0073 205 ALA A N 957 C CA . ALA A 123 ? 0.0549 0.0537 0.0644 -0.0028 0.0132 -0.0066 205 ALA A CA 958 C C . ALA A 123 ? 0.0842 0.0822 0.0918 -0.0023 0.0138 -0.0070 205 ALA A C 959 O O . ALA A 123 ? 0.1076 0.1057 0.1172 -0.0022 0.0154 -0.0079 205 ALA A O 960 C CB . ALA A 123 ? 0.0845 0.0825 0.0925 -0.0033 0.0153 -0.0063 205 ALA A CB 961 N N . VAL A 124 ? 0.0751 0.0722 0.0791 -0.0021 0.0125 -0.0064 206 VAL A N 962 C CA . VAL A 124 ? 0.0837 0.0799 0.0853 -0.0018 0.0131 -0.0069 206 VAL A CA 963 C C . VAL A 124 ? 0.1060 0.1008 0.1026 -0.0020 0.0137 -0.0063 206 VAL A C 964 O O . VAL A 124 ? 0.0896 0.0841 0.0842 -0.0021 0.0125 -0.0053 206 VAL A O 965 C CB . VAL A 124 ? 0.0821 0.0784 0.0841 -0.0014 0.0111 -0.0069 206 VAL A CB 966 C CG1 . VAL A 124 ? 0.1080 0.1032 0.1078 -0.0011 0.0117 -0.0076 206 VAL A CG1 967 C CG2 . VAL A 124 ? 0.0742 0.0718 0.0811 -0.0011 0.0102 -0.0072 206 VAL A CG2 968 N N . VAL A 125 ? 0.0746 0.0684 0.0691 -0.0020 0.0157 -0.0068 207 VAL A N 969 C CA . VAL A 125 ? 0.0873 0.0796 0.0767 -0.0021 0.0163 -0.0062 207 VAL A CA 970 C C . VAL A 125 ? 0.1111 0.1025 0.0975 -0.0017 0.0154 -0.0066 207 VAL A C 971 O O . VAL A 125 ? 0.1250 0.1161 0.1116 -0.0014 0.0162 -0.0078 207 VAL A O 972 C CB . VAL A 125 ? 0.0855 0.0769 0.0737 -0.0023 0.0191 -0.0064 207 VAL A CB 973 C CG1 . VAL A 125 ? 0.1016 0.0915 0.0846 -0.0023 0.0195 -0.0055 207 VAL A CG1 974 C CG2 . VAL A 125 ? 0.1164 0.1089 0.1086 -0.0027 0.0201 -0.0062 207 VAL A CG2 975 N N . TRP A 126 ? 0.0931 0.0841 0.0771 -0.0016 0.0136 -0.0057 208 TRP A N 976 C CA . TRP A 126 ? 0.1087 0.0989 0.0900 -0.0013 0.0125 -0.0061 208 TRP A CA 977 C C . TRP A 126 ? 0.1286 0.1173 0.1050 -0.0013 0.0130 -0.0057 208 TRP A C 978 O O . TRP A 126 ? 0.0996 0.0881 0.0748 -0.0015 0.0134 -0.0046 208 TRP A O 979 C CB . TRP A 126 ? 0.0926 0.0835 0.0749 -0.0013 0.0101 -0.0054 208 TRP A CB 980 C CG . TRP A 126 ? 0.0836 0.0756 0.0699 -0.0012 0.0092 -0.0056 208 TRP A CG 981 C CD1 . TRP A 126 ? 0.0803 0.0734 0.0700 -0.0013 0.0094 -0.0054 208 TRP A CD1 982 C CD2 . TRP A 126 ? 0.0852 0.0773 0.0729 -0.0010 0.0078 -0.0059 208 TRP A CD2 983 N NE1 . TRP A 126 ? 0.0704 0.0642 0.0630 -0.0011 0.0082 -0.0055 208 TRP A NE1 984 C CE2 . TRP A 126 ? 0.1131 0.1064 0.1047 -0.0009 0.0073 -0.0058 208 TRP A CE2 985 C CE3 . TRP A 126 ? 0.1074 0.0989 0.0936 -0.0008 0.0069 -0.0064 208 TRP A CE3 986 C CZ2 . TRP A 126 ? 0.1316 0.1251 0.1253 -0.0007 0.0060 -0.0059 208 TRP A CZ2 987 C CZ3 . TRP A 126 ? 0.0971 0.0889 0.0859 -0.0006 0.0057 -0.0066 208 TRP A CZ3 988 C CH2 . TRP A 126 ? 0.1235 0.1162 0.1158 -0.0005 0.0053 -0.0063 208 TRP A CH2 989 N N . TYR A 127 ? 0.0977 0.0854 0.0714 -0.0011 0.0131 -0.0066 209 TYR A N 990 C CA . TYR A 127 ? 0.0949 0.0811 0.0634 -0.0010 0.0132 -0.0063 209 TYR A CA 991 C C . TYR A 127 ? 0.1111 0.0969 0.0779 -0.0007 0.0113 -0.0070 209 TYR A C 992 O O . TYR A 127 ? 0.0935 0.0793 0.0615 -0.0005 0.0113 -0.0085 209 TYR A O 993 C CB . TYR A 127 ? 0.1125 0.0978 0.0788 -0.0010 0.0156 -0.0067 209 TYR A CB 994 C CG . TYR A 127 ? 0.1059 0.0905 0.0684 -0.0007 0.0150 -0.0058 209 TYR A CG 995 C CD1 . TYR A 127 ? 0.1287 0.1133 0.0907 -0.0008 0.0147 -0.0041 209 TYR A CD1 996 C CD2 . TYR A 127 ? 0.1488 0.1328 0.1084 -0.0004 0.0146 -0.0066 209 TYR A CD2 997 C CE1 . TYR A 127 ? 0.1506 0.1346 0.1094 -0.0006 0.0141 -0.0032 209 TYR A CE1 998 C CE2 . TYR A 127 ? 0.1273 0.1107 0.0834 -0.0002 0.0139 -0.0058 209 TYR A CE2 999 C CZ . TYR A 127 ? 0.1644 0.1477 0.1201 -0.0003 0.0137 -0.0040 209 TYR A CZ 1000 O OH . TYR A 127 ? 0.1393 0.1220 0.0918 -0.0001 0.0130 -0.0032 209 TYR A OH 1001 N N . ASN A 128 ? 0.1153 0.1006 0.0795 -0.0006 0.0097 -0.0062 210 ASN A N 1002 C CA . ASN A 128 ? 0.1669 0.1519 0.1301 -0.0004 0.0076 -0.0068 210 ASN A CA 1003 C C . ASN A 128 ? 0.1459 0.1320 0.1135 -0.0004 0.0065 -0.0074 210 ASN A C 1004 O O . ASN A 128 ? 0.1390 0.1249 0.1069 -0.0003 0.0059 -0.0088 210 ASN A O 1005 C CB . ASN A 128 ? 0.1889 0.1724 0.1480 -0.0001 0.0081 -0.0082 210 ASN A CB 1006 C CG . ASN A 128 ? 0.2554 0.2384 0.2127 0.0001 0.0057 -0.0088 210 ASN A CG 1007 O OD1 . ASN A 128 ? 0.2585 0.2420 0.2164 0.0001 0.0039 -0.0077 210 ASN A OD1 1008 N ND2 . ASN A 128 ? 0.3273 0.3098 0.2833 0.0003 0.0056 -0.0104 210 ASN A ND2 1009 N N . ARG A 129 ? 0.1582 0.1455 0.1293 -0.0006 0.0064 -0.0065 211 ARG A N 1010 C CA . ARG A 129 ? 0.1718 0.1602 0.1469 -0.0006 0.0053 -0.0065 211 ARG A CA 1011 C C . ARG A 129 ? 0.1415 0.1302 0.1193 -0.0005 0.0061 -0.0078 211 ARG A C 1012 O O . ARG A 129 ? 0.1191 0.1083 0.0998 -0.0005 0.0051 -0.0080 211 ARG A O 1013 C CB . ARG A 129 ? 0.1558 0.1441 0.1308 -0.0006 0.0033 -0.0065 211 ARG A CB 1014 C CG . ARG A 129 ? 0.3276 0.3156 0.3000 -0.0006 0.0024 -0.0054 211 ARG A CG 1015 C CD . ARG A 129 ? 0.4216 0.4101 0.3957 -0.0006 0.0005 -0.0049 211 ARG A CD 1016 N NE . ARG A 129 ? 0.5711 0.5602 0.5460 -0.0007 0.0005 -0.0034 211 ARG A NE 1017 C CZ . ARG A 129 ? 0.4865 0.4765 0.4639 -0.0009 0.0010 -0.0028 211 ARG A CZ 1018 N NH1 . ARG A 129 ? 0.5328 0.5232 0.5125 -0.0009 0.0015 -0.0034 211 ARG A NH1 1019 N NH2 . ARG A 129 ? 0.4937 0.4841 0.4714 -0.0010 0.0010 -0.0016 211 ARG A NH2 1020 N N . ARG A 130 ? 0.0915 0.0798 0.0686 -0.0005 0.0081 -0.0085 212 ARG A N 1021 C CA . ARG A 130 ? 0.0823 0.0710 0.0624 -0.0004 0.0091 -0.0098 212 ARG A CA 1022 C C . ARG A 130 ? 0.0904 0.0797 0.0724 -0.0005 0.0109 -0.0095 212 ARG A C 1023 O O . ARG A 130 ? 0.0968 0.0857 0.0764 -0.0007 0.0121 -0.0089 212 ARG A O 1024 C CB . ARG A 130 ? 0.0916 0.0791 0.0692 -0.0002 0.0100 -0.0115 212 ARG A CB 1025 C CG . ARG A 130 ? 0.1123 0.0990 0.0881 -0.0001 0.0082 -0.0121 212 ARG A CG 1026 C CD . ARG A 130 ? 0.1328 0.1182 0.1061 0.0001 0.0091 -0.0141 212 ARG A CD 1027 N NE . ARG A 130 ? 0.1279 0.1128 0.1004 0.0002 0.0072 -0.0151 212 ARG A NE 1028 C CZ . ARG A 130 ? 0.2445 0.2284 0.2127 0.0003 0.0061 -0.0152 212 ARG A CZ 1029 N NH1 . ARG A 130 ? 0.2891 0.2724 0.2531 0.0003 0.0068 -0.0143 212 ARG A NH1 1030 N NH2 . ARG A 130 ? 0.1776 0.1611 0.1458 0.0003 0.0042 -0.0162 212 ARG A NH2 1031 N N . PRO A 131 ? 0.1091 0.0995 0.0956 -0.0004 0.0110 -0.0098 213 PRO A N 1032 C CA . PRO A 131 ? 0.1053 0.0964 0.0942 -0.0006 0.0127 -0.0098 213 PRO A CA 1033 C C . PRO A 131 ? 0.1111 0.1014 0.0986 -0.0005 0.0152 -0.0110 213 PRO A C 1034 O O . PRO A 131 ? 0.1471 0.1368 0.1343 -0.0003 0.0155 -0.0124 213 PRO A O 1035 C CB . PRO A 131 ? 0.1317 0.1240 0.1257 -0.0004 0.0118 -0.0100 213 PRO A CB 1036 C CG . PRO A 131 ? 0.1405 0.1322 0.1345 -0.0001 0.0106 -0.0107 213 PRO A CG 1037 C CD . PRO A 131 ? 0.1128 0.1036 0.1026 -0.0002 0.0096 -0.0102 213 PRO A CD 1038 N N . VAL A 132 ? 0.0753 0.0655 0.0619 -0.0008 0.0170 -0.0106 214 VAL A N 1039 C CA . VAL A 132 ? 0.1134 0.1026 0.0980 -0.0008 0.0197 -0.0115 214 VAL A CA 1040 C C . VAL A 132 ? 0.1396 0.1297 0.1282 -0.0010 0.0218 -0.0118 214 VAL A C 1041 O O . VAL A 132 ? 0.1612 0.1512 0.1510 -0.0008 0.0239 -0.0131 214 VAL A O 1042 C CB . VAL A 132 ? 0.1437 0.1314 0.1224 -0.0009 0.0203 -0.0107 214 VAL A CB 1043 C CG1 . VAL A 132 ? 0.2106 0.1975 0.1876 -0.0010 0.0230 -0.0112 214 VAL A CG1 1044 C CG2 . VAL A 132 ? 0.1478 0.1345 0.1227 -0.0007 0.0184 -0.0109 214 VAL A CG2 1045 N N . ALA A 133 ? 0.0984 0.0896 0.0894 -0.0013 0.0214 -0.0106 215 ALA A N 1046 C CA . ALA A 133 ? 0.1019 0.0940 0.0971 -0.0016 0.0233 -0.0108 215 ALA A CA 1047 C C . ALA A 133 ? 0.1066 0.1005 0.1064 -0.0017 0.0214 -0.0102 215 ALA A C 1048 O O . ALA A 133 ? 0.0946 0.0886 0.0932 -0.0017 0.0192 -0.0092 215 ALA A O 1049 C CB . ALA A 133 ? 0.1096 0.1008 0.1022 -0.0020 0.0257 -0.0102 215 ALA A CB 1050 N N . GLU A 134 ? 0.0835 0.0786 0.0886 -0.0017 0.0223 -0.0107 216 GLU A N 1051 C CA . GLU A 134 ? 0.0916 0.0884 0.1011 -0.0018 0.0204 -0.0103 216 GLU A CA 1052 C C . GLU A 134 ? 0.1199 0.1175 0.1330 -0.0023 0.0221 -0.0104 216 GLU A C 1053 O O . GLU A 134 ? 0.1491 0.1465 0.1636 -0.0024 0.0248 -0.0112 216 GLU A O 1054 C CB . GLU A 134 ? 0.0858 0.0835 0.0992 -0.0013 0.0188 -0.0109 216 GLU A CB 1055 C CG . GLU A 134 ? 0.1388 0.1356 0.1494 -0.0009 0.0174 -0.0111 216 GLU A CG 1056 C CD . GLU A 134 ? 0.1416 0.1372 0.1501 -0.0007 0.0195 -0.0123 216 GLU A CD 1057 O OE1 . GLU A 134 ? 0.1659 0.1619 0.1776 -0.0006 0.0214 -0.0135 216 GLU A OE1 1058 O OE2 . GLU A 134 ? 0.1291 0.1234 0.1327 -0.0007 0.0192 -0.0122 216 GLU A OE2 1059 N N . ILE A 135 ? 0.0733 0.0718 0.0882 -0.0026 0.0206 -0.0096 217 ILE A N 1060 C CA . ILE A 135 ? 0.0733 0.0727 0.0922 -0.0031 0.0220 -0.0098 217 ILE A CA 1061 C C . ILE A 135 ? 0.1345 0.1358 0.1584 -0.0030 0.0196 -0.0099 217 ILE A C 1062 O O . ILE A 135 ? 0.1036 0.1050 0.1260 -0.0030 0.0171 -0.0091 217 ILE A O 1063 C CB . ILE A 135 ? 0.0972 0.0956 0.1128 -0.0037 0.0229 -0.0087 217 ILE A CB 1064 C CG1 . ILE A 135 ? 0.1184 0.1149 0.1284 -0.0036 0.0249 -0.0084 217 ILE A CG1 1065 C CG2 . ILE A 135 ? 0.0982 0.0975 0.1185 -0.0043 0.0244 -0.0090 217 ILE A CG2 1066 C CD1 . ILE A 135 ? 0.1546 0.1498 0.1605 -0.0040 0.0249 -0.0071 217 ILE A CD1 1067 N N . ASN A 136 ? 0.0951 0.0977 0.1248 -0.0030 0.0202 -0.0108 218 ASN A N 1068 C CA . ASN A 136 ? 0.0947 0.0991 0.1294 -0.0029 0.0178 -0.0110 218 ASN A CA 1069 C C . ASN A 136 ? 0.0898 0.0948 0.1263 -0.0036 0.0177 -0.0108 218 ASN A C 1070 O O . ASN A 136 ? 0.1083 0.1127 0.1446 -0.0041 0.0203 -0.0108 218 ASN A O 1071 C CB . ASN A 136 ? 0.0850 0.0906 0.1258 -0.0025 0.0183 -0.0121 218 ASN A CB 1072 C CG . ASN A 136 ? 0.1094 0.1166 0.1542 -0.0021 0.0150 -0.0121 218 ASN A CG 1073 O OD1 . ASN A 136 ? 0.1127 0.1195 0.1545 -0.0018 0.0124 -0.0113 218 ASN A OD1 1074 N ND2 . ASN A 136 ? 0.1161 0.1250 0.1676 -0.0021 0.0150 -0.0130 218 ASN A ND2 1075 N N . THR A 137 ? 0.0678 0.0738 0.1061 -0.0035 0.0148 -0.0106 219 THR A N 1076 C CA . THR A 137 ? 0.0713 0.0781 0.1121 -0.0042 0.0143 -0.0107 219 THR A CA 1077 C C . THR A 137 ? 0.1195 0.1272 0.1662 -0.0046 0.0166 -0.0117 219 THR A C 1078 O O . THR A 137 ? 0.0837 0.0925 0.1347 -0.0042 0.0172 -0.0125 219 THR A O 1079 C CB . THR A 137 ? 0.0591 0.0672 0.1017 -0.0039 0.0106 -0.0107 219 THR A CB 1080 O OG1 . THR A 137 ? 0.0691 0.0779 0.1143 -0.0045 0.0101 -0.0111 219 THR A OG1 1081 C CG2 . THR A 137 ? 0.1004 0.1098 0.1478 -0.0032 0.0092 -0.0114 219 THR A CG2 1082 N N . TRP A 138 ? 0.0789 0.0864 0.1261 -0.0054 0.0182 -0.0116 220 TRP A N 1083 C CA . TRP A 138 ? 0.1411 0.1494 0.1940 -0.0059 0.0207 -0.0124 220 TRP A CA 1084 C C . TRP A 138 ? 0.1503 0.1603 0.2089 -0.0064 0.0190 -0.0131 220 TRP A C 1085 O O . TRP A 138 ? 0.1278 0.1386 0.1921 -0.0067 0.0203 -0.0139 220 TRP A O 1086 C CB . TRP A 138 ? 0.0926 0.0992 0.1427 -0.0064 0.0244 -0.0119 220 TRP A CB 1087 C CG . TRP A 138 ? 0.0923 0.0974 0.1375 -0.0069 0.0242 -0.0108 220 TRP A CG 1088 C CD1 . TRP A 138 ? 0.1069 0.1123 0.1543 -0.0076 0.0241 -0.0108 220 TRP A CD1 1089 C CD2 . TRP A 138 ? 0.0825 0.0858 0.1204 -0.0066 0.0241 -0.0097 220 TRP A CD2 1090 N NE1 . TRP A 138 ? 0.1103 0.1140 0.1520 -0.0078 0.0240 -0.0097 220 TRP A NE1 1091 C CE2 . TRP A 138 ? 0.0984 0.1008 0.1343 -0.0072 0.0240 -0.0090 220 TRP A CE2 1092 C CE3 . TRP A 138 ? 0.1017 0.1040 0.1347 -0.0060 0.0241 -0.0093 220 TRP A CE3 1093 C CZ2 . TRP A 138 ? 0.1036 0.1042 0.1330 -0.0070 0.0238 -0.0078 220 TRP A CZ2 1094 C CZ3 . TRP A 138 ? 0.1027 0.1033 0.1292 -0.0059 0.0238 -0.0082 220 TRP A CZ3 1095 C CH2 . TRP A 138 ? 0.0785 0.0783 0.1033 -0.0064 0.0237 -0.0074 220 TRP A CH2 1096 N N . ALA A 139 ? 0.0776 0.0876 0.1340 -0.0064 0.0159 -0.0128 221 ALA A N 1097 C CA . ALA A 139 ? 0.0936 0.1050 0.1546 -0.0068 0.0138 -0.0136 221 ALA A CA 1098 C C . ALA A 139 ? 0.1046 0.1170 0.1656 -0.0062 0.0096 -0.0137 221 ALA A C 1099 O O . ALA A 139 ? 0.0927 0.1063 0.1570 -0.0064 0.0074 -0.0145 221 ALA A O 1100 C CB . ALA A 139 ? 0.0924 0.1027 0.1509 -0.0076 0.0145 -0.0132 221 ALA A CB 1101 N N . ARG A 140 ? 0.0785 0.0904 0.1357 -0.0054 0.0086 -0.0130 222 ARG A N 1102 C CA . ARG A 140 ? 0.0692 0.0818 0.1261 -0.0047 0.0049 -0.0129 222 ARG A CA 1103 C C . ARG A 140 ? 0.0953 0.1078 0.1495 -0.0049 0.0023 -0.0128 222 ARG A C 1104 O O . ARG A 140 ? 0.0916 0.1053 0.1480 -0.0047 -0.0008 -0.0133 222 ARG A O 1105 C CB . ARG A 140 ? 0.0958 0.1104 0.1599 -0.0043 0.0037 -0.0139 222 ARG A CB 1106 C CG . ARG A 140 ? 0.1618 0.1765 0.2281 -0.0039 0.0060 -0.0141 222 ARG A CG 1107 C CD . ARG A 140 ? 0.3496 0.3662 0.4244 -0.0040 0.0067 -0.0153 222 ARG A CD 1108 N NE . ARG A 140 ? 0.7109 0.7268 0.7868 -0.0044 0.0110 -0.0156 222 ARG A NE 1109 C CZ . ARG A 140 ? 0.4940 0.5091 0.5704 -0.0052 0.0130 -0.0159 222 ARG A CZ 1110 N NH1 . ARG A 140 ? 0.3096 0.3252 0.3871 -0.0056 0.0112 -0.0161 222 ARG A NH1 1111 N NH2 . ARG A 140 ? 0.5519 0.5656 0.6277 -0.0054 0.0167 -0.0158 222 ARG A NH2 1112 N N . ASN A 141 ? 0.0851 0.0961 0.1345 -0.0054 0.0035 -0.0122 223 ASN A N 1113 C CA . ASN A 141 ? 0.0748 0.0855 0.1214 -0.0056 0.0014 -0.0122 223 ASN A CA 1114 C C . ASN A 141 ? 0.0930 0.1017 0.1328 -0.0057 0.0024 -0.0111 223 ASN A C 1115 O O . ASN A 141 ? 0.0807 0.0885 0.1194 -0.0063 0.0040 -0.0111 223 ASN A O 1116 C CB . ASN A 141 ? 0.0918 0.1032 0.1428 -0.0065 0.0016 -0.0133 223 ASN A CB 1117 C CG . ASN A 141 ? 0.1205 0.1318 0.1694 -0.0067 -0.0010 -0.0137 223 ASN A CG 1118 O OD1 . ASN A 141 ? 0.0936 0.1041 0.1373 -0.0062 -0.0026 -0.0130 223 ASN A OD1 1119 N ND2 . ASN A 141 ? 0.1471 0.1591 0.2001 -0.0074 -0.0013 -0.0149 223 ASN A ND2 1120 N N . ILE A 142 ? 0.0801 0.0882 0.1157 -0.0050 0.0014 -0.0102 224 ILE A N 1121 C CA . ILE A 142 ? 0.0786 0.0851 0.1081 -0.0049 0.0019 -0.0091 224 ILE A CA 1122 C C . ILE A 142 ? 0.0638 0.0690 0.0916 -0.0053 0.0051 -0.0087 224 ILE A C 1123 O O . ILE A 142 ? 0.0743 0.0786 0.1003 -0.0058 0.0061 -0.0085 224 ILE A O 1124 C CB . ILE A 142 ? 0.0764 0.0825 0.1034 -0.0052 0.0002 -0.0092 224 ILE A CB 1125 C CG1 . ILE A 142 ? 0.0716 0.0789 0.1003 -0.0049 -0.0029 -0.0098 224 ILE A CG1 1126 C CG2 . ILE A 142 ? 0.0751 0.0798 0.0961 -0.0049 0.0003 -0.0081 224 ILE A CG2 1127 C CD1 . ILE A 142 ? 0.1268 0.1338 0.1527 -0.0051 -0.0047 -0.0101 224 ILE A CD1 1128 N N . LEU A 143 ? 0.0796 0.0847 0.1079 -0.0050 0.0067 -0.0085 225 LEU A N 1129 C CA . LEU A 143 ? 0.0738 0.0776 0.0994 -0.0052 0.0094 -0.0079 225 LEU A CA 1130 C C . LEU A 143 ? 0.0865 0.0889 0.1064 -0.0051 0.0089 -0.0069 225 LEU A C 1131 O O . LEU A 143 ? 0.0737 0.0760 0.0912 -0.0046 0.0070 -0.0066 225 LEU A O 1132 C CB . LEU A 143 ? 0.0724 0.0762 0.0982 -0.0047 0.0106 -0.0080 225 LEU A CB 1133 C CG . LEU A 143 ? 0.0653 0.0675 0.0875 -0.0047 0.0131 -0.0074 225 LEU A CG 1134 C CD1 . LEU A 143 ? 0.0822 0.0839 0.1059 -0.0054 0.0158 -0.0076 225 LEU A CD1 1135 C CD2 . LEU A 143 ? 0.0771 0.0793 0.0995 -0.0042 0.0138 -0.0078 225 LEU A CD2 1136 N N . ARG A 144 ? 0.0616 0.0628 0.0795 -0.0055 0.0106 -0.0065 226 ARG A N 1137 C CA . ARG A 144 ? 0.0954 0.0954 0.1086 -0.0054 0.0100 -0.0056 226 ARG A CA 1138 C C . ARG A 144 ? 0.0800 0.0785 0.0908 -0.0057 0.0123 -0.0049 226 ARG A C 1139 O O . ARG A 144 ? 0.0811 0.0793 0.0938 -0.0061 0.0144 -0.0050 226 ARG A O 1140 C CB . ARG A 144 ? 0.0712 0.0717 0.0852 -0.0057 0.0083 -0.0060 226 ARG A CB 1141 C CG . ARG A 144 ? 0.0803 0.0811 0.0981 -0.0064 0.0090 -0.0068 226 ARG A CG 1142 C CD . ARG A 144 ? 0.0678 0.0696 0.0872 -0.0065 0.0066 -0.0077 226 ARG A CD 1143 N NE . ARG A 144 ? 0.0824 0.0844 0.1054 -0.0072 0.0071 -0.0086 226 ARG A NE 1144 C CZ . ARG A 144 ? 0.1525 0.1558 0.1808 -0.0076 0.0072 -0.0096 226 ARG A CZ 1145 N NH1 . ARG A 144 ? 0.0902 0.0946 0.1208 -0.0072 0.0069 -0.0098 226 ARG A NH1 1146 N NH2 . ARG A 144 ? 0.0778 0.0812 0.1094 -0.0083 0.0077 -0.0104 226 ARG A NH2 1147 N N . THR A 145 ? 0.0799 0.0772 0.0863 -0.0054 0.0119 -0.0040 227 THR A N 1148 C CA . THR A 145 ? 0.0666 0.0624 0.0701 -0.0055 0.0138 -0.0031 227 THR A CA 1149 C C . THR A 145 ? 0.0570 0.0518 0.0578 -0.0055 0.0132 -0.0023 227 THR A C 1150 O O . THR A 145 ? 0.0891 0.0844 0.0911 -0.0057 0.0120 -0.0027 227 THR A O 1151 C CB . THR A 145 ? 0.0975 0.0927 0.0985 -0.0051 0.0146 -0.0028 227 THR A CB 1152 O OG1 . THR A 145 ? 0.0910 0.0847 0.0893 -0.0051 0.0165 -0.0019 227 THR A OG1 1153 C CG2 . THR A 145 ? 0.0732 0.0685 0.0715 -0.0045 0.0127 -0.0025 227 THR A CG2 1154 N N . GLN A 146 ? 0.0598 0.0532 0.0570 -0.0053 0.0140 -0.0013 228 GLN A N 1155 C CA . GLN A 146 ? 0.0668 0.0591 0.0623 -0.0054 0.0141 -0.0005 228 GLN A CA 1156 C C . GLN A 146 ? 0.0651 0.0576 0.0594 -0.0051 0.0122 -0.0005 228 GLN A C 1157 O O . GLN A 146 ? 0.0852 0.0774 0.0801 -0.0054 0.0121 -0.0005 228 GLN A O 1158 C CB . GLN A 146 ? 0.0664 0.0571 0.0585 -0.0052 0.0155 0.0006 228 GLN A CB 1159 C CG . GLN A 146 ? 0.0760 0.0662 0.0690 -0.0055 0.0178 0.0007 228 GLN A CG 1160 C CD . GLN A 146 ? 0.1205 0.1089 0.1097 -0.0052 0.0192 0.0019 228 GLN A CD 1161 O OE1 . GLN A 146 ? 0.1535 0.1412 0.1427 -0.0054 0.0213 0.0021 228 GLN A OE1 1162 N NE2 . GLN A 146 ? 0.1089 0.0965 0.0949 -0.0048 0.0181 0.0028 228 GLN A NE2 1163 N N . GLU A 147 ? 0.0750 0.0680 0.0678 -0.0047 0.0109 -0.0005 229 GLU A N 1164 C CA . GLU A 147 ? 0.0516 0.0447 0.0428 -0.0044 0.0094 -0.0002 229 GLU A CA 1165 C C . GLU A 147 ? 0.0602 0.0520 0.0489 -0.0042 0.0097 0.0008 229 GLU A C 1166 O O . GLU A 147 ? 0.0686 0.0604 0.0566 -0.0041 0.0089 0.0010 229 GLU A O 1167 C CB . GLU A 147 ? 0.0763 0.0702 0.0692 -0.0046 0.0083 -0.0009 229 GLU A CB 1168 C CG . GLU A 147 ? 0.0904 0.0855 0.0865 -0.0049 0.0080 -0.0020 229 GLU A CG 1169 C CD . GLU A 147 ? 0.1294 0.1253 0.1258 -0.0046 0.0071 -0.0022 229 GLU A CD 1170 O OE1 . GLU A 147 ? 0.0907 0.0864 0.0850 -0.0042 0.0068 -0.0016 229 GLU A OE1 1171 O OE2 . GLU A 147 ? 0.1120 0.1089 0.1112 -0.0047 0.0067 -0.0030 229 GLU A OE2 1172 N N . SER A 148 ? 0.0726 0.0634 0.0600 -0.0042 0.0110 0.0015 230 SER A N 1173 C CA . SER A 148 ? 0.0621 0.0517 0.0468 -0.0038 0.0110 0.0025 230 SER A CA 1174 C C . SER A 148 ? 0.0909 0.0797 0.0735 -0.0036 0.0119 0.0030 230 SER A C 1175 O O . SER A 148 ? 0.0989 0.0881 0.0824 -0.0038 0.0128 0.0024 230 SER A O 1176 C CB . SER A 148 ? 0.0868 0.0755 0.0719 -0.0040 0.0116 0.0031 230 SER A CB 1177 O OG . SER A 148 ? 0.1102 0.0982 0.0965 -0.0044 0.0132 0.0032 230 SER A OG 1178 N N . GLU A 149 ? 0.0684 0.0560 0.0483 -0.0033 0.0118 0.0040 231 GLU A N 1179 C CA . GLU A 149 ? 0.0989 0.0857 0.0760 -0.0030 0.0123 0.0043 231 GLU A CA 1180 C C . GLU A 149 ? 0.1288 0.1149 0.1060 -0.0033 0.0143 0.0045 231 GLU A C 1181 O O . GLU A 149 ? 0.1063 0.0919 0.0850 -0.0036 0.0153 0.0049 231 GLU A O 1182 C CB . GLU A 149 ? 0.0635 0.0496 0.0382 -0.0024 0.0111 0.0052 231 GLU A CB 1183 C CG . GLU A 149 ? 0.1023 0.0873 0.0765 -0.0023 0.0116 0.0063 231 GLU A CG 1184 C CD . GLU A 149 ? 0.1211 0.1057 0.0930 -0.0017 0.0103 0.0071 231 GLU A CD 1185 O OE1 . GLU A 149 ? 0.1003 0.0854 0.0712 -0.0014 0.0090 0.0067 231 GLU A OE1 1186 O OE2 . GLU A 149 ? 0.1093 0.0929 0.0803 -0.0015 0.0106 0.0081 231 GLU A OE2 1187 N N . CYS A 150 ? 0.0964 0.0825 0.0726 -0.0031 0.0148 0.0040 232 CYS A N 1188 C CA . CYS A 150 ? 0.1225 0.1080 0.0984 -0.0032 0.0164 0.0043 232 CYS A CA 1189 C C . CYS A 150 ? 0.1167 0.1012 0.0895 -0.0027 0.0158 0.0053 232 CYS A C 1190 O O . CYS A 150 ? 0.1055 0.0899 0.0770 -0.0023 0.0142 0.0058 232 CYS A O 1191 C CB . CYS A 150 ? 0.1298 0.1157 0.1061 -0.0033 0.0175 0.0032 232 CYS A CB 1192 S SG . CYS A 150 ? 0.1311 0.1176 0.1057 -0.0029 0.0160 0.0023 232 CYS A SG 1193 N N . VAL A 151 ? 0.1238 0.1075 0.0957 -0.0027 0.0172 0.0057 233 VAL A N 1194 C CA . VAL A 151 ? 0.0896 0.0722 0.0584 -0.0023 0.0168 0.0068 233 VAL A CA 1195 C C . VAL A 151 ? 0.1163 0.0985 0.0830 -0.0022 0.0179 0.0065 233 VAL A C 1196 O O . VAL A 151 ? 0.1396 0.1219 0.1077 -0.0025 0.0196 0.0059 233 VAL A O 1197 C CB . VAL A 151 ? 0.1423 0.1240 0.1117 -0.0024 0.0175 0.0081 233 VAL A CB 1198 C CG1 . VAL A 151 ? 0.1708 0.1514 0.1370 -0.0019 0.0168 0.0093 233 VAL A CG1 1199 C CG2 . VAL A 151 ? 0.1896 0.1717 0.1615 -0.0026 0.0167 0.0082 233 VAL A CG2 1200 N N . CYS A 152 ? 0.1044 0.0861 0.0676 -0.0017 0.0169 0.0069 234 CYS A N 1201 C CA . CYS A 152 ? 0.1171 0.0983 0.0778 -0.0016 0.0179 0.0065 234 CYS A CA 1202 C C . CYS A 152 ? 0.1489 0.1287 0.1064 -0.0013 0.0182 0.0078 234 CYS A C 1203 O O . CYS A 152 ? 0.1367 0.1162 0.0931 -0.0011 0.0168 0.0089 234 CYS A O 1204 C CB . CYS A 152 ? 0.1445 0.1262 0.1036 -0.0013 0.0165 0.0054 234 CYS A CB 1205 S SG . CYS A 152 ? 0.1341 0.1172 0.0964 -0.0015 0.0160 0.0040 234 CYS A SG 1206 N N . HIS A 153 ? 0.1392 0.1184 0.0953 -0.0014 0.0200 0.0077 235 HIS A N 1207 C CA . HIS A 153 ? 0.1639 0.1418 0.1162 -0.0012 0.0204 0.0089 235 HIS A CA 1208 C C . HIS A 153 ? 0.1518 0.1293 0.1011 -0.0010 0.0213 0.0080 235 HIS A C 1209 O O . HIS A 153 ? 0.1488 0.1264 0.0995 -0.0013 0.0233 0.0072 235 HIS A O 1210 C CB . HIS A 153 ? 0.1291 0.1061 0.0826 -0.0015 0.0222 0.0101 235 HIS A CB 1211 C CG . HIS A 153 ? 0.1775 0.1530 0.1270 -0.0013 0.0229 0.0114 235 HIS A CG 1212 N ND1 . HIS A 153 ? 0.2094 0.1841 0.1565 -0.0009 0.0213 0.0128 235 HIS A ND1 1213 C CD2 . HIS A 153 ? 0.2070 0.1815 0.1543 -0.0014 0.0249 0.0115 235 HIS A CD2 1214 C CE1 . HIS A 153 ? 0.2433 0.2167 0.1868 -0.0008 0.0223 0.0138 235 HIS A CE1 1215 N NE2 . HIS A 153 ? 0.1987 0.1720 0.1423 -0.0010 0.0245 0.0130 235 HIS A NE2 1216 N N . ASN A 154 ? 0.1361 0.1133 0.0816 -0.0006 0.0198 0.0081 236 ASN A N 1217 C CA . ASN A 154 ? 0.1689 0.1458 0.1112 -0.0004 0.0204 0.0072 236 ASN A CA 1218 C C . ASN A 154 ? 0.1649 0.1427 0.1094 -0.0006 0.0212 0.0053 236 ASN A C 1219 O O . ASN A 154 ? 0.1621 0.1396 0.1060 -0.0007 0.0231 0.0045 236 ASN A O 1220 C CB . ASN A 154 ? 0.1775 0.1530 0.1173 -0.0005 0.0227 0.0081 236 ASN A CB 1221 C CG . ASN A 154 ? 0.2506 0.2255 0.1860 -0.0002 0.0230 0.0073 236 ASN A CG 1222 O OD1 . ASN A 154 ? 0.2210 0.1962 0.1541 0.0002 0.0210 0.0066 236 ASN A OD1 1223 N ND2 . ASN A 154 ? 0.2947 0.2687 0.2289 -0.0004 0.0256 0.0074 236 ASN A ND2 1224 N N . GLY A 155 ? 0.1528 0.1317 0.1001 -0.0006 0.0197 0.0046 237 GLY A N 1225 C CA . GLY A 155 ? 0.1746 0.1544 0.1240 -0.0007 0.0201 0.0029 237 GLY A CA 1226 C C . GLY A 155 ? 0.1890 0.1694 0.1428 -0.0012 0.0218 0.0026 237 GLY A C 1227 O O . GLY A 155 ? 0.1563 0.1376 0.1126 -0.0013 0.0219 0.0013 237 GLY A O 1228 N N . VAL A 156 ? 0.1301 0.1100 0.0851 -0.0015 0.0233 0.0037 238 VAL A N 1229 C CA . VAL A 156 ? 0.1166 0.0971 0.0760 -0.0020 0.0249 0.0034 238 VAL A CA 1230 C C . VAL A 156 ? 0.1466 0.1278 0.1089 -0.0022 0.0237 0.0039 238 VAL A C 1231 O O . VAL A 156 ? 0.1206 0.1012 0.0821 -0.0021 0.0229 0.0052 238 VAL A O 1232 C CB . VAL A 156 ? 0.1638 0.1434 0.1234 -0.0023 0.0274 0.0042 238 VAL A CB 1233 C CG1 . VAL A 156 ? 0.1320 0.1122 0.0967 -0.0028 0.0289 0.0037 238 VAL A CG1 1234 C CG2 . VAL A 156 ? 0.1869 0.1657 0.1436 -0.0021 0.0289 0.0037 238 VAL A CG2 1235 N N . CYS A 157 ? 0.1232 0.1055 0.0888 -0.0024 0.0235 0.0028 239 CYS A N 1236 C CA . CYS A 157 ? 0.1320 0.1150 0.1001 -0.0026 0.0223 0.0031 239 CYS A CA 1237 C C . CYS A 157 ? 0.1031 0.0869 0.0758 -0.0032 0.0238 0.0026 239 CYS A C 1238 O O . CYS A 157 ? 0.1134 0.0981 0.0884 -0.0033 0.0242 0.0014 239 CYS A O 1239 C CB . CYS A 157 ? 0.1261 0.1100 0.0941 -0.0024 0.0203 0.0023 239 CYS A CB 1240 S SG . CYS A 157 ? 0.1343 0.1176 0.0976 -0.0017 0.0184 0.0024 239 CYS A SG 1241 N N . PRO A 158 ? 0.1155 0.0989 0.0898 -0.0035 0.0246 0.0035 240 PRO A N 1242 C CA . PRO A 158 ? 0.1088 0.0929 0.0877 -0.0041 0.0260 0.0030 240 PRO A CA 1243 C C . PRO A 158 ? 0.1111 0.0963 0.0925 -0.0043 0.0246 0.0025 240 PRO A C 1244 O O . PRO A 158 ? 0.0988 0.0839 0.0786 -0.0041 0.0229 0.0031 240 PRO A O 1245 C CB . PRO A 158 ? 0.1173 0.1004 0.0967 -0.0043 0.0271 0.0041 240 PRO A CB 1246 C CG . PRO A 158 ? 0.1554 0.1371 0.1301 -0.0038 0.0268 0.0053 240 PRO A CG 1247 C CD . PRO A 158 ? 0.1205 0.1026 0.0924 -0.0034 0.0246 0.0050 240 PRO A CD 1248 N N . VAL A 159 ? 0.0865 0.0731 0.0721 -0.0048 0.0253 0.0014 241 VAL A N 1249 C CA . VAL A 159 ? 0.1087 0.0965 0.0970 -0.0051 0.0243 0.0009 241 VAL A CA 1250 C C . VAL A 159 ? 0.1223 0.1111 0.1159 -0.0058 0.0255 0.0002 241 VAL A C 1251 O O . VAL A 159 ? 0.1169 0.1062 0.1130 -0.0059 0.0270 -0.0005 241 VAL A O 1252 C CB . VAL A 159 ? 0.0914 0.0802 0.0795 -0.0048 0.0233 -0.0002 241 VAL A CB 1253 C CG1 . VAL A 159 ? 0.0717 0.0621 0.0631 -0.0049 0.0210 -0.0007 241 VAL A CG1 1254 C CG2 . VAL A 159 ? 0.0830 0.0709 0.0662 -0.0042 0.0219 0.0003 241 VAL A CG2 1255 N N . VAL A 160 ? 0.0627 0.0520 0.0584 -0.0062 0.0247 0.0003 242 VAL A N 1256 C CA . VAL A 160 ? 0.0891 0.0796 0.0903 -0.0068 0.0250 -0.0005 242 VAL A CA 1257 C C . VAL A 160 ? 0.1035 0.0961 0.1078 -0.0066 0.0227 -0.0018 242 VAL A C 1258 O O . VAL A 160 ? 0.1000 0.0929 0.1027 -0.0063 0.0204 -0.0018 242 VAL A O 1259 C CB . VAL A 160 ? 0.0654 0.0552 0.0675 -0.0072 0.0251 0.0001 242 VAL A CB 1260 C CG1 . VAL A 160 ? 0.0816 0.0726 0.0898 -0.0079 0.0256 -0.0009 242 VAL A CG1 1261 C CG2 . VAL A 160 ? 0.1073 0.0950 0.1061 -0.0069 0.0262 0.0016 242 VAL A CG2 1262 N N . PHE A 161 ? 0.0832 0.0771 0.0920 -0.0069 0.0234 -0.0029 243 PHE A N 1263 C CA . PHE A 161 ? 0.0753 0.0711 0.0875 -0.0068 0.0212 -0.0041 243 PHE A CA 1264 C C . PHE A 161 ? 0.1115 0.1085 0.1293 -0.0074 0.0212 -0.0049 243 PHE A C 1265 O O . PHE A 161 ? 0.1242 0.1208 0.1443 -0.0079 0.0235 -0.0048 243 PHE A O 1266 C CB . PHE A 161 ? 0.0808 0.0774 0.0943 -0.0064 0.0217 -0.0048 243 PHE A CB 1267 C CG . PHE A 161 ? 0.1044 0.1002 0.1132 -0.0058 0.0213 -0.0044 243 PHE A CG 1268 C CD1 . PHE A 161 ? 0.1000 0.0942 0.1050 -0.0057 0.0234 -0.0037 243 PHE A CD1 1269 C CD2 . PHE A 161 ? 0.0890 0.0856 0.0973 -0.0052 0.0188 -0.0047 243 PHE A CD2 1270 C CE1 . PHE A 161 ? 0.1142 0.1077 0.1152 -0.0051 0.0229 -0.0036 243 PHE A CE1 1271 C CE2 . PHE A 161 ? 0.0897 0.0856 0.0942 -0.0047 0.0185 -0.0044 243 PHE A CE2 1272 C CZ . PHE A 161 ? 0.1350 0.1293 0.1358 -0.0046 0.0204 -0.0040 243 PHE A CZ 1273 N N . THR A 162 ? 0.0614 0.0598 0.0815 -0.0073 0.0186 -0.0057 244 THR A N 1274 C CA . THR A 162 ? 0.0658 0.0656 0.0916 -0.0078 0.0181 -0.0069 244 THR A CA 1275 C C . THR A 162 ? 0.1095 0.1112 0.1381 -0.0074 0.0159 -0.0078 244 THR A C 1276 O O . THR A 162 ? 0.0672 0.0690 0.0929 -0.0068 0.0138 -0.0076 244 THR A O 1277 C CB . THR A 162 ? 0.0920 0.0915 0.1178 -0.0083 0.0169 -0.0069 244 THR A CB 1278 O OG1 . THR A 162 ? 0.1027 0.1004 0.1264 -0.0086 0.0190 -0.0059 244 THR A OG1 1279 C CG2 . THR A 162 ? 0.0983 0.0992 0.1301 -0.0088 0.0161 -0.0083 244 THR A CG2 1280 N N . ASP A 163 ? 0.0843 0.0874 0.1187 -0.0077 0.0163 -0.0089 245 ASP A N 1281 C CA . ASP A 163 ? 0.0929 0.0978 0.1308 -0.0073 0.0140 -0.0098 245 ASP A CA 1282 C C . ASP A 163 ? 0.1025 0.1088 0.1465 -0.0080 0.0134 -0.0110 245 ASP A C 1283 O O . ASP A 163 ? 0.1091 0.1153 0.1565 -0.0086 0.0158 -0.0113 245 ASP A O 1284 C CB . ASP A 163 ? 0.0878 0.0931 0.1271 -0.0069 0.0154 -0.0099 245 ASP A CB 1285 C CG . ASP A 163 ? 0.0978 0.1046 0.1392 -0.0062 0.0128 -0.0105 245 ASP A CG 1286 O OD1 . ASP A 163 ? 0.0834 0.0911 0.1260 -0.0062 0.0100 -0.0109 245 ASP A OD1 1287 O OD2 . ASP A 163 ? 0.1193 0.1261 0.1609 -0.0058 0.0137 -0.0105 245 ASP A OD2 1288 N N . GLY A 164 ? 0.0608 0.0681 0.1059 -0.0078 0.0101 -0.0117 246 GLY A N 1289 C CA . GLY A 164 ? 0.0929 0.1016 0.1436 -0.0084 0.0091 -0.0129 246 GLY A CA 1290 C C . GLY A 164 ? 0.1243 0.1326 0.1728 -0.0086 0.0067 -0.0132 246 GLY A C 1291 O O . GLY A 164 ? 0.0928 0.1001 0.1357 -0.0082 0.0056 -0.0125 246 GLY A O 1292 N N . SER A 165 ? 0.1060 0.1152 0.1591 -0.0093 0.0061 -0.0145 247 SER A N 1293 C CA . SER A 165 ? 0.0762 0.0853 0.1279 -0.0095 0.0036 -0.0152 247 SER A CA 1294 C C . SER A 165 ? 0.0849 0.0919 0.1309 -0.0096 0.0045 -0.0143 247 SER A C 1295 O O . SER A 165 ? 0.1060 0.1117 0.1510 -0.0099 0.0074 -0.0134 247 SER A O 1296 C CB . SER A 165 ? 0.1242 0.1343 0.1824 -0.0103 0.0031 -0.0168 247 SER A CB 1297 O OG . SER A 165 ? 0.1468 0.1569 0.2036 -0.0104 0.0004 -0.0178 247 SER A OG 1298 N N . ALA A 166 ? 0.1055 0.1122 0.1479 -0.0093 0.0021 -0.0146 248 ALA A N 1299 C CA . ALA A 166 ? 0.0976 0.1026 0.1356 -0.0095 0.0028 -0.0141 248 ALA A CA 1300 C C . ALA A 166 ? 0.1236 0.1285 0.1645 -0.0103 0.0023 -0.0155 248 ALA A C 1301 O O . ALA A 166 ? 0.1307 0.1342 0.1691 -0.0105 0.0031 -0.0153 248 ALA A O 1302 C CB . ALA A 166 ? 0.1448 0.1493 0.1769 -0.0088 0.0008 -0.0135 248 ALA A CB 1303 N N . THR A 167 ? 0.1280 0.1345 0.1746 -0.0107 0.0011 -0.0170 249 THR A N 1304 C CA . THR A 167 ? 0.1585 0.1651 0.2084 -0.0115 0.0001 -0.0187 249 THR A CA 1305 C C . THR A 167 ? 0.2053 0.2129 0.2625 -0.0122 0.0016 -0.0195 249 THR A C 1306 O O . THR A 167 ? 0.1925 0.2007 0.2527 -0.0122 0.0001 -0.0208 249 THR A O 1307 C CB . THR A 167 ? 0.1450 0.1528 0.1944 -0.0111 -0.0039 -0.0201 249 THR A CB 1308 O OG1 . THR A 167 ? 0.1651 0.1748 0.2179 -0.0107 -0.0054 -0.0204 249 THR A OG1 1309 C CG2 . THR A 167 ? 0.1978 0.2046 0.2398 -0.0104 -0.0051 -0.0193 249 THR A CG2 1310 N N . GLY A 168 ? 0.1166 0.1238 0.1750 -0.0122 0.0046 -0.0183 250 GLY A N 1311 C CA . GLY A 168 ? 0.1165 0.1241 0.1799 -0.0123 0.0066 -0.0183 250 GLY A CA 1312 C C . GLY A 168 ? 0.1487 0.1554 0.2111 -0.0122 0.0101 -0.0167 250 GLY A C 1313 O O . GLY A 168 ? 0.1265 0.1324 0.1845 -0.0123 0.0108 -0.0156 250 GLY A O 1314 N N . PRO A 169 ? 0.1312 0.1380 0.1974 -0.0121 0.0123 -0.0165 251 PRO A N 1315 C CA . PRO A 169 ? 0.1631 0.1688 0.2279 -0.0120 0.0157 -0.0151 251 PRO A CA 1316 C C . PRO A 169 ? 0.1543 0.1609 0.2172 -0.0116 0.0153 -0.0146 251 PRO A C 1317 O O . PRO A 169 ? 0.1546 0.1629 0.2199 -0.0112 0.0130 -0.0155 251 PRO A O 1318 C CB . PRO A 169 ? 0.2080 0.2141 0.2781 -0.0119 0.0173 -0.0156 251 PRO A CB 1319 C CG . PRO A 169 ? 0.1950 0.2016 0.2685 -0.0122 0.0155 -0.0169 251 PRO A CG 1320 C CD . PRO A 169 ? 0.1508 0.1585 0.2226 -0.0122 0.0118 -0.0178 251 PRO A CD 1321 N N . ALA A 170 ? 0.1129 0.1181 0.1712 -0.0115 0.0175 -0.0131 252 ALA A N 1322 C CA . ALA A 170 ? 0.1697 0.1754 0.2256 -0.0111 0.0174 -0.0126 252 ALA A CA 1323 C C . ALA A 170 ? 0.1571 0.1615 0.2112 -0.0108 0.0209 -0.0114 252 ALA A C 1324 O O . ALA A 170 ? 0.1411 0.1440 0.1950 -0.0110 0.0231 -0.0109 252 ALA A O 1325 C CB . ALA A 170 ? 0.0897 0.0944 0.1387 -0.0105 0.0154 -0.0118 252 ALA A CB 1326 N N . ASP A 171 ? 0.0966 0.1014 0.1488 -0.0103 0.0211 -0.0111 253 ASP A N 1327 C CA . ASP A 171 ? 0.0898 0.0933 0.1397 -0.0100 0.0241 -0.0102 253 ASP A CA 1328 C C . ASP A 171 ? 0.1423 0.1441 0.1852 -0.0097 0.0249 -0.0088 253 ASP A C 1329 O O . ASP A 171 ? 0.1122 0.1142 0.1517 -0.0089 0.0233 -0.0087 253 ASP A O 1330 C CB . ASP A 171 ? 0.1214 0.1262 0.1743 -0.0094 0.0241 -0.0110 253 ASP A CB 1331 C CG . ASP A 171 ? 0.2925 0.2987 0.3521 -0.0095 0.0233 -0.0123 253 ASP A CG 1332 O OD1 . ASP A 171 ? 0.2372 0.2427 0.2988 -0.0098 0.0243 -0.0124 253 ASP A OD1 1333 O OD2 . ASP A 171 ? 0.2936 0.3015 0.3566 -0.0091 0.0216 -0.0132 253 ASP A OD2 1334 N N . THR A 172 ? 0.0898 0.0895 0.1294 -0.0099 0.0266 -0.0077 254 THR A N 1335 C CA . THR A 172 ? 0.0694 0.0673 0.1022 -0.0096 0.0272 -0.0063 254 THR A CA 1336 C C . THR A 172 ? 0.1083 0.1046 0.1378 -0.0091 0.0295 -0.0055 254 THR A C 1337 O O . THR A 172 ? 0.1391 0.1347 0.1705 -0.0092 0.0312 -0.0055 254 THR A O 1338 C CB . THR A 172 ? 0.1198 0.1162 0.1506 -0.0099 0.0272 -0.0054 254 THR A CB 1339 O OG1 . THR A 172 ? 0.0909 0.0883 0.1228 -0.0100 0.0242 -0.0062 254 THR A OG1 1340 C CG2 . THR A 172 ? 0.0814 0.0757 0.1053 -0.0094 0.0278 -0.0038 254 THR A CG2 1341 N N . ARG A 173 ? 0.0903 0.0861 0.1150 -0.0085 0.0294 -0.0050 255 ARG A N 1342 C CA . ARG A 173 ? 0.0847 0.0789 0.1056 -0.0080 0.0311 -0.0044 255 ARG A CA 1343 C C . ARG A 173 ? 0.1427 0.1351 0.1567 -0.0076 0.0307 -0.0030 255 ARG A C 1344 O O . ARG A 173 ? 0.1307 0.1235 0.1428 -0.0075 0.0291 -0.0028 255 ARG A O 1345 C CB . ARG A 173 ? 0.0891 0.0846 0.1112 -0.0076 0.0311 -0.0054 255 ARG A CB 1346 C CG . ARG A 173 ? 0.1138 0.1109 0.1427 -0.0078 0.0314 -0.0067 255 ARG A CG 1347 C CD . ARG A 173 ? 0.0824 0.0805 0.1122 -0.0073 0.0315 -0.0076 255 ARG A CD 1348 N NE . ARG A 173 ? 0.1292 0.1289 0.1658 -0.0075 0.0316 -0.0088 255 ARG A NE 1349 C CZ . ARG A 173 ? 0.1279 0.1285 0.1668 -0.0070 0.0317 -0.0098 255 ARG A CZ 1350 N NH1 . ARG A 173 ? 0.1286 0.1286 0.1635 -0.0065 0.0318 -0.0097 255 ARG A NH1 1351 N NH2 . ARG A 173 ? 0.1452 0.1471 0.1905 -0.0071 0.0317 -0.0108 255 ARG A NH2 1352 N N . ILE A 174 ? 0.0994 0.0899 0.1098 -0.0073 0.0322 -0.0020 256 ILE A N 1353 C CA . ILE A 174 ? 0.1337 0.1226 0.1376 -0.0068 0.0316 -0.0009 256 ILE A CA 1354 C C . ILE A 174 ? 0.1660 0.1546 0.1672 -0.0063 0.0322 -0.0012 256 ILE A C 1355 O O . ILE A 174 ? 0.1487 0.1368 0.1505 -0.0063 0.0340 -0.0014 256 ILE A O 1356 C CB . ILE A 174 ? 0.1393 0.1263 0.1408 -0.0068 0.0325 0.0006 256 ILE A CB 1357 C CG1 . ILE A 174 ? 0.1781 0.1652 0.1820 -0.0072 0.0318 0.0009 256 ILE A CG1 1358 C CG2 . ILE A 174 ? 0.1352 0.1208 0.1303 -0.0062 0.0317 0.0017 256 ILE A CG2 1359 C CD1 . ILE A 174 ? 0.2591 0.2469 0.2689 -0.0079 0.0330 0.0001 256 ILE A CD1 1360 N N . TYR A 175 ? 0.1112 0.1001 0.1094 -0.0059 0.0306 -0.0014 257 TYR A N 1361 C CA . TYR A 175 ? 0.1161 0.1047 0.1116 -0.0054 0.0309 -0.0019 257 TYR A CA 1362 C C . TYR A 175 ? 0.1460 0.1329 0.1353 -0.0049 0.0303 -0.0007 257 TYR A C 1363 O O . TYR A 175 ? 0.1503 0.1367 0.1373 -0.0048 0.0289 0.0002 257 TYR A O 1364 C CB . TYR A 175 ? 0.1153 0.1054 0.1120 -0.0052 0.0295 -0.0029 257 TYR A CB 1365 C CG . TYR A 175 ? 0.1144 0.1062 0.1169 -0.0054 0.0303 -0.0043 257 TYR A CG 1366 C CD1 . TYR A 175 ? 0.1341 0.1275 0.1420 -0.0059 0.0300 -0.0047 257 TYR A CD1 1367 C CD2 . TYR A 175 ? 0.1201 0.1121 0.1230 -0.0050 0.0311 -0.0053 257 TYR A CD2 1368 C CE1 . TYR A 175 ? 0.0986 0.0938 0.1124 -0.0060 0.0303 -0.0060 257 TYR A CE1 1369 C CE2 . TYR A 175 ? 0.1324 0.1261 0.1411 -0.0051 0.0316 -0.0066 257 TYR A CE2 1370 C CZ . TYR A 175 ? 0.1303 0.1256 0.1445 -0.0056 0.0311 -0.0069 257 TYR A CZ 1371 O OH . TYR A 175 ? 0.1299 0.1270 0.1503 -0.0056 0.0312 -0.0082 257 TYR A OH 1372 N N . TYR A 176 ? 0.1126 0.0987 0.0994 -0.0046 0.0314 -0.0009 258 TYR A N 1373 C CA . TYR A 176 ? 0.1108 0.0954 0.0918 -0.0041 0.0308 0.0000 258 TYR A CA 1374 C C . TYR A 176 ? 0.1450 0.1298 0.1238 -0.0037 0.0300 -0.0010 258 TYR A C 1375 O O . TYR A 176 ? 0.1521 0.1371 0.1319 -0.0037 0.0314 -0.0021 258 TYR A O 1376 C CB . TYR A 176 ? 0.1469 0.1302 0.1264 -0.0042 0.0328 0.0007 258 TYR A CB 1377 C CG . TYR A 176 ? 0.1248 0.1077 0.1066 -0.0046 0.0337 0.0017 258 TYR A CG 1378 C CD1 . TYR A 176 ? 0.1283 0.1118 0.1153 -0.0052 0.0353 0.0011 258 TYR A CD1 1379 C CD2 . TYR A 176 ? 0.1352 0.1171 0.1145 -0.0045 0.0328 0.0032 258 TYR A CD2 1380 C CE1 . TYR A 176 ? 0.1357 0.1189 0.1252 -0.0056 0.0360 0.0018 258 TYR A CE1 1381 C CE2 . TYR A 176 ? 0.1533 0.1348 0.1350 -0.0049 0.0336 0.0040 258 TYR A CE2 1382 C CZ . TYR A 176 ? 0.1502 0.1322 0.1369 -0.0055 0.0353 0.0033 258 TYR A CZ 1383 O OH . TYR A 176 ? 0.1537 0.1353 0.1431 -0.0059 0.0361 0.0039 258 TYR A OH 1384 N N . PHE A 177 ? 0.1195 0.1043 0.0956 -0.0033 0.0278 -0.0008 259 PHE A N 1385 C CA . PHE A 177 ? 0.1220 0.1070 0.0962 -0.0029 0.0269 -0.0019 259 PHE A CA 1386 C C . PHE A 177 ? 0.1272 0.1111 0.0961 -0.0024 0.0260 -0.0013 259 PHE A C 1387 O O . PHE A 177 ? 0.1601 0.1432 0.1267 -0.0024 0.0253 0.0000 259 PHE A O 1388 C CB . PHE A 177 ? 0.1031 0.0891 0.0785 -0.0028 0.0249 -0.0022 259 PHE A CB 1389 C CG . PHE A 177 ? 0.0933 0.0807 0.0739 -0.0033 0.0254 -0.0029 259 PHE A CG 1390 C CD1 . PHE A 177 ? 0.1050 0.0934 0.0887 -0.0032 0.0261 -0.0043 259 PHE A CD1 1391 C CD2 . PHE A 177 ? 0.1044 0.0922 0.0870 -0.0036 0.0250 -0.0021 259 PHE A CD2 1392 C CE1 . PHE A 177 ? 0.1071 0.0970 0.0959 -0.0036 0.0264 -0.0050 259 PHE A CE1 1393 C CE2 . PHE A 177 ? 0.1095 0.0988 0.0969 -0.0040 0.0253 -0.0028 259 PHE A CE2 1394 C CZ . PHE A 177 ? 0.0870 0.0774 0.0777 -0.0040 0.0259 -0.0042 259 PHE A CZ 1395 N N . LYS A 178 ? 0.1164 0.1001 0.0835 -0.0021 0.0261 -0.0025 260 LYS A N 1396 C CA . LYS A 178 ? 0.1160 0.0989 0.0782 -0.0016 0.0248 -0.0023 260 LYS A CA 1397 C C . LYS A 178 ? 0.1682 0.1514 0.1300 -0.0013 0.0238 -0.0038 260 LYS A C 1398 O O . LYS A 178 ? 0.1640 0.1475 0.1274 -0.0013 0.0251 -0.0052 260 LYS A O 1399 C CB . LYS A 178 ? 0.1510 0.1327 0.1102 -0.0016 0.0265 -0.0019 260 LYS A CB 1400 C CG . LYS A 178 ? 0.1409 0.1218 0.0949 -0.0011 0.0250 -0.0017 260 LYS A CG 1401 C CD . LYS A 178 ? 0.2010 0.1807 0.1517 -0.0010 0.0267 -0.0011 260 LYS A CD 1402 C CE . LYS A 178 ? 0.3215 0.3004 0.2670 -0.0005 0.0251 -0.0010 260 LYS A CE 1403 N NZ . LYS A 178 ? 0.4534 0.4312 0.3953 -0.0005 0.0269 -0.0007 260 LYS A NZ 1404 N N . GLU A 179 ? 0.1398 0.1231 0.0999 -0.0011 0.0214 -0.0037 261 GLU A N 1405 C CA . GLU A 179 ? 0.1342 0.1178 0.0942 -0.0008 0.0201 -0.0051 261 GLU A CA 1406 C C . GLU A 179 ? 0.1741 0.1586 0.1386 -0.0011 0.0208 -0.0062 261 GLU A C 1407 O O . GLU A 179 ? 0.1472 0.1318 0.1125 -0.0009 0.0209 -0.0077 261 GLU A O 1408 C CB . GLU A 179 ? 0.1651 0.1480 0.1220 -0.0005 0.0204 -0.0063 261 GLU A CB 1409 C CG . GLU A 179 ? 0.1467 0.1287 0.0990 -0.0002 0.0193 -0.0054 261 GLU A CG 1410 C CD . GLU A 179 ? 0.2999 0.2812 0.2487 0.0001 0.0197 -0.0065 261 GLU A CD 1411 O OE1 . GLU A 179 ? 0.4044 0.3858 0.3544 0.0001 0.0215 -0.0078 261 GLU A OE1 1412 O OE2 . GLU A 179 ? 0.4117 0.3925 0.3568 0.0004 0.0181 -0.0062 261 GLU A OE2 1413 N N . GLY A 180 ? 0.1444 0.1295 0.1119 -0.0014 0.0212 -0.0053 262 GLY A N 1414 C CA . GLY A 180 ? 0.1585 0.1447 0.1304 -0.0017 0.0217 -0.0062 262 GLY A CA 1415 C C . GLY A 180 ? 0.1934 0.1802 0.1687 -0.0018 0.0241 -0.0070 262 GLY A C 1416 O O . GLY A 180 ? 0.1580 0.1460 0.1379 -0.0020 0.0246 -0.0075 262 GLY A O 1417 N N . LYS A 181 ? 0.1200 0.1060 0.0934 -0.0018 0.0255 -0.0070 263 LYS A N 1418 C CA . LYS A 181 ? 0.1525 0.1389 0.1290 -0.0020 0.0279 -0.0077 263 LYS A CA 1419 C C . LYS A 181 ? 0.1716 0.1581 0.1500 -0.0024 0.0293 -0.0065 263 LYS A C 1420 O O . LYS A 181 ? 0.1814 0.1670 0.1570 -0.0025 0.0288 -0.0051 263 LYS A O 1421 C CB . LYS A 181 ? 0.2033 0.1887 0.1767 -0.0017 0.0290 -0.0084 263 LYS A CB 1422 C CG . LYS A 181 ? 0.3532 0.3385 0.3255 -0.0012 0.0280 -0.0100 263 LYS A CG 1423 C CD . LYS A 181 ? 0.4261 0.4105 0.3956 -0.0010 0.0294 -0.0108 263 LYS A CD 1424 C CE . LYS A 181 ? 0.6230 0.6072 0.5911 -0.0005 0.0282 -0.0124 263 LYS A CE 1425 N NZ . LYS A 181 ? 0.6727 0.6560 0.6375 -0.0002 0.0295 -0.0133 263 LYS A NZ 1426 N N . ILE A 182 ? 0.1413 0.1287 0.1246 -0.0027 0.0308 -0.0072 264 ILE A N 1427 C CA . ILE A 182 ? 0.1175 0.1050 0.1033 -0.0032 0.0322 -0.0063 264 ILE A CA 1428 C C . ILE A 182 ? 0.1878 0.1740 0.1713 -0.0033 0.0343 -0.0060 264 ILE A C 1429 O O . ILE A 182 ? 0.1545 0.1407 0.1391 -0.0032 0.0359 -0.0070 264 ILE A O 1430 C CB . ILE A 182 ? 0.1369 0.1261 0.1296 -0.0035 0.0329 -0.0073 264 ILE A CB 1431 C CG1 . ILE A 182 ? 0.1939 0.1845 0.1888 -0.0034 0.0309 -0.0076 264 ILE A CG1 1432 C CG2 . ILE A 182 ? 0.1516 0.1409 0.1473 -0.0041 0.0343 -0.0065 264 ILE A CG2 1433 C CD1 . ILE A 182 ? 0.2375 0.2300 0.2391 -0.0035 0.0312 -0.0088 264 ILE A CD1 1434 N N . LEU A 183 ? 0.1349 0.1200 0.1154 -0.0034 0.0343 -0.0045 265 LEU A N 1435 C CA . LEU A 183 ? 0.1635 0.1473 0.1418 -0.0034 0.0364 -0.0039 265 LEU A CA 1436 C C . LEU A 183 ? 0.1822 0.1663 0.1654 -0.0040 0.0384 -0.0038 265 LEU A C 1437 O O . LEU A 183 ? 0.1770 0.1606 0.1608 -0.0041 0.0407 -0.0042 265 LEU A O 1438 C CB . LEU A 183 ? 0.1602 0.1426 0.1336 -0.0033 0.0356 -0.0023 265 LEU A CB 1439 C CG . LEU A 183 ? 0.1798 0.1619 0.1483 -0.0027 0.0334 -0.0022 265 LEU A CG 1440 C CD1 . LEU A 183 ? 0.1871 0.1679 0.1512 -0.0026 0.0327 -0.0006 265 LEU A CD1 1441 C CD2 . LEU A 183 ? 0.2458 0.2275 0.2121 -0.0024 0.0341 -0.0036 265 LEU A CD2 1442 N N . LYS A 184 ? 0.1301 0.1151 0.1168 -0.0043 0.0376 -0.0034 266 LYS A N 1443 C CA . LYS A 184 ? 0.1598 0.1450 0.1510 -0.0049 0.0392 -0.0032 266 LYS A CA 1444 C C . LYS A 184 ? 0.1567 0.1432 0.1518 -0.0052 0.0376 -0.0031 266 LYS A C 1445 O O . LYS A 184 ? 0.1415 0.1281 0.1342 -0.0050 0.0356 -0.0027 266 LYS A O 1446 C CB . LYS A 184 ? 0.2013 0.1847 0.1892 -0.0050 0.0404 -0.0016 266 LYS A CB 1447 C CG . LYS A 184 ? 0.2073 0.1906 0.1994 -0.0055 0.0418 -0.0012 266 LYS A CG 1448 C CD . LYS A 184 ? 0.2108 0.1922 0.1991 -0.0055 0.0429 0.0005 266 LYS A CD 1449 C CE . LYS A 184 ? 0.2452 0.2264 0.2378 -0.0061 0.0445 0.0009 266 LYS A CE 1450 N NZ . LYS A 184 ? 0.2644 0.2437 0.2534 -0.0060 0.0456 0.0026 266 LYS A NZ 1451 N N . TRP A 185 ? 0.1463 0.1338 0.1472 -0.0057 0.0385 -0.0037 267 TRP A N 1452 C CA . TRP A 185 ? 0.1458 0.1343 0.1502 -0.0061 0.0374 -0.0035 267 TRP A CA 1453 C C . TRP A 185 ? 0.1527 0.1411 0.1612 -0.0066 0.0391 -0.0033 267 TRP A C 1454 O O . TRP A 185 ? 0.1713 0.1592 0.1813 -0.0067 0.0411 -0.0037 267 TRP A O 1455 C CB . TRP A 185 ? 0.1172 0.1079 0.1258 -0.0061 0.0358 -0.0047 267 TRP A CB 1456 C CG . TRP A 185 ? 0.1260 0.1181 0.1403 -0.0062 0.0367 -0.0061 267 TRP A CG 1457 C CD1 . TRP A 185 ? 0.1650 0.1576 0.1797 -0.0058 0.0371 -0.0071 267 TRP A CD1 1458 C CD2 . TRP A 185 ? 0.1133 0.1066 0.1342 -0.0067 0.0373 -0.0067 267 TRP A CD2 1459 N NE1 . TRP A 185 ? 0.1557 0.1496 0.1768 -0.0060 0.0378 -0.0083 267 TRP A NE1 1460 C CE2 . TRP A 185 ? 0.1454 0.1397 0.1703 -0.0066 0.0379 -0.0080 267 TRP A CE2 1461 C CE3 . TRP A 185 ? 0.1172 0.1106 0.1410 -0.0072 0.0372 -0.0063 267 TRP A CE3 1462 C CZ2 . TRP A 185 ? 0.1236 0.1193 0.1555 -0.0069 0.0382 -0.0089 267 TRP A CZ2 1463 C CZ3 . TRP A 185 ? 0.1554 0.1501 0.1860 -0.0076 0.0376 -0.0073 267 TRP A CZ3 1464 C CH2 . TRP A 185 ? 0.1587 0.1545 0.1933 -0.0074 0.0381 -0.0085 267 TRP A CH2 1465 N N . GLU A 186 ? 0.1177 0.1062 0.1278 -0.0070 0.0383 -0.0027 268 GLU A N 1466 C CA . GLU A 186 ? 0.1470 0.1352 0.1609 -0.0075 0.0395 -0.0025 268 GLU A CA 1467 C C . GLU A 186 ? 0.1568 0.1468 0.1761 -0.0079 0.0380 -0.0032 268 GLU A C 1468 O O . GLU A 186 ? 0.1505 0.1410 0.1684 -0.0078 0.0361 -0.0030 268 GLU A O 1469 C CB . GLU A 186 ? 0.3086 0.2950 0.3189 -0.0075 0.0399 -0.0009 268 GLU A CB 1470 C CG . GLU A 186 ? 0.3283 0.3128 0.3328 -0.0071 0.0410 0.0002 268 GLU A CG 1471 C CD . GLU A 186 ? 0.2456 0.2285 0.2475 -0.0071 0.0412 0.0018 268 GLU A CD 1472 O OE1 . GLU A 186 ? 0.1951 0.1777 0.1942 -0.0069 0.0395 0.0025 268 GLU A OE1 1473 O OE2 . GLU A 186 ? 0.3556 0.3374 0.3585 -0.0073 0.0433 0.0022 268 GLU A OE2 1474 N N A SER A 187 ? 0.1237 0.1143 0.1486 -0.0084 0.0389 -0.0039 269 SER A N 1475 N N B SER A 187 ? 0.1230 0.1136 0.1479 -0.0084 0.0389 -0.0039 269 SER A N 1476 C CA A SER A 187 ? 0.1407 0.1328 0.1703 -0.0088 0.0373 -0.0045 269 SER A CA 1477 C CA B SER A 187 ? 0.1411 0.1332 0.1708 -0.0088 0.0374 -0.0045 269 SER A CA 1478 C C A SER A 187 ? 0.1381 0.1287 0.1656 -0.0090 0.0374 -0.0033 269 SER A C 1479 C C B SER A 187 ? 0.1379 0.1285 0.1653 -0.0090 0.0374 -0.0033 269 SER A C 1480 O O A SER A 187 ? 0.1328 0.1216 0.1576 -0.0089 0.0391 -0.0022 269 SER A O 1481 O O B SER A 187 ? 0.1325 0.1211 0.1569 -0.0089 0.0391 -0.0021 269 SER A O 1482 C CB A SER A 187 ? 0.1692 0.1626 0.2059 -0.0092 0.0379 -0.0058 269 SER A CB 1483 C CB B SER A 187 ? 0.1690 0.1621 0.2057 -0.0092 0.0382 -0.0057 269 SER A CB 1484 O OG A SER A 187 ? 0.1674 0.1592 0.2045 -0.0093 0.0405 -0.0053 269 SER A OG 1485 O OG B SER A 187 ? 0.1789 0.1737 0.2186 -0.0090 0.0378 -0.0069 269 SER A OG 1486 N N . LEU A 188 ? 0.1491 0.1407 0.1782 -0.0093 0.0354 -0.0036 270 LEU A N 1487 C CA . LEU A 188 ? 0.1551 0.1454 0.1828 -0.0095 0.0353 -0.0026 270 LEU A CA 1488 C C . LEU A 188 ? 0.1365 0.1260 0.1674 -0.0098 0.0372 -0.0025 270 LEU A C 1489 O O . LEU A 188 ? 0.1394 0.1300 0.1759 -0.0101 0.0376 -0.0037 270 LEU A O 1490 C CB . LEU A 188 ? 0.1081 0.0999 0.1383 -0.0098 0.0329 -0.0034 270 LEU A CB 1491 C CG . LEU A 188 ? 0.1252 0.1160 0.1552 -0.0101 0.0326 -0.0028 270 LEU A CG 1492 C CD1 . LEU A 188 ? 0.0973 0.0862 0.1208 -0.0097 0.0326 -0.0011 270 LEU A CD1 1493 C CD2 . LEU A 188 ? 0.1298 0.1222 0.1632 -0.0106 0.0304 -0.0040 270 LEU A CD2 1494 N N . THR A 189 ? 0.1124 0.0998 0.1398 -0.0096 0.0383 -0.0010 271 THR A N 1495 C CA . THR A 189 ? 0.1425 0.1288 0.1727 -0.0099 0.0401 -0.0006 271 THR A CA 1496 C C . THR A 189 ? 0.2004 0.1857 0.2297 -0.0101 0.0393 0.0002 271 THR A C 1497 O O . THR A 189 ? 0.1582 0.1436 0.1843 -0.0099 0.0376 0.0006 271 THR A O 1498 C CB . THR A 189 ? 0.1340 0.1185 0.1613 -0.0097 0.0426 0.0005 271 THR A CB 1499 O OG1 . THR A 189 ? 0.3030 0.2867 0.3340 -0.0100 0.0445 0.0006 271 THR A OG1 1500 C CG2 . THR A 189 ? 0.1284 0.1111 0.1487 -0.0092 0.0425 0.0023 271 THR A CG2 1501 N N . GLY A 190 ? 0.1822 0.1667 0.2145 -0.0104 0.0406 0.0004 272 GLY A N 1502 C CA . GLY A 190 ? 0.1735 0.1571 0.2054 -0.0105 0.0401 0.0012 272 GLY A CA 1503 C C . GLY A 190 ? 0.1342 0.1193 0.1717 -0.0110 0.0386 -0.0004 272 GLY A C 1504 O O . GLY A 190 ? 0.1544 0.1412 0.1967 -0.0113 0.0383 -0.0020 272 GLY A O 1505 N N . THR A 191 ? 0.1016 0.0861 0.1383 -0.0111 0.0376 0.0000 273 THR A N 1506 C CA . THR A 191 ? 0.1238 0.1095 0.1658 -0.0116 0.0363 -0.0015 273 THR A CA 1507 C C . THR A 191 ? 0.1055 0.0926 0.1470 -0.0118 0.0336 -0.0026 273 THR A C 1508 O O . THR A 191 ? 0.0958 0.0840 0.1414 -0.0122 0.0322 -0.0041 273 THR A O 1509 C CB . THR A 191 ? 0.1249 0.1090 0.1678 -0.0117 0.0372 -0.0007 273 THR A CB 1510 O OG1 . THR A 191 ? 0.1177 0.1002 0.1552 -0.0113 0.0368 0.0009 273 THR A OG1 1511 C CG2 . THR A 191 ? 0.1499 0.1327 0.1942 -0.0117 0.0399 0.0001 273 THR A CG2 1512 N N . ALA A 192 ? 0.1023 0.0893 0.1390 -0.0114 0.0328 -0.0020 274 ALA A N 1513 C CA . ALA A 192 ? 0.1107 0.0992 0.1473 -0.0116 0.0303 -0.0031 274 ALA A CA 1514 C C . ALA A 192 ? 0.1293 0.1202 0.1708 -0.0119 0.0293 -0.0050 274 ALA A C 1515 O O . ALA A 192 ? 0.1287 0.1201 0.1711 -0.0118 0.0304 -0.0050 274 ALA A O 1516 C CB . ALA A 192 ? 0.0940 0.0821 0.1247 -0.0111 0.0299 -0.0020 274 ALA A CB 1517 N N . LYS A 193 ? 0.0799 0.0721 0.1245 -0.0124 0.0272 -0.0066 275 LYS A N 1518 C CA . LYS A 193 ? 0.1217 0.1163 0.1714 -0.0127 0.0258 -0.0085 275 LYS A CA 1519 C C . LYS A 193 ? 0.1646 0.1608 0.2132 -0.0126 0.0235 -0.0093 275 LYS A C 1520 O O . LYS A 193 ? 0.1107 0.1089 0.1630 -0.0127 0.0223 -0.0106 275 LYS A O 1521 C CB . LYS A 193 ? 0.1122 0.1074 0.1665 -0.0131 0.0246 -0.0100 275 LYS A CB 1522 C CG . LYS A 193 ? 0.1145 0.1082 0.1709 -0.0132 0.0268 -0.0094 275 LYS A CG 1523 C CD . LYS A 193 ? 0.1128 0.1064 0.1710 -0.0129 0.0291 -0.0089 275 LYS A CD 1524 C CE . LYS A 193 ? 0.1230 0.1155 0.1845 -0.0131 0.0311 -0.0086 275 LYS A CE 1525 N NZ . LYS A 193 ? 0.1216 0.1117 0.1794 -0.0130 0.0324 -0.0070 275 LYS A NZ 1526 N N . HIS A 194 ? 0.1077 0.1032 0.1516 -0.0126 0.0229 -0.0084 276 HIS A N 1527 C CA . HIS A 194 ? 0.1001 0.0969 0.1424 -0.0125 0.0210 -0.0089 276 HIS A CA 1528 C C . HIS A 194 ? 0.1078 0.1030 0.1431 -0.0117 0.0211 -0.0073 276 HIS A C 1529 O O . HIS A 194 ? 0.1268 0.1203 0.1598 -0.0118 0.0216 -0.0065 276 HIS A O 1530 C CB . HIS A 194 ? 0.1077 0.1057 0.1514 -0.0126 0.0177 -0.0107 276 HIS A CB 1531 C CG . HIS A 194 ? 0.1043 0.1038 0.1462 -0.0118 0.0150 -0.0113 276 HIS A CG 1532 N ND1 . HIS A 194 ? 0.1143 0.1135 0.1509 -0.0111 0.0132 -0.0109 276 HIS A ND1 1533 C CD2 . HIS A 194 ? 0.1050 0.1064 0.1500 -0.0117 0.0140 -0.0121 276 HIS A CD2 1534 C CE1 . HIS A 194 ? 0.1315 0.1322 0.1678 -0.0106 0.0111 -0.0114 276 HIS A CE1 1535 N NE2 . HIS A 194 ? 0.1136 0.1157 0.1550 -0.0109 0.0115 -0.0121 276 HIS A NE2 1536 N N . ILE A 195 ? 0.0987 0.0945 0.1310 -0.0110 0.0207 -0.0068 277 ILE A N 1537 C CA . ILE A 195 ? 0.0812 0.0756 0.1072 -0.0103 0.0209 -0.0053 277 ILE A CA 1538 C C . ILE A 195 ? 0.1187 0.1142 0.1419 -0.0096 0.0183 -0.0057 277 ILE A C 1539 O O . ILE A 195 ? 0.1022 0.0991 0.1270 -0.0094 0.0177 -0.0063 277 ILE A O 1540 C CB . ILE A 195 ? 0.0816 0.0750 0.1060 -0.0102 0.0237 -0.0040 277 ILE A CB 1541 C CG1 . ILE A 195 ? 0.1283 0.1201 0.1541 -0.0107 0.0262 -0.0032 277 ILE A CG1 1542 C CG2 . ILE A 195 ? 0.0893 0.0817 0.1074 -0.0094 0.0233 -0.0028 277 ILE A CG2 1543 C CD1 . ILE A 195 ? 0.1353 0.1252 0.1573 -0.0105 0.0264 -0.0019 277 ILE A CD1 1544 N N . GLU A 196 ? 0.0807 0.0754 0.0998 -0.0092 0.0170 -0.0052 278 GLU A N 1545 C CA . GLU A 196 ? 0.0992 0.0945 0.1149 -0.0084 0.0150 -0.0051 278 GLU A CA 1546 C C . GLU A 196 ? 0.0828 0.0766 0.0935 -0.0079 0.0151 -0.0037 278 GLU A C 1547 O O . GLU A 196 ? 0.1235 0.1160 0.1336 -0.0081 0.0160 -0.0032 278 GLU A O 1548 C CB . GLU A 196 ? 0.0900 0.0866 0.1069 -0.0084 0.0123 -0.0064 278 GLU A CB 1549 C CG . GLU A 196 ? 0.0990 0.0973 0.1205 -0.0087 0.0114 -0.0077 278 GLU A CG 1550 C CD . GLU A 196 ? 0.1713 0.1707 0.1928 -0.0085 0.0085 -0.0088 278 GLU A CD 1551 O OE1 . GLU A 196 ? 0.1492 0.1502 0.1743 -0.0085 0.0072 -0.0098 278 GLU A OE1 1552 O OE2 . GLU A 196 ? 0.2748 0.2736 0.2927 -0.0082 0.0074 -0.0085 278 GLU A OE2 1553 N N . GLU A 197 ? 0.0692 0.0632 0.0768 -0.0073 0.0143 -0.0033 279 GLU A N 1554 C CA . GLU A 197 ? 0.0733 0.0663 0.0766 -0.0068 0.0136 -0.0023 279 GLU A CA 1555 C C . GLU A 197 ? 0.0667 0.0579 0.0680 -0.0068 0.0153 -0.0010 279 GLU A C 1556 O O . GLU A 197 ? 0.0753 0.0657 0.0754 -0.0067 0.0149 -0.0006 279 GLU A O 1557 C CB . GLU A 197 ? 0.0896 0.0831 0.0926 -0.0067 0.0117 -0.0029 279 GLU A CB 1558 C CG . GLU A 197 ? 0.1053 0.1004 0.1091 -0.0065 0.0098 -0.0039 279 GLU A CG 1559 C CD . GLU A 197 ? 0.1396 0.1350 0.1429 -0.0065 0.0080 -0.0046 279 GLU A CD 1560 O OE1 . GLU A 197 ? 0.1194 0.1140 0.1229 -0.0068 0.0083 -0.0048 279 GLU A OE1 1561 O OE2 . GLU A 197 ? 0.1271 0.1234 0.1297 -0.0062 0.0064 -0.0049 279 GLU A OE2 1562 N N . CYS A 198 ? 0.0768 0.0673 0.0777 -0.0069 0.0172 -0.0003 280 CYS A N 1563 C CA . CYS A 198 ? 0.0901 0.0787 0.0888 -0.0068 0.0188 0.0011 280 CYS A CA 1564 C C . CYS A 198 ? 0.1069 0.0947 0.1014 -0.0062 0.0178 0.0022 280 CYS A C 1565 O O . CYS A 198 ? 0.0752 0.0635 0.0676 -0.0057 0.0168 0.0021 280 CYS A O 1566 C CB . CYS A 198 ? 0.0879 0.0759 0.0866 -0.0070 0.0210 0.0016 280 CYS A CB 1567 S SG . CYS A 198 ? 0.1456 0.1343 0.1501 -0.0079 0.0227 0.0007 280 CYS A SG 1568 N N . SER A 199 ? 0.0960 0.0823 0.0895 -0.0061 0.0181 0.0031 281 SER A N 1569 C CA . SER A 199 ? 0.1226 0.1080 0.1125 -0.0055 0.0174 0.0043 281 SER A CA 1570 C C . SER A 199 ? 0.1278 0.1113 0.1154 -0.0053 0.0190 0.0058 281 SER A C 1571 O O . SER A 199 ? 0.1191 0.1018 0.1084 -0.0056 0.0201 0.0063 281 SER A O 1572 C CB . SER A 199 ? 0.1005 0.0856 0.0910 -0.0054 0.0164 0.0043 281 SER A CB 1573 O OG . SER A 199 ? 0.1010 0.0876 0.0931 -0.0055 0.0149 0.0029 281 SER A OG 1574 N N . CYS A 200 ? 0.0951 0.0786 0.0796 -0.0047 0.0184 0.0063 282 CYS A N 1575 C CA . CYS A 200 ? 0.1051 0.0877 0.0878 -0.0044 0.0191 0.0072 282 CYS A CA 1576 C C . CYS A 200 ? 0.1210 0.1028 0.1004 -0.0036 0.0178 0.0084 282 CYS A C 1577 O O . CYS A 200 ? 0.1079 0.0902 0.0862 -0.0033 0.0162 0.0082 282 CYS A O 1578 C CB . CYS A 200 ? 0.1195 0.1025 0.1016 -0.0044 0.0199 0.0067 282 CYS A CB 1579 S SG . CYS A 200 ? 0.1330 0.1172 0.1195 -0.0052 0.0214 0.0052 282 CYS A SG 1580 N N . TYR A 201 ? 0.0883 0.0689 0.0664 -0.0034 0.0184 0.0095 283 TYR A N 1581 C CA . TYR A 201 ? 0.1095 0.0895 0.0844 -0.0027 0.0172 0.0106 283 TYR A CA 1582 C C . TYR A 201 ? 0.1273 0.1062 0.1003 -0.0027 0.0183 0.0114 283 TYR A C 1583 O O . TYR A 201 ? 0.1324 0.1110 0.1070 -0.0031 0.0201 0.0114 283 TYR A O 1584 C CB . TYR A 201 ? 0.1131 0.0923 0.0887 -0.0025 0.0164 0.0115 283 TYR A CB 1585 C CG . TYR A 201 ? 0.1227 0.1008 0.1000 -0.0028 0.0178 0.0123 283 TYR A CG 1586 C CD1 . TYR A 201 ? 0.1147 0.0929 0.0956 -0.0034 0.0188 0.0116 283 TYR A CD1 1587 C CD2 . TYR A 201 ? 0.1532 0.1299 0.1286 -0.0025 0.0181 0.0137 283 TYR A CD2 1588 C CE1 . TYR A 201 ? 0.0932 0.0703 0.0760 -0.0037 0.0201 0.0122 283 TYR A CE1 1589 C CE2 . TYR A 201 ? 0.1274 0.1030 0.1044 -0.0027 0.0194 0.0146 283 TYR A CE2 1590 C CZ . TYR A 201 ? 0.1468 0.1225 0.1276 -0.0033 0.0204 0.0138 283 TYR A CZ 1591 O OH . TYR A 201 ? 0.1497 0.1243 0.1325 -0.0035 0.0217 0.0145 283 TYR A OH 1592 N N . GLY A 202 ? 0.1239 0.1025 0.0935 -0.0021 0.0173 0.0121 284 GLY A N 1593 C CA . GLY A 202 ? 0.1485 0.1260 0.1156 -0.0020 0.0183 0.0129 284 GLY A CA 1594 C C . GLY A 202 ? 0.1352 0.1115 0.1002 -0.0016 0.0175 0.0146 284 GLY A C 1595 O O . GLY A 202 ? 0.1302 0.1066 0.0945 -0.0012 0.0156 0.0150 284 GLY A O 1596 N N . GLU A 203 ? 0.1533 0.1283 0.1171 -0.0017 0.0189 0.0157 285 GLU A N 1597 C CA . GLU A 203 ? 0.1467 0.1204 0.1079 -0.0012 0.0182 0.0174 285 GLU A CA 1598 C C . GLU A 203 ? 0.2112 0.1838 0.1703 -0.0014 0.0200 0.0182 285 GLU A C 1599 O O . GLU A 203 ? 0.2693 0.2422 0.2297 -0.0018 0.0219 0.0173 285 GLU A O 1600 C CB . GLU A 203 ? 0.1420 0.1151 0.1057 -0.0012 0.0179 0.0184 285 GLU A CB 1601 C CG . GLU A 203 ? 0.2088 0.1814 0.1759 -0.0018 0.0200 0.0183 285 GLU A CG 1602 C CD . GLU A 203 ? 0.2973 0.2681 0.2644 -0.0018 0.0208 0.0201 285 GLU A CD 1603 O OE1 . GLU A 203 ? 0.3000 0.2698 0.2636 -0.0015 0.0208 0.0213 285 GLU A OE1 1604 O OE2 . GLU A 203 ? 0.4682 0.4386 0.4386 -0.0020 0.0213 0.0202 285 GLU A OE2 1605 N N . ARG A 204 ? 0.1595 0.1309 0.1154 -0.0010 0.0196 0.0198 286 ARG A N 1606 C CA . ARG A 204 ? 0.1800 0.1502 0.1331 -0.0011 0.0213 0.0206 286 ARG A CA 1607 C C . ARG A 204 ? 0.2627 0.2324 0.2185 -0.0017 0.0240 0.0204 286 ARG A C 1608 O O . ARG A 204 ? 0.2105 0.1797 0.1645 -0.0019 0.0258 0.0203 286 ARG A O 1609 C CB . ARG A 204 ? 0.3528 0.3214 0.3028 -0.0007 0.0204 0.0227 286 ARG A CB 1610 C CG . ARG A 204 ? 0.2156 0.1833 0.1683 -0.0007 0.0202 0.0240 286 ARG A CG 1611 C CD . ARG A 204 ? 0.3940 0.3602 0.3436 -0.0002 0.0190 0.0261 286 ARG A CD 1612 N NE . ARG A 204 ? 0.2911 0.2566 0.2435 -0.0001 0.0183 0.0272 286 ARG A NE 1613 C CZ . ARG A 204 ? 0.3385 0.3030 0.2893 0.0004 0.0165 0.0289 286 ARG A CZ 1614 N NH1 . ARG A 204 ? 0.3134 0.2778 0.2599 0.0008 0.0150 0.0296 286 ARG A NH1 1615 N NH2 . ARG A 204 ? 0.3519 0.3157 0.3056 0.0004 0.0160 0.0297 286 ARG A NH2 1616 N N . THR A 205 ? 0.4316 0.4014 0.3916 -0.0020 0.0245 0.0203 287 THR A N 1617 C CA . THR A 205 ? 0.3818 0.3514 0.3450 -0.0026 0.0270 0.0200 287 THR A CA 1618 C C . THR A 205 ? 0.5052 0.4761 0.4702 -0.0030 0.0280 0.0181 287 THR A C 1619 O O . THR A 205 ? 0.4899 0.4607 0.4571 -0.0035 0.0302 0.0177 287 THR A O 1620 C CB . THR A 205 ? 0.5258 0.4951 0.4932 -0.0029 0.0272 0.0202 287 THR A CB 1621 O OG1 . THR A 205 ? 0.5549 0.5257 0.5250 -0.0030 0.0259 0.0188 287 THR A OG1 1622 C CG2 . THR A 205 ? 0.4402 0.4080 0.4062 -0.0025 0.0262 0.0221 287 THR A CG2 1623 N N . GLY A 206 ? 0.3228 0.2952 0.2873 -0.0028 0.0264 0.0168 288 GLY A N 1624 C CA . GLY A 206 ? 0.2174 0.1910 0.1837 -0.0031 0.0270 0.0150 288 GLY A CA 1625 C C . GLY A 206 ? 0.2329 0.2080 0.2016 -0.0031 0.0254 0.0139 288 GLY A C 1626 O O . GLY A 206 ? 0.2270 0.2023 0.1947 -0.0028 0.0234 0.0143 288 GLY A O 1627 N N . ILE A 207 ? 0.1548 0.1310 0.1266 -0.0036 0.0261 0.0124 289 ILE A N 1628 C CA . ILE A 207 ? 0.1220 0.0996 0.0961 -0.0037 0.0247 0.0113 289 ILE A CA 1629 C C . ILE A 207 ? 0.1556 0.1334 0.1343 -0.0042 0.0256 0.0109 289 ILE A C 1630 O O . ILE A 207 ? 0.1637 0.1414 0.1448 -0.0047 0.0275 0.0106 289 ILE A O 1631 C CB . ILE A 207 ? 0.1195 0.0984 0.0936 -0.0037 0.0245 0.0098 289 ILE A CB 1632 C CG1 . ILE A 207 ? 0.1343 0.1131 0.1041 -0.0031 0.0232 0.0100 289 ILE A CG1 1633 C CG2 . ILE A 207 ? 0.1241 0.1043 0.1010 -0.0039 0.0235 0.0087 289 ILE A CG2 1634 C CD1 . ILE A 207 ? 0.1503 0.1299 0.1195 -0.0031 0.0235 0.0087 289 ILE A CD1 1635 N N . THR A 208 ? 0.1147 0.0926 0.0945 -0.0042 0.0243 0.0110 290 THR A N 1636 C CA . THR A 208 ? 0.0883 0.0664 0.0724 -0.0048 0.0249 0.0106 290 THR A CA 1637 C C . THR A 208 ? 0.1369 0.1164 0.1229 -0.0050 0.0238 0.0092 290 THR A C 1638 O O . THR A 208 ? 0.1272 0.1071 0.1114 -0.0046 0.0222 0.0092 290 THR A O 1639 C CB . THR A 208 ? 0.1313 0.1082 0.1155 -0.0046 0.0245 0.0118 290 THR A CB 1640 O OG1 . THR A 208 ? 0.1652 0.1406 0.1476 -0.0044 0.0256 0.0132 290 THR A OG1 1641 C CG2 . THR A 208 ? 0.1378 0.1148 0.1265 -0.0052 0.0251 0.0111 290 THR A CG2 1642 N N . CYS A 209 ? 0.1374 0.1178 0.1273 -0.0057 0.0248 0.0080 291 CYS A N 1643 C CA . CYS A 209 ? 0.1296 0.1114 0.1214 -0.0061 0.0239 0.0067 291 CYS A CA 1644 C C . CYS A 209 ? 0.1401 0.1220 0.1361 -0.0067 0.0242 0.0060 291 CYS A C 1645 O O . CYS A 209 ? 0.1701 0.1519 0.1692 -0.0072 0.0255 0.0058 291 CYS A O 1646 C CB . CYS A 209 ? 0.1014 0.0846 0.0944 -0.0063 0.0243 0.0055 291 CYS A CB 1647 S SG . CYS A 209 ? 0.1380 0.1211 0.1265 -0.0056 0.0239 0.0058 291 CYS A SG 1648 N N . THR A 210 ? 0.0950 0.0771 0.0912 -0.0068 0.0229 0.0057 292 THR A N 1649 C CA . THR A 210 ? 0.1067 0.0890 0.1068 -0.0075 0.0230 0.0048 292 THR A CA 1650 C C . THR A 210 ? 0.1112 0.0956 0.1130 -0.0077 0.0215 0.0030 292 THR A C 1651 O O . THR A 210 ? 0.0958 0.0811 0.0952 -0.0072 0.0197 0.0027 292 THR A O 1652 C CB . THR A 210 ? 0.0969 0.0781 0.0961 -0.0073 0.0222 0.0054 292 THR A CB 1653 O OG1 . THR A 210 ? 0.1434 0.1231 0.1406 -0.0066 0.0226 0.0070 292 THR A OG1 1654 C CG2 . THR A 210 ? 0.1099 0.0914 0.1132 -0.0079 0.0219 0.0040 292 THR A CG2 1655 N N . CYS A 211 ? 0.0991 0.0846 0.1051 -0.0084 0.0218 0.0016 293 CYS A N 1656 C CA . CYS A 211 ? 0.1110 0.0986 0.1187 -0.0085 0.0202 0.0000 293 CYS A CA 1657 C C . CYS A 211 ? 0.1012 0.0896 0.1120 -0.0089 0.0188 -0.0016 293 CYS A C 1658 O O . CYS A 211 ? 0.0824 0.0696 0.0934 -0.0090 0.0189 -0.0015 293 CYS A O 1659 C CB . CYS A 211 ? 0.1112 0.0996 0.1212 -0.0088 0.0215 -0.0004 293 CYS A CB 1660 S SG . CYS A 211 ? 0.1255 0.1125 0.1318 -0.0085 0.0237 0.0014 293 CYS A SG 1661 N N . LYS A 212 ? 0.0890 0.0792 0.1020 -0.0091 0.0175 -0.0031 294 LYS A N 1662 C CA . LYS A 212 ? 0.0908 0.0818 0.1065 -0.0094 0.0160 -0.0048 294 LYS A CA 1663 C C . LYS A 212 ? 0.1151 0.1074 0.1359 -0.0101 0.0162 -0.0061 294 LYS A C 1664 O O . LYS A 212 ? 0.1334 0.1268 0.1549 -0.0100 0.0162 -0.0061 294 LYS A O 1665 C CB . LYS A 212 ? 0.1489 0.1410 0.1621 -0.0089 0.0135 -0.0055 294 LYS A CB 1666 C CG . LYS A 212 ? 0.1814 0.1747 0.1971 -0.0092 0.0116 -0.0074 294 LYS A CG 1667 C CD . LYS A 212 ? 0.1809 0.1752 0.1938 -0.0087 0.0094 -0.0078 294 LYS A CD 1668 C CE . LYS A 212 ? 0.1780 0.1736 0.1910 -0.0084 0.0087 -0.0077 294 LYS A CE 1669 N NZ . LYS A 212 ? 0.1914 0.1882 0.2037 -0.0081 0.0062 -0.0086 294 LYS A NZ 1670 N N . ASP A 213 ? 0.0776 0.0698 0.1021 -0.0108 0.0163 -0.0071 295 ASP A N 1671 C CA . ASP A 213 ? 0.0822 0.0758 0.1120 -0.0115 0.0160 -0.0087 295 ASP A CA 1672 C C . ASP A 213 ? 0.1013 0.0962 0.1312 -0.0114 0.0129 -0.0105 295 ASP A C 1673 O O . ASP A 213 ? 0.0835 0.0779 0.1133 -0.0115 0.0121 -0.0114 295 ASP A O 1674 C CB . ASP A 213 ? 0.0911 0.0836 0.1252 -0.0124 0.0178 -0.0089 295 ASP A CB 1675 C CG . ASP A 213 ? 0.1136 0.1077 0.1540 -0.0131 0.0175 -0.0107 295 ASP A CG 1676 O OD1 . ASP A 213 ? 0.1250 0.1209 0.1666 -0.0130 0.0150 -0.0122 295 ASP A OD1 1677 O OD2 . ASP A 213 ? 0.1174 0.1110 0.1610 -0.0134 0.0193 -0.0104 295 ASP A OD2 1678 N N . ASN A 214 ? 0.0676 0.0642 0.0974 -0.0110 0.0113 -0.0110 296 ASN A N 1679 C CA . ASN A 214 ? 0.0795 0.0772 0.1087 -0.0108 0.0084 -0.0124 296 ASN A CA 1680 C C . ASN A 214 ? 0.1372 0.1360 0.1718 -0.0115 0.0072 -0.0144 296 ASN A C 1681 O O . ASN A 214 ? 0.1631 0.1624 0.1972 -0.0115 0.0049 -0.0158 296 ASN A O 1682 C CB . ASN A 214 ? 0.0907 0.0896 0.1178 -0.0101 0.0069 -0.0120 296 ASN A CB 1683 C CG . ASN A 214 ? 0.1186 0.1180 0.1429 -0.0096 0.0042 -0.0128 296 ASN A CG 1684 O OD1 . ASN A 214 ? 0.1335 0.1319 0.1535 -0.0093 0.0040 -0.0122 296 ASN A OD1 1685 N ND2 . ASN A 214 ? 0.1192 0.1202 0.1459 -0.0096 0.0020 -0.0141 296 ASN A ND2 1686 N N . TRP A 215 ? 0.1055 0.1046 0.1450 -0.0121 0.0088 -0.0146 297 TRP A N 1687 C CA . TRP A 215 ? 0.1151 0.1157 0.1607 -0.0128 0.0077 -0.0165 297 TRP A CA 1688 C C . TRP A 215 ? 0.1178 0.1174 0.1655 -0.0135 0.0076 -0.0178 297 TRP A C 1689 O O . TRP A 215 ? 0.1454 0.1457 0.1934 -0.0136 0.0050 -0.0196 297 TRP A O 1690 C CB . TRP A 215 ? 0.1236 0.1250 0.1742 -0.0132 0.0097 -0.0162 297 TRP A CB 1691 C CG . TRP A 215 ? 0.1700 0.1728 0.2264 -0.0134 0.0088 -0.0176 297 TRP A CG 1692 C CD1 . TRP A 215 ? 0.1593 0.1632 0.2172 -0.0133 0.0059 -0.0195 297 TRP A CD1 1693 C CD2 . TRP A 215 ? 0.1339 0.1370 0.1945 -0.0134 0.0110 -0.0173 297 TRP A CD2 1694 N NE1 . TRP A 215 ? 0.1441 0.1491 0.2075 -0.0133 0.0060 -0.0202 297 TRP A NE1 1695 C CE2 . TRP A 215 ? 0.1621 0.1666 0.2273 -0.0134 0.0092 -0.0189 297 TRP A CE2 1696 C CE3 . TRP A 215 ? 0.1787 0.1809 0.2393 -0.0133 0.0143 -0.0157 297 TRP A CE3 1697 C CZ2 . TRP A 215 ? 0.1505 0.1555 0.2208 -0.0133 0.0107 -0.0191 297 TRP A CZ2 1698 C CZ3 . TRP A 215 ? 0.1973 0.1999 0.2626 -0.0132 0.0159 -0.0159 297 TRP A CZ3 1699 C CH2 . TRP A 215 ? 0.1647 0.1687 0.2351 -0.0133 0.0141 -0.0176 297 TRP A CH2 1700 N N . GLN A 216 ? 0.1194 0.1176 0.1682 -0.0139 0.0103 -0.0169 298 GLN A N 1701 C CA . GLN A 216 ? 0.1524 0.1499 0.2032 -0.0141 0.0103 -0.0178 298 GLN A CA 1702 C C . GLN A 216 ? 0.1276 0.1228 0.1756 -0.0142 0.0120 -0.0167 298 GLN A C 1703 O O . GLN A 216 ? 0.1369 0.1314 0.1859 -0.0143 0.0118 -0.0175 298 GLN A O 1704 C CB . GLN A 216 ? 0.1760 0.1741 0.2321 -0.0142 0.0118 -0.0178 298 GLN A CB 1705 C CG . GLN A 216 ? 0.1802 0.1806 0.2403 -0.0141 0.0102 -0.0190 298 GLN A CG 1706 C CD . GLN A 216 ? 0.2965 0.2971 0.3615 -0.0142 0.0124 -0.0187 298 GLN A CD 1707 O OE1 . GLN A 216 ? 0.3384 0.3399 0.4077 -0.0143 0.0114 -0.0201 298 GLN A OE1 1708 N NE2 . GLN A 216 ? 0.2218 0.2215 0.2860 -0.0141 0.0152 -0.0169 298 GLN A NE2 1709 N N . GLY A 217 ? 0.1017 0.0956 0.1461 -0.0140 0.0137 -0.0147 299 GLY A N 1710 C CA . GLY A 217 ? 0.1159 0.1076 0.1581 -0.0139 0.0157 -0.0133 299 GLY A CA 1711 C C . GLY A 217 ? 0.1887 0.1793 0.2258 -0.0133 0.0147 -0.0129 299 GLY A C 1712 O O . GLY A 217 ? 0.1363 0.1277 0.1694 -0.0126 0.0133 -0.0127 299 GLY A O 1713 N N . SER A 218 ? 0.1239 0.1128 0.1612 -0.0135 0.0156 -0.0129 300 SER A N 1714 C CA . SER A 218 ? 0.0680 0.0558 0.1006 -0.0128 0.0150 -0.0123 300 SER A CA 1715 C C . SER A 218 ? 0.1374 0.1232 0.1683 -0.0125 0.0173 -0.0099 300 SER A C 1716 O O . SER A 218 ? 0.1237 0.1086 0.1510 -0.0118 0.0171 -0.0091 300 SER A O 1717 C CB . SER A 218 ? 0.0958 0.0832 0.1294 -0.0131 0.0137 -0.0145 300 SER A CB 1718 O OG . SER A 218 ? 0.1502 0.1395 0.1837 -0.0131 0.0112 -0.0165 300 SER A OG 1719 N N . ASN A 219 ? 0.0995 0.0847 0.1332 -0.0129 0.0194 -0.0088 301 ASN A N 1720 C CA . ASN A 219 ? 0.0869 0.0705 0.1178 -0.0123 0.0213 -0.0062 301 ASN A CA 1721 C C . ASN A 219 ? 0.1009 0.0854 0.1291 -0.0121 0.0215 -0.0051 301 ASN A C 1722 O O . ASN A 219 ? 0.1215 0.1079 0.1510 -0.0122 0.0204 -0.0064 301 ASN A O 1723 C CB . ASN A 219 ? 0.1023 0.0853 0.1358 -0.0122 0.0231 -0.0053 301 ASN A CB 1724 C CG . ASN A 219 ? 0.1231 0.1076 0.1607 -0.0127 0.0234 -0.0063 301 ASN A CG 1725 O OD1 . ASN A 219 ? 0.0957 0.0820 0.1349 -0.0131 0.0219 -0.0080 301 ASN A OD1 1726 N ND2 . ASN A 219 ? 0.1283 0.1122 0.1677 -0.0126 0.0253 -0.0053 301 ASN A ND2 1727 N N . ARG A 220 ? 0.0761 0.0594 0.1003 -0.0114 0.0224 -0.0030 302 ARG A N 1728 C CA . ARG A 220 ? 0.0850 0.0693 0.1060 -0.0109 0.0223 -0.0021 302 ARG A CA 1729 C C . ARG A 220 ? 0.1194 0.1033 0.1409 -0.0109 0.0243 -0.0009 302 ARG A C 1730 O O . ARG A 220 ? 0.1157 0.0982 0.1365 -0.0105 0.0256 0.0005 302 ARG A O 1731 C CB . ARG A 220 ? 0.0504 0.0339 0.0660 -0.0099 0.0215 -0.0008 302 ARG A CB 1732 C CG . ARG A 220 ? 0.0920 0.0765 0.1063 -0.0096 0.0192 -0.0020 302 ARG A CG 1733 C CD . ARG A 220 ? 0.0970 0.0812 0.1065 -0.0086 0.0184 -0.0008 302 ARG A CD 1734 N NE . ARG A 220 ? 0.0972 0.0823 0.1056 -0.0083 0.0165 -0.0021 302 ARG A NE 1735 C CZ . ARG A 220 ? 0.0784 0.0653 0.0864 -0.0083 0.0149 -0.0032 302 ARG A CZ 1736 N NH1 . ARG A 220 ? 0.0657 0.0536 0.0744 -0.0084 0.0150 -0.0033 302 ARG A NH1 1737 N NH2 . ARG A 220 ? 0.0630 0.0504 0.0696 -0.0080 0.0134 -0.0042 302 ARG A NH2 1738 N N . PRO A 221 ? 0.0894 0.0749 0.1118 -0.0111 0.0244 -0.0015 303 PRO A N 1739 C CA . PRO A 221 ? 0.0970 0.0822 0.1188 -0.0107 0.0261 -0.0004 303 PRO A CA 1740 C C . PRO A 221 ? 0.1175 0.1014 0.1335 -0.0099 0.0265 0.0015 303 PRO A C 1741 O O . PRO A 221 ? 0.1275 0.1114 0.1403 -0.0096 0.0253 0.0018 303 PRO A O 1742 C CB . PRO A 221 ? 0.1171 0.1043 0.1415 -0.0111 0.0257 -0.0018 303 PRO A CB 1743 C CG . PRO A 221 ? 0.1273 0.1158 0.1514 -0.0112 0.0234 -0.0030 303 PRO A CG 1744 C CD . PRO A 221 ? 0.0817 0.0693 0.1054 -0.0112 0.0223 -0.0033 303 PRO A CD 1745 N N . VAL A 222 ? 0.0885 0.0714 0.1033 -0.0095 0.0280 0.0028 304 VAL A N 1746 C CA . VAL A 222 ? 0.1119 0.0936 0.1213 -0.0086 0.0282 0.0045 304 VAL A CA 1747 C C . VAL A 222 ? 0.1580 0.1399 0.1666 -0.0085 0.0295 0.0047 304 VAL A C 1748 O O . VAL A 222 ? 0.1543 0.1362 0.1661 -0.0088 0.0310 0.0044 304 VAL A O 1749 C CB . VAL A 222 ? 0.1320 0.1117 0.1399 -0.0082 0.0287 0.0061 304 VAL A CB 1750 C CG1 . VAL A 222 ? 0.1409 0.1196 0.1435 -0.0074 0.0287 0.0077 304 VAL A CG1 1751 C CG2 . VAL A 222 ? 0.1215 0.1009 0.1300 -0.0083 0.0275 0.0059 304 VAL A CG2 1752 N N . ILE A 223 ? 0.0854 0.0675 0.0902 -0.0080 0.0289 0.0050 305 ILE A N 1753 C CA . ILE A 223 ? 0.1094 0.0914 0.1126 -0.0077 0.0302 0.0053 305 ILE A CA 1754 C C . ILE A 223 ? 0.1370 0.1174 0.1348 -0.0070 0.0301 0.0070 305 ILE A C 1755 O O . ILE A 223 ? 0.1376 0.1180 0.1321 -0.0065 0.0285 0.0074 305 ILE A O 1756 C CB . ILE A 223 ? 0.1304 0.1140 0.1339 -0.0077 0.0297 0.0041 305 ILE A CB 1757 C CG1 . ILE A 223 ? 0.1019 0.0873 0.1111 -0.0085 0.0295 0.0024 305 ILE A CG1 1758 C CG2 . ILE A 223 ? 0.1531 0.1363 0.1547 -0.0074 0.0310 0.0043 305 ILE A CG2 1759 C CD1 . ILE A 223 ? 0.1388 0.1260 0.1488 -0.0086 0.0287 0.0012 305 ILE A CD1 1760 N N . GLN A 224 ? 0.0972 0.0765 0.0942 -0.0069 0.0318 0.0078 306 GLN A N 1761 C CA . GLN A 224 ? 0.1121 0.0900 0.1040 -0.0063 0.0318 0.0094 306 GLN A CA 1762 C C . GLN A 224 ? 0.1485 0.1264 0.1381 -0.0061 0.0327 0.0092 306 GLN A C 1763 O O . GLN A 224 ? 0.1681 0.1460 0.1599 -0.0064 0.0347 0.0089 306 GLN A O 1764 C CB . GLN A 224 ? 0.1487 0.1250 0.1409 -0.0063 0.0329 0.0108 306 GLN A CB 1765 C CG . GLN A 224 ? 0.2389 0.2149 0.2332 -0.0064 0.0319 0.0109 306 GLN A CG 1766 C CD . GLN A 224 ? 0.3236 0.2980 0.3188 -0.0065 0.0331 0.0122 306 GLN A CD 1767 O OE1 . GLN A 224 ? 0.3673 0.3416 0.3666 -0.0070 0.0346 0.0117 306 GLN A OE1 1768 N NE2 . GLN A 224 ? 0.3771 0.3502 0.3690 -0.0059 0.0324 0.0138 306 GLN A NE2 1769 N N . ILE A 225 ? 0.1346 0.1126 0.1201 -0.0055 0.0314 0.0093 307 ILE A N 1770 C CA . ILE A 225 ? 0.1300 0.1083 0.1134 -0.0053 0.0321 0.0088 307 ILE A CA 1771 C C . ILE A 225 ? 0.1791 0.1561 0.1573 -0.0048 0.0321 0.0101 307 ILE A C 1772 O O . ILE A 225 ? 0.1749 0.1514 0.1500 -0.0043 0.0304 0.0109 307 ILE A O 1773 C CB . ILE A 225 ? 0.1463 0.1262 0.1296 -0.0052 0.0304 0.0075 307 ILE A CB 1774 C CG1 . ILE A 225 ? 0.1353 0.1165 0.1236 -0.0058 0.0303 0.0063 307 ILE A CG1 1775 C CG2 . ILE A 225 ? 0.1319 0.1119 0.1134 -0.0050 0.0312 0.0068 307 ILE A CG2 1776 C CD1 . ILE A 225 ? 0.1086 0.0912 0.0967 -0.0056 0.0285 0.0053 307 ILE A CD1 1777 N N . ASP A 226 ? 0.1483 0.1246 0.1257 -0.0049 0.0341 0.0102 308 ASP A N 1778 C CA . ASP A 226 ? 0.1770 0.1521 0.1492 -0.0044 0.0344 0.0111 308 ASP A CA 1779 C C . ASP A 226 ? 0.1587 0.1347 0.1291 -0.0042 0.0339 0.0099 308 ASP A C 1780 O O . ASP A 226 ? 0.1501 0.1265 0.1223 -0.0044 0.0355 0.0088 308 ASP A O 1781 C CB . ASP A 226 ? 0.1640 0.1377 0.1363 -0.0047 0.0371 0.0119 308 ASP A CB 1782 C CG . ASP A 226 ? 0.2312 0.2037 0.1980 -0.0042 0.0376 0.0129 308 ASP A CG 1783 O OD1 . ASP A 226 ? 0.2191 0.1918 0.1821 -0.0038 0.0360 0.0127 308 ASP A OD1 1784 O OD2 . ASP A 226 ? 0.2522 0.2232 0.2183 -0.0044 0.0396 0.0140 308 ASP A OD2 1785 N N . PRO A 227 ? 0.1497 0.1259 0.1167 -0.0037 0.0317 0.0099 309 PRO A N 1786 C CA . PRO A 227 ? 0.1445 0.1216 0.1101 -0.0034 0.0309 0.0086 309 PRO A CA 1787 C C . PRO A 227 ? 0.1630 0.1392 0.1248 -0.0032 0.0322 0.0086 309 PRO A C 1788 O O . PRO A 227 ? 0.1654 0.1422 0.1261 -0.0030 0.0320 0.0074 309 PRO A O 1789 C CB . PRO A 227 ? 0.1610 0.1385 0.1245 -0.0030 0.0281 0.0088 309 PRO A CB 1790 C CG . PRO A 227 ? 0.1759 0.1522 0.1375 -0.0028 0.0277 0.0105 309 PRO A CG 1791 C CD . PRO A 227 ? 0.1790 0.1547 0.1438 -0.0033 0.0297 0.0111 309 PRO A CD 1792 N N . VAL A 228 ? 0.1870 0.1618 0.1466 -0.0032 0.0335 0.0099 310 VAL A N 1793 C CA . VAL A 228 ? 0.1976 0.1713 0.1534 -0.0030 0.0350 0.0100 310 VAL A CA 1794 C C . VAL A 228 ? 0.2148 0.1885 0.1735 -0.0035 0.0380 0.0094 310 VAL A C 1795 O O . VAL A 228 ? 0.2020 0.1760 0.1604 -0.0034 0.0389 0.0081 310 VAL A O 1796 C CB . VAL A 228 ? 0.2050 0.1771 0.1565 -0.0027 0.0350 0.0119 310 VAL A CB 1797 C CG1 . VAL A 228 ? 0.2219 0.1930 0.1694 -0.0026 0.0368 0.0120 310 VAL A CG1 1798 C CG2 . VAL A 228 ? 0.1811 0.1534 0.1298 -0.0022 0.0320 0.0125 310 VAL A CG2 1799 N N . ALA A 229 ? 0.1651 0.1383 0.1271 -0.0039 0.0394 0.0101 311 ALA A N 1800 C CA . ALA A 229 ? 0.2144 0.1876 0.1802 -0.0044 0.0421 0.0094 311 ALA A CA 1801 C C . ALA A 229 ? 0.2246 0.1996 0.1954 -0.0047 0.0417 0.0077 311 ALA A C 1802 O O . ALA A 229 ? 0.1888 0.1643 0.1628 -0.0050 0.0437 0.0067 311 ALA A O 1803 C CB . ALA A 229 ? 0.2113 0.1836 0.1795 -0.0048 0.0436 0.0107 311 ALA A CB 1804 N N . MET A 230 ? 0.1614 0.1376 0.1330 -0.0045 0.0392 0.0073 312 MET A N 1805 C CA . MET A 230 ? 0.1547 0.1326 0.1309 -0.0048 0.0386 0.0058 312 MET A CA 1806 C C . MET A 230 ? 0.1607 0.1390 0.1427 -0.0054 0.0402 0.0055 312 MET A C 1807 O O . MET A 230 ? 0.1624 0.1416 0.1483 -0.0058 0.0413 0.0043 312 MET A O 1808 C CB . MET A 230 ? 0.1318 0.1105 0.1076 -0.0046 0.0388 0.0043 312 MET A CB 1809 C CG . MET A 230 ? 0.1520 0.1304 0.1225 -0.0040 0.0370 0.0043 312 MET A CG 1810 S SD . MET A 230 ? 0.2058 0.1853 0.1761 -0.0038 0.0368 0.0024 312 MET A SD 1811 C CE . MET A 230 ? 0.2645 0.2431 0.2348 -0.0040 0.0401 0.0020 312 MET A CE 1812 N N . THR A 231 ? 0.1462 0.1238 0.1289 -0.0056 0.0401 0.0067 313 THR A N 1813 C CA . THR A 231 ? 0.1408 0.1187 0.1289 -0.0062 0.0413 0.0066 313 THR A CA 1814 C C . THR A 231 ? 0.1567 0.1348 0.1462 -0.0063 0.0394 0.0070 313 THR A C 1815 O O . THR A 231 ? 0.1663 0.1441 0.1521 -0.0059 0.0376 0.0077 313 THR A O 1816 C CB . THR A 231 ? 0.1790 0.1551 0.1668 -0.0064 0.0438 0.0077 313 THR A CB 1817 O OG1 . THR A 231 ? 0.1912 0.1658 0.1740 -0.0060 0.0433 0.0094 313 THR A OG1 1818 C CG2 . THR A 231 ? 0.2197 0.1956 0.2071 -0.0064 0.0460 0.0071 313 THR A CG2 1819 N N . HIS A 232 ? 0.1322 0.1110 0.1270 -0.0068 0.0399 0.0065 314 HIS A N 1820 C CA . HIS A 232 ? 0.1500 0.1291 0.1464 -0.0070 0.0383 0.0067 314 HIS A CA 1821 C C . HIS A 232 ? 0.1650 0.1439 0.1663 -0.0075 0.0396 0.0066 314 HIS A C 1822 O O . HIS A 232 ? 0.1698 0.1488 0.1743 -0.0079 0.0415 0.0061 314 HIS A O 1823 C CB . HIS A 232 ? 0.1203 0.1012 0.1185 -0.0070 0.0364 0.0053 314 HIS A CB 1824 C CG . HIS A 232 ? 0.1221 0.1046 0.1262 -0.0076 0.0370 0.0038 314 HIS A CG 1825 N ND1 . HIS A 232 ? 0.1481 0.1313 0.1537 -0.0077 0.0381 0.0028 314 HIS A ND1 1826 C CD2 . HIS A 232 ? 0.1349 0.1185 0.1441 -0.0081 0.0365 0.0030 314 HIS A CD2 1827 C CE1 . HIS A 232 ? 0.1752 0.1599 0.1868 -0.0082 0.0383 0.0015 314 HIS A CE1 1828 N NE2 . HIS A 232 ? 0.1326 0.1176 0.1464 -0.0085 0.0372 0.0015 314 HIS A NE2 1829 N N . THR A 233 ? 0.1576 0.1363 0.1598 -0.0076 0.0385 0.0071 315 THR A N 1830 C CA . THR A 233 ? 0.1373 0.1161 0.1447 -0.0082 0.0392 0.0068 315 THR A CA 1831 C C . THR A 233 ? 0.1727 0.1528 0.1823 -0.0084 0.0371 0.0058 315 THR A C 1832 O O . THR A 233 ? 0.1458 0.1263 0.1523 -0.0081 0.0353 0.0059 315 THR A O 1833 C CB . THR A 233 ? 0.2047 0.1815 0.2108 -0.0081 0.0402 0.0084 315 THR A CB 1834 O OG1 . THR A 233 ? 0.2100 0.1861 0.2120 -0.0076 0.0385 0.0096 315 THR A OG1 1835 C CG2 . THR A 233 ? 0.3059 0.2813 0.3097 -0.0079 0.0424 0.0095 315 THR A CG2 1836 N N . SER A 234 ? 0.1242 0.1050 0.1392 -0.0090 0.0372 0.0049 316 SER A N 1837 C CA . SER A 234 ? 0.1057 0.0875 0.1227 -0.0092 0.0352 0.0040 316 SER A CA 1838 C C . SER A 234 ? 0.1475 0.1289 0.1687 -0.0097 0.0356 0.0038 316 SER A C 1839 O O . SER A 234 ? 0.1377 0.1186 0.1620 -0.0100 0.0373 0.0037 316 SER A O 1840 C CB . SER A 234 ? 0.1157 0.0997 0.1354 -0.0096 0.0341 0.0022 316 SER A CB 1841 O OG . SER A 234 ? 0.1080 0.0931 0.1337 -0.0101 0.0348 0.0009 316 SER A OG 1842 N N . GLN A 235 ? 0.1258 0.1072 0.1470 -0.0098 0.0340 0.0036 317 GLN A N 1843 C CA . GLN A 235 ? 0.1028 0.0841 0.1283 -0.0103 0.0339 0.0030 317 GLN A CA 1844 C C . GLN A 235 ? 0.1249 0.1069 0.1502 -0.0104 0.0318 0.0022 317 GLN A C 1845 O O . GLN A 235 ? 0.1159 0.0989 0.1393 -0.0103 0.0305 0.0017 317 GLN A O 1846 C CB . GLN A 235 ? 0.1217 0.1009 0.1459 -0.0100 0.0353 0.0047 317 GLN A CB 1847 C CG . GLN A 235 ? 0.1276 0.1053 0.1464 -0.0093 0.0346 0.0064 317 GLN A CG 1848 C CD . GLN A 235 ? 0.2369 0.2127 0.2554 -0.0091 0.0358 0.0080 317 GLN A CD 1849 O OE1 . GLN A 235 ? 0.2062 0.1809 0.2227 -0.0089 0.0373 0.0093 317 GLN A OE1 1850 N NE2 . GLN A 235 ? 0.1711 0.1465 0.1915 -0.0093 0.0351 0.0078 317 GLN A NE2 1851 N N . TYR A 236 ? 0.1089 0.0902 0.1362 -0.0106 0.0314 0.0020 318 TYR A N 1852 C CA . TYR A 236 ? 0.1093 0.0908 0.1359 -0.0107 0.0296 0.0013 318 TYR A CA 1853 C C . TYR A 236 ? 0.1142 0.0937 0.1380 -0.0102 0.0298 0.0030 318 TYR A C 1854 O O . TYR A 236 ? 0.1290 0.1072 0.1525 -0.0099 0.0313 0.0043 318 TYR A O 1855 C CB . TYR A 236 ? 0.0978 0.0805 0.1298 -0.0114 0.0287 -0.0008 318 TYR A CB 1856 C CG . TYR A 236 ? 0.0984 0.0832 0.1333 -0.0119 0.0277 -0.0027 318 TYR A CG 1857 C CD1 . TYR A 236 ? 0.0981 0.0838 0.1365 -0.0121 0.0288 -0.0032 318 TYR A CD1 1858 C CD2 . TYR A 236 ? 0.0874 0.0735 0.1219 -0.0122 0.0256 -0.0040 318 TYR A CD2 1859 C CE1 . TYR A 236 ? 0.1134 0.1013 0.1549 -0.0125 0.0277 -0.0049 318 TYR A CE1 1860 C CE2 . TYR A 236 ? 0.0953 0.0835 0.1326 -0.0126 0.0245 -0.0057 318 TYR A CE2 1861 C CZ . TYR A 236 ? 0.0933 0.0824 0.1342 -0.0127 0.0255 -0.0061 318 TYR A CZ 1862 O OH . TYR A 236 ? 0.1119 0.1032 0.1560 -0.0130 0.0242 -0.0077 318 TYR A OH 1863 N N . ILE A 237 ? 0.1112 0.0905 0.1328 -0.0100 0.0283 0.0030 319 ILE A N 1864 C CA . ILE A 237 ? 0.0958 0.0735 0.1161 -0.0095 0.0283 0.0042 319 ILE A CA 1865 C C . ILE A 237 ? 0.0839 0.0612 0.1089 -0.0100 0.0289 0.0033 319 ILE A C 1866 O O . ILE A 237 ? 0.1147 0.0931 0.1432 -0.0106 0.0279 0.0012 319 ILE A O 1867 C CB . ILE A 237 ? 0.1118 0.0894 0.1297 -0.0093 0.0266 0.0040 319 ILE A CB 1868 C CG1 . ILE A 237 ? 0.1092 0.0872 0.1225 -0.0088 0.0260 0.0048 319 ILE A CG1 1869 C CG2 . ILE A 237 ? 0.1065 0.0824 0.1236 -0.0087 0.0266 0.0051 319 ILE A CG2 1870 C CD1 . ILE A 237 ? 0.1210 0.0990 0.1320 -0.0085 0.0245 0.0046 319 ILE A CD1 1871 N N . CYS A 238 ? 0.1144 0.0902 0.1397 -0.0097 0.0303 0.0047 320 CYS A N 1872 C CA . CYS A 238 ? 0.1299 0.1053 0.1599 -0.0101 0.0311 0.0040 320 CYS A CA 1873 C C . CYS A 238 ? 0.1489 0.1240 0.1805 -0.0102 0.0299 0.0030 320 CYS A C 1874 O O . CYS A 238 ? 0.1350 0.1104 0.1711 -0.0107 0.0299 0.0015 320 CYS A O 1875 C CB . CYS A 238 ? 0.1427 0.1163 0.1721 -0.0098 0.0328 0.0061 320 CYS A CB 1876 S SG . CYS A 238 ? 0.2010 0.1747 0.2302 -0.0098 0.0348 0.0069 320 CYS A SG 1877 N N . SER A 239 ? 0.1456 0.1200 0.1737 -0.0097 0.0289 0.0039 321 SER A N 1878 C CA . SER A 239 ? 0.1540 0.1278 0.1832 -0.0096 0.0281 0.0032 321 SER A CA 1879 C C . SER A 239 ? 0.1133 0.0883 0.1457 -0.0103 0.0269 0.0004 321 SER A C 1880 O O . SER A 239 ? 0.1200 0.0965 0.1521 -0.0107 0.0260 -0.0009 321 SER A O 1881 C CB . SER A 239 ? 0.1214 0.0945 0.1461 -0.0088 0.0271 0.0044 321 SER A CB 1882 O OG . SER A 239 ? 0.1097 0.0821 0.1356 -0.0087 0.0264 0.0037 321 SER A OG 1883 N N . PRO A 240 ? 0.1239 0.0983 0.1593 -0.0104 0.0268 -0.0007 322 PRO A N 1884 C CA . PRO A 240 ? 0.1197 0.0953 0.1576 -0.0110 0.0255 -0.0035 322 PRO A CA 1885 C C . PRO A 240 ? 0.1157 0.0911 0.1506 -0.0107 0.0241 -0.0041 322 PRO A C 1886 O O . PRO A 240 ? 0.1196 0.0958 0.1555 -0.0111 0.0228 -0.0065 322 PRO A O 1887 C CB . PRO A 240 ? 0.1343 0.1090 0.1760 -0.0111 0.0261 -0.0040 322 PRO A CB 1888 C CG . PRO A 240 ? 0.1424 0.1152 0.1822 -0.0103 0.0272 -0.0014 322 PRO A CG 1889 C CD . PRO A 240 ? 0.1175 0.0903 0.1542 -0.0100 0.0280 0.0007 322 PRO A CD 1890 N N . VAL A 241 ? 0.0985 0.0731 0.1295 -0.0100 0.0242 -0.0020 323 VAL A N 1891 C CA . VAL A 241 ? 0.1397 0.1143 0.1677 -0.0097 0.0230 -0.0025 323 VAL A CA 1892 C C . VAL A 241 ? 0.1024 0.0784 0.1287 -0.0101 0.0223 -0.0032 323 VAL A C 1893 O O . VAL A 241 ? 0.1101 0.0862 0.1336 -0.0098 0.0226 -0.0014 323 VAL A O 1894 C CB . VAL A 241 ? 0.1071 0.0803 0.1318 -0.0087 0.0233 -0.0001 323 VAL A CB 1895 C CG1 . VAL A 241 ? 0.1141 0.0874 0.1361 -0.0084 0.0222 -0.0006 323 VAL A CG1 1896 C CG2 . VAL A 241 ? 0.1016 0.0734 0.1284 -0.0083 0.0240 0.0006 323 VAL A CG2 1897 N N . LEU A 242 ? 0.0781 0.0553 0.1060 -0.0108 0.0211 -0.0058 324 LEU A N 1898 C CA . LEU A 242 ? 0.1140 0.0928 0.1412 -0.0112 0.0202 -0.0067 324 LEU A CA 1899 C C . LEU A 242 ? 0.0894 0.0693 0.1117 -0.0103 0.0188 -0.0063 324 LEU A C 1900 O O . LEU A 242 ? 0.1053 0.0849 0.1260 -0.0099 0.0180 -0.0068 324 LEU A O 1901 C CB . LEU A 242 ? 0.0720 0.0522 0.1025 -0.0120 0.0189 -0.0096 324 LEU A CB 1902 C CG . LEU A 242 ? 0.1100 0.0905 0.1449 -0.0123 0.0197 -0.0100 324 LEU A CG 1903 C CD1 . LEU A 242 ? 0.1209 0.1029 0.1586 -0.0129 0.0180 -0.0129 324 LEU A CD1 1904 C CD2 . LEU A 242 ? 0.1170 0.0978 0.1528 -0.0123 0.0211 -0.0083 324 LEU A CD2 1905 N N . THR A 243 ? 0.1096 0.0906 0.1296 -0.0101 0.0185 -0.0054 325 THR A N 1906 C CA . THR A 243 ? 0.1028 0.0846 0.1184 -0.0092 0.0174 -0.0046 325 THR A CA 1907 C C . THR A 243 ? 0.0898 0.0737 0.1038 -0.0092 0.0158 -0.0056 325 THR A C 1908 O O . THR A 243 ? 0.1199 0.1044 0.1304 -0.0085 0.0150 -0.0049 325 THR A O 1909 C CB . THR A 243 ? 0.1057 0.0864 0.1186 -0.0086 0.0184 -0.0020 325 THR A CB 1910 O OG1 . THR A 243 ? 0.0876 0.0686 0.1009 -0.0089 0.0194 -0.0011 325 THR A OG1 1911 C CG2 . THR A 243 ? 0.0976 0.0761 0.1115 -0.0085 0.0197 -0.0008 325 THR A CG2 1912 N N . ASP A 244 ? 0.0847 0.0698 0.1015 -0.0098 0.0151 -0.0073 326 ASP A N 1913 C CA . ASP A 244 ? 0.0711 0.0581 0.0865 -0.0097 0.0133 -0.0083 326 ASP A CA 1914 C C . ASP A 244 ? 0.0951 0.0824 0.1091 -0.0095 0.0117 -0.0100 326 ASP A C 1915 O O . ASP A 244 ? 0.1240 0.1101 0.1384 -0.0095 0.0121 -0.0105 326 ASP A O 1916 C CB . ASP A 244 ? 0.0983 0.0865 0.1173 -0.0104 0.0131 -0.0094 326 ASP A CB 1917 C CG . ASP A 244 ? 0.1344 0.1244 0.1519 -0.0101 0.0118 -0.0095 326 ASP A CG 1918 O OD1 . ASP A 244 ? 0.1031 0.0934 0.1168 -0.0094 0.0108 -0.0089 326 ASP A OD1 1919 O OD2 . ASP A 244 ? 0.1244 0.1155 0.1449 -0.0105 0.0117 -0.0100 326 ASP A OD2 1920 N N . ASN A 245 ? 0.0752 0.0640 0.0876 -0.0093 0.0100 -0.0108 327 ASN A N 1921 C CA . ASN A 245 ? 0.1053 0.0944 0.1160 -0.0092 0.0084 -0.0125 327 ASN A CA 1922 C C . ASN A 245 ? 0.1116 0.1025 0.1223 -0.0093 0.0064 -0.0137 327 ASN A C 1923 O O . ASN A 245 ? 0.1026 0.0944 0.1121 -0.0090 0.0060 -0.0126 327 ASN A O 1924 C CB . ASN A 245 ? 0.0867 0.0753 0.0933 -0.0084 0.0084 -0.0116 327 ASN A CB 1925 C CG . ASN A 245 ? 0.1704 0.1593 0.1749 -0.0083 0.0071 -0.0132 327 ASN A CG 1926 O OD1 . ASN A 245 ? 0.1273 0.1172 0.1293 -0.0080 0.0057 -0.0134 327 ASN A OD1 1927 N ND2 . ASN A 245 ? 0.1248 0.1126 0.1302 -0.0085 0.0076 -0.0144 327 ASN A ND2 1928 N N . PRO A 246 ? 0.1169 0.1081 0.1289 -0.0097 0.0051 -0.0159 328 PRO A N 1929 C CA . PRO A 246 ? 0.1139 0.1040 0.1276 -0.0102 0.0054 -0.0175 328 PRO A CA 1930 C C . PRO A 246 ? 0.1254 0.1149 0.1440 -0.0109 0.0070 -0.0174 328 PRO A C 1931 O O . PRO A 246 ? 0.1336 0.1236 0.1542 -0.0111 0.0077 -0.0163 328 PRO A O 1932 C CB . PRO A 246 ? 0.1451 0.1362 0.1588 -0.0104 0.0031 -0.0199 328 PRO A CB 1933 C CG . PRO A 246 ? 0.1628 0.1556 0.1775 -0.0104 0.0019 -0.0195 328 PRO A CG 1934 C CD . PRO A 246 ? 0.1635 0.1563 0.1755 -0.0098 0.0029 -0.0170 328 PRO A CD 1935 N N . ARG A 247 ? 0.0924 0.0805 0.1129 -0.0113 0.0077 -0.0185 329 ARG A N 1936 C CA . ARG A 247 ? 0.0801 0.0673 0.1054 -0.0119 0.0094 -0.0182 329 ARG A CA 1937 C C . ARG A 247 ? 0.1351 0.1212 0.1631 -0.0125 0.0094 -0.0203 329 ARG A C 1938 O O . ARG A 247 ? 0.0968 0.0825 0.1223 -0.0122 0.0085 -0.0217 329 ARG A O 1939 C CB . ARG A 247 ? 0.0778 0.0636 0.1019 -0.0115 0.0116 -0.0155 329 ARG A CB 1940 C CG . ARG A 247 ? 0.0993 0.0838 0.1205 -0.0109 0.0120 -0.0151 329 ARG A CG 1941 C CD . ARG A 247 ? 0.1091 0.0921 0.1299 -0.0105 0.0139 -0.0125 329 ARG A CD 1942 N NE . ARG A 247 ? 0.0991 0.0808 0.1182 -0.0099 0.0143 -0.0124 329 ARG A NE 1943 C CZ . ARG A 247 ? 0.1093 0.0913 0.1245 -0.0091 0.0138 -0.0115 329 ARG A CZ 1944 N NH1 . ARG A 247 ? 0.0876 0.0709 0.1000 -0.0088 0.0130 -0.0107 329 ARG A NH1 1945 N NH2 . ARG A 247 ? 0.0839 0.0648 0.0984 -0.0086 0.0143 -0.0116 329 ARG A NH2 1946 N N . PRO A 248 ? 0.1295 0.1153 0.1625 -0.0132 0.0104 -0.0206 330 PRO A N 1947 C CA . PRO A 248 ? 0.1296 0.1147 0.1647 -0.0133 0.0105 -0.0218 330 PRO A CA 1948 C C . PRO A 248 ? 0.1417 0.1248 0.1757 -0.0129 0.0123 -0.0205 330 PRO A C 1949 O O . PRO A 248 ? 0.1428 0.1249 0.1745 -0.0125 0.0134 -0.0185 330 PRO A O 1950 C CB . PRO A 248 ? 0.1361 0.1219 0.1764 -0.0137 0.0114 -0.0214 330 PRO A CB 1951 C CG . PRO A 248 ? 0.1808 0.1681 0.2215 -0.0139 0.0110 -0.0208 330 PRO A CG 1952 C CD . PRO A 248 ? 0.1250 0.1116 0.1612 -0.0135 0.0112 -0.0194 330 PRO A CD 1953 N N . ASN A 249 ? 0.1261 0.1086 0.1617 -0.0128 0.0124 -0.0217 331 ASN A N 1954 C CA . ASN A 249 ? 0.1465 0.1271 0.1821 -0.0124 0.0141 -0.0204 331 ASN A CA 1955 C C . ASN A 249 ? 0.1438 0.1236 0.1820 -0.0125 0.0161 -0.0179 331 ASN A C 1956 O O . ASN A 249 ? 0.1450 0.1258 0.1861 -0.0129 0.0163 -0.0178 331 ASN A O 1957 C CB . ASN A 249 ? 0.1576 0.1377 0.1945 -0.0124 0.0138 -0.0224 331 ASN A CB 1958 C CG . ASN A 249 ? 0.2055 0.1858 0.2385 -0.0121 0.0122 -0.0244 331 ASN A CG 1959 O OD1 . ASN A 249 ? 0.2025 0.1824 0.2318 -0.0116 0.0124 -0.0237 331 ASN A OD1 1960 N ND2 . ASN A 249 ? 0.2343 0.2154 0.2681 -0.0124 0.0107 -0.0268 331 ASN A ND2 1961 N N . ASP A 250 ? 0.0864 0.0646 0.1235 -0.0119 0.0176 -0.0159 332 ASP A N 1962 C CA . ASP A 250 ? 0.1166 0.0940 0.1553 -0.0118 0.0194 -0.0134 332 ASP A CA 1963 C C . ASP A 250 ? 0.1563 0.1335 0.1996 -0.0121 0.0201 -0.0139 332 ASP A C 1964 O O . ASP A 250 ? 0.1764 0.1529 0.2211 -0.0120 0.0201 -0.0150 332 ASP A O 1965 C CB . ASP A 250 ? 0.1403 0.1160 0.1767 -0.0110 0.0205 -0.0111 332 ASP A CB 1966 C CG . ASP A 250 ? 0.1713 0.1469 0.2034 -0.0106 0.0201 -0.0100 332 ASP A CG 1967 O OD1 . ASP A 250 ? 0.1447 0.1215 0.1757 -0.0110 0.0194 -0.0103 332 ASP A OD1 1968 O OD2 . ASP A 250 ? 0.1573 0.1318 0.1873 -0.0099 0.0205 -0.0087 332 ASP A OD2 1969 N N . PRO A 251 ? 0.1060 0.0839 0.1519 -0.0125 0.0209 -0.0132 333 PRO A N 1970 C CA . PRO A 251 ? 0.1303 0.1079 0.1807 -0.0127 0.0220 -0.0133 333 PRO A CA 1971 C C . PRO A 251 ? 0.1361 0.1118 0.1863 -0.0122 0.0239 -0.0106 333 PRO A C 1972 O O . PRO A 251 ? 0.1305 0.1052 0.1771 -0.0115 0.0241 -0.0090 333 PRO A O 1973 C CB . PRO A 251 ? 0.1330 0.1120 0.1856 -0.0132 0.0221 -0.0134 333 PRO A CB 1974 C CG . PRO A 251 ? 0.1403 0.1195 0.1890 -0.0129 0.0223 -0.0117 333 PRO A CG 1975 C CD . PRO A 251 ? 0.0817 0.0606 0.1264 -0.0126 0.0209 -0.0123 333 PRO A CD 1976 N N . ASN A 252 ? 0.1052 0.0805 0.1591 -0.0123 0.0252 -0.0101 334 ASN A N 1977 C CA . ASN A 252 ? 0.1234 0.0968 0.1770 -0.0118 0.0270 -0.0074 334 ASN A CA 1978 C C . ASN A 252 ? 0.1149 0.0883 0.1684 -0.0118 0.0285 -0.0054 334 ASN A C 1979 O O . ASN A 252 ? 0.1263 0.0983 0.1786 -0.0113 0.0298 -0.0029 334 ASN A O 1980 C CB . ASN A 252 ? 0.1516 0.1241 0.2091 -0.0118 0.0277 -0.0080 334 ASN A CB 1981 C CG . ASN A 252 ? 0.2087 0.1806 0.2655 -0.0115 0.0268 -0.0091 334 ASN A CG 1982 O OD1 . ASN A 252 ? 0.1863 0.1582 0.2393 -0.0111 0.0259 -0.0089 334 ASN A OD1 1983 N ND2 . ASN A 252 ? 0.1596 0.1310 0.2200 -0.0117 0.0271 -0.0103 334 ASN A ND2 1984 N N . ILE A 253 ? 0.1458 0.1209 0.2007 -0.0124 0.0281 -0.0066 335 ILE A N 1985 C CA . ILE A 253 ? 0.1402 0.1155 0.1949 -0.0124 0.0294 -0.0051 335 ILE A CA 1986 C C . ILE A 253 ? 0.1270 0.1039 0.1793 -0.0125 0.0283 -0.0057 335 ILE A C 1987 O O . ILE A 253 ? 0.1204 0.0989 0.1743 -0.0130 0.0267 -0.0081 335 ILE A O 1988 C CB . ILE A 253 ? 0.1620 0.1378 0.2220 -0.0129 0.0305 -0.0059 335 ILE A CB 1989 C CG1 . ILE A 253 ? 0.1710 0.1453 0.2339 -0.0128 0.0315 -0.0055 335 ILE A CG1 1990 C CG2 . ILE A 253 ? 0.1372 0.1130 0.1967 -0.0128 0.0321 -0.0042 335 ILE A CG2 1991 C CD1 . ILE A 253 ? 0.1757 0.1503 0.2440 -0.0133 0.0328 -0.0061 335 ILE A CD1 1992 N N . GLY A 254 ? 0.1170 0.0933 0.1651 -0.0121 0.0289 -0.0036 336 GLY A N 1993 C CA . GLY A 254 ? 0.1215 0.0993 0.1675 -0.0122 0.0280 -0.0040 336 GLY A CA 1994 C C . GLY A 254 ? 0.1307 0.1095 0.1789 -0.0125 0.0291 -0.0040 336 GLY A C 1995 O O . GLY A 254 ? 0.1353 0.1139 0.1874 -0.0127 0.0302 -0.0042 336 GLY A O 1996 N N . LYS A 255 ? 0.1137 0.0934 0.1595 -0.0124 0.0288 -0.0037 337 LYS A N 1997 C CA . LYS A 255 ? 0.1147 0.0954 0.1625 -0.0126 0.0298 -0.0037 337 LYS A CA 1998 C C . LYS A 255 ? 0.1777 0.1579 0.2209 -0.0121 0.0308 -0.0017 337 LYS A C 1999 O O . LYS A 255 ? 0.1440 0.1246 0.1836 -0.0119 0.0296 -0.0016 337 LYS A O 2000 C CB . LYS A 255 ? 0.1117 0.0947 0.1626 -0.0132 0.0281 -0.0062 337 LYS A CB 2001 C CG . LYS A 255 ? 0.1620 0.1457 0.2179 -0.0137 0.0272 -0.0084 337 LYS A CG 2002 C CD . LYS A 255 ? 0.1882 0.1720 0.2489 -0.0139 0.0290 -0.0084 337 LYS A CD 2003 C CE . LYS A 255 ? 0.2177 0.2033 0.2810 -0.0141 0.0288 -0.0093 337 LYS A CE 2004 N NZ . LYS A 255 ? 0.2142 0.1999 0.2827 -0.0143 0.0305 -0.0095 337 LYS A NZ 2005 N N . CYS A 256 ? 0.1247 0.1040 0.1681 -0.0119 0.0328 -0.0003 338 CYS A N 2006 C CA . CYS A 256 ? 0.1468 0.1254 0.1856 -0.0114 0.0338 0.0016 338 CYS A CA 2007 C C . CYS A 256 ? 0.1868 0.1670 0.2264 -0.0116 0.0340 0.0007 338 CYS A C 2008 O O . CYS A 256 ? 0.1386 0.1188 0.1741 -0.0112 0.0339 0.0016 338 CYS A O 2009 C CB . CYS A 256 ? 0.1691 0.1457 0.2072 -0.0111 0.0360 0.0036 338 CYS A CB 2010 S SG . CYS A 256 ? 0.2119 0.1865 0.2491 -0.0108 0.0361 0.0050 338 CYS A SG 2011 N N . ASN A 257 ? 0.1191 0.1006 0.1641 -0.0122 0.0341 -0.0009 339 ASN A N 2012 C CA . ASN A 257 ? 0.1576 0.1405 0.2042 -0.0123 0.0347 -0.0015 339 ASN A CA 2013 C C . ASN A 257 ? 0.1510 0.1362 0.2017 -0.0128 0.0329 -0.0040 339 ASN A C 2014 O O . ASN A 257 ? 0.1384 0.1249 0.1921 -0.0129 0.0334 -0.0048 339 ASN A O 2015 C CB . ASN A 257 ? 0.1475 0.1293 0.1965 -0.0123 0.0372 -0.0008 339 ASN A CB 2016 C CG . ASN A 257 ? 0.2019 0.1815 0.2462 -0.0118 0.0390 0.0017 339 ASN A CG 2017 O OD1 . ASN A 257 ? 0.2559 0.2339 0.3010 -0.0117 0.0401 0.0026 339 ASN A OD1 2018 N ND2 . ASN A 257 ? 0.1503 0.1295 0.1895 -0.0113 0.0391 0.0028 339 ASN A ND2 2019 N N . ASP A 258 ? 0.1237 0.1096 0.1746 -0.0130 0.0307 -0.0052 340 ASP A N 2020 C CA . ASP A 258 ? 0.1045 0.0926 0.1588 -0.0134 0.0285 -0.0075 340 ASP A CA 2021 C C . ASP A 258 ? 0.1152 0.1035 0.1669 -0.0135 0.0263 -0.0082 340 ASP A C 2022 O O . ASP A 258 ? 0.1068 0.0935 0.1557 -0.0133 0.0265 -0.0072 340 ASP A O 2023 C CB . ASP A 258 ? 0.1392 0.1281 0.1997 -0.0138 0.0285 -0.0091 340 ASP A CB 2024 C CG . ASP A 258 ? 0.2439 0.2340 0.3084 -0.0139 0.0295 -0.0096 340 ASP A CG 2025 O OD1 . ASP A 258 ? 0.1618 0.1532 0.2255 -0.0138 0.0288 -0.0099 340 ASP A OD1 2026 O OD2 . ASP A 258 ? 0.1705 0.1602 0.2391 -0.0141 0.0309 -0.0098 340 ASP A OD2 2027 N N . PRO A 259 ? 0.1246 0.1149 0.1773 -0.0137 0.0240 -0.0099 341 PRO A N 2028 C CA . PRO A 259 ? 0.1206 0.1109 0.1708 -0.0138 0.0218 -0.0108 341 PRO A CA 2029 C C . PRO A 259 ? 0.1660 0.1558 0.2182 -0.0141 0.0210 -0.0120 341 PRO A C 2030 O O . PRO A 259 ? 0.1326 0.1232 0.1895 -0.0143 0.0208 -0.0133 341 PRO A O 2031 C CB . PRO A 259 ? 0.1122 0.1048 0.1640 -0.0140 0.0194 -0.0126 341 PRO A CB 2032 C CG . PRO A 259 ? 0.1456 0.1394 0.2024 -0.0141 0.0202 -0.0132 341 PRO A CG 2033 C CD . PRO A 259 ? 0.1031 0.0954 0.1589 -0.0138 0.0233 -0.0111 341 PRO A CD 2034 N N . TYR A 260 ? 0.1054 0.0937 0.1543 -0.0139 0.0207 -0.0116 342 TYR A N 2035 C CA . TYR A 260 ? 0.1274 0.1153 0.1778 -0.0141 0.0197 -0.0131 342 TYR A CA 2036 C C . TYR A 260 ? 0.1183 0.1079 0.1689 -0.0143 0.0167 -0.0155 342 TYR A C 2037 O O . TYR A 260 ? 0.1208 0.1106 0.1678 -0.0142 0.0155 -0.0156 342 TYR A O 2038 C CB . TYR A 260 ? 0.1180 0.1039 0.1649 -0.0138 0.0203 -0.0118 342 TYR A CB 2039 C CG . TYR A 260 ? 0.1103 0.0955 0.1594 -0.0139 0.0199 -0.0132 342 TYR A CG 2040 C CD1 . TYR A 260 ? 0.1661 0.1517 0.2143 -0.0140 0.0177 -0.0153 342 TYR A CD1 2041 C CD2 . TYR A 260 ? 0.1661 0.1504 0.2183 -0.0139 0.0216 -0.0125 342 TYR A CD2 2042 C CE1 . TYR A 260 ? 0.1910 0.1761 0.2412 -0.0141 0.0173 -0.0166 342 TYR A CE1 2043 C CE2 . TYR A 260 ? 0.1721 0.1559 0.2266 -0.0141 0.0212 -0.0138 342 TYR A CE2 2044 C CZ . TYR A 260 ? 0.2188 0.2031 0.2723 -0.0142 0.0191 -0.0159 342 TYR A CZ 2045 O OH . TYR A 260 ? 0.2896 0.2733 0.3452 -0.0143 0.0187 -0.0174 342 TYR A OH 2046 N N . PRO A 261 ? 0.0962 0.0868 0.1508 -0.0147 0.0155 -0.0175 343 PRO A N 2047 C CA . PRO A 261 ? 0.1112 0.1036 0.1664 -0.0148 0.0126 -0.0198 343 PRO A CA 2048 C C . PRO A 261 ? 0.1477 0.1395 0.2001 -0.0147 0.0107 -0.0214 343 PRO A C 2049 O O . PRO A 261 ? 0.1628 0.1529 0.2140 -0.0147 0.0117 -0.0210 343 PRO A O 2050 C CB . PRO A 261 ? 0.1696 0.1631 0.2305 -0.0151 0.0125 -0.0211 343 PRO A CB 2051 C CG . PRO A 261 ? 0.1501 0.1419 0.2126 -0.0152 0.0147 -0.0202 343 PRO A CG 2052 C CD . PRO A 261 ? 0.1653 0.1554 0.2242 -0.0148 0.0170 -0.0176 343 PRO A CD 2053 N N . GLY A 262 ? 0.1583 0.1515 0.2095 -0.0147 0.0079 -0.0231 344 GLY A N 2054 C CA . GLY A 262 ? 0.1560 0.1488 0.2040 -0.0146 0.0060 -0.0247 344 GLY A CA 2055 C C . GLY A 262 ? 0.1979 0.1914 0.2416 -0.0142 0.0039 -0.0251 344 GLY A C 2056 O O . GLY A 262 ? 0.1589 0.1530 0.2006 -0.0141 0.0015 -0.0269 344 GLY A O 2057 N N . ASN A 263 ? 0.1481 0.1417 0.1902 -0.0141 0.0048 -0.0234 345 ASN A N 2058 C CA . ASN A 263 ? 0.1312 0.1256 0.1695 -0.0138 0.0031 -0.0236 345 ASN A CA 2059 C C . ASN A 263 ? 0.1736 0.1694 0.2138 -0.0138 0.0032 -0.0226 345 ASN A C 2060 O O . ASN A 263 ? 0.1806 0.1758 0.2219 -0.0139 0.0056 -0.0208 345 ASN A O 2061 C CB . ASN A 263 ? 0.1646 0.1575 0.1974 -0.0132 0.0041 -0.0221 345 ASN A CB 2062 C CG . ASN A 263 ? 0.2379 0.2295 0.2684 -0.0131 0.0036 -0.0235 345 ASN A CG 2063 O OD1 . ASN A 263 ? 0.1769 0.1670 0.2093 -0.0134 0.0052 -0.0236 345 ASN A OD1 2064 N ND2 . ASN A 263 ? 0.1670 0.1592 0.1935 -0.0126 0.0015 -0.0245 345 ASN A ND2 2065 N N . ASN A 264 ? 0.1481 0.1457 0.1885 -0.0136 0.0006 -0.0237 346 ASN A N 2066 C CA . ASN A 264 ? 0.1712 0.1704 0.2138 -0.0135 0.0005 -0.0229 346 ASN A CA 2067 C C . ASN A 264 ? 0.1576 0.1575 0.1951 -0.0126 -0.0010 -0.0220 346 ASN A C 2068 O O . ASN A 264 ? 0.1286 0.1281 0.1616 -0.0121 -0.0027 -0.0225 346 ASN A O 2069 C CB . ASN A 264 ? 0.2075 0.2085 0.2547 -0.0135 -0.0011 -0.0242 346 ASN A CB 2070 C CG . ASN A 264 ? 0.2526 0.2534 0.3049 -0.0139 0.0010 -0.0240 346 ASN A CG 2071 O OD1 . ASN A 264 ? 0.2579 0.2573 0.3102 -0.0142 0.0024 -0.0240 346 ASN A OD1 2072 N ND2 . ASN A 264 ? 0.3168 0.3190 0.3736 -0.0139 0.0014 -0.0238 346 ASN A ND2 2073 N N . ASN A 265 ? 0.1293 0.1300 0.1675 -0.0123 -0.0002 -0.0205 347 ASN A N 2074 C CA . ASN A 265 ? 0.0991 0.1007 0.1335 -0.0114 -0.0017 -0.0197 347 ASN A CA 2075 C C . ASN A 265 ? 0.1194 0.1198 0.1472 -0.0107 -0.0017 -0.0186 347 ASN A C 2076 O O . ASN A 265 ? 0.1444 0.1452 0.1687 -0.0101 -0.0038 -0.0187 347 ASN A O 2077 C CB . ASN A 265 ? 0.1347 0.1379 0.1708 -0.0113 -0.0051 -0.0214 347 ASN A CB 2078 C CG . ASN A 265 ? 0.1953 0.1999 0.2386 -0.0120 -0.0053 -0.0226 347 ASN A CG 2079 O OD1 . ASN A 265 ? 0.2066 0.2112 0.2536 -0.0124 -0.0027 -0.0219 347 ASN A OD1 2080 N ND2 . ASN A 265 ? 0.2380 0.2439 0.2830 -0.0119 -0.0083 -0.0242 347 ASN A ND2 2081 N N . ASN A 266 ? 0.1174 0.1162 0.1435 -0.0107 0.0007 -0.0173 348 ASN A N 2082 C CA . ASN A 266 ? 0.1177 0.1154 0.1381 -0.0100 0.0010 -0.0162 348 ASN A CA 2083 C C . ASN A 266 ? 0.1421 0.1384 0.1619 -0.0101 0.0037 -0.0145 348 ASN A C 2084 O O . ASN A 266 ? 0.0963 0.0922 0.1197 -0.0106 0.0054 -0.0143 348 ASN A O 2085 C CB . ASN A 266 ? 0.1347 0.1319 0.1526 -0.0100 -0.0005 -0.0176 348 ASN A CB 2086 C CG . ASN A 266 ? 0.2738 0.2705 0.2859 -0.0092 -0.0010 -0.0166 348 ASN A CG 2087 O OD1 . ASN A 266 ? 0.2766 0.2732 0.2867 -0.0087 0.0000 -0.0148 348 ASN A OD1 2088 N ND2 . ASN A 266 ? 0.3997 0.3962 0.4092 -0.0091 -0.0025 -0.0179 348 ASN A ND2 2089 N N . GLY A 267 ? 0.1108 0.1062 0.1260 -0.0095 0.0041 -0.0133 349 GLY A N 2090 C CA . GLY A 267 ? 0.0963 0.0903 0.1105 -0.0093 0.0064 -0.0117 349 GLY A CA 2091 C C . GLY A 267 ? 0.1195 0.1133 0.1290 -0.0085 0.0062 -0.0103 349 GLY A C 2092 O O . GLY A 267 ? 0.1378 0.1324 0.1452 -0.0082 0.0045 -0.0106 349 GLY A O 2093 N N . VAL A 268 ? 0.0879 0.0804 0.0959 -0.0083 0.0078 -0.0088 350 VAL A N 2094 C CA . VAL A 268 ? 0.0685 0.0608 0.0727 -0.0076 0.0077 -0.0074 350 VAL A CA 2095 C C . VAL A 268 ? 0.0819 0.0735 0.0859 -0.0075 0.0095 -0.0057 350 VAL A C 2096 O O . VAL A 268 ? 0.1013 0.0920 0.1073 -0.0079 0.0109 -0.0055 350 VAL A O 2097 C CB . VAL A 268 ? 0.0703 0.0617 0.0721 -0.0073 0.0076 -0.0075 350 VAL A CB 2098 C CG1 . VAL A 268 ? 0.0880 0.0779 0.0908 -0.0074 0.0092 -0.0069 350 VAL A CG1 2099 C CG2 . VAL A 268 ? 0.0690 0.0606 0.0673 -0.0066 0.0071 -0.0064 350 VAL A CG2 2100 N N . LYS A 269 ? 0.0785 0.0704 0.0800 -0.0069 0.0093 -0.0047 351 LYS A N 2101 C CA . LYS A 269 ? 0.0777 0.0687 0.0781 -0.0067 0.0107 -0.0031 351 LYS A CA 2102 C C . LYS A 269 ? 0.0678 0.0573 0.0670 -0.0065 0.0115 -0.0022 351 LYS A C 2103 O O . LYS A 269 ? 0.0822 0.0716 0.0800 -0.0062 0.0107 -0.0024 351 LYS A O 2104 C CB . LYS A 269 ? 0.0615 0.0530 0.0594 -0.0062 0.0101 -0.0024 351 LYS A CB 2105 C CG . LYS A 269 ? 0.0524 0.0431 0.0486 -0.0059 0.0113 -0.0009 351 LYS A CG 2106 C CD . LYS A 269 ? 0.0867 0.0779 0.0806 -0.0054 0.0105 -0.0005 351 LYS A CD 2107 C CE . LYS A 269 ? 0.0948 0.0850 0.0865 -0.0051 0.0114 0.0009 351 LYS A CE 2108 N NZ . LYS A 269 ? 0.0659 0.0556 0.0585 -0.0054 0.0130 0.0011 351 LYS A NZ 2109 N N . GLY A 270 ? 0.0715 0.0598 0.0713 -0.0067 0.0131 -0.0012 352 GLY A N 2110 C CA . GLY A 270 ? 0.0763 0.0630 0.0754 -0.0065 0.0138 -0.0002 352 GLY A CA 2111 C C . GLY A 270 ? 0.0939 0.0794 0.0916 -0.0063 0.0152 0.0015 352 GLY A C 2112 O O . GLY A 270 ? 0.1050 0.0910 0.1020 -0.0063 0.0156 0.0018 352 GLY A O 2113 N N . PHE A 271 ? 0.0880 0.0718 0.0854 -0.0061 0.0160 0.0026 353 PHE A N 2114 C CA . PHE A 271 ? 0.0696 0.0521 0.0650 -0.0058 0.0171 0.0045 353 PHE A CA 2115 C C . PHE A 271 ? 0.0931 0.0737 0.0895 -0.0059 0.0182 0.0055 353 PHE A C 2116 O O . PHE A 271 ? 0.0997 0.0800 0.0981 -0.0060 0.0180 0.0048 353 PHE A O 2117 C CB . PHE A 271 ? 0.0579 0.0405 0.0498 -0.0051 0.0160 0.0054 353 PHE A CB 2118 C CG . PHE A 271 ? 0.0656 0.0475 0.0569 -0.0045 0.0153 0.0059 353 PHE A CG 2119 C CD1 . PHE A 271 ? 0.0916 0.0744 0.0839 -0.0045 0.0142 0.0048 353 PHE A CD1 2120 C CD2 . PHE A 271 ? 0.0927 0.0729 0.0826 -0.0041 0.0158 0.0077 353 PHE A CD2 2121 C CE1 . PHE A 271 ? 0.0780 0.0601 0.0701 -0.0040 0.0138 0.0052 353 PHE A CE1 2122 C CE2 . PHE A 271 ? 0.0905 0.0701 0.0805 -0.0036 0.0151 0.0082 353 PHE A CE2 2123 C CZ . PHE A 271 ? 0.1028 0.0834 0.0941 -0.0035 0.0142 0.0069 353 PHE A CZ 2124 N N . SER A 272 ? 0.0676 0.0467 0.0624 -0.0057 0.0195 0.0073 354 SER A N 2125 C CA . SER A 272 ? 0.0885 0.0658 0.0837 -0.0054 0.0201 0.0086 354 SER A CA 2126 C C . SER A 272 ? 0.1017 0.0785 0.0935 -0.0046 0.0199 0.0102 354 SER A C 2127 O O . SER A 272 ? 0.1082 0.0858 0.0979 -0.0045 0.0197 0.0102 354 SER A O 2128 C CB . SER A 272 ? 0.1612 0.1381 0.1600 -0.0061 0.0215 0.0081 354 SER A CB 2129 O OG . SER A 272 ? 0.1338 0.1110 0.1323 -0.0062 0.0225 0.0084 354 SER A OG 2130 N N . TYR A 273 ? 0.0784 0.0539 0.0697 -0.0041 0.0197 0.0115 355 TYR A N 2131 C CA . TYR A 273 ? 0.0968 0.0716 0.0852 -0.0036 0.0196 0.0131 355 TYR A CA 2132 C C . TYR A 273 ? 0.1467 0.1202 0.1369 -0.0038 0.0210 0.0139 355 TYR A C 2133 O O . TYR A 273 ? 0.1323 0.1048 0.1245 -0.0037 0.0211 0.0143 355 TYR A O 2134 C CB . TYR A 273 ? 0.0924 0.0667 0.0785 -0.0027 0.0180 0.0142 355 TYR A CB 2135 C CG . TYR A 273 ? 0.0953 0.0710 0.0790 -0.0024 0.0166 0.0137 355 TYR A CG 2136 C CD1 . TYR A 273 ? 0.1035 0.0794 0.0840 -0.0022 0.0162 0.0141 355 TYR A CD1 2137 C CD2 . TYR A 273 ? 0.1095 0.0859 0.0941 -0.0025 0.0159 0.0127 355 TYR A CD2 2138 C CE1 . TYR A 273 ? 0.0907 0.0678 0.0693 -0.0019 0.0149 0.0135 355 TYR A CE1 2139 C CE2 . TYR A 273 ? 0.0674 0.0449 0.0499 -0.0022 0.0147 0.0122 355 TYR A CE2 2140 C CZ . TYR A 273 ? 0.0733 0.0513 0.0531 -0.0019 0.0141 0.0126 355 TYR A CZ 2141 O OH . TYR A 273 ? 0.0891 0.0681 0.0671 -0.0017 0.0129 0.0120 355 TYR A OH 2142 N N . LEU A 274 ? 0.0947 0.0682 0.0844 -0.0040 0.0222 0.0141 356 LEU A N 2143 C CA . LEU A 274 ? 0.1149 0.0873 0.1065 -0.0043 0.0238 0.0148 356 LEU A CA 2144 C C . LEU A 274 ? 0.1290 0.1001 0.1172 -0.0038 0.0239 0.0167 356 LEU A C 2145 O O . LEU A 274 ? 0.1612 0.1325 0.1467 -0.0037 0.0243 0.0170 356 LEU A O 2146 C CB . LEU A 274 ? 0.1151 0.0883 0.1090 -0.0051 0.0254 0.0136 356 LEU A CB 2147 C CG . LEU A 274 ? 0.1321 0.1067 0.1290 -0.0057 0.0250 0.0116 356 LEU A CG 2148 C CD1 . LEU A 274 ? 0.1342 0.1098 0.1332 -0.0063 0.0261 0.0104 356 LEU A CD1 2149 C CD2 . LEU A 274 ? 0.1334 0.1076 0.1340 -0.0060 0.0250 0.0110 356 LEU A CD2 2150 N N . ASP A 275 ? 0.1299 0.0996 0.1182 -0.0034 0.0236 0.0180 357 ASP A N 2151 C CA . ASP A 275 ? 0.1277 0.0961 0.1124 -0.0029 0.0232 0.0200 357 ASP A CA 2152 C C . ASP A 275 ? 0.1415 0.1082 0.1279 -0.0028 0.0238 0.0214 357 ASP A C 2153 O O . ASP A 275 ? 0.1340 0.0997 0.1192 -0.0022 0.0225 0.0226 357 ASP A O 2154 C CB . ASP A 275 ? 0.1388 0.1077 0.1207 -0.0022 0.0209 0.0203 357 ASP A CB 2155 C CG . ASP A 275 ? 0.1763 0.1442 0.1541 -0.0017 0.0201 0.0221 357 ASP A CG 2156 O OD1 . ASP A 275 ? 0.1846 0.1519 0.1606 -0.0018 0.0213 0.0228 357 ASP A OD1 2157 O OD2 . ASP A 275 ? 0.2006 0.1682 0.1770 -0.0010 0.0183 0.0229 357 ASP A OD2 2158 N N . GLY A 276 ? 0.1412 0.1074 0.1307 -0.0034 0.0257 0.0211 358 GLY A N 2159 C CA . GLY A 276 ? 0.1594 0.1239 0.1508 -0.0033 0.0264 0.0224 358 GLY A CA 2160 C C . GLY A 276 ? 0.1548 0.1190 0.1486 -0.0030 0.0253 0.0221 358 GLY A C 2161 O O . GLY A 276 ? 0.1462 0.1115 0.1430 -0.0033 0.0251 0.0203 358 GLY A O 2162 N N . ALA A 277 ? 0.1471 0.1098 0.1398 -0.0024 0.0245 0.0239 359 ALA A N 2163 C CA . ALA A 277 ? 0.1591 0.1214 0.1543 -0.0020 0.0235 0.0238 359 ALA A CA 2164 C C . ALA A 277 ? 0.1543 0.1178 0.1483 -0.0016 0.0217 0.0230 359 ALA A C 2165 O O . ALA A 277 ? 0.1928 0.1564 0.1894 -0.0013 0.0210 0.0224 359 ALA A O 2166 C CB . ALA A 277 ? 0.1574 0.1176 0.1518 -0.0015 0.0232 0.0260 359 ALA A CB 2167 N N . ASN A 278 ? 0.1380 0.1025 0.1285 -0.0015 0.0210 0.0229 360 ASN A N 2168 C CA . ASN A 278 ? 0.1285 0.0943 0.1177 -0.0011 0.0192 0.0222 360 ASN A CA 2169 C C . ASN A 278 ? 0.1723 0.1398 0.1629 -0.0017 0.0197 0.0200 360 ASN A C 2170 O O . ASN A 278 ? 0.1518 0.1205 0.1404 -0.0016 0.0186 0.0193 360 ASN A O 2171 C CB . ASN A 278 ? 0.1506 0.1164 0.1349 -0.0007 0.0180 0.0233 360 ASN A CB 2172 C CG . ASN A 278 ? 0.1417 0.1085 0.1247 -0.0001 0.0159 0.0229 360 ASN A CG 2173 O OD1 . ASN A 278 ? 0.1535 0.1202 0.1386 0.0003 0.0151 0.0228 360 ASN A OD1 2174 N ND2 . ASN A 278 ? 0.1488 0.1166 0.1285 -0.0001 0.0153 0.0227 360 ASN A ND2 2175 N N . THR A 279 ? 0.1013 0.0688 0.0953 -0.0024 0.0212 0.0188 361 THR A N 2176 C CA . THR A 279 ? 0.1075 0.0766 0.1032 -0.0031 0.0217 0.0168 361 THR A CA 2177 C C . THR A 279 ? 0.1307 0.1003 0.1285 -0.0031 0.0209 0.0154 361 THR A C 2178 O O . THR A 279 ? 0.1252 0.0941 0.1259 -0.0030 0.0210 0.0153 361 THR A O 2179 C CB . THR A 279 ? 0.1307 0.0998 0.1295 -0.0039 0.0235 0.0160 361 THR A CB 2180 O OG1 . THR A 279 ? 0.1165 0.0851 0.1131 -0.0039 0.0244 0.0171 361 THR A OG1 2181 C CG2 . THR A 279 ? 0.0975 0.0681 0.0983 -0.0046 0.0237 0.0138 361 THR A CG2 2182 N N . TRP A 280 ? 0.1056 0.0767 0.1022 -0.0032 0.0202 0.0143 362 TRP A N 2183 C CA . TRP A 280 ? 0.1077 0.0793 0.1061 -0.0033 0.0196 0.0128 362 TRP A CA 2184 C C . TRP A 280 ? 0.1169 0.0899 0.1161 -0.0042 0.0200 0.0110 362 TRP A C 2185 O O . TRP A 280 ? 0.0938 0.0677 0.0907 -0.0042 0.0199 0.0110 362 TRP A O 2186 C CB . TRP A 280 ? 0.1071 0.0789 0.1032 -0.0025 0.0181 0.0135 362 TRP A CB 2187 C CG . TRP A 280 ? 0.1003 0.0709 0.0968 -0.0017 0.0175 0.0149 362 TRP A CG 2188 C CD1 . TRP A 280 ? 0.1093 0.0788 0.1039 -0.0012 0.0172 0.0168 362 TRP A CD1 2189 C CD2 . TRP A 280 ? 0.1045 0.0746 0.1034 -0.0013 0.0171 0.0146 362 TRP A CD2 2190 N NE1 . TRP A 280 ? 0.1088 0.0774 0.1047 -0.0005 0.0165 0.0177 362 TRP A NE1 2191 C CE2 . TRP A 280 ? 0.1102 0.0791 0.1088 -0.0005 0.0165 0.0163 362 TRP A CE2 2192 C CE3 . TRP A 280 ? 0.0929 0.0634 0.0940 -0.0016 0.0173 0.0128 362 TRP A CE3 2193 C CZ2 . TRP A 280 ? 0.1291 0.0975 0.1301 0.0001 0.0160 0.0164 362 TRP A CZ2 2194 C CZ3 . TRP A 280 ? 0.1206 0.0904 0.1239 -0.0010 0.0170 0.0128 362 TRP A CZ3 2195 C CH2 . TRP A 280 ? 0.1401 0.1090 0.1436 -0.0002 0.0163 0.0146 362 TRP A CH2 2196 N N . LEU A 281 ? 0.0986 0.0716 0.1009 -0.0048 0.0203 0.0093 363 LEU A N 2197 C CA . LEU A 281 ? 0.1083 0.0828 0.1116 -0.0056 0.0203 0.0073 363 LEU A CA 2198 C C . LEU A 281 ? 0.1186 0.0947 0.1213 -0.0053 0.0186 0.0058 363 LEU A C 2199 O O . LEU A 281 ? 0.1132 0.0887 0.1169 -0.0049 0.0183 0.0056 363 LEU A O 2200 C CB . LEU A 281 ? 0.1038 0.0781 0.1113 -0.0065 0.0214 0.0060 363 LEU A CB 2201 C CG . LEU A 281 ? 0.1530 0.1266 0.1619 -0.0066 0.0226 0.0069 363 LEU A CG 2202 C CD1 . LEU A 281 ? 0.0922 0.0660 0.1057 -0.0075 0.0232 0.0051 363 LEU A CD1 2203 C CD2 . LEU A 281 ? 0.1261 0.1003 0.1326 -0.0065 0.0230 0.0080 363 LEU A CD2 2204 N N . GLY A 282 ? 0.0919 0.0699 0.0932 -0.0054 0.0177 0.0048 364 GLY A N 2205 C CA . GLY A 282 ? 0.0751 0.0545 0.0759 -0.0052 0.0163 0.0033 364 GLY A CA 2206 C C . GLY A 282 ? 0.0978 0.0782 0.1009 -0.0059 0.0161 0.0010 364 GLY A C 2207 O O . GLY A 282 ? 0.1022 0.0829 0.1066 -0.0065 0.0166 0.0006 364 GLY A O 2208 N N . ARG A 283 ? 0.0614 0.0423 0.0649 -0.0058 0.0154 -0.0004 365 ARG A N 2209 C CA . ARG A 283 ? 0.0714 0.0534 0.0762 -0.0064 0.0148 -0.0027 365 ARG A CA 2210 C C . ARG A 283 ? 0.0942 0.0768 0.0977 -0.0061 0.0138 -0.0040 365 ARG A C 2211 O O . ARG A 283 ? 0.0895 0.0715 0.0923 -0.0056 0.0140 -0.0034 365 ARG A O 2212 C CB . ARG A 283 ? 0.0712 0.0522 0.0797 -0.0072 0.0157 -0.0037 365 ARG A CB 2213 C CG . ARG A 283 ? 0.0982 0.0776 0.1083 -0.0070 0.0163 -0.0040 365 ARG A CG 2214 C CD . ARG A 283 ? 0.0908 0.0694 0.1048 -0.0078 0.0171 -0.0052 365 ARG A CD 2215 N NE . ARG A 283 ? 0.1256 0.1026 0.1418 -0.0078 0.0178 -0.0057 365 ARG A NE 2216 C CZ . ARG A 283 ? 0.1408 0.1168 0.1608 -0.0085 0.0186 -0.0068 365 ARG A CZ 2217 N NH1 . ARG A 283 ? 0.1016 0.0782 0.1237 -0.0093 0.0187 -0.0075 365 ARG A NH1 2218 N NH2 . ARG A 283 ? 0.1315 0.1059 0.1535 -0.0084 0.0192 -0.0073 365 ARG A NH2 2219 N N . THR A 284 ? 0.0752 0.0591 0.0785 -0.0065 0.0128 -0.0058 366 THR A N 2220 C CA . THR A 284 ? 0.0880 0.0722 0.0900 -0.0063 0.0121 -0.0073 366 THR A CA 2221 C C . THR A 284 ? 0.1334 0.1163 0.1377 -0.0065 0.0129 -0.0085 366 THR A C 2222 O O . THR A 284 ? 0.1087 0.0908 0.1159 -0.0071 0.0135 -0.0087 366 THR A O 2223 C CB . THR A 284 ? 0.0957 0.0814 0.0969 -0.0067 0.0107 -0.0089 366 THR A CB 2224 O OG1 . THR A 284 ? 0.0984 0.0840 0.1025 -0.0074 0.0107 -0.0103 366 THR A OG1 2225 C CG2 . THR A 284 ? 0.0764 0.0633 0.0759 -0.0065 0.0100 -0.0077 366 THR A CG2 2226 N N . ILE A 285 ? 0.0938 0.0764 0.0971 -0.0061 0.0129 -0.0092 367 ILE A N 2227 C CA . ILE A 285 ? 0.0871 0.0684 0.0926 -0.0063 0.0136 -0.0106 367 ILE A CA 2228 C C . ILE A 285 ? 0.1177 0.0994 0.1240 -0.0070 0.0129 -0.0132 367 ILE A C 2229 O O . ILE A 285 ? 0.1381 0.1189 0.1476 -0.0075 0.0134 -0.0142 367 ILE A O 2230 C CB . ILE A 285 ? 0.1343 0.1152 0.1386 -0.0056 0.0141 -0.0108 367 ILE A CB 2231 C CG1 . ILE A 285 ? 0.1339 0.1143 0.1383 -0.0049 0.0147 -0.0083 367 ILE A CG1 2232 C CG2 . ILE A 285 ? 0.1423 0.1220 0.1489 -0.0058 0.0149 -0.0127 367 ILE A CG2 2233 C CD1 . ILE A 285 ? 0.1506 0.1309 0.1544 -0.0042 0.0152 -0.0082 367 ILE A CD1 2234 N N . SER A 286 ? 0.1226 0.1056 0.1262 -0.0070 0.0116 -0.0141 368 SER A N 2235 C CA . SER A 286 ? 0.1443 0.1278 0.1482 -0.0076 0.0105 -0.0165 368 SER A CA 2236 C C . SER A 286 ? 0.1725 0.1565 0.1793 -0.0083 0.0101 -0.0165 368 SER A C 2237 O O . SER A 286 ? 0.1630 0.1476 0.1698 -0.0082 0.0102 -0.0147 368 SER A O 2238 C CB . SER A 286 ? 0.1313 0.1161 0.1312 -0.0074 0.0091 -0.0171 368 SER A CB 2239 O OG . SER A 286 ? 0.1275 0.1129 0.1276 -0.0079 0.0077 -0.0193 368 SER A OG 2240 N N . THR A 287 ? 0.1208 0.1046 0.1302 -0.0090 0.0097 -0.0186 369 THR A N 2241 C CA . THR A 287 ? 0.1132 0.0977 0.1257 -0.0097 0.0092 -0.0190 369 THR A CA 2242 C C . THR A 287 ? 0.1421 0.1282 0.1529 -0.0098 0.0070 -0.0201 369 THR A C 2243 O O . THR A 287 ? 0.1023 0.0894 0.1156 -0.0103 0.0064 -0.0203 369 THR A O 2244 C CB . THR A 287 ? 0.1180 0.1014 0.1349 -0.0105 0.0096 -0.0208 369 THR A CB 2245 O OG1 . THR A 287 ? 0.1177 0.1010 0.1335 -0.0106 0.0086 -0.0234 369 THR A OG1 2246 C CG2 . THR A 287 ? 0.1568 0.1384 0.1760 -0.0104 0.0117 -0.0194 369 THR A CG2 2247 N N . ALA A 288 ? 0.1208 0.1073 0.1276 -0.0094 0.0060 -0.0209 370 ALA A N 2248 C CA . ALA A 288 ? 0.1284 0.1162 0.1333 -0.0094 0.0038 -0.0221 370 ALA A CA 2249 C C . ALA A 288 ? 0.1432 0.1321 0.1447 -0.0088 0.0032 -0.0203 370 ALA A C 2250 O O . ALA A 288 ? 0.1423 0.1326 0.1438 -0.0089 0.0016 -0.0205 370 ALA A O 2251 C CB . ALA A 288 ? 0.1506 0.1379 0.1532 -0.0094 0.0029 -0.0245 370 ALA A CB 2252 N N . SER A 289 ? 0.1215 0.1099 0.1205 -0.0082 0.0044 -0.0187 371 SER A N 2253 C CA . SER A 289 ? 0.0965 0.0858 0.0922 -0.0076 0.0038 -0.0172 371 SER A CA 2254 C C . SER A 289 ? 0.0960 0.0850 0.0915 -0.0072 0.0054 -0.0148 371 SER A C 2255 O O . SER A 289 ? 0.1136 0.1015 0.1110 -0.0072 0.0068 -0.0143 371 SER A O 2256 C CB . SER A 289 ? 0.1920 0.1812 0.1834 -0.0072 0.0031 -0.0180 371 SER A CB 2257 O OG . SER A 289 ? 0.2953 0.2833 0.2858 -0.0070 0.0047 -0.0181 371 SER A OG 2258 N N . ARG A 290 ? 0.0849 0.0746 0.0781 -0.0067 0.0049 -0.0133 372 ARG A N 2259 C CA . ARG A 290 ? 0.0875 0.0771 0.0804 -0.0063 0.0060 -0.0112 372 ARG A CA 2260 C C . ARG A 290 ? 0.1023 0.0911 0.0931 -0.0058 0.0069 -0.0108 372 ARG A C 2261 O O . ARG A 290 ? 0.1085 0.0977 0.0968 -0.0054 0.0067 -0.0100 372 ARG A O 2262 C CB . ARG A 290 ? 0.0853 0.0760 0.0770 -0.0061 0.0051 -0.0100 372 ARG A CB 2263 C CG . ARG A 290 ? 0.0801 0.0716 0.0744 -0.0065 0.0045 -0.0103 372 ARG A CG 2264 C CD . ARG A 290 ? 0.1148 0.1075 0.1079 -0.0063 0.0033 -0.0096 372 ARG A CD 2265 N NE . ARG A 290 ? 0.0727 0.0661 0.0688 -0.0067 0.0031 -0.0097 372 ARG A NE 2266 C CZ . ARG A 290 ? 0.1053 0.0997 0.1017 -0.0065 0.0024 -0.0091 372 ARG A CZ 2267 N NH1 . ARG A 290 ? 0.1205 0.1152 0.1140 -0.0060 0.0017 -0.0082 372 ARG A NH1 2268 N NH2 . ARG A 290 ? 0.0824 0.0775 0.0819 -0.0068 0.0025 -0.0093 372 ARG A NH2 2269 N N . SER A 291 ? 0.0935 0.0812 0.0858 -0.0059 0.0079 -0.0115 373 SER A N 2270 C CA . SER A 291 ? 0.0956 0.0825 0.0867 -0.0054 0.0089 -0.0114 373 SER A CA 2271 C C . SER A 291 ? 0.1119 0.0977 0.1057 -0.0053 0.0103 -0.0106 373 SER A C 2272 O O . SER A 291 ? 0.1091 0.0944 0.1056 -0.0058 0.0106 -0.0111 373 SER A O 2273 C CB . SER A 291 ? 0.1630 0.1496 0.1526 -0.0055 0.0087 -0.0135 373 SER A CB 2274 O OG . SER A 291 ? 0.2471 0.2330 0.2390 -0.0060 0.0088 -0.0152 373 SER A OG 2275 N N . GLY A 292 ? 0.0768 0.0623 0.0701 -0.0048 0.0110 -0.0093 374 GLY A N 2276 C CA . GLY A 292 ? 0.0801 0.0646 0.0757 -0.0045 0.0121 -0.0083 374 GLY A CA 2277 C C . GLY A 292 ? 0.0883 0.0728 0.0849 -0.0046 0.0120 -0.0065 374 GLY A C 2278 O O . GLY A 292 ? 0.0990 0.0842 0.0951 -0.0049 0.0113 -0.0065 374 GLY A O 2279 N N . TYR A 293 ? 0.0690 0.0526 0.0668 -0.0041 0.0127 -0.0051 375 TYR A N 2280 C CA . TYR A 293 ? 0.0681 0.0512 0.0665 -0.0042 0.0129 -0.0034 375 TYR A CA 2281 C C . TYR A 293 ? 0.0834 0.0651 0.0837 -0.0038 0.0137 -0.0022 375 TYR A C 2282 O O . TYR A 293 ? 0.0876 0.0691 0.0881 -0.0032 0.0139 -0.0019 375 TYR A O 2283 C CB . TYR A 293 ? 0.0794 0.0636 0.0756 -0.0039 0.0121 -0.0020 375 TYR A CB 2284 C CG . TYR A 293 ? 0.0894 0.0735 0.0857 -0.0041 0.0122 -0.0011 375 TYR A CG 2285 C CD1 . TYR A 293 ? 0.0801 0.0651 0.0763 -0.0047 0.0118 -0.0019 375 TYR A CD1 2286 C CD2 . TYR A 293 ? 0.0796 0.0627 0.0761 -0.0038 0.0127 0.0007 375 TYR A CD2 2287 C CE1 . TYR A 293 ? 0.0919 0.0768 0.0886 -0.0050 0.0121 -0.0011 375 TYR A CE1 2288 C CE2 . TYR A 293 ? 0.0787 0.0615 0.0751 -0.0041 0.0130 0.0015 375 TYR A CE2 2289 C CZ . TYR A 293 ? 0.0786 0.0623 0.0752 -0.0047 0.0129 0.0006 375 TYR A CZ 2290 O OH . TYR A 293 ? 0.1148 0.0983 0.1115 -0.0050 0.0134 0.0014 375 TYR A OH 2291 N N . GLU A 294 ? 0.0773 0.0580 0.0792 -0.0041 0.0143 -0.0016 376 GLU A N 2292 C CA . GLU A 294 ? 0.0733 0.0523 0.0769 -0.0037 0.0151 -0.0002 376 GLU A CA 2293 C C . GLU A 294 ? 0.0828 0.0611 0.0861 -0.0038 0.0155 0.0016 376 GLU A C 2294 O O . GLU A 294 ? 0.0825 0.0614 0.0854 -0.0044 0.0155 0.0014 376 GLU A O 2295 C CB . GLU A 294 ? 0.1094 0.0873 0.1160 -0.0041 0.0160 -0.0016 376 GLU A CB 2296 C CG . GLU A 294 ? 0.1223 0.1001 0.1304 -0.0050 0.0163 -0.0029 376 GLU A CG 2297 C CD . GLU A 294 ? 0.1634 0.1399 0.1747 -0.0053 0.0171 -0.0044 376 GLU A CD 2298 O OE1 . GLU A 294 ? 0.1362 0.1119 0.1484 -0.0048 0.0175 -0.0045 376 GLU A OE1 2299 O OE2 . GLU A 294 ? 0.1268 0.1032 0.1400 -0.0061 0.0173 -0.0055 376 GLU A OE2 2300 N N . MET A 295 ? 0.1089 0.0859 0.1124 -0.0032 0.0158 0.0035 377 MET A N 2301 C CA . MET A 295 ? 0.1103 0.0861 0.1134 -0.0032 0.0164 0.0054 377 MET A CA 2302 C C . MET A 295 ? 0.1093 0.0831 0.1153 -0.0033 0.0175 0.0059 377 MET A C 2303 O O . MET A 295 ? 0.1069 0.0799 0.1146 -0.0029 0.0176 0.0057 377 MET A O 2304 C CB . MET A 295 ? 0.0937 0.0694 0.0943 -0.0024 0.0156 0.0075 377 MET A CB 2305 C CG . MET A 295 ? 0.0787 0.0562 0.0765 -0.0023 0.0144 0.0072 377 MET A CG 2306 S SD . MET A 295 ? 0.1077 0.0860 0.1041 -0.0031 0.0148 0.0066 377 MET A SD 2307 C CE . MET A 295 ? 0.1374 0.1138 0.1330 -0.0030 0.0158 0.0088 377 MET A CE 2308 N N . LEU A 296 ? 0.1122 0.0850 0.1190 -0.0039 0.0186 0.0064 378 LEU A N 2309 C CA . LEU A 296 ? 0.1310 0.1017 0.1408 -0.0041 0.0199 0.0070 378 LEU A CA 2310 C C . LEU A 296 ? 0.1265 0.0967 0.1350 -0.0038 0.0203 0.0093 378 LEU A C 2311 O O . LEU A 296 ? 0.1056 0.0764 0.1124 -0.0042 0.0205 0.0096 378 LEU A O 2312 C CB . LEU A 296 ? 0.0844 0.0554 0.0973 -0.0051 0.0206 0.0048 378 LEU A CB 2313 C CG . LEU A 296 ? 0.1336 0.1058 0.1476 -0.0053 0.0198 0.0021 378 LEU A CG 2314 C CD1 . LEU A 296 ? 0.1321 0.1048 0.1485 -0.0063 0.0201 -0.0001 378 LEU A CD1 2315 C CD2 . LEU A 296 ? 0.1419 0.1129 0.1578 -0.0047 0.0201 0.0019 378 LEU A CD2 2316 N N . LYS A 297 ? 0.0759 0.0449 0.0850 -0.0031 0.0202 0.0107 379 LYS A N 2317 C CA . LYS A 297 ? 0.1066 0.0749 0.1142 -0.0028 0.0205 0.0128 379 LYS A CA 2318 C C . LYS A 297 ? 0.1178 0.0856 0.1284 -0.0035 0.0219 0.0123 379 LYS A C 2319 O O . LYS A 297 ? 0.1329 0.0999 0.1468 -0.0035 0.0223 0.0118 379 LYS A O 2320 C CB . LYS A 297 ? 0.0868 0.0539 0.0940 -0.0018 0.0197 0.0146 379 LYS A CB 2321 C CG . LYS A 297 ? 0.1156 0.0818 0.1206 -0.0015 0.0197 0.0169 379 LYS A CG 2322 C CD . LYS A 297 ? 0.1410 0.1060 0.1459 -0.0005 0.0188 0.0186 379 LYS A CD 2323 C CE . LYS A 297 ? 0.1697 0.1336 0.1718 -0.0002 0.0186 0.0208 379 LYS A CE 2324 N NZ . LYS A 297 ? 0.1558 0.1183 0.1579 0.0007 0.0175 0.0225 379 LYS A NZ 2325 N N . VAL A 298 ? 0.0891 0.0573 0.0988 -0.0040 0.0226 0.0124 380 VAL A N 2326 C CA . VAL A 298 ? 0.1130 0.0810 0.1258 -0.0047 0.0240 0.0117 380 VAL A CA 2327 C C . VAL A 298 ? 0.1187 0.0861 0.1295 -0.0046 0.0248 0.0137 380 VAL A C 2328 O O . VAL A 298 ? 0.1199 0.0882 0.1289 -0.0049 0.0251 0.0136 380 VAL A O 2329 C CB . VAL A 298 ? 0.1115 0.0810 0.1261 -0.0057 0.0242 0.0094 380 VAL A CB 2330 C CG1 . VAL A 298 ? 0.1198 0.0892 0.1381 -0.0064 0.0255 0.0086 380 VAL A CG1 2331 C CG2 . VAL A 298 ? 0.1049 0.0749 0.1206 -0.0058 0.0234 0.0075 380 VAL A CG2 2332 N N . PRO A 299 ? 0.1625 0.1283 0.1737 -0.0042 0.0252 0.0153 381 PRO A N 2333 C CA . PRO A 299 ? 0.1695 0.1344 0.1782 -0.0040 0.0259 0.0173 381 PRO A CA 2334 C C . PRO A 299 ? 0.1419 0.1073 0.1518 -0.0048 0.0275 0.0167 381 PRO A C 2335 O O . PRO A 299 ? 0.1456 0.1112 0.1598 -0.0054 0.0285 0.0154 381 PRO A O 2336 C CB . PRO A 299 ? 0.2108 0.1739 0.2210 -0.0036 0.0262 0.0188 381 PRO A CB 2337 C CG . PRO A 299 ? 0.1587 0.1218 0.1703 -0.0031 0.0250 0.0181 381 PRO A CG 2338 C CD . PRO A 299 ? 0.1380 0.1028 0.1515 -0.0037 0.0249 0.0155 381 PRO A CD 2339 N N . ASN A 300 ? 0.1472 0.1129 0.1537 -0.0047 0.0277 0.0175 382 ASN A N 2340 C CA . ASN A 300 ? 0.1336 0.0998 0.1410 -0.0053 0.0293 0.0171 382 ASN A CA 2341 C C . ASN A 300 ? 0.1172 0.0850 0.1283 -0.0061 0.0295 0.0146 382 ASN A C 2342 O O . ASN A 300 ? 0.1385 0.1065 0.1527 -0.0067 0.0309 0.0139 382 ASN A O 2343 C CB . ASN A 300 ? 0.1354 0.1000 0.1445 -0.0055 0.0309 0.0183 382 ASN A CB 2344 C CG . ASN A 300 ? 0.2688 0.2317 0.2740 -0.0048 0.0307 0.0209 382 ASN A CG 2345 O OD1 . ASN A 300 ? 0.3173 0.2803 0.3182 -0.0045 0.0303 0.0218 382 ASN A OD1 2346 N ND2 . ASN A 300 ? 0.3328 0.2942 0.3397 -0.0045 0.0309 0.0220 382 ASN A ND2 2347 N N . ALA A 301 ? 0.1348 0.1037 0.1455 -0.0061 0.0281 0.0133 383 ALA A N 2348 C CA . ALA A 301 ? 0.0988 0.0693 0.1126 -0.0069 0.0280 0.0109 383 ALA A CA 2349 C C . ALA A 301 ? 0.0931 0.0646 0.1075 -0.0074 0.0290 0.0103 383 ALA A C 2350 O O . ALA A 301 ? 0.1015 0.0738 0.1198 -0.0081 0.0295 0.0086 383 ALA A O 2351 C CB . ALA A 301 ? 0.1179 0.0893 0.1301 -0.0067 0.0264 0.0099 383 ALA A CB 2352 N N . LEU A 302 ? 0.1111 0.0825 0.1216 -0.0070 0.0293 0.0116 384 LEU A N 2353 C CA . LEU A 302 ? 0.1039 0.0762 0.1148 -0.0074 0.0303 0.0110 384 LEU A CA 2354 C C . LEU A 302 ? 0.1192 0.0910 0.1338 -0.0079 0.0322 0.0110 384 LEU A C 2355 O O . LEU A 302 ? 0.1253 0.0982 0.1430 -0.0085 0.0328 0.0095 384 LEU A O 2356 C CB . LEU A 302 ? 0.1130 0.0851 0.1188 -0.0069 0.0303 0.0124 384 LEU A CB 2357 C CG . LEU A 302 ? 0.1114 0.0843 0.1175 -0.0072 0.0315 0.0119 384 LEU A CG 2358 C CD1 . LEU A 302 ? 0.1613 0.1361 0.1699 -0.0077 0.0310 0.0098 384 LEU A CD1 2359 C CD2 . LEU A 302 ? 0.1982 0.1707 0.1991 -0.0066 0.0315 0.0132 384 LEU A CD2 2360 N N . THR A 303 ? 0.1486 0.1187 0.1631 -0.0076 0.0330 0.0125 385 THR A N 2361 C CA . THR A 303 ? 0.1636 0.1329 0.1808 -0.0080 0.0350 0.0129 385 THR A CA 2362 C C . THR A 303 ? 0.1522 0.1209 0.1742 -0.0083 0.0354 0.0125 385 THR A C 2363 O O . THR A 303 ? 0.1990 0.1673 0.2242 -0.0087 0.0371 0.0124 385 THR A O 2364 C CB . THR A 303 ? 0.1650 0.1327 0.1782 -0.0074 0.0360 0.0154 385 THR A CB 2365 O OG1 . THR A 303 ? 0.1512 0.1176 0.1621 -0.0068 0.0350 0.0169 385 THR A OG1 2366 C CG2 . THR A 303 ? 0.1951 0.1634 0.2040 -0.0072 0.0358 0.0156 385 THR A CG2 2367 N N . ASP A 304 ? 0.1408 0.1094 0.1633 -0.0081 0.0340 0.0120 386 ASP A N 2368 C CA . ASP A 304 ? 0.1264 0.0942 0.1530 -0.0083 0.0343 0.0116 386 ASP A CA 2369 C C . ASP A 304 ? 0.1179 0.0873 0.1486 -0.0089 0.0334 0.0088 386 ASP A C 2370 O O . ASP A 304 ? 0.1695 0.1395 0.1990 -0.0088 0.0318 0.0079 386 ASP A O 2371 C CB . ASP A 304 ? 0.1231 0.0895 0.1475 -0.0076 0.0335 0.0131 386 ASP A CB 2372 C CG . ASP A 304 ? 0.1896 0.1551 0.2182 -0.0077 0.0339 0.0128 386 ASP A CG 2373 O OD1 . ASP A 304 ? 0.1497 0.1157 0.1830 -0.0084 0.0346 0.0112 386 ASP A OD1 2374 O OD2 . ASP A 304 ? 0.1977 0.1618 0.2250 -0.0071 0.0334 0.0142 386 ASP A OD2 2375 N N . ASP A 305 ? 0.1403 0.1104 0.1757 -0.0096 0.0343 0.0074 387 ASP A N 2376 C CA . ASP A 305 ? 0.1362 0.1078 0.1753 -0.0102 0.0332 0.0047 387 ASP A CA 2377 C C . ASP A 305 ? 0.1127 0.0838 0.1543 -0.0103 0.0325 0.0037 387 ASP A C 2378 O O . ASP A 305 ? 0.1263 0.0987 0.1711 -0.0108 0.0315 0.0013 387 ASP A O 2379 C CB . ASP A 305 ? 0.1330 0.1059 0.1765 -0.0109 0.0341 0.0033 387 ASP A CB 2380 C CG . ASP A 305 ? 0.2290 0.2008 0.2765 -0.0111 0.0358 0.0037 387 ASP A CG 2381 O OD1 . ASP A 305 ? 0.1811 0.1513 0.2284 -0.0108 0.0362 0.0049 387 ASP A OD1 2382 O OD2 . ASP A 305 ? 0.1741 0.1467 0.2252 -0.0116 0.0368 0.0028 387 ASP A OD2 2383 N N . ARG A 306 ? 0.1321 0.1014 0.1722 -0.0097 0.0328 0.0055 388 ARG A N 2384 C CA . ARG A 306 ? 0.1534 0.1222 0.1956 -0.0096 0.0321 0.0047 388 ARG A CA 2385 C C . ARG A 306 ? 0.1834 0.1516 0.2217 -0.0088 0.0309 0.0055 388 ARG A C 2386 O O . ARG A 306 ? 0.1466 0.1142 0.1862 -0.0086 0.0303 0.0049 388 ARG A O 2387 C CB . ARG A 306 ? 0.1789 0.1461 0.2238 -0.0095 0.0336 0.0059 388 ARG A CB 2388 C CG . ARG A 306 ? 0.1928 0.1602 0.2413 -0.0100 0.0352 0.0056 388 ARG A CG 2389 C CD . ARG A 306 ? 0.1764 0.1455 0.2297 -0.0108 0.0346 0.0026 388 ARG A CD 2390 N NE . ARG A 306 ? 0.2363 0.2057 0.2931 -0.0114 0.0361 0.0024 388 ARG A NE 2391 C CZ . ARG A 306 ? 0.2763 0.2451 0.3377 -0.0116 0.0373 0.0022 388 ARG A CZ 2392 N NH1 . ARG A 306 ? 0.2662 0.2339 0.3291 -0.0114 0.0371 0.0021 388 ARG A NH1 2393 N NH2 . ARG A 306 ? 0.3288 0.2980 0.3935 -0.0121 0.0387 0.0019 388 ARG A NH2 2394 N N . SER A 307 ? 0.1565 0.1248 0.1902 -0.0084 0.0305 0.0069 389 SER A N 2395 C CA . SER A 307 ? 0.1228 0.0904 0.1527 -0.0076 0.0295 0.0082 389 SER A CA 2396 C C . SER A 307 ? 0.1504 0.1187 0.1806 -0.0076 0.0280 0.0063 389 SER A C 2397 O O . SER A 307 ? 0.1483 0.1180 0.1791 -0.0082 0.0273 0.0043 389 SER A O 2398 C CB . SER A 307 ? 0.0979 0.0656 0.1229 -0.0072 0.0293 0.0098 389 SER A CB 2399 O OG . SER A 307 ? 0.1119 0.0813 0.1367 -0.0078 0.0291 0.0084 389 SER A OG 2400 N N . LYS A 308 ? 0.1262 0.0934 0.1560 -0.0070 0.0275 0.0070 390 LYS A N 2401 C CA . LYS A 308 ? 0.1784 0.1460 0.2085 -0.0069 0.0264 0.0053 390 LYS A CA 2402 C C . LYS A 308 ? 0.1073 0.0744 0.1338 -0.0059 0.0255 0.0069 390 LYS A C 2403 O O . LYS A 308 ? 0.1378 0.1040 0.1620 -0.0053 0.0256 0.0093 390 LYS A O 2404 C CB . LYS A 308 ? 0.2207 0.1876 0.2550 -0.0070 0.0267 0.0041 390 LYS A CB 2405 C CG . LYS A 308 ? 0.2367 0.2045 0.2750 -0.0079 0.0272 0.0019 390 LYS A CG 2406 C CD . LYS A 308 ? 0.1802 0.1497 0.2182 -0.0086 0.0262 -0.0005 390 LYS A CD 2407 C CE . LYS A 308 ? 0.3386 0.3090 0.3806 -0.0095 0.0263 -0.0028 390 LYS A CE 2408 N NZ . LYS A 308 ? 0.3032 0.2731 0.3485 -0.0095 0.0262 -0.0044 390 LYS A NZ 2409 N N . PRO A 309 ? 0.1294 0.0969 0.1554 -0.0058 0.0245 0.0055 391 PRO A N 2410 C CA . PRO A 309 ? 0.1329 0.1001 0.1558 -0.0049 0.0236 0.0070 391 PRO A CA 2411 C C . PRO A 309 ? 0.1575 0.1233 0.1816 -0.0040 0.0236 0.0084 391 PRO A C 2412 O O . PRO A 309 ? 0.1489 0.1142 0.1765 -0.0042 0.0242 0.0074 391 PRO A O 2413 C CB . PRO A 309 ? 0.1420 0.1100 0.1648 -0.0050 0.0228 0.0048 391 PRO A CB 2414 C CG . PRO A 309 ? 0.1207 0.0897 0.1451 -0.0061 0.0230 0.0024 391 PRO A CG 2415 C CD . PRO A 309 ? 0.1436 0.1121 0.1713 -0.0065 0.0240 0.0025 391 PRO A CD 2416 N N . ILE A 310 ? 0.1023 0.0675 0.1234 -0.0032 0.0230 0.0106 392 ILE A N 2417 C CA . ILE A 310 ? 0.1165 0.0806 0.1387 -0.0023 0.0227 0.0120 392 ILE A CA 2418 C C . ILE A 310 ? 0.1581 0.1224 0.1787 -0.0015 0.0214 0.0123 392 ILE A C 2419 O O . ILE A 310 ? 0.1548 0.1184 0.1765 -0.0007 0.0209 0.0133 392 ILE A O 2420 C CB . ILE A 310 ? 0.1360 0.0988 0.1566 -0.0019 0.0229 0.0147 392 ILE A CB 2421 C CG1 . ILE A 310 ? 0.1567 0.1198 0.1724 -0.0016 0.0220 0.0164 392 ILE A CG1 2422 C CG2 . ILE A 310 ? 0.1621 0.1246 0.1846 -0.0027 0.0244 0.0145 392 ILE A CG2 2423 C CD1 . ILE A 310 ? 0.1617 0.1234 0.1752 -0.0011 0.0219 0.0191 392 ILE A CD1 2424 N N . GLN A 311 ? 0.1199 0.0854 0.1382 -0.0017 0.0208 0.0114 393 GLN A N 2425 C CA . GLN A 311 ? 0.1066 0.0726 0.1236 -0.0009 0.0197 0.0116 393 GLN A CA 2426 C C . GLN A 311 ? 0.1267 0.0939 0.1420 -0.0015 0.0196 0.0100 393 GLN A C 2427 O O . GLN A 311 ? 0.1120 0.0797 0.1263 -0.0023 0.0201 0.0095 393 GLN A O 2428 C CB . GLN A 311 ? 0.1486 0.1142 0.1625 -0.0001 0.0186 0.0142 393 GLN A CB 2429 C CG . GLN A 311 ? 0.1055 0.0715 0.1191 0.0009 0.0174 0.0147 393 GLN A CG 2430 C CD . GLN A 311 ? 0.1505 0.1163 0.1607 0.0016 0.0160 0.0170 393 GLN A CD 2431 O OE1 . GLN A 311 ? 0.1410 0.1059 0.1496 0.0016 0.0159 0.0187 393 GLN A OE1 2432 N NE2 . GLN A 311 ? 0.0935 0.0602 0.1024 0.0021 0.0148 0.0171 393 GLN A NE2 2433 N N . GLY A 312 ? 0.1150 0.0828 0.1301 -0.0012 0.0190 0.0092 394 GLY A N 2434 C CA . GLY A 312 ? 0.1043 0.0735 0.1174 -0.0017 0.0186 0.0077 394 GLY A CA 2435 C C . GLY A 312 ? 0.1265 0.0972 0.1381 -0.0009 0.0174 0.0075 394 GLY A C 2436 O O . GLY A 312 ? 0.1170 0.0869 0.1297 0.0000 0.0171 0.0086 394 GLY A O 2437 N N . GLN A 313 ? 0.0991 0.0717 0.1085 -0.0012 0.0168 0.0062 395 GLN A N 2438 C CA . GLN A 313 ? 0.0903 0.0644 0.0987 -0.0007 0.0158 0.0059 395 GLN A CA 2439 C C . GLN A 313 ? 0.1261 0.1020 0.1331 -0.0013 0.0156 0.0037 395 GLN A C 2440 O O . GLN A 313 ? 0.1108 0.0874 0.1160 -0.0018 0.0154 0.0035 395 GLN A O 2441 C CB . GLN A 313 ? 0.0994 0.0739 0.1054 0.0000 0.0147 0.0080 395 GLN A CB 2442 C CG . GLN A 313 ? 0.0797 0.0555 0.0853 0.0006 0.0137 0.0078 395 GLN A CG 2443 C CD . GLN A 313 ? 0.1166 0.0925 0.1204 0.0013 0.0124 0.0098 395 GLN A CD 2444 O OE1 . GLN A 313 ? 0.1222 0.0967 0.1257 0.0016 0.0122 0.0116 395 GLN A OE1 2445 N NE2 . GLN A 313 ? 0.0844 0.0620 0.0869 0.0014 0.0114 0.0094 395 GLN A NE2 2446 N N . THR A 314 ? 0.1223 0.0988 0.1302 -0.0011 0.0158 0.0022 396 THR A N 2447 C CA . THR A 314 ? 0.1286 0.1067 0.1348 -0.0015 0.0155 0.0004 396 THR A CA 2448 C C . THR A 314 ? 0.1170 0.0965 0.1207 -0.0012 0.0145 0.0013 396 THR A C 2449 O O . THR A 314 ? 0.1293 0.1089 0.1335 -0.0005 0.0141 0.0025 396 THR A O 2450 C CB . THR A 314 ? 0.1851 0.1632 0.1926 -0.0015 0.0162 -0.0017 396 THR A CB 2451 O OG1 . THR A 314 ? 0.1751 0.1518 0.1848 -0.0020 0.0170 -0.0029 396 THR A OG1 2452 C CG2 . THR A 314 ? 0.1368 0.1164 0.1417 -0.0019 0.0158 -0.0033 396 THR A CG2 2453 N N . ILE A 315 ? 0.0968 0.0775 0.0982 -0.0017 0.0139 0.0008 397 ILE A N 2454 C CA . ILE A 315 ? 0.0712 0.0532 0.0703 -0.0014 0.0130 0.0016 397 ILE A CA 2455 C C . ILE A 315 ? 0.0808 0.0640 0.0788 -0.0016 0.0129 0.0001 397 ILE A C 2456 O O . ILE A 315 ? 0.0806 0.0646 0.0781 -0.0012 0.0126 0.0004 397 ILE A O 2457 C CB . ILE A 315 ? 0.0820 0.0644 0.0792 -0.0018 0.0124 0.0023 397 ILE A CB 2458 C CG1 . ILE A 315 ? 0.0707 0.0517 0.0687 -0.0018 0.0128 0.0036 397 ILE A CG1 2459 C CG2 . ILE A 315 ? 0.0894 0.0729 0.0846 -0.0015 0.0114 0.0031 397 ILE A CG2 2460 C CD1 . ILE A 315 ? 0.1155 0.0955 0.1139 -0.0010 0.0125 0.0054 397 ILE A CD1 2461 N N . VAL A 316 ? 0.0748 0.0581 0.0724 -0.0022 0.0132 -0.0016 398 VAL A N 2462 C CA . VAL A 316 ? 0.0812 0.0654 0.0773 -0.0023 0.0131 -0.0031 398 VAL A CA 2463 C C . VAL A 316 ? 0.1001 0.0836 0.0972 -0.0027 0.0139 -0.0050 398 VAL A C 2464 O O . VAL A 316 ? 0.0982 0.0811 0.0964 -0.0032 0.0139 -0.0056 398 VAL A O 2465 C CB . VAL A 316 ? 0.0753 0.0607 0.0691 -0.0028 0.0121 -0.0032 398 VAL A CB 2466 C CG1 . VAL A 316 ? 0.0946 0.0807 0.0864 -0.0029 0.0120 -0.0045 398 VAL A CG1 2467 C CG2 . VAL A 316 ? 0.1103 0.0963 0.1032 -0.0025 0.0114 -0.0014 398 VAL A CG2 2468 N N . LEU A 317 ? 0.0775 0.0610 0.0744 -0.0024 0.0145 -0.0061 399 LEU A N 2469 C CA . LEU A 317 ? 0.1207 0.1033 0.1182 -0.0027 0.0153 -0.0082 399 LEU A CA 2470 C C . LEU A 317 ? 0.1206 0.1038 0.1163 -0.0034 0.0144 -0.0097 399 LEU A C 2471 O O . LEU A 317 ? 0.1040 0.0882 0.0973 -0.0035 0.0135 -0.0093 399 LEU A O 2472 C CB . LEU A 317 ? 0.1422 0.1249 0.1393 -0.0023 0.0163 -0.0092 399 LEU A CB 2473 C CG . LEU A 317 ? 0.1433 0.1256 0.1430 -0.0016 0.0172 -0.0081 399 LEU A CG 2474 C CD1 . LEU A 317 ? 0.1788 0.1612 0.1779 -0.0013 0.0184 -0.0092 399 LEU A CD1 2475 C CD2 . LEU A 317 ? 0.1591 0.1399 0.1621 -0.0015 0.0177 -0.0081 399 LEU A CD2 2476 N N . ASN A 318 ? 0.1119 0.0942 0.1089 -0.0038 0.0147 -0.0115 400 ASN A N 2477 C CA . ASN A 318 ? 0.1334 0.1161 0.1291 -0.0045 0.0137 -0.0131 400 ASN A CA 2478 C C . ASN A 318 ? 0.1560 0.1395 0.1479 -0.0044 0.0132 -0.0141 400 ASN A C 2479 O O . ASN A 318 ? 0.1810 0.1653 0.1710 -0.0048 0.0120 -0.0146 400 ASN A O 2480 C CB . ASN A 318 ? 0.1667 0.1483 0.1647 -0.0049 0.0141 -0.0151 400 ASN A CB 2481 C CG . ASN A 318 ? 0.2300 0.2121 0.2277 -0.0057 0.0128 -0.0165 400 ASN A CG 2482 O OD1 . ASN A 318 ? 0.2352 0.2183 0.2323 -0.0059 0.0118 -0.0155 400 ASN A OD1 2483 N ND2 . ASN A 318 ? 0.3500 0.3315 0.3483 -0.0061 0.0128 -0.0190 400 ASN A ND2 2484 N N . ALA A 319 ? 0.1394 0.1227 0.1303 -0.0039 0.0143 -0.0142 401 ALA A N 2485 C CA . ALA A 319 ? 0.1562 0.1400 0.1433 -0.0038 0.0142 -0.0149 401 ALA A CA 2486 C C . ALA A 319 ? 0.2197 0.2048 0.2047 -0.0037 0.0133 -0.0131 401 ALA A C 2487 O O . ALA A 319 ? 0.1973 0.1827 0.1789 -0.0036 0.0129 -0.0135 401 ALA A O 2488 C CB . ALA A 319 ? 0.1947 0.1779 0.1818 -0.0033 0.0159 -0.0154 401 ALA A CB 2489 N N . ASP A 320 ? 0.1195 0.1049 0.1063 -0.0035 0.0130 -0.0112 402 ASP A N 2490 C CA . ASP A 320 ? 0.1008 0.0873 0.0860 -0.0034 0.0122 -0.0095 402 ASP A CA 2491 C C . ASP A 320 ? 0.1321 0.1192 0.1175 -0.0038 0.0108 -0.0091 402 ASP A C 2492 O O . ASP A 320 ? 0.1218 0.1085 0.1094 -0.0041 0.0107 -0.0093 402 ASP A O 2493 C CB . ASP A 320 ? 0.1082 0.0948 0.0951 -0.0029 0.0128 -0.0077 402 ASP A CB 2494 C CG . ASP A 320 ? 0.1876 0.1739 0.1744 -0.0025 0.0142 -0.0080 402 ASP A CG 2495 O OD1 . ASP A 320 ? 0.2022 0.1889 0.1864 -0.0024 0.0144 -0.0084 402 ASP A OD1 2496 O OD2 . ASP A 320 ? 0.1330 0.1188 0.1225 -0.0021 0.0151 -0.0077 402 ASP A OD2 2497 N N . TRP A 321 ? 0.1134 0.1014 0.0965 -0.0038 0.0098 -0.0085 403 TRP A N 2498 C CA . TRP A 321 ? 0.1056 0.0944 0.0891 -0.0041 0.0085 -0.0083 403 TRP A CA 2499 C C . TRP A 321 ? 0.1307 0.1196 0.1161 -0.0040 0.0086 -0.0066 403 TRP A C 2500 O O . TRP A 321 ? 0.1193 0.1083 0.1046 -0.0036 0.0090 -0.0053 403 TRP A O 2501 C CB . TRP A 321 ? 0.1225 0.1121 0.1032 -0.0040 0.0074 -0.0081 403 TRP A CB 2502 C CG . TRP A 321 ? 0.1347 0.1240 0.1128 -0.0041 0.0071 -0.0096 403 TRP A CG 2503 C CD1 . TRP A 321 ? 0.1629 0.1521 0.1380 -0.0038 0.0075 -0.0095 403 TRP A CD1 2504 C CD2 . TRP A 321 ? 0.1341 0.1231 0.1122 -0.0045 0.0064 -0.0115 403 TRP A CD2 2505 N NE1 . TRP A 321 ? 0.1640 0.1528 0.1368 -0.0040 0.0071 -0.0112 403 TRP A NE1 2506 C CE2 . TRP A 321 ? 0.1503 0.1391 0.1250 -0.0044 0.0062 -0.0126 403 TRP A CE2 2507 C CE3 . TRP A 321 ? 0.1706 0.1597 0.1515 -0.0050 0.0058 -0.0125 403 TRP A CE3 2508 C CZ2 . TRP A 321 ? 0.1841 0.1725 0.1577 -0.0047 0.0054 -0.0147 403 TRP A CZ2 2509 C CZ3 . TRP A 321 ? 0.2133 0.2021 0.1936 -0.0053 0.0050 -0.0146 403 TRP A CZ3 2510 C CH2 . TRP A 321 ? 0.1865 0.1750 0.1631 -0.0052 0.0047 -0.0157 403 TRP A CH2 2511 N N . SER A 322 ? 0.0803 0.0692 0.0674 -0.0043 0.0082 -0.0067 404 SER A N 2512 C CA . SER A 322 ? 0.0419 0.0310 0.0302 -0.0043 0.0083 -0.0052 404 SER A CA 2513 C C . SER A 322 ? 0.0832 0.0732 0.0711 -0.0045 0.0072 -0.0051 404 SER A C 2514 O O . SER A 322 ? 0.0957 0.0864 0.0817 -0.0044 0.0064 -0.0053 404 SER A O 2515 C CB . SER A 322 ? 0.0813 0.0694 0.0720 -0.0044 0.0092 -0.0051 404 SER A CB 2516 O OG . SER A 322 ? 0.0826 0.0704 0.0748 -0.0050 0.0091 -0.0065 404 SER A OG 2517 N N . GLY A 323 ? 0.0828 0.0727 0.0724 -0.0048 0.0074 -0.0048 405 GLY A N 2518 C CA . GLY A 323 ? 0.0771 0.0680 0.0670 -0.0050 0.0066 -0.0047 405 GLY A CA 2519 C C . GLY A 323 ? 0.0768 0.0674 0.0682 -0.0051 0.0073 -0.0038 405 GLY A C 2520 O O . GLY A 323 ? 0.1027 0.0923 0.0956 -0.0053 0.0083 -0.0037 405 GLY A O 2521 N N . TYR A 324 ? 0.0885 0.0797 0.0794 -0.0050 0.0070 -0.0031 406 TYR A N 2522 C CA . TYR A 324 ? 0.0768 0.0677 0.0687 -0.0050 0.0078 -0.0022 406 TYR A CA 2523 C C . TYR A 324 ? 0.0846 0.0744 0.0757 -0.0047 0.0087 -0.0009 406 TYR A C 2524 O O . TYR A 324 ? 0.0880 0.0776 0.0778 -0.0043 0.0084 -0.0005 406 TYR A O 2525 C CB . TYR A 324 ? 0.0831 0.0749 0.0743 -0.0049 0.0073 -0.0018 406 TYR A CB 2526 C CG . TYR A 324 ? 0.0908 0.0837 0.0837 -0.0052 0.0066 -0.0027 406 TYR A CG 2527 C CD1 . TYR A 324 ? 0.1203 0.1135 0.1146 -0.0056 0.0060 -0.0041 406 TYR A CD1 2528 C CD2 . TYR A 324 ? 0.0692 0.0627 0.0624 -0.0051 0.0065 -0.0024 406 TYR A CD2 2529 C CE1 . TYR A 324 ? 0.1027 0.0970 0.0989 -0.0058 0.0052 -0.0050 406 TYR A CE1 2530 C CE2 . TYR A 324 ? 0.0919 0.0864 0.0872 -0.0054 0.0059 -0.0033 406 TYR A CE2 2531 C CZ . TYR A 324 ? 0.0946 0.0895 0.0914 -0.0057 0.0052 -0.0045 406 TYR A CZ 2532 O OH . TYR A 324 ? 0.1105 0.1065 0.1096 -0.0059 0.0043 -0.0054 406 TYR A OH 2533 N N . SER A 325 ? 0.0651 0.0540 0.0571 -0.0049 0.0098 -0.0003 407 SER A N 2534 C CA . SER A 325 ? 0.0572 0.0450 0.0481 -0.0045 0.0104 0.0011 407 SER A CA 2535 C C . SER A 325 ? 0.0803 0.0677 0.0710 -0.0046 0.0112 0.0020 407 SER A C 2536 O O . SER A 325 ? 0.0859 0.0737 0.0782 -0.0051 0.0118 0.0014 407 SER A O 2537 C CB . SER A 325 ? 0.0795 0.0661 0.0717 -0.0045 0.0111 0.0012 407 SER A CB 2538 O OG . SER A 325 ? 0.0796 0.0658 0.0742 -0.0051 0.0119 0.0005 407 SER A OG 2539 N N . GLY A 326 ? 0.0524 0.0391 0.0412 -0.0041 0.0113 0.0033 408 GLY A N 2540 C CA . GLY A 326 ? 0.0745 0.0606 0.0622 -0.0041 0.0122 0.0041 408 GLY A CA 2541 C C . GLY A 326 ? 0.0840 0.0689 0.0694 -0.0036 0.0123 0.0056 408 GLY A C 2542 O O . GLY A 326 ? 0.0762 0.0609 0.0611 -0.0031 0.0114 0.0060 408 GLY A O 2543 N N . SER A 327 ? 0.0782 0.0622 0.0623 -0.0036 0.0133 0.0064 409 SER A N 2544 C CA . SER A 327 ? 0.0950 0.0775 0.0766 -0.0031 0.0134 0.0080 409 SER A CA 2545 C C . SER A 327 ? 0.0961 0.0790 0.0749 -0.0027 0.0125 0.0082 409 SER A C 2546 O O . SER A 327 ? 0.0984 0.0822 0.0771 -0.0029 0.0126 0.0073 409 SER A O 2547 C CB . SER A 327 ? 0.1035 0.0847 0.0853 -0.0033 0.0150 0.0088 409 SER A CB 2548 O OG . SER A 327 ? 0.1009 0.0828 0.0833 -0.0038 0.0160 0.0081 409 SER A OG 2549 N N . PHE A 328 ? 0.0928 0.0752 0.0699 -0.0020 0.0114 0.0091 410 PHE A N 2550 C CA . PHE A 328 ? 0.1060 0.0888 0.0807 -0.0016 0.0103 0.0092 410 PHE A CA 2551 C C . PHE A 328 ? 0.0945 0.0763 0.0678 -0.0011 0.0096 0.0105 410 PHE A C 2552 O O . PHE A 328 ? 0.0995 0.0806 0.0738 -0.0009 0.0095 0.0112 410 PHE A O 2553 C CB . PHE A 328 ? 0.0973 0.0812 0.0719 -0.0015 0.0090 0.0084 410 PHE A CB 2554 C CG . PHE A 328 ? 0.0961 0.0798 0.0711 -0.0011 0.0079 0.0089 410 PHE A CG 2555 C CD1 . PHE A 328 ? 0.1062 0.0905 0.0838 -0.0014 0.0081 0.0084 410 PHE A CD1 2556 C CD2 . PHE A 328 ? 0.1070 0.0905 0.0805 -0.0006 0.0065 0.0095 410 PHE A CD2 2557 C CE1 . PHE A 328 ? 0.1248 0.1094 0.1036 -0.0010 0.0072 0.0085 410 PHE A CE1 2558 C CE2 . PHE A 328 ? 0.1231 0.1068 0.0979 -0.0002 0.0055 0.0098 410 PHE A CE2 2559 C CZ . PHE A 328 ? 0.0956 0.0800 0.0732 -0.0004 0.0059 0.0093 410 PHE A CZ 2560 N N . MET A 329 ? 0.0910 0.0728 0.0619 -0.0007 0.0089 0.0108 411 MET A N 2561 C CA . MET A 329 ? 0.0842 0.0651 0.0534 -0.0001 0.0078 0.0120 411 MET A CA 2562 C C . MET A 329 ? 0.1030 0.0844 0.0700 0.0002 0.0063 0.0117 411 MET A C 2563 O O . MET A 329 ? 0.1166 0.0987 0.0829 0.0000 0.0065 0.0107 411 MET A O 2564 C CB . MET A 329 ? 0.1004 0.0802 0.0687 -0.0002 0.0088 0.0131 411 MET A CB 2565 C CG . MET A 329 ? 0.1028 0.0818 0.0735 -0.0005 0.0102 0.0136 411 MET A CG 2566 S SD . MET A 329 ? 0.1155 0.0928 0.0852 -0.0004 0.0110 0.0153 411 MET A SD 2567 C CE . MET A 329 ? 0.1251 0.1025 0.0928 -0.0007 0.0124 0.0148 411 MET A CE 2568 N N . ASP A 330 ? 0.1039 0.0850 0.0700 0.0008 0.0047 0.0125 412 ASP A N 2569 C CA . ASP A 330 ? 0.1118 0.0933 0.0758 0.0012 0.0031 0.0122 412 ASP A CA 2570 C C . ASP A 330 ? 0.1189 0.0995 0.0800 0.0013 0.0034 0.0129 412 ASP A C 2571 O O . ASP A 330 ? 0.1304 0.1102 0.0904 0.0018 0.0026 0.0142 412 ASP A O 2572 C CB . ASP A 330 ? 0.1021 0.0835 0.0665 0.0018 0.0011 0.0128 412 ASP A CB 2573 C CG . ASP A 330 ? 0.1594 0.1412 0.1221 0.0021 -0.0007 0.0122 412 ASP A CG 2574 O OD1 . ASP A 330 ? 0.1253 0.1073 0.0860 0.0019 -0.0003 0.0114 412 ASP A OD1 2575 O OD2 . ASP A 330 ? 0.1258 0.1077 0.0891 0.0026 -0.0025 0.0125 412 ASP A OD2 2576 N N . TYR A 331 ? 0.1104 0.0913 0.0704 0.0010 0.0045 0.0121 413 TYR A N 2577 C CA . TYR A 331 ? 0.1208 0.1007 0.0778 0.0011 0.0052 0.0127 413 TYR A CA 2578 C C . TYR A 331 ? 0.1673 0.1470 0.1214 0.0016 0.0034 0.0129 413 TYR A C 2579 O O . TYR A 331 ? 0.1907 0.1695 0.1419 0.0018 0.0036 0.0135 413 TYR A O 2580 C CB . TYR A 331 ? 0.1225 0.1026 0.0793 0.0006 0.0071 0.0116 413 TYR A CB 2581 C CG . TYR A 331 ? 0.1171 0.0973 0.0768 0.0001 0.0088 0.0116 413 TYR A CG 2582 C CD1 . TYR A 331 ? 0.1055 0.0846 0.0651 -0.0001 0.0102 0.0128 413 TYR A CD1 2583 C CD2 . TYR A 331 ? 0.1015 0.0827 0.0639 -0.0003 0.0091 0.0106 413 TYR A CD2 2584 C CE1 . TYR A 331 ? 0.1067 0.0858 0.0691 -0.0006 0.0118 0.0127 413 TYR A CE1 2585 C CE2 . TYR A 331 ? 0.1317 0.1129 0.0966 -0.0007 0.0105 0.0105 413 TYR A CE2 2586 C CZ . TYR A 331 ? 0.1242 0.1044 0.0893 -0.0009 0.0119 0.0115 413 TYR A CZ 2587 O OH . TYR A 331 ? 0.1174 0.0976 0.0853 -0.0014 0.0133 0.0113 413 TYR A OH 2588 N N . TRP A 332 ? 0.1254 0.1059 0.0801 0.0019 0.0015 0.0123 414 TRP A N 2589 C CA . TRP A 332 ? 0.1415 0.1218 0.0937 0.0024 -0.0005 0.0122 414 TRP A CA 2590 C C . TRP A 332 ? 0.1749 0.1551 0.1278 0.0030 -0.0025 0.0133 414 TRP A C 2591 O O . TRP A 332 ? 0.2160 0.1962 0.1675 0.0035 -0.0046 0.0131 414 TRP A O 2592 C CB . TRP A 332 ? 0.1168 0.0980 0.0691 0.0023 -0.0012 0.0104 414 TRP A CB 2593 C CG . TRP A 332 ? 0.1153 0.0966 0.0668 0.0018 0.0008 0.0094 414 TRP A CG 2594 C CD1 . TRP A 332 ? 0.1506 0.1314 0.0990 0.0019 0.0012 0.0089 414 TRP A CD1 2595 C CD2 . TRP A 332 ? 0.1174 0.0992 0.0713 0.0013 0.0026 0.0088 414 TRP A CD2 2596 N NE1 . TRP A 332 ? 0.1601 0.1411 0.1089 0.0014 0.0032 0.0080 414 TRP A NE1 2597 C CE2 . TRP A 332 ? 0.1336 0.1152 0.0858 0.0011 0.0040 0.0080 414 TRP A CE2 2598 C CE3 . TRP A 332 ? 0.1364 0.1188 0.0935 0.0010 0.0031 0.0088 414 TRP A CE3 2599 C CZ2 . TRP A 332 ? 0.1297 0.1118 0.0838 0.0006 0.0058 0.0072 414 TRP A CZ2 2600 C CZ3 . TRP A 332 ? 0.1339 0.1168 0.0927 0.0005 0.0048 0.0081 414 TRP A CZ3 2601 C CH2 . TRP A 332 ? 0.1350 0.1176 0.0923 0.0003 0.0061 0.0073 414 TRP A CH2 2602 N N . ALA A 333 ? 0.1164 0.0962 0.0715 0.0030 -0.0020 0.0144 415 ALA A N 2603 C CA . ALA A 333 ? 0.1209 0.1004 0.0770 0.0036 -0.0037 0.0156 415 ALA A CA 2604 C C . ALA A 333 ? 0.2042 0.1827 0.1576 0.0041 -0.0045 0.0170 415 ALA A C 2605 O O . ALA A 333 ? 0.2265 0.2043 0.1774 0.0039 -0.0031 0.0174 415 ALA A O 2606 C CB . ALA A 333 ? 0.1304 0.1096 0.0897 0.0035 -0.0028 0.0164 415 ALA A CB 2607 N N . GLU A 334 ? 0.1949 0.1733 0.1487 0.0048 -0.0067 0.0179 416 GLU A N 2608 C CA . GLU A 334 ? 0.2684 0.2459 0.2198 0.0054 -0.0076 0.0194 416 GLU A CA 2609 C C . GLU A 334 ? 0.2680 0.2444 0.2203 0.0054 -0.0063 0.0212 416 GLU A C 2610 O O . GLU A 334 ? 0.2299 0.2063 0.1853 0.0050 -0.0051 0.0212 416 GLU A O 2611 C CB . GLU A 334 ? 0.3516 0.3296 0.3038 0.0062 -0.0105 0.0197 416 GLU A CB 2612 C CG . GLU A 334 ? 0.4234 0.4023 0.3747 0.0063 -0.0122 0.0179 416 GLU A CG 2613 C CD . GLU A 334 ? 0.4714 0.4499 0.4182 0.0061 -0.0121 0.0174 416 GLU A CD 2614 O OE1 . GLU A 334 ? 0.5794 0.5573 0.5237 0.0067 -0.0135 0.0184 416 GLU A OE1 2615 O OE2 . GLU A 334 ? 0.6080 0.5867 0.5536 0.0055 -0.0105 0.0161 416 GLU A OE2 2616 N N . GLY A 335 ? 0.2725 0.2479 0.2222 0.0057 -0.0064 0.0227 417 GLY A N 2617 C CA . GLY A 335 ? 0.2542 0.2284 0.2051 0.0056 -0.0054 0.0246 417 GLY A CA 2618 C C . GLY A 335 ? 0.2279 0.2010 0.1763 0.0050 -0.0031 0.0251 417 GLY A C 2619 O O . GLY A 335 ? 0.2844 0.2577 0.2300 0.0046 -0.0023 0.0240 417 GLY A O 2620 N N A ASP A 336 ? 0.2178 0.1897 0.1674 0.0048 -0.0020 0.0267 418 ASP A N 2621 N N B ASP A 336 ? 0.2178 0.1896 0.1673 0.0048 -0.0020 0.0267 418 ASP A N 2622 C CA A ASP A 336 ? 0.2367 0.2073 0.1841 0.0043 0.0001 0.0274 418 ASP A CA 2623 C CA B ASP A 336 ? 0.2365 0.2070 0.1838 0.0043 0.0001 0.0274 418 ASP A CA 2624 C C A ASP A 336 ? 0.2212 0.1916 0.1710 0.0035 0.0027 0.0266 418 ASP A C 2625 C C B ASP A 336 ? 0.2211 0.1915 0.1709 0.0035 0.0027 0.0266 418 ASP A C 2626 O O A ASP A 336 ? 0.2043 0.1737 0.1528 0.0030 0.0047 0.0270 418 ASP A O 2627 O O B ASP A 336 ? 0.2040 0.1734 0.1527 0.0030 0.0047 0.0271 418 ASP A O 2628 C CB A ASP A 336 ? 0.2391 0.2080 0.1856 0.0047 -0.0005 0.0299 418 ASP A CB 2629 C CB B ASP A 336 ? 0.2387 0.2076 0.1848 0.0047 -0.0005 0.0299 418 ASP A CB 2630 C CG A ASP A 336 ? 0.3195 0.2886 0.2633 0.0056 -0.0030 0.0309 418 ASP A CG 2631 C CG B ASP A 336 ? 0.3031 0.2711 0.2532 0.0047 -0.0003 0.0310 418 ASP A CG 2632 O OD1 A ASP A 336 ? 0.3350 0.3049 0.2759 0.0057 -0.0037 0.0297 418 ASP A OD1 2633 O OD1 B ASP A 336 ? 0.2585 0.2273 0.2123 0.0045 -0.0001 0.0298 418 ASP A OD1 2634 O OD2 A ASP A 336 ? 0.3506 0.3189 0.2952 0.0062 -0.0043 0.0329 418 ASP A OD2 2635 O OD2 B ASP A 336 ? 0.3517 0.3181 0.3013 0.0048 -0.0003 0.0330 418 ASP A OD2 2636 N N . CYS A 337 ? 0.1654 0.1368 0.1188 0.0033 0.0027 0.0253 419 CYS A N 2637 C CA . CYS A 337 ? 0.1261 0.0975 0.0822 0.0026 0.0049 0.0244 419 CYS A CA 2638 C C . CYS A 337 ? 0.1586 0.1316 0.1165 0.0024 0.0048 0.0224 419 CYS A C 2639 O O . CYS A 337 ? 0.1516 0.1255 0.1097 0.0028 0.0029 0.0219 419 CYS A O 2640 C CB . CYS A 337 ? 0.1585 0.1287 0.1176 0.0026 0.0054 0.0256 419 CYS A CB 2641 S SG . CYS A 337 ? 0.1919 0.1622 0.1538 0.0033 0.0030 0.0260 419 CYS A SG 2642 N N . TYR A 338 ? 0.1469 0.1203 0.1064 0.0017 0.0068 0.0213 420 TYR A N 2643 C CA . TYR A 338 ? 0.1125 0.0873 0.0740 0.0014 0.0069 0.0195 420 TYR A CA 2644 C C . TYR A 338 ? 0.1380 0.1127 0.1031 0.0014 0.0070 0.0195 420 TYR A C 2645 O O . TYR A 338 ? 0.1081 0.0818 0.0750 0.0011 0.0084 0.0200 420 TYR A O 2646 C CB . TYR A 338 ? 0.1253 0.1006 0.0870 0.0008 0.0089 0.0183 420 TYR A CB 2647 C CG . TYR A 338 ? 0.1524 0.1279 0.1108 0.0008 0.0091 0.0179 420 TYR A CG 2648 C CD1 . TYR A 338 ? 0.1470 0.1232 0.1032 0.0012 0.0073 0.0175 420 TYR A CD1 2649 C CD2 . TYR A 338 ? 0.1612 0.1362 0.1189 0.0003 0.0112 0.0178 420 TYR A CD2 2650 C CE1 . TYR A 338 ? 0.1381 0.1143 0.0912 0.0012 0.0076 0.0170 420 TYR A CE1 2651 C CE2 . TYR A 338 ? 0.1692 0.1443 0.1239 0.0004 0.0116 0.0174 420 TYR A CE2 2652 C CZ . TYR A 338 ? 0.1683 0.1440 0.1206 0.0008 0.0098 0.0169 420 TYR A CZ 2653 O OH . TYR A 338 ? 0.1584 0.1340 0.1076 0.0008 0.0102 0.0164 420 TYR A OH 2654 N N . ARG A 339 ? 0.1276 0.1031 0.0939 0.0017 0.0056 0.0188 421 ARG A N 2655 C CA . ARG A 339 ? 0.1043 0.0798 0.0740 0.0018 0.0058 0.0187 421 ARG A CA 2656 C C . ARG A 339 ? 0.0924 0.0687 0.0640 0.0011 0.0073 0.0172 421 ARG A C 2657 O O . ARG A 339 ? 0.1126 0.0902 0.0837 0.0009 0.0069 0.0159 421 ARG A O 2658 C CB . ARG A 339 ? 0.1181 0.0939 0.0882 0.0024 0.0037 0.0188 421 ARG A CB 2659 C CG . ARG A 339 ? 0.1249 0.1006 0.0984 0.0026 0.0039 0.0187 421 ARG A CG 2660 C CD . ARG A 339 ? 0.1404 0.1166 0.1144 0.0034 0.0019 0.0187 421 ARG A CD 2661 N NE . ARG A 339 ? 0.1258 0.1013 0.0987 0.0041 0.0000 0.0201 421 ARG A NE 2662 C CZ . ARG A 339 ? 0.2119 0.1871 0.1869 0.0049 -0.0014 0.0209 421 ARG A CZ 2663 N NH1 . ARG A 339 ? 0.1237 0.0992 0.1020 0.0051 -0.0009 0.0204 421 ARG A NH1 2664 N NH2 . ARG A 339 ? 0.1710 0.1459 0.1451 0.0056 -0.0032 0.0222 421 ARG A NH2 2665 N N . ALA A 340 ? 0.1039 0.0795 0.0776 0.0007 0.0089 0.0172 422 ALA A N 2666 C CA . ALA A 340 ? 0.1256 0.1020 0.1014 0.0000 0.0102 0.0158 422 ALA A CA 2667 C C . ALA A 340 ? 0.0917 0.0689 0.0688 0.0001 0.0095 0.0148 422 ALA A C 2668 O O . ALA A 340 ? 0.1027 0.0794 0.0809 0.0007 0.0087 0.0154 422 ALA A O 2669 C CB . ALA A 340 ? 0.1137 0.0890 0.0920 -0.0003 0.0118 0.0160 422 ALA A CB 2670 N N . CYS A 341 ? 0.0909 0.0694 0.0680 -0.0003 0.0097 0.0135 423 CYS A N 2671 C CA . CYS A 341 ? 0.1017 0.0811 0.0800 -0.0003 0.0092 0.0125 423 CYS A CA 2672 C C . CYS A 341 ? 0.1033 0.0838 0.0836 -0.0011 0.0102 0.0110 423 CYS A C 2673 O O . CYS A 341 ? 0.0851 0.0653 0.0650 -0.0016 0.0114 0.0108 423 CYS A O 2674 C CB . CYS A 341 ? 0.1433 0.1238 0.1199 0.0000 0.0076 0.0122 423 CYS A CB 2675 S SG . CYS A 341 ? 0.1250 0.1047 0.0996 0.0009 0.0058 0.0137 423 CYS A SG 2676 N N . PHE A 342 ? 0.0599 0.0416 0.0422 -0.0012 0.0097 0.0098 424 PHE A N 2677 C CA . PHE A 342 ? 0.0720 0.0549 0.0557 -0.0019 0.0102 0.0083 424 PHE A CA 2678 C C . PHE A 342 ? 0.0480 0.0323 0.0325 -0.0018 0.0092 0.0073 424 PHE A C 2679 O O . PHE A 342 ? 0.0752 0.0596 0.0599 -0.0013 0.0084 0.0077 424 PHE A O 2680 C CB . PHE A 342 ? 0.0651 0.0473 0.0512 -0.0023 0.0114 0.0079 424 PHE A CB 2681 C CG . PHE A 342 ? 0.1123 0.0942 0.1003 -0.0021 0.0113 0.0077 424 PHE A CG 2682 C CD1 . PHE A 342 ? 0.1142 0.0945 0.1025 -0.0016 0.0115 0.0090 424 PHE A CD1 2683 C CD2 . PHE A 342 ? 0.0669 0.0499 0.0564 -0.0023 0.0111 0.0062 424 PHE A CD2 2684 C CE1 . PHE A 342 ? 0.0948 0.0749 0.0854 -0.0014 0.0116 0.0088 424 PHE A CE1 2685 C CE2 . PHE A 342 ? 0.0875 0.0701 0.0788 -0.0021 0.0112 0.0059 424 PHE A CE2 2686 C CZ . PHE A 342 ? 0.1009 0.0821 0.0929 -0.0016 0.0115 0.0071 424 PHE A CZ 2687 N N . TYR A 343 ? 0.0764 0.0619 0.0614 -0.0022 0.0092 0.0060 425 TYR A N 2688 C CA . TYR A 343 ? 0.0893 0.0760 0.0748 -0.0022 0.0085 0.0051 425 TYR A CA 2689 C C . TYR A 343 ? 0.0697 0.0567 0.0568 -0.0027 0.0091 0.0039 425 TYR A C 2690 O O . TYR A 343 ? 0.0690 0.0557 0.0570 -0.0031 0.0098 0.0035 425 TYR A O 2691 C CB . TYR A 343 ? 0.0640 0.0518 0.0483 -0.0022 0.0078 0.0048 425 TYR A CB 2692 C CG . TYR A 343 ? 0.0761 0.0643 0.0605 -0.0027 0.0082 0.0042 425 TYR A CG 2693 C CD1 . TYR A 343 ? 0.0680 0.0570 0.0536 -0.0031 0.0081 0.0030 425 TYR A CD1 2694 C CD2 . TYR A 343 ? 0.0845 0.0721 0.0680 -0.0028 0.0087 0.0047 425 TYR A CD2 2695 C CE1 . TYR A 343 ? 0.0669 0.0564 0.0532 -0.0035 0.0083 0.0024 425 TYR A CE1 2696 C CE2 . TYR A 343 ? 0.0701 0.0582 0.0543 -0.0032 0.0093 0.0040 425 TYR A CE2 2697 C CZ . TYR A 343 ? 0.0743 0.0634 0.0601 -0.0036 0.0090 0.0029 425 TYR A CZ 2698 O OH . TYR A 343 ? 0.0781 0.0677 0.0651 -0.0040 0.0094 0.0022 425 TYR A OH 2699 N N . VAL A 344 ? 0.0618 0.0494 0.0493 -0.0026 0.0087 0.0031 426 VAL A N 2700 C CA . VAL A 344 ? 0.0677 0.0557 0.0561 -0.0031 0.0089 0.0018 426 VAL A CA 2701 C C . VAL A 344 ? 0.0666 0.0558 0.0539 -0.0030 0.0081 0.0012 426 VAL A C 2702 O O . VAL A 344 ? 0.0658 0.0552 0.0525 -0.0027 0.0078 0.0017 426 VAL A O 2703 C CB . VAL A 344 ? 0.0809 0.0682 0.0706 -0.0030 0.0095 0.0012 426 VAL A CB 2704 C CG1 . VAL A 344 ? 0.0782 0.0659 0.0685 -0.0035 0.0095 -0.0004 426 VAL A CG1 2705 C CG2 . VAL A 344 ? 0.0888 0.0748 0.0798 -0.0030 0.0103 0.0020 426 VAL A CG2 2706 N N . GLU A 345 ? 0.0581 0.0480 0.0453 -0.0034 0.0077 0.0004 427 GLU A N 2707 C CA . GLU A 345 ? 0.0830 0.0738 0.0692 -0.0034 0.0069 0.0000 427 GLU A CA 2708 C C . GLU A 345 ? 0.0961 0.0869 0.0822 -0.0035 0.0071 -0.0010 427 GLU A C 2709 O O . GLU A 345 ? 0.0699 0.0602 0.0568 -0.0038 0.0074 -0.0020 427 GLU A O 2710 C CB . GLU A 345 ? 0.0810 0.0725 0.0675 -0.0037 0.0064 -0.0006 427 GLU A CB 2711 C CG . GLU A 345 ? 0.0629 0.0553 0.0483 -0.0037 0.0054 -0.0010 427 GLU A CG 2712 C CD . GLU A 345 ? 0.0814 0.0745 0.0677 -0.0040 0.0047 -0.0017 427 GLU A CD 2713 O OE1 . GLU A 345 ? 0.1065 0.0995 0.0943 -0.0043 0.0050 -0.0024 427 GLU A OE1 2714 O OE2 . GLU A 345 ? 0.0712 0.0649 0.0568 -0.0038 0.0039 -0.0014 427 GLU A OE2 2715 N N . LEU A 346 ? 0.0625 0.0535 0.0474 -0.0032 0.0070 -0.0008 428 LEU A N 2716 C CA . LEU A 346 ? 0.0542 0.0449 0.0384 -0.0032 0.0073 -0.0018 428 LEU A CA 2717 C C . LEU A 346 ? 0.0605 0.0520 0.0429 -0.0033 0.0065 -0.0022 428 LEU A C 2718 O O . LEU A 346 ? 0.0679 0.0596 0.0491 -0.0030 0.0063 -0.0015 428 LEU A O 2719 C CB . LEU A 346 ? 0.0586 0.0490 0.0430 -0.0028 0.0081 -0.0012 428 LEU A CB 2720 C CG . LEU A 346 ? 0.0784 0.0682 0.0646 -0.0026 0.0086 -0.0004 428 LEU A CG 2721 C CD1 . LEU A 346 ? 0.0836 0.0733 0.0704 -0.0021 0.0091 0.0002 428 LEU A CD1 2722 C CD2 . LEU A 346 ? 0.1011 0.0900 0.0886 -0.0028 0.0091 -0.0013 428 LEU A CD2 2723 N N . ILE A 347 ? 0.0624 0.0540 0.0447 -0.0036 0.0058 -0.0033 429 ILE A N 2724 C CA . ILE A 347 ? 0.0629 0.0551 0.0435 -0.0036 0.0047 -0.0036 429 ILE A CA 2725 C C . ILE A 347 ? 0.0889 0.0809 0.0672 -0.0035 0.0049 -0.0041 429 ILE A C 2726 O O . ILE A 347 ? 0.0841 0.0754 0.0621 -0.0036 0.0055 -0.0052 429 ILE A O 2727 C CB . ILE A 347 ? 0.0652 0.0578 0.0469 -0.0040 0.0038 -0.0046 429 ILE A CB 2728 C CG1 . ILE A 347 ? 0.0735 0.0663 0.0574 -0.0042 0.0039 -0.0041 429 ILE A CG1 2729 C CG2 . ILE A 347 ? 0.0974 0.0906 0.0773 -0.0040 0.0024 -0.0049 429 ILE A CG2 2730 C CD1 . ILE A 347 ? 0.0753 0.0685 0.0612 -0.0046 0.0033 -0.0052 429 ILE A CD1 2731 N N . ARG A 348 ? 0.0440 0.0363 0.0204 -0.0033 0.0045 -0.0033 430 ARG A N 2732 C CA . ARG A 348 ? 0.0682 0.0600 0.0418 -0.0031 0.0048 -0.0036 430 ARG A CA 2733 C C . ARG A 348 ? 0.1031 0.0953 0.0747 -0.0031 0.0033 -0.0036 430 ARG A C 2734 O O . ARG A 348 ? 0.0862 0.0791 0.0588 -0.0031 0.0024 -0.0029 430 ARG A O 2735 C CB . ARG A 348 ? 0.0827 0.0743 0.0558 -0.0028 0.0060 -0.0025 430 ARG A CB 2736 C CG . ARG A 348 ? 0.1083 0.0997 0.0836 -0.0028 0.0073 -0.0023 430 ARG A CG 2737 C CD . ARG A 348 ? 0.0827 0.0735 0.0583 -0.0029 0.0080 -0.0038 430 ARG A CD 2738 N NE . ARG A 348 ? 0.0992 0.0894 0.0720 -0.0029 0.0086 -0.0048 430 ARG A NE 2739 C CZ . ARG A 348 ? 0.1080 0.0978 0.0803 -0.0026 0.0101 -0.0046 430 ARG A CZ 2740 N NH1 . ARG A 348 ? 0.1051 0.0951 0.0797 -0.0024 0.0110 -0.0036 430 ARG A NH1 2741 N NH2 . ARG A 348 ? 0.1021 0.0913 0.0715 -0.0026 0.0107 -0.0056 430 ARG A NH2 2742 N N . GLY A 349 ? 0.0763 0.0681 0.0450 -0.0031 0.0031 -0.0044 431 GLY A N 2743 C CA . GLY A 349 ? 0.0923 0.0842 0.0587 -0.0030 0.0015 -0.0043 431 GLY A CA 2744 C C . GLY A 349 ? 0.1117 0.1040 0.0788 -0.0033 -0.0001 -0.0058 431 GLY A C 2745 O O . GLY A 349 ? 0.1028 0.0949 0.0708 -0.0036 0.0002 -0.0073 431 GLY A O 2746 N N . ARG A 350 ? 0.0956 0.0885 0.0627 -0.0032 -0.0019 -0.0055 432 ARG A N 2747 C CA . ARG A 350 ? 0.1134 0.1068 0.0813 -0.0034 -0.0037 -0.0069 432 ARG A CA 2748 C C . ARG A 350 ? 0.0904 0.0844 0.0626 -0.0038 -0.0035 -0.0076 432 ARG A C 2749 O O . ARG A 350 ? 0.0978 0.0920 0.0723 -0.0038 -0.0026 -0.0066 432 ARG A O 2750 C CB . ARG A 350 ? 0.1025 0.0963 0.0691 -0.0031 -0.0057 -0.0062 432 ARG A CB 2751 C CG . ARG A 350 ? 0.1212 0.1142 0.0829 -0.0027 -0.0060 -0.0058 432 ARG A CG 2752 C CD . ARG A 350 ? 0.1194 0.1126 0.0793 -0.0024 -0.0082 -0.0050 432 ARG A CD 2753 N NE . ARG A 350 ? 0.1576 0.1504 0.1134 -0.0020 -0.0081 -0.0049 432 ARG A NE 2754 C CZ . ARG A 350 ? 0.2029 0.1961 0.1571 -0.0017 -0.0100 -0.0049 432 ARG A CZ 2755 N NH1 . ARG A 350 ? 0.2045 0.1983 0.1605 -0.0017 -0.0124 -0.0052 432 ARG A NH1 2756 N NH2 . ARG A 350 ? 0.1982 0.1914 0.1494 -0.0014 -0.0095 -0.0047 432 ARG A NH2 2757 N N . PRO A 351 ? 0.0998 0.0939 0.0733 -0.0042 -0.0044 -0.0094 433 PRO A N 2758 C CA . PRO A 351 ? 0.1077 0.1015 0.0786 -0.0042 -0.0058 -0.0109 433 PRO A CA 2759 C C . PRO A 351 ? 0.1343 0.1270 0.1028 -0.0043 -0.0046 -0.0121 433 PRO A C 2760 O O . PRO A 351 ? 0.1609 0.1532 0.1261 -0.0043 -0.0055 -0.0132 433 PRO A O 2761 C CB . PRO A 351 ? 0.1300 0.1246 0.1045 -0.0047 -0.0072 -0.0124 433 PRO A CB 2762 C CG . PRO A 351 ? 0.1447 0.1393 0.1231 -0.0050 -0.0054 -0.0121 433 PRO A CG 2763 C CD . PRO A 351 ? 0.1274 0.1220 0.1052 -0.0046 -0.0041 -0.0100 433 PRO A CD 2764 N N . LYS A 352 ? 0.1146 0.1068 0.0848 -0.0044 -0.0025 -0.0119 434 LYS A N 2765 C CA . LYS A 352 ? 0.1319 0.1231 0.1008 -0.0046 -0.0012 -0.0132 434 LYS A CA 2766 C C . LYS A 352 ? 0.1824 0.1728 0.1468 -0.0042 -0.0003 -0.0127 434 LYS A C 2767 O O . LYS A 352 ? 0.1557 0.1452 0.1177 -0.0042 0.0002 -0.0142 434 LYS A O 2768 C CB . LYS A 352 ? 0.1085 0.0994 0.0809 -0.0047 0.0007 -0.0130 434 LYS A CB 2769 C CG . LYS A 352 ? 0.1454 0.1366 0.1219 -0.0052 0.0003 -0.0139 434 LYS A CG 2770 C CD . LYS A 352 ? 0.1853 0.1762 0.1616 -0.0056 -0.0007 -0.0163 434 LYS A CD 2771 C CE . LYS A 352 ? 0.1963 0.1874 0.1774 -0.0062 -0.0008 -0.0172 434 LYS A CE 2772 N NZ . LYS A 352 ? 0.3053 0.2976 0.2884 -0.0064 -0.0025 -0.0170 434 LYS A NZ 2773 N N . GLU A 353 ? 0.1186 0.1092 0.0819 -0.0038 0.0001 -0.0107 435 GLU A N 2774 C CA . GLU A 353 ? 0.1141 0.1040 0.0735 -0.0034 0.0012 -0.0100 435 GLU A CA 2775 C C . GLU A 353 ? 0.1657 0.1560 0.1225 -0.0031 -0.0003 -0.0088 435 GLU A C 2776 O O . GLU A 353 ? 0.1600 0.1506 0.1174 -0.0029 -0.0001 -0.0069 435 GLU A O 2777 C CB . GLU A 353 ? 0.1232 0.1129 0.0841 -0.0033 0.0034 -0.0086 435 GLU A CB 2778 C CG . GLU A 353 ? 0.1381 0.1276 0.1023 -0.0035 0.0047 -0.0096 435 GLU A CG 2779 C CD . GLU A 353 ? 0.1402 0.1298 0.1064 -0.0033 0.0064 -0.0081 435 GLU A CD 2780 O OE1 . GLU A 353 ? 0.1343 0.1246 0.1027 -0.0032 0.0060 -0.0068 435 GLU A OE1 2781 O OE2 . GLU A 353 ? 0.1420 0.1309 0.1078 -0.0031 0.0081 -0.0085 435 GLU A OE2 2782 N N . ASP A 354 ? 0.1380 0.1285 0.0927 -0.0029 -0.0019 -0.0097 436 ASP A N 2783 C CA . ASP A 354 ? 0.1756 0.1668 0.1290 -0.0025 -0.0038 -0.0086 436 ASP A CA 2784 C C . ASP A 354 ? 0.1868 0.1782 0.1375 -0.0019 -0.0031 -0.0072 436 ASP A C 2785 O O . ASP A 354 ? 0.1893 0.1813 0.1387 -0.0016 -0.0046 -0.0062 436 ASP A O 2786 C CB . ASP A 354 ? 0.1839 0.1756 0.1372 -0.0027 -0.0064 -0.0102 436 ASP A CB 2787 C CG . ASP A 354 ? 0.3124 0.3040 0.2634 -0.0026 -0.0065 -0.0120 436 ASP A CG 2788 O OD1 . ASP A 354 ? 0.2698 0.2609 0.2189 -0.0023 -0.0046 -0.0119 436 ASP A OD1 2789 O OD2 . ASP A 354 ? 0.4094 0.4015 0.3607 -0.0029 -0.0085 -0.0136 436 ASP A OD2 2790 N N . LYS A 355 ? 0.1703 0.1613 0.1204 -0.0018 -0.0008 -0.0070 437 LYS A N 2791 C CA . LYS A 355 ? 0.1939 0.1850 0.1418 -0.0014 0.0002 -0.0055 437 LYS A CA 2792 C C . LYS A 355 ? 0.2080 0.1994 0.1574 -0.0012 0.0005 -0.0032 437 LYS A C 2793 O O . LYS A 355 ? 0.1655 0.1571 0.1133 -0.0010 0.0006 -0.0017 437 LYS A O 2794 C CB . LYS A 355 ? 0.2368 0.2274 0.1837 -0.0013 0.0025 -0.0061 437 LYS A CB 2795 C CG . LYS A 355 ? 0.2668 0.2572 0.2116 -0.0013 0.0021 -0.0084 437 LYS A CG 2796 C CD . LYS A 355 ? 0.4271 0.4169 0.3710 -0.0012 0.0045 -0.0091 437 LYS A CD 2797 C CE . LYS A 355 ? 0.4635 0.4530 0.4049 -0.0011 0.0039 -0.0114 437 LYS A CE 2798 N NZ . LYS A 355 ? 0.5648 0.5541 0.5083 -0.0014 0.0028 -0.0135 437 LYS A NZ 2799 N N . VAL A 356 ? 0.1540 0.1454 0.1064 -0.0015 0.0005 -0.0029 438 VAL A N 2800 C CA . VAL A 356 ? 0.1118 0.1035 0.0658 -0.0014 0.0003 -0.0010 438 VAL A CA 2801 C C . VAL A 356 ? 0.1352 0.1272 0.0900 -0.0015 -0.0021 -0.0011 438 VAL A C 2802 O O . VAL A 356 ? 0.1481 0.1401 0.1029 -0.0017 -0.0033 -0.0028 438 VAL A O 2803 C CB . VAL A 356 ? 0.1157 0.1073 0.0727 -0.0016 0.0019 -0.0005 438 VAL A CB 2804 C CG1 . VAL A 356 ? 0.1480 0.1394 0.1049 -0.0016 0.0041 -0.0003 438 VAL A CG1 2805 C CG2 . VAL A 356 ? 0.1213 0.1127 0.0800 -0.0021 0.0015 -0.0019 438 VAL A CG2 2806 N N . TRP A 357 ? 0.0867 0.0790 0.0424 -0.0012 -0.0027 0.0005 439 TRP A N 2807 C CA . TRP A 357 ? 0.1076 0.1001 0.0640 -0.0012 -0.0050 0.0006 439 TRP A CA 2808 C C . TRP A 357 ? 0.1197 0.1123 0.0791 -0.0015 -0.0051 0.0007 439 TRP A C 2809 O O . TRP A 357 ? 0.1225 0.1156 0.0837 -0.0015 -0.0068 0.0007 439 TRP A O 2810 C CB . TRP A 357 ? 0.1323 0.1250 0.0877 -0.0007 -0.0059 0.0022 439 TRP A CB 2811 C CG . TRP A 357 ? 0.1876 0.1804 0.1397 -0.0004 -0.0064 0.0020 439 TRP A CG 2812 C CD1 . TRP A 357 ? 0.2850 0.2776 0.2349 -0.0003 -0.0048 0.0025 439 TRP A CD1 2813 C CD2 . TRP A 357 ? 0.1877 0.1808 0.1385 -0.0003 -0.0087 0.0011 439 TRP A CD2 2814 N NE1 . TRP A 357 ? 0.3573 0.3500 0.3041 -0.0002 -0.0058 0.0020 439 TRP A NE1 2815 C CE2 . TRP A 357 ? 0.2802 0.2733 0.2276 -0.0001 -0.0083 0.0011 439 TRP A CE2 2816 C CE3 . TRP A 357 ? 0.2107 0.2044 0.1632 -0.0004 -0.0111 0.0002 439 TRP A CE3 2817 C CZ2 . TRP A 357 ? 0.3323 0.3257 0.2775 0.0000 -0.0103 0.0003 439 TRP A CZ2 2818 C CZ3 . TRP A 357 ? 0.3268 0.3209 0.2777 -0.0002 -0.0131 -0.0006 439 TRP A CZ3 2819 C CH2 . TRP A 357 ? 0.2752 0.2691 0.2223 -0.0001 -0.0127 -0.0005 439 TRP A CH2 2820 N N . TRP A 358 ? 0.1176 0.1099 0.0783 -0.0018 -0.0031 0.0008 440 TRP A N 2821 C CA . TRP A 358 ? 0.0836 0.0767 0.0485 -0.0019 -0.0028 0.0009 440 TRP A CA 2822 C C . TRP A 358 ? 0.1109 0.1043 0.0780 -0.0023 -0.0022 -0.0006 440 TRP A C 2823 O O . TRP A 358 ? 0.0995 0.0925 0.0652 -0.0025 -0.0018 -0.0018 440 TRP A O 2824 C CB . TRP A 358 ? 0.0909 0.0838 0.0565 -0.0019 -0.0013 0.0024 440 TRP A CB 2825 C CG . TRP A 358 ? 0.0843 0.0766 0.0483 -0.0019 0.0006 0.0025 440 TRP A CG 2826 C CD1 . TRP A 358 ? 0.1027 0.0950 0.0655 -0.0016 0.0013 0.0034 440 TRP A CD1 2827 C CD2 . TRP A 358 ? 0.0939 0.0860 0.0590 -0.0021 0.0020 0.0016 440 TRP A CD2 2828 N NE1 . TRP A 358 ? 0.1093 0.1014 0.0722 -0.0016 0.0032 0.0030 440 TRP A NE1 2829 C CE2 . TRP A 358 ? 0.1470 0.1389 0.1112 -0.0019 0.0036 0.0020 440 TRP A CE2 2830 C CE3 . TRP A 358 ? 0.0802 0.0728 0.0480 -0.0024 0.0022 0.0006 440 TRP A CE3 2831 C CZ2 . TRP A 358 ? 0.0963 0.0880 0.0613 -0.0021 0.0052 0.0014 440 TRP A CZ2 2832 C CZ3 . TRP A 358 ? 0.0852 0.0775 0.0537 -0.0024 0.0037 0.0001 440 TRP A CZ3 2833 C CH2 . TRP A 358 ? 0.0974 0.0890 0.0642 -0.0023 0.0052 0.0005 440 TRP A CH2 2834 N N . THR A 359 ? 0.0596 0.0537 0.0302 -0.0024 -0.0022 -0.0005 441 THR A N 2835 C CA . THR A 359 ? 0.0725 0.0667 0.0453 -0.0028 -0.0013 -0.0014 441 THR A CA 2836 C C . THR A 359 ? 0.0543 0.0486 0.0289 -0.0027 -0.0003 -0.0004 441 THR A C 2837 O O . THR A 359 ? 0.0761 0.0708 0.0520 -0.0026 -0.0008 0.0003 441 THR A O 2838 C CB . THR A 359 ? 0.0718 0.0667 0.0469 -0.0030 -0.0024 -0.0025 441 THR A CB 2839 O OG1 . THR A 359 ? 0.0929 0.0877 0.0665 -0.0031 -0.0036 -0.0037 441 THR A OG1 2840 C CG2 . THR A 359 ? 0.0600 0.0549 0.0377 -0.0034 -0.0012 -0.0031 441 THR A CG2 2841 N N . SER A 360 ? 0.0578 0.0517 0.0328 -0.0028 0.0012 -0.0005 442 SER A N 2842 C CA . SER A 360 ? 0.0711 0.0651 0.0479 -0.0027 0.0019 0.0003 442 SER A CA 2843 C C . SER A 360 ? 0.0870 0.0806 0.0649 -0.0029 0.0029 -0.0002 442 SER A C 2844 O O . SER A 360 ? 0.0964 0.0899 0.0744 -0.0031 0.0030 -0.0013 442 SER A O 2845 C CB . SER A 360 ? 0.0679 0.0617 0.0439 -0.0025 0.0024 0.0015 442 SER A CB 2846 O OG . SER A 360 ? 0.0860 0.0800 0.0637 -0.0024 0.0026 0.0022 442 SER A OG 2847 N N . ASN A 361 ? 0.0677 0.0612 0.0467 -0.0028 0.0037 0.0005 443 ASN A N 2848 C CA . ASN A 361 ? 0.0601 0.0532 0.0402 -0.0028 0.0046 0.0002 443 ASN A CA 2849 C C . ASN A 361 ? 0.0597 0.0527 0.0405 -0.0026 0.0051 0.0011 443 ASN A C 2850 O O . ASN A 361 ? 0.0809 0.0742 0.0617 -0.0024 0.0048 0.0019 443 ASN A O 2851 C CB . ASN A 361 ? 0.0506 0.0437 0.0322 -0.0030 0.0044 -0.0001 443 ASN A CB 2852 C CG . ASN A 361 ? 0.0711 0.0645 0.0534 -0.0029 0.0041 0.0007 443 ASN A CG 2853 O OD1 . ASN A 361 ? 0.0763 0.0702 0.0584 -0.0029 0.0033 0.0009 443 ASN A OD1 2854 N ND2 . ASN A 361 ? 0.0649 0.0579 0.0478 -0.0028 0.0046 0.0013 443 ASN A ND2 2855 N N . SER A 362 ? 0.0602 0.0527 0.0419 -0.0025 0.0059 0.0010 444 SER A N 2856 C CA . SER A 362 ? 0.0716 0.0640 0.0545 -0.0022 0.0061 0.0019 444 SER A CA 2857 C C . SER A 362 ? 0.0893 0.0812 0.0731 -0.0023 0.0062 0.0020 444 SER A C 2858 O O . SER A 362 ? 0.0781 0.0698 0.0620 -0.0025 0.0063 0.0013 444 SER A O 2859 C CB . SER A 362 ? 0.0610 0.0532 0.0444 -0.0020 0.0070 0.0021 444 SER A CB 2860 O OG . SER A 362 ? 0.0838 0.0754 0.0677 -0.0020 0.0078 0.0014 444 SER A OG 2861 N N . ILE A 363 ? 0.0599 0.0516 0.0446 -0.0020 0.0062 0.0027 445 ILE A N 2862 C CA . ILE A 363 ? 0.0631 0.0542 0.0482 -0.0019 0.0063 0.0031 445 ILE A CA 2863 C C . ILE A 363 ? 0.0676 0.0580 0.0539 -0.0016 0.0067 0.0035 445 ILE A C 2864 O O . ILE A 363 ? 0.0654 0.0561 0.0523 -0.0013 0.0066 0.0039 445 ILE A O 2865 C CB . ILE A 363 ? 0.0733 0.0645 0.0579 -0.0018 0.0056 0.0037 445 ILE A CB 2866 C CG1 . ILE A 363 ? 0.0977 0.0894 0.0815 -0.0021 0.0052 0.0033 445 ILE A CG1 2867 C CG2 . ILE A 363 ? 0.0775 0.0678 0.0620 -0.0017 0.0057 0.0043 445 ILE A CG2 2868 C CD1 . ILE A 363 ? 0.0761 0.0680 0.0594 -0.0020 0.0045 0.0037 445 ILE A CD1 2869 N N . VAL A 364 ? 0.0616 0.0512 0.0485 -0.0016 0.0072 0.0034 446 VAL A N 2870 C CA . VAL A 364 ? 0.0692 0.0580 0.0573 -0.0012 0.0074 0.0042 446 VAL A CA 2871 C C . VAL A 364 ? 0.0753 0.0633 0.0628 -0.0012 0.0073 0.0049 446 VAL A C 2872 O O . VAL A 364 ? 0.0746 0.0625 0.0617 -0.0016 0.0077 0.0045 446 VAL A O 2873 C CB . VAL A 364 ? 0.0663 0.0547 0.0559 -0.0012 0.0083 0.0035 446 VAL A CB 2874 C CG1 . VAL A 364 ? 0.0927 0.0804 0.0823 -0.0016 0.0090 0.0027 446 VAL A CG1 2875 C CG2 . VAL A 364 ? 0.0870 0.0747 0.0783 -0.0006 0.0084 0.0044 446 VAL A CG2 2876 N N A SER A 365 ? 0.0699 0.0573 0.0576 -0.0007 0.0069 0.0060 447 SER A N 2877 N N B SER A 365 ? 0.0699 0.0573 0.0575 -0.0008 0.0069 0.0060 447 SER A N 2878 C CA A SER A 365 ? 0.0812 0.0676 0.0677 -0.0007 0.0068 0.0069 447 SER A CA 2879 C CA B SER A 365 ? 0.0813 0.0676 0.0679 -0.0007 0.0069 0.0069 447 SER A CA 2880 C C A SER A 365 ? 0.0876 0.0729 0.0750 -0.0001 0.0067 0.0080 447 SER A C 2881 C C B SER A 365 ? 0.0876 0.0729 0.0752 -0.0001 0.0068 0.0079 447 SER A C 2882 O O A SER A 365 ? 0.0847 0.0704 0.0734 0.0003 0.0061 0.0083 447 SER A O 2883 O O B SER A 365 ? 0.0847 0.0704 0.0732 0.0003 0.0061 0.0082 447 SER A O 2884 C CB A SER A 365 ? 0.0805 0.0674 0.0651 -0.0006 0.0058 0.0073 447 SER A CB 2885 C CB B SER A 365 ? 0.0809 0.0674 0.0655 -0.0006 0.0061 0.0074 447 SER A CB 2886 O OG A SER A 365 ? 0.1882 0.1740 0.1712 -0.0005 0.0060 0.0081 447 SER A OG 2887 O OG B SER A 365 ? 0.1863 0.1735 0.1710 -0.0003 0.0051 0.0075 447 SER A OG 2888 N N . MET A 366 ? 0.0903 0.0744 0.0774 -0.0002 0.0073 0.0087 448 MET A N 2889 C CA . MET A 366 ? 0.0801 0.0629 0.0679 0.0004 0.0072 0.0099 448 MET A CA 2890 C C . MET A 366 ? 0.0881 0.0696 0.0735 0.0005 0.0071 0.0113 448 MET A C 2891 O O . MET A 366 ? 0.0955 0.0770 0.0792 0.0001 0.0077 0.0110 448 MET A O 2892 C CB . MET A 366 ? 0.0576 0.0395 0.0476 0.0002 0.0084 0.0095 448 MET A CB 2893 C CG . MET A 366 ? 0.1321 0.1150 0.1238 -0.0002 0.0090 0.0079 448 MET A CG 2894 S SD . MET A 366 ? 0.1935 0.1770 0.1873 0.0004 0.0086 0.0077 448 MET A SD 2895 C CE . MET A 366 ? 0.1418 0.1236 0.1382 0.0009 0.0093 0.0084 448 MET A CE 2896 N N . CYS A 367 ? 0.0953 0.0758 0.0805 0.0012 0.0063 0.0127 449 CYS A N 2897 C CA . CYS A 367 ? 0.1137 0.0926 0.0963 0.0014 0.0063 0.0142 449 CYS A CA 2898 C C . CYS A 367 ? 0.1143 0.0915 0.0983 0.0019 0.0067 0.0155 449 CYS A C 2899 O O . CYS A 367 ? 0.1158 0.0933 0.1028 0.0022 0.0066 0.0152 449 CYS A O 2900 C CB . CYS A 367 ? 0.1303 0.1094 0.1102 0.0020 0.0046 0.0148 449 CYS A CB 2901 S SG . CYS A 367 ? 0.1332 0.1138 0.1112 0.0015 0.0043 0.0135 449 CYS A SG 2902 N N . SER A 368 ? 0.1100 0.0854 0.0920 0.0019 0.0073 0.0169 450 SER A N 2903 C CA . SER A 368 ? 0.1034 0.0772 0.0870 0.0023 0.0077 0.0182 450 SER A CA 2904 C C . SER A 368 ? 0.0959 0.0692 0.0794 0.0033 0.0058 0.0196 450 SER A C 2905 O O . SER A 368 ? 0.1202 0.0940 0.1013 0.0037 0.0042 0.0199 450 SER A O 2906 C CB . SER A 368 ? 0.0940 0.0671 0.0765 0.0018 0.0088 0.0186 450 SER A CB 2907 O OG . SER A 368 ? 0.1297 0.1028 0.1087 0.0019 0.0079 0.0194 450 SER A OG 2908 N N . SER A 369 ? 0.1147 0.0870 0.1011 0.0037 0.0060 0.0203 451 SER A N 2909 C CA . SER A 369 ? 0.1103 0.0819 0.0971 0.0047 0.0042 0.0218 451 SER A CA 2910 C C . SER A 369 ? 0.1268 0.0967 0.1138 0.0047 0.0047 0.0230 451 SER A C 2911 O O . SER A 369 ? 0.1198 0.0892 0.1085 0.0041 0.0065 0.0225 451 SER A O 2912 C CB . SER A 369 ? 0.1225 0.0948 0.1136 0.0053 0.0038 0.0213 451 SER A CB 2913 O OG . SER A 369 ? 0.1320 0.1037 0.1243 0.0063 0.0021 0.0227 451 SER A OG 2914 N N . THR A 370 ? 0.1071 0.0760 0.0923 0.0053 0.0029 0.0245 452 THR A N 2915 C CA . THR A 370 ? 0.1299 0.0969 0.1154 0.0055 0.0032 0.0259 452 THR A CA 2916 C C . THR A 370 ? 0.1771 0.1436 0.1670 0.0062 0.0029 0.0261 452 THR A C 2917 O O . THR A 370 ? 0.1423 0.1073 0.1334 0.0064 0.0033 0.0271 452 THR A O 2918 C CB . THR A 370 ? 0.1445 0.1106 0.1261 0.0058 0.0014 0.0276 452 THR A CB 2919 O OG1 . THR A 370 ? 0.1591 0.1254 0.1404 0.0067 -0.0011 0.0280 452 THR A OG1 2920 C CG2 . THR A 370 ? 0.1615 0.1283 0.1391 0.0050 0.0020 0.0273 452 THR A CG2 2921 N N . GLU A 371 ? 0.1274 0.0953 0.1201 0.0067 0.0023 0.0252 453 GLU A N 2922 C CA . GLU A 371 ? 0.1341 0.1021 0.1318 0.0073 0.0025 0.0249 453 GLU A CA 2923 C C . GLU A 371 ? 0.1181 0.0863 0.1188 0.0065 0.0049 0.0234 453 GLU A C 2924 O O . GLU A 371 ? 0.1351 0.1038 0.1341 0.0056 0.0062 0.0225 453 GLU A O 2925 C CB . GLU A 371 ? 0.1357 0.1054 0.1357 0.0080 0.0010 0.0245 453 GLU A CB 2926 C CG . GLU A 371 ? 0.1815 0.1512 0.1788 0.0087 -0.0017 0.0256 453 GLU A CG 2927 C CD . GLU A 371 ? 0.2409 0.2088 0.2380 0.0096 -0.0030 0.0272 453 GLU A CD 2928 O OE1 . GLU A 371 ? 0.2967 0.2642 0.2978 0.0099 -0.0022 0.0272 453 GLU A OE1 2929 O OE2 . GLU A 371 ? 0.3733 0.3404 0.3663 0.0100 -0.0047 0.0283 453 GLU A OE2 2930 N N . PHE A 372 ? 0.1063 0.0742 0.1114 0.0068 0.0055 0.0230 454 PHE A N 2931 C CA . PHE A 372 ? 0.1310 0.0991 0.1392 0.0062 0.0077 0.0213 454 PHE A CA 2932 C C . PHE A 372 ? 0.1701 0.1397 0.1813 0.0064 0.0077 0.0198 454 PHE A C 2933 O O . PHE A 372 ? 0.1452 0.1149 0.1604 0.0070 0.0076 0.0195 454 PHE A O 2934 C CB . PHE A 372 ? 0.1672 0.1339 0.1782 0.0062 0.0086 0.0215 454 PHE A CB 2935 C CG . PHE A 372 ? 0.1262 0.0915 0.1347 0.0058 0.0091 0.0227 454 PHE A CG 2936 C CD1 . PHE A 372 ? 0.1858 0.1499 0.1915 0.0064 0.0076 0.0248 454 PHE A CD1 2937 C CD2 . PHE A 372 ? 0.1622 0.1272 0.1711 0.0048 0.0110 0.0217 454 PHE A CD2 2938 C CE1 . PHE A 372 ? 0.1971 0.1598 0.2005 0.0059 0.0082 0.0259 454 PHE A CE1 2939 C CE2 . PHE A 372 ? 0.1501 0.1138 0.1570 0.0044 0.0116 0.0228 454 PHE A CE2 2940 C CZ . PHE A 372 ? 0.1771 0.1397 0.1813 0.0049 0.0103 0.0250 454 PHE A CZ 2941 N N . LEU A 373 ? 0.1153 0.0862 0.1246 0.0060 0.0077 0.0190 455 LEU A N 2942 C CA . LEU A 373 ? 0.1090 0.0820 0.1202 0.0061 0.0073 0.0173 455 LEU A CA 2943 C C . LEU A 373 ? 0.1326 0.1061 0.1463 0.0055 0.0092 0.0150 455 LEU A C 2944 O O . LEU A 373 ? 0.1356 0.1085 0.1485 0.0047 0.0106 0.0141 455 LEU A O 2945 C CB . LEU A 373 ? 0.1060 0.0807 0.1136 0.0057 0.0063 0.0169 455 LEU A CB 2946 C CG . LEU A 373 ? 0.1064 0.0808 0.1111 0.0063 0.0043 0.0188 455 LEU A CG 2947 C CD1 . LEU A 373 ? 0.1316 0.1077 0.1331 0.0057 0.0036 0.0179 455 LEU A CD1 2948 C CD2 . LEU A 373 ? 0.1025 0.0770 0.1100 0.0074 0.0026 0.0198 455 LEU A CD2 2949 N N . GLY A 374 ? 0.1259 0.1005 0.1428 0.0059 0.0092 0.0140 456 GLY A N 2950 C CA . GLY A 374 ? 0.1060 0.0813 0.1246 0.0054 0.0110 0.0116 456 GLY A CA 2951 C C . GLY A 374 ? 0.1054 0.0821 0.1207 0.0044 0.0113 0.0101 456 GLY A C 2952 O O . GLY A 374 ? 0.1177 0.0954 0.1302 0.0043 0.0102 0.0107 456 GLY A O 2953 N N . GLN A 375 ? 0.1026 0.0793 0.1182 0.0037 0.0129 0.0082 457 GLN A N 2954 C CA . GLN A 375 ? 0.0992 0.0771 0.1116 0.0028 0.0131 0.0068 457 GLN A CA 2955 C C . GLN A 375 ? 0.0984 0.0778 0.1112 0.0027 0.0137 0.0050 457 GLN A C 2956 O O . GLN A 375 ? 0.1053 0.0845 0.1208 0.0030 0.0148 0.0040 457 GLN A O 2957 C CB . GLN A 375 ? 0.0964 0.0733 0.1082 0.0020 0.0141 0.0059 457 GLN A CB 2958 C CG . GLN A 375 ? 0.1133 0.0893 0.1281 0.0019 0.0155 0.0042 457 GLN A CG 2959 C CD . GLN A 375 ? 0.2092 0.1842 0.2236 0.0011 0.0164 0.0032 457 GLN A CD 2960 O OE1 . GLN A 375 ? 0.2397 0.2149 0.2518 0.0005 0.0160 0.0036 457 GLN A OE1 2961 N NE2 . GLN A 375 ? 0.2520 0.2261 0.2691 0.0010 0.0175 0.0016 457 GLN A NE2 2962 N N . TRP A 376 ? 0.0869 0.0677 0.0968 0.0023 0.0132 0.0047 458 TRP A N 2963 C CA . TRP A 376 ? 0.0880 0.0700 0.0973 0.0020 0.0139 0.0030 458 TRP A CA 2964 C C . TRP A 376 ? 0.1303 0.1125 0.1366 0.0011 0.0141 0.0019 458 TRP A C 2965 O O . TRP A 376 ? 0.1911 0.1726 0.1965 0.0007 0.0138 0.0023 458 TRP A O 2966 C CB . TRP A 376 ? 0.0876 0.0711 0.0964 0.0022 0.0131 0.0037 458 TRP A CB 2967 C CG . TRP A 376 ? 0.0979 0.0823 0.1080 0.0023 0.0142 0.0025 458 TRP A CG 2968 C CD1 . TRP A 376 ? 0.1052 0.0892 0.1166 0.0023 0.0158 0.0009 458 TRP A CD1 2969 C CD2 . TRP A 376 ? 0.0983 0.0841 0.1086 0.0025 0.0139 0.0028 458 TRP A CD2 2970 N NE1 . TRP A 376 ? 0.0791 0.0641 0.0913 0.0024 0.0167 0.0003 458 TRP A NE1 2971 C CE2 . TRP A 376 ? 0.1001 0.0862 0.1117 0.0025 0.0155 0.0015 458 TRP A CE2 2972 C CE3 . TRP A 376 ? 0.0723 0.0591 0.0818 0.0026 0.0124 0.0040 458 TRP A CE3 2973 C CZ2 . TRP A 376 ? 0.1225 0.1099 0.1350 0.0027 0.0159 0.0015 458 TRP A CZ2 2974 C CZ3 . TRP A 376 ? 0.0796 0.0676 0.0901 0.0027 0.0126 0.0039 458 TRP A CZ3 2975 C CH2 . TRP A 376 ? 0.0670 0.0554 0.0790 0.0027 0.0144 0.0028 458 TRP A CH2 2976 N N . ASN A 377 ? 0.1120 0.0953 0.1169 0.0007 0.0146 0.0005 459 ASN A N 2977 C CA . ASN A 377 ? 0.0821 0.0657 0.0840 0.0000 0.0144 -0.0004 459 ASN A CA 2978 C C . ASN A 377 ? 0.1102 0.0953 0.1100 -0.0001 0.0138 -0.0001 459 ASN A C 2979 O O . ASN A 377 ? 0.0974 0.0831 0.0983 0.0004 0.0141 0.0002 459 ASN A O 2980 C CB . ASN A 377 ? 0.0885 0.0717 0.0903 -0.0004 0.0155 -0.0025 459 ASN A CB 2981 C CG . ASN A 377 ? 0.1186 0.1024 0.1203 -0.0002 0.0165 -0.0036 459 ASN A CG 2982 O OD1 . ASN A 377 ? 0.1104 0.0951 0.1096 -0.0005 0.0164 -0.0041 459 ASN A OD1 2983 N ND2 . ASN A 377 ? 0.1195 0.1027 0.1242 0.0003 0.0175 -0.0038 459 ASN A ND2 2984 N N . TRP A 378 ? 0.0869 0.0725 0.0842 -0.0006 0.0130 -0.0001 460 TRP A N 2985 C CA . TRP A 378 ? 0.0780 0.0648 0.0735 -0.0006 0.0122 0.0006 460 TRP A CA 2986 C C . TRP A 378 ? 0.0734 0.0608 0.0664 -0.0011 0.0121 -0.0005 460 TRP A C 2987 O O . TRP A 378 ? 0.1242 0.1118 0.1158 -0.0015 0.0113 -0.0003 460 TRP A O 2988 C CB . TRP A 378 ? 0.0754 0.0622 0.0706 -0.0004 0.0111 0.0021 460 TRP A CB 2989 C CG . TRP A 378 ? 0.0748 0.0610 0.0721 0.0002 0.0108 0.0033 460 TRP A CG 2990 C CD1 . TRP A 378 ? 0.0935 0.0785 0.0921 0.0004 0.0109 0.0039 460 TRP A CD1 2991 C CD2 . TRP A 378 ? 0.0705 0.0574 0.0692 0.0007 0.0102 0.0042 460 TRP A CD2 2992 N NE1 . TRP A 378 ? 0.0970 0.0817 0.0973 0.0011 0.0104 0.0052 460 TRP A NE1 2993 C CE2 . TRP A 378 ? 0.0767 0.0626 0.0772 0.0013 0.0099 0.0053 460 TRP A CE2 2994 C CE3 . TRP A 378 ? 0.0698 0.0578 0.0684 0.0008 0.0100 0.0042 460 TRP A CE3 2995 C CZ2 . TRP A 378 ? 0.0840 0.0703 0.0864 0.0019 0.0091 0.0063 460 TRP A CZ2 2996 C CZ3 . TRP A 378 ? 0.0820 0.0704 0.0827 0.0014 0.0093 0.0052 460 TRP A CZ3 2997 C CH2 . TRP A 378 ? 0.0939 0.0815 0.0965 0.0019 0.0088 0.0061 460 TRP A CH2 2998 N N . PRO A 379 ? 0.0643 0.0520 0.0566 -0.0011 0.0129 -0.0014 461 PRO A N 2999 C CA . PRO A 379 ? 0.0873 0.0755 0.0768 -0.0015 0.0128 -0.0024 461 PRO A CA 3000 C C . PRO A 379 ? 0.0558 0.0450 0.0440 -0.0015 0.0119 -0.0013 461 PRO A C 3001 O O . PRO A 379 ? 0.0841 0.0736 0.0734 -0.0012 0.0118 -0.0002 461 PRO A O 3002 C CB . PRO A 379 ? 0.1147 0.1027 0.1039 -0.0014 0.0141 -0.0035 461 PRO A CB 3003 C CG . PRO A 379 ? 0.1576 0.1450 0.1499 -0.0010 0.0151 -0.0034 461 PRO A CG 3004 C CD . PRO A 379 ? 0.0978 0.0853 0.0918 -0.0007 0.0141 -0.0017 461 PRO A CD 3005 N N . ASP A 380 ? 0.0600 0.0495 0.0457 -0.0019 0.0113 -0.0018 462 ASP A N 3006 C CA . ASP A 380 ? 0.0523 0.0427 0.0368 -0.0019 0.0107 -0.0009 462 ASP A CA 3007 C C . ASP A 380 ? 0.0766 0.0671 0.0613 -0.0016 0.0117 -0.0005 462 ASP A C 3008 O O . ASP A 380 ? 0.0982 0.0893 0.0839 -0.0014 0.0114 0.0006 462 ASP A O 3009 C CB . ASP A 380 ? 0.0645 0.0551 0.0464 -0.0022 0.0100 -0.0015 462 ASP A CB 3010 C CG . ASP A 380 ? 0.0867 0.0779 0.0673 -0.0022 0.0096 -0.0006 462 ASP A CG 3011 O OD1 . ASP A 380 ? 0.1119 0.1035 0.0931 -0.0021 0.0088 0.0003 462 ASP A OD1 3012 O OD2 . ASP A 380 ? 0.0955 0.0866 0.0742 -0.0022 0.0102 -0.0009 462 ASP A OD2 3013 N N . GLY A 381 ? 0.0608 0.0509 0.0447 -0.0016 0.0129 -0.0015 463 GLY A N 3014 C CA . GLY A 381 ? 0.0955 0.0857 0.0801 -0.0013 0.0143 -0.0013 463 GLY A CA 3015 C C . GLY A 381 ? 0.1058 0.0962 0.0878 -0.0015 0.0147 -0.0011 463 GLY A C 3016 O O . GLY A 381 ? 0.1024 0.0929 0.0848 -0.0013 0.0162 -0.0010 463 GLY A O 3017 N N . ALA A 382 ? 0.0882 0.0787 0.0675 -0.0017 0.0136 -0.0011 464 ALA A N 3018 C CA . ALA A 382 ? 0.0761 0.0667 0.0527 -0.0018 0.0139 -0.0007 464 ALA A CA 3019 C C . ALA A 382 ? 0.0976 0.0874 0.0711 -0.0019 0.0148 -0.0021 464 ALA A C 3020 O O . ALA A 382 ? 0.1036 0.0930 0.0767 -0.0020 0.0144 -0.0034 464 ALA A O 3021 C CB . ALA A 382 ? 0.0809 0.0719 0.0561 -0.0020 0.0122 0.0000 464 ALA A CB 3022 N N . LYS A 383 ? 0.1237 0.1133 0.0951 -0.0018 0.0160 -0.0018 465 LYS A N 3023 C CA . LYS A 383 ? 0.1587 0.1480 0.1275 -0.0018 0.0162 -0.0029 465 LYS A CA 3024 C C . LYS A 383 ? 0.1189 0.1085 0.0847 -0.0018 0.0145 -0.0023 465 LYS A C 3025 O O . LYS A 383 ? 0.1227 0.1128 0.0884 -0.0017 0.0145 -0.0009 465 LYS A O 3026 C CB . LYS A 383 ? 0.1483 0.1375 0.1176 -0.0015 0.0182 -0.0028 465 LYS A CB 3027 C CG . LYS A 383 ? 0.2171 0.2060 0.1897 -0.0014 0.0199 -0.0033 465 LYS A CG 3028 C CD . LYS A 383 ? 0.3487 0.3377 0.3226 -0.0012 0.0219 -0.0030 465 LYS A CD 3029 C CE . LYS A 383 ? 0.3859 0.3744 0.3571 -0.0011 0.0228 -0.0043 465 LYS A CE 3030 N NZ . LYS A 383 ? 0.5612 0.5490 0.5332 -0.0011 0.0233 -0.0061 465 LYS A NZ 3031 N N . ILE A 384 ? 0.1257 0.1151 0.0897 -0.0019 0.0132 -0.0035 466 ILE A N 3032 C CA . ILE A 384 ? 0.1487 0.1385 0.1103 -0.0019 0.0113 -0.0031 466 ILE A CA 3033 C C . ILE A 384 ? 0.1766 0.1665 0.1357 -0.0016 0.0117 -0.0024 466 ILE A C 3034 O O . ILE A 384 ? 0.1465 0.1369 0.1047 -0.0015 0.0107 -0.0011 466 ILE A O 3035 C CB . ILE A 384 ? 0.2845 0.2739 0.2446 -0.0021 0.0099 -0.0048 466 ILE A CB 3036 C CG1 . ILE A 384 ? 0.2746 0.2642 0.2365 -0.0024 0.0087 -0.0048 466 ILE A CG1 3037 C CG2 . ILE A 384 ? 0.4667 0.4564 0.4235 -0.0019 0.0085 -0.0048 466 ILE A CG2 3038 C CD1 . ILE A 384 ? 0.2194 0.2096 0.1813 -0.0024 0.0072 -0.0032 466 ILE A CD1 3039 N N . GLU A 385 ? 0.1917 0.1813 0.1500 -0.0015 0.0133 -0.0032 467 GLU A N 3040 C CA . GLU A 385 ? 0.2017 0.1913 0.1575 -0.0013 0.0141 -0.0026 467 GLU A CA 3041 C C . GLU A 385 ? 0.1725 0.1625 0.1294 -0.0013 0.0147 -0.0006 467 GLU A C 3042 O O . GLU A 385 ? 0.1693 0.1594 0.1239 -0.0012 0.0146 0.0004 467 GLU A O 3043 C CB . GLU A 385 ? 0.2383 0.2274 0.1936 -0.0012 0.0161 -0.0038 467 GLU A CB 3044 C CG . GLU A 385 ? 0.3545 0.3435 0.3133 -0.0012 0.0181 -0.0033 467 GLU A CG 3045 C CD . GLU A 385 ? 0.6347 0.6231 0.5943 -0.0012 0.0198 -0.0050 467 GLU A CD 3046 O OE1 . GLU A 385 ? 0.6322 0.6204 0.5909 -0.0010 0.0215 -0.0051 467 GLU A OE1 3047 O OE2 . GLU A 385 ? 0.6152 0.6032 0.5763 -0.0013 0.0195 -0.0061 467 GLU A OE2 3048 N N . TYR A 386 ? 0.1243 0.1145 0.0847 -0.0014 0.0152 0.0002 468 TYR A N 3049 C CA . TYR A 386 ? 0.1287 0.1192 0.0906 -0.0015 0.0158 0.0019 468 TYR A CA 3050 C C . TYR A 386 ? 0.1514 0.1423 0.1125 -0.0015 0.0139 0.0031 468 TYR A C 3051 O O . TYR A 386 ? 0.1280 0.1190 0.0894 -0.0015 0.0142 0.0046 468 TYR A O 3052 C CB . TYR A 386 ? 0.1125 0.1032 0.0785 -0.0016 0.0165 0.0023 468 TYR A CB 3053 C CG . TYR A 386 ? 0.1230 0.1134 0.0909 -0.0015 0.0186 0.0016 468 TYR A CG 3054 C CD1 . TYR A 386 ? 0.1653 0.1553 0.1314 -0.0014 0.0201 0.0011 468 TYR A CD1 3055 C CD2 . TYR A 386 ? 0.0903 0.0808 0.0617 -0.0015 0.0192 0.0015 468 TYR A CD2 3056 C CE1 . TYR A 386 ? 0.1685 0.1583 0.1367 -0.0013 0.0222 0.0004 468 TYR A CE1 3057 C CE2 . TYR A 386 ? 0.1158 0.1061 0.0894 -0.0014 0.0212 0.0009 468 TYR A CE2 3058 C CZ . TYR A 386 ? 0.1459 0.1359 0.1181 -0.0013 0.0227 0.0003 468 TYR A CZ 3059 O OH . TYR A 386 ? 0.1450 0.1349 0.1198 -0.0011 0.0246 -0.0003 468 TYR A OH 3060 N N . PHE A 387 ? 0.1273 0.1183 0.0875 -0.0015 0.0121 0.0025 469 PHE A N 3061 C CA . PHE A 387 ? 0.1463 0.1377 0.1061 -0.0014 0.0102 0.0035 469 PHE A CA 3062 C C . PHE A 387 ? 0.2269 0.2181 0.1831 -0.0013 0.0093 0.0037 469 PHE A C 3063 O O . PHE A 387 ? 0.2190 0.2105 0.1748 -0.0012 0.0078 0.0046 469 PHE A O 3064 C CB . PHE A 387 ? 0.1163 0.1077 0.0772 -0.0015 0.0087 0.0028 469 PHE A CB 3065 C CG . PHE A 387 ? 0.1277 0.1192 0.0919 -0.0017 0.0091 0.0031 469 PHE A CG 3066 C CD1 . PHE A 387 ? 0.1175 0.1088 0.0831 -0.0018 0.0102 0.0021 469 PHE A CD1 3067 C CD2 . PHE A 387 ? 0.1270 0.1189 0.0929 -0.0017 0.0084 0.0043 469 PHE A CD2 3068 C CE1 . PHE A 387 ? 0.1223 0.1137 0.0908 -0.0019 0.0105 0.0025 469 PHE A CE1 3069 C CE2 . PHE A 387 ? 0.0996 0.0915 0.0682 -0.0018 0.0087 0.0046 469 PHE A CE2 3070 C CZ . PHE A 387 ? 0.1353 0.1270 0.1051 -0.0019 0.0097 0.0037 469 PHE A CZ 3071 N N . LEU A 388 ? 0.1765 0.1675 0.1303 -0.0012 0.0103 0.0029 470 LEU A N 3072 C CA . LEU A 388 ? 0.2240 0.2149 0.1740 -0.0010 0.0093 0.0029 470 LEU A CA 3073 C C . LEU A 388 ? 0.3135 0.3043 0.2621 -0.0010 0.0103 0.0046 470 LEU A C 3074 O O . LEU A 388 ? 0.2487 0.2394 0.1991 -0.0011 0.0120 0.0055 470 LEU A O 3075 C CB . LEU A 388 ? 0.1951 0.1857 0.1428 -0.0009 0.0097 0.0010 470 LEU A CB 3076 C CG . LEU A 388 ? 0.2280 0.2185 0.1768 -0.0010 0.0088 -0.0009 470 LEU A CG 3077 C CD1 . LEU A 388 ? 0.2724 0.2625 0.2187 -0.0009 0.0090 -0.0029 470 LEU A CD1 3078 C CD2 . LEU A 388 ? 0.1805 0.1714 0.1297 -0.0010 0.0063 -0.0007 470 LEU A CD2 3079 O OXT . LEU A 388 ? 0.3803 0.3710 0.3259 -0.0008 0.0092 0.0052 470 LEU A OXT 3080 C C1 . NAG B . ? 0.4903 0.4638 0.4172 0.0011 0.0155 0.0109 501 NAG A C1 3081 C C2 . NAG B . ? 0.4383 0.4120 0.3619 0.0016 0.0130 0.0103 501 NAG A C2 3082 C C3 . NAG B . ? 0.5551 0.5287 0.4760 0.0017 0.0137 0.0085 501 NAG A C3 3083 C C4 . NAG B . ? 0.5286 0.5011 0.4468 0.0015 0.0164 0.0091 501 NAG A C4 3084 C C5 . NAG B . ? 0.5781 0.5506 0.5004 0.0010 0.0189 0.0096 501 NAG A C5 3085 C C6 . NAG B . ? 0.5544 0.5258 0.4747 0.0008 0.0219 0.0101 501 NAG A C6 3086 C C7 . NAG B . ? 0.5097 0.4844 0.4348 0.0022 0.0081 0.0106 501 NAG A C7 3087 C C8 . NAG B . ? 0.3952 0.3710 0.3238 0.0023 0.0060 0.0102 501 NAG A C8 3088 N N2 . NAG B . ? 0.4783 0.4531 0.4047 0.0018 0.0106 0.0098 501 NAG A N2 3089 O O3 . NAG B . ? 0.5582 0.5318 0.4757 0.0021 0.0113 0.0080 501 NAG A O3 3090 O O4 . NAG B . ? 0.6916 0.6641 0.6076 0.0016 0.0173 0.0073 501 NAG A O4 3091 O O5 . NAG B . ? 0.5317 0.5041 0.4560 0.0010 0.0180 0.0113 501 NAG A O5 3092 O O6 . NAG B . ? 0.6542 0.6242 0.5701 0.0011 0.0217 0.0118 501 NAG A O6 3093 O O7 . NAG B . ? 0.5996 0.5733 0.5209 0.0025 0.0074 0.0117 501 NAG A O7 3094 C C1 . NAG C . ? 0.2932 0.2865 0.2463 0.0008 -0.0113 0.0058 502 NAG A C1 3095 C C2 . NAG C . ? 0.3003 0.2933 0.2499 0.0010 -0.0102 0.0069 502 NAG A C2 3096 C C3 . NAG C . ? 0.4281 0.4213 0.3747 0.0011 -0.0118 0.0059 502 NAG A C3 3097 C C4 . NAG C . ? 0.4337 0.4274 0.3816 0.0015 -0.0146 0.0062 502 NAG A C4 3098 C C5 . NAG C . ? 0.4690 0.4631 0.4208 0.0012 -0.0155 0.0051 502 NAG A C5 3099 C C6 . NAG C . ? 0.4278 0.4225 0.3818 0.0016 -0.0184 0.0051 502 NAG A C6 3100 C C7 . NAG C . ? 0.3773 0.3696 0.3260 0.0007 -0.0058 0.0083 502 NAG A C7 3101 C C8 . NAG C . ? 0.4239 0.4160 0.3727 0.0003 -0.0032 0.0079 502 NAG A C8 3102 N N2 . NAG C . ? 0.3295 0.3222 0.2786 0.0006 -0.0075 0.0067 502 NAG A N2 3103 O O3 . NAG C . ? 0.4571 0.4500 0.4003 0.0013 -0.0107 0.0069 502 NAG A O3 3104 O O4 . NAG C . ? 0.6242 0.6182 0.5695 0.0016 -0.0163 0.0052 502 NAG A O4 3105 O O5 . NAG C . ? 0.3549 0.3485 0.3089 0.0011 -0.0139 0.0060 502 NAG A O5 3106 O O6 . NAG C . ? 0.6139 0.6091 0.5709 0.0012 -0.0193 0.0033 502 NAG A O6 3107 O O7 . NAG C . ? 0.4572 0.4493 0.4058 0.0010 -0.0062 0.0101 502 NAG A O7 3108 C C1 . NAG D . ? 0.1036 0.1170 0.1667 0.0009 -0.0011 -0.0114 503 NAG A C1 3109 C C2 . NAG D . ? 0.1339 0.1489 0.2025 0.0016 -0.0043 -0.0114 503 NAG A C2 3110 C C3 . NAG D . ? 0.1096 0.1254 0.1846 0.0022 -0.0034 -0.0122 503 NAG A C3 3111 C C4 . NAG D . ? 0.1162 0.1304 0.1884 0.0026 -0.0015 -0.0120 503 NAG A C4 3112 C C5 . NAG D . ? 0.1238 0.1366 0.1903 0.0018 0.0015 -0.0122 503 NAG A C5 3113 C C6 . NAG D . ? 0.0837 0.0949 0.1471 0.0021 0.0033 -0.0121 503 NAG A C6 3114 C C7 . NAG D . ? 0.2085 0.2253 0.2792 0.0012 -0.0089 -0.0115 503 NAG A C7 3115 C C8 . NAG D . ? 0.2148 0.2332 0.2896 0.0006 -0.0098 -0.0126 503 NAG A C8 3116 N N2 . NAG D . ? 0.1373 0.1537 0.2090 0.0011 -0.0055 -0.0120 503 NAG A N2 3117 O O3 . NAG D . ? 0.1308 0.1477 0.2100 0.0030 -0.0067 -0.0119 503 NAG A O3 3118 O O4 . NAG D . ? 0.1210 0.1360 0.1995 0.0031 -0.0001 -0.0131 503 NAG A O4 3119 O O5 . NAG D . ? 0.1070 0.1192 0.1680 0.0013 0.0001 -0.0112 503 NAG A O5 3120 O O6 . NAG D . ? 0.1028 0.1132 0.1635 0.0027 0.0007 -0.0109 503 NAG A O6 3121 O O7 . NAG D . ? 0.2193 0.2353 0.2860 0.0017 -0.0112 -0.0103 503 NAG A O7 3122 C C1 . NAG E . ? 0.1211 0.1355 0.2003 0.0041 -0.0015 -0.0125 504 NAG A C1 3123 C C2 . NAG E . ? 0.0801 0.0943 0.1630 0.0044 0.0013 -0.0138 504 NAG A C2 3124 C C3 . NAG E . ? 0.0919 0.1050 0.1747 0.0053 -0.0002 -0.0131 504 NAG A C3 3125 C C4 . NAG E . ? 0.0798 0.0933 0.1646 0.0058 -0.0042 -0.0119 504 NAG A C4 3126 C C5 . NAG E . ? 0.1237 0.1380 0.2056 0.0056 -0.0067 -0.0108 504 NAG A C5 3127 C C6 . NAG E . ? 0.2061 0.2205 0.2888 0.0061 -0.0107 -0.0096 504 NAG A C6 3128 C C7 . NAG E . ? 0.1687 0.1823 0.2497 0.0030 0.0078 -0.0157 504 NAG A C7 3129 C C8 . NAG E . ? 0.1472 0.1595 0.2240 0.0026 0.0116 -0.0164 504 NAG A C8 3130 N N2 . NAG E . ? 0.1044 0.1176 0.1836 0.0037 0.0050 -0.0146 504 NAG A N2 3131 O O3 . NAG E . ? 0.1012 0.1135 0.1861 0.0053 0.0022 -0.0142 504 NAG A O3 3132 O O4 . NAG E . ? 0.0784 0.0907 0.1625 0.0066 -0.0055 -0.0109 504 NAG A O4 3133 O O5 . NAG E . ? 0.1281 0.1435 0.2107 0.0048 -0.0052 -0.0118 504 NAG A O5 3134 O O6 . NAG E . ? 0.2452 0.2602 0.3329 0.0060 -0.0109 -0.0104 504 NAG A O6 3135 O O7 . NAG E . ? 0.1485 0.1629 0.2334 0.0027 0.0073 -0.0160 504 NAG A O7 3136 C C1 . BMA F . ? 0.1026 0.1148 0.1911 0.0070 -0.0067 -0.0109 505 BMA A C1 3137 C C2 . BMA F . ? 0.1395 0.1505 0.2262 0.0078 -0.0090 -0.0093 505 BMA A C2 3138 C C3 . BMA F . ? 0.1284 0.1390 0.2195 0.0082 -0.0100 -0.0091 505 BMA A C3 3139 C C4 . BMA F . ? 0.1534 0.1640 0.2485 0.0079 -0.0068 -0.0111 505 BMA A C4 3140 C C5 . BMA F . ? 0.1112 0.1230 0.2076 0.0071 -0.0047 -0.0125 505 BMA A C5 3141 C C6 . BMA F . ? 0.1019 0.1135 0.2011 0.0067 -0.0012 -0.0144 505 BMA A C6 3142 O O2 . BMA F . ? 0.1143 0.1241 0.1981 0.0079 -0.0071 -0.0095 505 BMA A O2 3143 O O3 . BMA F . ? 0.1341 0.1432 0.2231 0.0088 -0.0114 -0.0077 505 BMA A O3 3144 O O4 . BMA F . ? 0.1573 0.1678 0.2571 0.0082 -0.0080 -0.0110 505 BMA A O4 3145 O O5 . BMA F . ? 0.0999 0.1118 0.1915 0.0067 -0.0037 -0.0125 505 BMA A O5 3146 O O6 . BMA F . ? 0.1505 0.1631 0.2518 0.0060 0.0005 -0.0155 505 BMA A O6 3147 C C1 . MAN G . ? 0.1106 0.1196 0.2019 0.0093 -0.0143 -0.0065 506 MAN A C1 3148 C C2 . MAN G . ? 0.1794 0.1867 0.2693 0.0098 -0.0151 -0.0051 506 MAN A C2 3149 C C3 . MAN G . ? 0.1440 0.1505 0.2278 0.0099 -0.0159 -0.0037 506 MAN A C3 3150 C C4 . MAN G . ? 0.1708 0.1778 0.2520 0.0099 -0.0188 -0.0022 506 MAN A C4 3151 C C5 . MAN G . ? 0.1883 0.1971 0.2715 0.0094 -0.0182 -0.0038 506 MAN A C5 3152 C C6 . MAN G . ? 0.2235 0.2330 0.3044 0.0094 -0.0211 -0.0027 506 MAN A C6 3153 O O2 . MAN G . ? 0.1422 0.1495 0.2347 0.0103 -0.0177 -0.0040 506 MAN A O2 3154 O O3 . MAN G . ? 0.1191 0.1239 0.2014 0.0102 -0.0162 -0.0024 506 MAN A O3 3155 O O4 . MAN G . ? 0.1295 0.1358 0.2050 0.0099 -0.0194 -0.0009 506 MAN A O4 3156 O O5 . MAN G . ? 0.1405 0.1500 0.2295 0.0094 -0.0172 -0.0052 506 MAN A O5 3157 O O6 . MAN G . ? 0.3224 0.3334 0.4042 0.0088 -0.0202 -0.0041 506 MAN A O6 3158 C C1 . MAN H . ? 0.1311 0.1369 0.2236 0.0108 -0.0186 -0.0027 507 MAN A C1 3159 C C2 . MAN H . ? 0.1693 0.1752 0.2643 0.0113 -0.0216 -0.0015 507 MAN A C2 3160 C C3 . MAN H . ? 0.2035 0.2105 0.3050 0.0112 -0.0207 -0.0032 507 MAN A C3 3161 C C4 . MAN H . ? 0.1994 0.2057 0.3039 0.0111 -0.0180 -0.0045 507 MAN A C4 3162 C C5 . MAN H . ? 0.1602 0.1663 0.2613 0.0106 -0.0152 -0.0056 507 MAN A C5 3163 C C6 . MAN H . ? 0.1552 0.1606 0.2588 0.0105 -0.0126 -0.0070 507 MAN A C6 3164 O O2 . MAN H . ? 0.1644 0.1688 0.2587 0.0118 -0.0227 0.0002 507 MAN A O2 3165 O O3 . MAN H . ? 0.1787 0.1858 0.2828 0.0117 -0.0235 -0.0022 507 MAN A O3 3166 O O4 . MAN H . ? 0.2072 0.2145 0.3177 0.0109 -0.0169 -0.0062 507 MAN A O4 3167 O O5 . MAN H . ? 0.1498 0.1550 0.2452 0.0107 -0.0163 -0.0040 507 MAN A O5 3168 O O6 . MAN H . ? 0.1889 0.1931 0.2935 0.0110 -0.0140 -0.0057 507 MAN A O6 3169 C C1 . MAN I . ? 0.1653 0.1691 0.2548 0.0121 -0.0254 0.0025 508 MAN A C1 3170 C C2 . MAN I . ? 0.1604 0.1627 0.2504 0.0126 -0.0264 0.0042 508 MAN A C2 3171 C C3 . MAN I . ? 0.1446 0.1456 0.2335 0.0124 -0.0240 0.0038 508 MAN A C3 3172 C C4 . MAN I . ? 0.1843 0.1849 0.2671 0.0121 -0.0236 0.0045 508 MAN A C4 3173 C C5 . MAN I . ? 0.1922 0.1945 0.2745 0.0116 -0.0228 0.0029 508 MAN A C5 3174 C C6 . MAN I . ? 0.1777 0.1796 0.2540 0.0113 -0.0225 0.0035 508 MAN A C6 3175 O O2 . MAN I . ? 0.1646 0.1662 0.2502 0.0130 -0.0290 0.0066 508 MAN A O2 3176 O O3 . MAN I . ? 0.1924 0.1920 0.2820 0.0128 -0.0248 0.0053 508 MAN A O3 3177 O O4 . MAN I . ? 0.1247 0.1241 0.2065 0.0119 -0.0215 0.0041 508 MAN A O4 3178 O O5 . MAN I . ? 0.1683 0.1717 0.2520 0.0118 -0.0248 0.0030 508 MAN A O5 3179 O O6 . MAN I . ? 0.1736 0.1747 0.2456 0.0115 -0.0249 0.0058 508 MAN A O6 3180 C C1 . MAN J . ? 0.1363 0.1496 0.2428 0.0061 -0.0013 -0.0155 509 MAN A C1 3181 C C2 . MAN J . ? 0.1774 0.1916 0.2859 0.0053 0.0003 -0.0166 509 MAN A C2 3182 C C3 . MAN J . ? 0.1795 0.1933 0.2887 0.0047 0.0047 -0.0181 509 MAN A C3 3183 C C4 . MAN J . ? 0.1868 0.2001 0.2999 0.0050 0.0053 -0.0188 509 MAN A C4 3184 C C5 . MAN J . ? 0.1289 0.1414 0.2401 0.0058 0.0033 -0.0177 509 MAN A C5 3185 C C6 . MAN J . ? 0.2630 0.2750 0.3783 0.0061 0.0037 -0.0183 509 MAN A C6 3186 O O2 . MAN J . ? 0.2369 0.2518 0.3506 0.0055 -0.0017 -0.0166 509 MAN A O2 3187 O O3 . MAN J . ? 0.2232 0.2377 0.3346 0.0039 0.0060 -0.0189 509 MAN A O3 3188 O O4 . MAN J . ? 0.1972 0.2099 0.3099 0.0044 0.0093 -0.0202 509 MAN A O4 3189 O O5 . MAN J . ? 0.1314 0.1443 0.2422 0.0063 -0.0006 -0.0162 509 MAN A O5 3190 O O6 . MAN J . ? 0.2546 0.2673 0.3759 0.0061 0.0026 -0.0186 509 MAN A O6 3191 C C1 . MAN K . ? 0.4018 0.4142 0.5276 0.0065 0.0024 -0.0189 510 MAN A C1 3192 C C2 . MAN K . ? 0.4703 0.4835 0.6025 0.0065 0.0011 -0.0192 510 MAN A C2 3193 C C3 . MAN K . ? 0.3838 0.3975 0.5174 0.0056 0.0039 -0.0206 510 MAN A C3 3194 C C4 . MAN K . ? 0.4636 0.4767 0.5968 0.0051 0.0082 -0.0221 510 MAN A C4 3195 C C5 . MAN K . ? 0.3711 0.3833 0.4979 0.0052 0.0091 -0.0217 510 MAN A C5 3196 C C6 . MAN K . ? 0.4777 0.4891 0.6038 0.0048 0.0130 -0.0232 510 MAN A C6 3197 O O2 . MAN K . ? 0.4358 0.4487 0.5728 0.0068 0.0011 -0.0197 510 MAN A O2 3198 O O3 . MAN K . ? 0.4737 0.4882 0.6135 0.0056 0.0028 -0.0210 510 MAN A O3 3199 O O4 . MAN K . ? 0.4480 0.4613 0.5811 0.0043 0.0110 -0.0231 510 MAN A O4 3200 O O5 . MAN K . ? 0.3532 0.3650 0.4794 0.0061 0.0061 -0.0205 510 MAN A O5 3201 O O6 . MAN K . ? 0.7491 0.7608 0.8790 0.0042 0.0156 -0.0245 510 MAN A O6 3202 C C1 . MAN L . ? 0.2241 0.2382 0.3310 0.0032 0.0089 -0.0193 511 MAN A C1 3203 C C2 . MAN L . ? 0.2386 0.2531 0.3484 0.0024 0.0111 -0.0202 511 MAN A C2 3204 C C3 . MAN L . ? 0.2866 0.3022 0.3987 0.0024 0.0081 -0.0198 511 MAN A C3 3205 C C4 . MAN L . ? 0.3059 0.3218 0.4128 0.0025 0.0063 -0.0187 511 MAN A C4 3206 C C5 . MAN L . ? 0.1692 0.1846 0.2731 0.0033 0.0045 -0.0177 511 MAN A C5 3207 C C6 . MAN L . ? 0.1947 0.2104 0.2934 0.0034 0.0029 -0.0166 511 MAN A C6 3208 O O2 . MAN L . ? 0.3058 0.3197 0.4111 0.0017 0.0142 -0.0205 511 MAN A O2 3209 O O3 . MAN L . ? 0.3806 0.3963 0.4954 0.0017 0.0101 -0.0206 511 MAN A O3 3210 O O4 . MAN L . ? 0.3250 0.3418 0.4337 0.0026 0.0033 -0.0182 511 MAN A O4 3211 O O5 . MAN L . ? 0.2328 0.2472 0.3351 0.0033 0.0074 -0.0183 511 MAN A O5 3212 O O6 . MAN L . ? 0.1817 0.1970 0.2784 0.0042 0.0006 -0.0155 511 MAN A O6 3213 CA CA . CA M . ? 0.2369 0.2303 0.2640 -0.0115 0.0097 -0.0131 512 CA A CA 3214 O O . HOH N . ? 0.1204 0.1024 0.0930 -0.0020 0.0132 0.0094 601 HOH A O 3215 O O . HOH N . ? 0.0663 0.0585 0.0495 -0.0017 0.0097 0.0020 602 HOH A O 3216 O O . HOH N . ? 0.0750 0.0605 0.0815 -0.0078 0.0124 -0.0068 603 HOH A O 3217 O O . HOH N . ? 0.1088 0.0924 0.0756 -0.0013 0.0112 0.0072 604 HOH A O 3218 O O . HOH N . ? 0.0687 0.0644 0.0494 -0.0027 -0.0013 -0.0001 605 HOH A O 3219 O O . HOH N . ? 0.0801 0.0744 0.0734 -0.0007 0.0047 0.0062 606 HOH A O 3220 O O . HOH N . ? 0.0591 0.0457 0.0379 -0.0027 0.0101 0.0055 607 HOH A O 3221 O O . HOH N . ? 0.1038 0.1014 0.0934 -0.0037 -0.0018 -0.0030 608 HOH A O 3222 O O . HOH N . ? 0.0546 0.0460 0.0418 -0.0014 0.0079 0.0028 609 HOH A O 3223 O O . HOH N . ? 0.0851 0.0821 0.0954 -0.0068 0.0121 -0.0046 610 HOH A O 3224 O O . HOH N . ? 0.1069 0.0860 0.1344 -0.0112 0.0161 -0.0144 611 HOH A O 3225 O O . HOH N . ? 0.1241 0.1173 0.1072 -0.0021 0.0044 0.0034 612 HOH A O 3226 O O . HOH N . ? 0.1015 0.1064 0.1309 -0.0006 0.0034 -0.0076 613 HOH A O 3227 O O . HOH N . ? 0.0880 0.0779 0.0779 0.0015 -0.0005 0.0089 614 HOH A O 3228 O O . HOH N . ? 0.0779 0.0759 0.0813 -0.0014 0.0062 -0.0046 615 HOH A O 3229 O O . HOH N . ? 0.0689 0.0623 0.0519 -0.0024 0.0037 0.0027 616 HOH A O 3230 O O . HOH N . ? 0.1139 0.1013 0.0834 -0.0005 0.0017 0.0041 617 HOH A O 3231 O O . HOH N . ? 0.1373 0.1080 0.1157 0.0032 0.0056 0.0226 618 HOH A O 3232 O O . HOH N . ? 0.1056 0.0907 0.0870 -0.0039 0.0149 0.0056 619 HOH A O 3233 O O . HOH N . ? 0.0845 0.0640 0.0893 0.0034 0.0085 0.0111 620 HOH A O 3234 O O . HOH N . ? 0.1125 0.1084 0.1476 -0.0125 0.0072 -0.0167 621 HOH A O 3235 O O . HOH N . ? 0.0667 0.0670 0.0791 -0.0012 0.0058 -0.0058 622 HOH A O 3236 O O . HOH N . ? 0.0908 0.0876 0.0745 -0.0032 -0.0029 -0.0024 623 HOH A O 3237 O O . HOH N . ? 0.0991 0.0933 0.0885 -0.0014 -0.0012 0.0051 624 HOH A O 3238 O O . HOH N . ? 0.0902 0.0823 0.0719 -0.0018 0.0176 0.0062 625 HOH A O 3239 O O . HOH N . ? 0.0738 0.0658 0.0625 -0.0042 0.0076 0.0004 626 HOH A O 3240 O O . HOH N . ? 0.1130 0.0978 0.0785 -0.0008 0.0081 0.0058 627 HOH A O 3241 O O . HOH N . ? 0.0842 0.0662 0.0888 0.0023 0.0102 0.0074 628 HOH A O 3242 O O . HOH N . ? 0.1018 0.0935 0.1449 -0.0142 0.0106 -0.0186 629 HOH A O 3243 O O . HOH N . ? 0.0846 0.0770 0.0882 -0.0068 0.0183 -0.0014 630 HOH A O 3244 O O . HOH N . ? 0.0845 0.0697 0.0788 -0.0017 0.0146 -0.0049 631 HOH A O 3245 O O . HOH N . ? 0.0503 0.0474 0.0470 -0.0005 -0.0033 0.0019 632 HOH A O 3246 O O . HOH N . ? 0.1034 0.0874 0.0703 -0.0005 0.0067 0.0081 633 HOH A O 3247 O O . HOH N . ? 0.1423 0.1337 0.1201 -0.0019 0.0058 0.0120 634 HOH A O 3248 O O . HOH N . ? 0.1209 0.1147 0.1024 -0.0022 0.0038 0.0033 635 HOH A O 3249 O O . HOH N . ? 0.0838 0.0783 0.0730 -0.0035 0.0060 -0.0002 636 HOH A O 3250 O O . HOH N . ? 0.1117 0.0912 0.1482 -0.0117 0.0265 -0.0028 637 HOH A O 3251 O O . HOH N . ? 0.1165 0.1091 0.0992 -0.0051 0.0015 -0.0094 638 HOH A O 3252 O O . HOH N . ? 0.1260 0.1181 0.1518 -0.0116 0.0082 -0.0153 639 HOH A O 3253 O O . HOH N . ? 0.0743 0.0710 0.0597 -0.0040 -0.0029 -0.0051 640 HOH A O 3254 O O . HOH N . ? 0.1741 0.1382 0.1746 0.0020 0.0145 0.0223 641 HOH A O 3255 O O . HOH N . ? 0.1112 0.1056 0.0980 -0.0053 0.0001 -0.0085 642 HOH A O 3256 O O . HOH N . ? 0.1029 0.0825 0.1087 -0.0073 0.0193 0.0026 643 HOH A O 3257 O O . HOH N . ? 0.0766 0.0800 0.0990 -0.0001 0.0002 -0.0055 644 HOH A O 3258 O O . HOH N . ? 0.1087 0.0808 0.1186 0.0027 0.0129 0.0124 645 HOH A O 3259 O O . HOH N . ? 0.1302 0.1000 0.1309 -0.0054 0.0275 0.0152 646 HOH A O 3260 O O . HOH N . ? 0.1496 0.1417 0.1052 -0.0008 0.0003 0.0038 647 HOH A O 3261 O O . HOH N . ? 0.0900 0.0983 0.1279 -0.0038 0.0040 -0.0098 648 HOH A O 3262 O O . HOH N . ? 0.1646 0.1565 0.1219 0.0008 -0.0056 0.0107 649 HOH A O 3263 O O . HOH N . ? 0.0923 0.0849 0.0680 -0.0043 0.0005 -0.0087 650 HOH A O 3264 O O . HOH N . ? 0.1397 0.1175 0.1029 0.0023 0.0024 0.0171 651 HOH A O 3265 O O . HOH N . ? 0.0858 0.0739 0.0824 -0.0059 0.0105 -0.0028 652 HOH A O 3266 O O . HOH N . ? 0.1172 0.0994 0.1200 0.0039 0.0054 0.0119 653 HOH A O 3267 O O . HOH N . ? 0.1332 0.1016 0.1458 0.0020 0.0154 0.0130 654 HOH A O 3268 O O . HOH N . ? 0.1511 0.1339 0.1093 -0.0011 0.0188 -0.0007 655 HOH A O 3269 O O . HOH N . ? 0.1817 0.1795 0.1856 -0.0056 0.0061 -0.0046 656 HOH A O 3270 O O . HOH N . ? 0.1439 0.1271 0.1042 0.0021 -0.0030 0.0094 657 HOH A O 3271 O O . HOH N . ? 0.0866 0.0859 0.0875 -0.0010 -0.0026 -0.0006 658 HOH A O 3272 O O . HOH N . ? 0.1548 0.1351 0.1447 -0.0053 0.0198 0.0079 659 HOH A O 3273 O O . HOH N . ? 0.1747 0.1508 0.1259 -0.0019 0.0284 0.0079 660 HOH A O 3274 O O . HOH N . ? 0.1512 0.1642 0.2452 0.0048 0.0043 -0.0162 661 HOH A O 3275 O O . HOH N . ? 0.1286 0.1110 0.0902 -0.0009 0.0122 0.0071 662 HOH A O 3276 O O . HOH N . ? 0.1314 0.1266 0.0995 -0.0019 -0.0093 -0.0016 663 HOH A O 3277 O O . HOH N . ? 0.1472 0.1196 0.1223 0.0010 0.0097 0.0201 664 HOH A O 3278 O O . HOH N . ? 0.1405 0.1202 0.0900 -0.0004 0.0154 0.0061 665 HOH A O 3279 O O . HOH N . ? 0.2063 0.1744 0.2005 -0.0048 0.0290 0.0183 666 HOH A O 3280 O O . HOH N . ? 0.1564 0.1411 0.1227 -0.0017 0.0201 -0.0020 667 HOH A O 3281 O O . HOH N . ? 0.1146 0.1095 0.1022 -0.0014 -0.0013 0.0046 668 HOH A O 3282 O O . HOH N . ? 0.1350 0.1356 0.1868 -0.0120 0.0219 -0.0106 669 HOH A O 3283 O O . HOH N . ? 0.0921 0.0782 0.0940 -0.0068 0.0125 -0.0035 670 HOH A O 3284 O O . HOH N . ? 0.1874 0.1827 0.2329 -0.0103 0.0341 -0.0068 671 HOH A O 3285 O O . HOH N . ? 0.1088 0.1012 0.0850 -0.0019 0.0060 0.0089 672 HOH A O 3286 O O . HOH N . ? 0.1700 0.1468 0.2252 -0.0126 0.0347 -0.0013 673 HOH A O 3287 O O . HOH N . ? 0.1408 0.1516 0.2064 -0.0102 0.0102 -0.0157 674 HOH A O 3288 O O . HOH N . ? 0.1262 0.1180 0.1045 -0.0010 -0.0002 0.0117 675 HOH A O 3289 O O . HOH N . ? 0.1452 0.1507 0.1628 -0.0021 -0.0072 -0.0056 676 HOH A O 3290 O O . HOH N . ? 0.1830 0.1638 0.1795 -0.0032 0.0174 -0.0154 677 HOH A O 3291 O O . HOH N . ? 0.1162 0.1277 0.1673 0.0015 -0.0083 -0.0080 678 HOH A O 3292 O O . HOH N . ? 0.2417 0.2290 0.2477 -0.0059 0.0433 -0.0054 679 HOH A O 3293 O O . HOH N . ? 0.1402 0.1195 0.1081 0.0015 0.0039 0.0150 680 HOH A O 3294 O O . HOH N . ? 0.1617 0.1530 0.1357 -0.0040 0.0035 -0.0080 681 HOH A O 3295 O O . HOH N . ? 0.1391 0.1467 0.1754 -0.0072 -0.0002 -0.0124 682 HOH A O 3296 O O . HOH N . ? 0.1387 0.1360 0.1250 -0.0010 -0.0066 0.0031 683 HOH A O 3297 O O . HOH N . ? 0.1057 0.0952 0.1291 -0.0110 0.0163 -0.0073 684 HOH A O 3298 O O . HOH N . ? 0.1821 0.1701 0.1475 -0.0023 0.0138 -0.0071 685 HOH A O 3299 O O . HOH N . ? 0.1879 0.1563 0.1556 -0.0010 0.0184 0.0232 686 HOH A O 3300 O O . HOH N . ? 0.2052 0.1823 0.1701 0.0038 -0.0013 0.0193 687 HOH A O 3301 O O . HOH N . ? 0.0953 0.0840 0.0978 -0.0073 0.0154 -0.0008 688 HOH A O 3302 O O . HOH N . ? 0.1677 0.1643 0.1635 -0.0056 0.0008 -0.0070 689 HOH A O 3303 O O . HOH N . ? 0.1248 0.1268 0.1575 -0.0031 0.0269 -0.0126 690 HOH A O 3304 O O . HOH N . ? 0.1687 0.1592 0.1519 -0.0009 0.0251 0.0000 691 HOH A O 3305 O O . HOH N . ? 0.2688 0.2456 0.2150 0.0015 0.0068 0.0149 692 HOH A O 3306 O O . HOH N . ? 0.1985 0.1659 0.1497 0.0019 0.0092 0.0278 693 HOH A O 3307 O O . HOH N . ? 0.1648 0.1600 0.1293 -0.0017 -0.0132 -0.0033 694 HOH A O 3308 O O . HOH N . ? 0.1183 0.1094 0.1026 -0.0049 0.0048 -0.0082 695 HOH A O 3309 O O . HOH N . ? 0.1409 0.1347 0.1200 -0.0022 0.0036 0.0038 696 HOH A O 3310 O O . HOH N . ? 0.1569 0.1315 0.2080 -0.0119 0.0223 -0.0145 697 HOH A O 3311 O O . HOH N . ? 0.1051 0.1004 0.0875 -0.0044 -0.0019 -0.0067 698 HOH A O 3312 O O . HOH N . ? 0.1465 0.1423 0.1366 -0.0012 -0.0020 0.0033 699 HOH A O 3313 O O . HOH N . ? 0.1818 0.1745 0.1704 -0.0009 0.0023 -0.0033 700 HOH A O 3314 O O . HOH N . ? 0.1398 0.1336 0.1320 0.0001 -0.0028 0.0064 701 HOH A O 3315 O O . HOH N . ? 0.1793 0.1747 0.1840 -0.0072 0.0056 -0.0073 702 HOH A O 3316 O O . HOH N . ? 0.1114 0.1003 0.0951 -0.0027 0.0106 -0.0044 703 HOH A O 3317 O O . HOH N . ? 0.1272 0.1253 0.1723 -0.0106 0.0289 -0.0078 704 HOH A O 3318 O O . HOH N . ? 0.1592 0.1718 0.2086 0.0010 -0.0124 -0.0079 705 HOH A O 3319 O O . HOH N . ? 0.1155 0.1146 0.1553 -0.0111 0.0211 -0.0085 706 HOH A O 3320 O O . HOH N . ? 0.0896 0.0697 0.1109 -0.0106 0.0222 -0.0018 707 HOH A O 3321 O O . HOH N . ? 0.1520 0.1357 0.1532 -0.0065 0.0150 0.0001 708 HOH A O 3322 O O . HOH N . ? 0.2002 0.1660 0.1711 0.0001 0.0155 0.0261 709 HOH A O 3323 O O . HOH N . ? 0.1803 0.1636 0.2294 -0.0140 0.0154 -0.0203 710 HOH A O 3324 O O . HOH N . ? 0.1177 0.1296 0.1788 -0.0009 0.0088 -0.0133 711 HOH A O 3325 O O . HOH N . ? 0.1723 0.1574 0.1694 -0.0004 0.0188 -0.0066 712 HOH A O 3326 O O . HOH N . ? 0.2376 0.2330 0.2151 -0.0002 -0.0091 0.0060 713 HOH A O 3327 O O . HOH N . ? 0.1255 0.1213 0.1386 -0.0075 0.0173 -0.0040 714 HOH A O 3328 O O . HOH N . ? 0.1473 0.1402 0.1498 -0.0079 0.0035 -0.0125 715 HOH A O 3329 O O . HOH N . ? 0.1510 0.1308 0.1214 0.0024 0.0010 0.0150 716 HOH A O 3330 O O . HOH N . ? 0.1663 0.1556 0.1396 -0.0009 0.0015 0.0011 717 HOH A O 3331 O O . HOH N . ? 0.1420 0.1224 0.1449 0.0007 0.0123 0.0055 718 HOH A O 3332 O O . HOH N . ? 0.2125 0.2124 0.2837 -0.0132 0.0239 -0.0139 719 HOH A O 3333 O O . HOH N . ? 0.2071 0.2118 0.2312 -0.0067 -0.0005 -0.0106 720 HOH A O 3334 O O . HOH N . ? 0.1879 0.1682 0.1432 -0.0004 0.0124 0.0089 721 HOH A O 3335 O O . HOH N . ? 0.1572 0.1514 0.1672 0.0000 0.0248 -0.0163 722 HOH A O 3336 O O . HOH N . ? 0.1430 0.1294 0.1400 0.0039 -0.0005 0.0123 723 HOH A O 3337 O O . HOH N . ? 0.2422 0.2389 0.2969 -0.0146 0.0076 -0.0218 724 HOH A O 3338 O O . HOH N . ? 0.2795 0.2700 0.3250 -0.0112 0.0367 -0.0044 725 HOH A O 3339 O O . HOH N . ? 0.2560 0.2245 0.2928 -0.0098 0.0384 0.0099 726 HOH A O 3340 O O . HOH N . ? 0.1471 0.1458 0.1589 -0.0067 0.0075 -0.0063 727 HOH A O 3341 O O . HOH N . ? 0.1925 0.1944 0.2124 -0.0075 0.0024 -0.0101 728 HOH A O 3342 O O . HOH N . ? 0.1605 0.1451 0.2009 -0.0136 0.0092 -0.0265 729 HOH A O 3343 O O . HOH N . ? 0.2325 0.2071 0.2186 -0.0060 0.0377 0.0116 730 HOH A O 3344 O O . HOH N . ? 0.2010 0.1834 0.2570 -0.0131 0.0339 -0.0038 731 HOH A O 3345 O O . HOH N . ? 0.1978 0.1967 0.2012 -0.0061 0.0003 -0.0078 732 HOH A O 3346 O O . HOH N . ? 0.1700 0.1620 0.1611 -0.0068 0.0011 -0.0147 733 HOH A O 3347 O O . HOH N . ? 0.1880 0.1866 0.2316 -0.0094 0.0315 -0.0081 734 HOH A O 3348 O O . HOH N . ? 0.1795 0.1767 0.2325 -0.0137 0.0170 -0.0136 735 HOH A O 3349 O O . HOH N . ? 0.1631 0.1535 0.1430 0.0004 -0.0043 0.0057 736 HOH A O 3350 O O . HOH N . ? 0.1601 0.1396 0.1634 -0.0035 0.0169 -0.0121 737 HOH A O 3351 O O . HOH N . ? 0.2712 0.2656 0.3209 -0.0117 0.0309 -0.0070 738 HOH A O 3352 O O . HOH N . ? 0.2147 0.2137 0.2257 -0.0071 0.0040 -0.0081 739 HOH A O 3353 O O . HOH N . ? 0.1988 0.1735 0.2203 0.0021 0.0191 -0.0009 740 HOH A O 3354 O O . HOH N . ? 0.2055 0.2035 0.2566 -0.0115 0.0277 -0.0088 741 HOH A O 3355 O O . HOH N . ? 0.2597 0.2219 0.2706 0.0013 0.0176 0.0205 742 HOH A O 3356 O O . HOH N . ? 0.1917 0.1887 0.2125 -0.0047 0.0328 -0.0100 743 HOH A O 3357 O O . HOH N . ? 0.1456 0.1230 0.1700 -0.0102 0.0244 0.0000 744 HOH A O 3358 O O . HOH N . ? 0.2419 0.2240 0.2013 -0.0011 0.0285 -0.0062 745 HOH A O 3359 O O . HOH N . ? 0.2043 0.1972 0.1900 -0.0012 -0.0029 0.0026 746 HOH A O 3360 O O . HOH N . ? 0.2837 0.2721 0.2435 -0.0016 0.0159 -0.0064 747 HOH A O 3361 O O . HOH N . ? 0.2263 0.1868 0.2192 0.0030 0.0124 0.0278 748 HOH A O 3362 O O . HOH N . ? 0.2024 0.1680 0.1709 0.0036 0.0042 0.0292 749 HOH A O 3363 O O . HOH N . ? 0.2012 0.1700 0.2502 -0.0099 0.0300 -0.0001 750 HOH A O 3364 O O . HOH N . ? 0.1834 0.1758 0.1428 -0.0006 -0.0022 0.0060 751 HOH A O 3365 O O . HOH N . ? 0.2251 0.2044 0.1876 0.0055 -0.0086 0.0182 752 HOH A O 3366 O O . HOH N . ? 0.2463 0.2340 0.3085 -0.0130 0.0373 -0.0056 753 HOH A O 3367 O O . HOH N . ? 0.1984 0.1850 0.1764 -0.0001 0.0022 -0.0123 754 HOH A O 3368 O O . HOH N . ? 0.1850 0.1631 0.2374 -0.0125 0.0360 -0.0004 755 HOH A O 3369 O O . HOH N . ? 0.1913 0.1892 0.2112 -0.0034 0.0306 -0.0116 756 HOH A O 3370 O O . HOH N . ? 0.1814 0.1609 0.1224 0.0017 0.0041 0.0073 757 HOH A O 3371 O O . HOH N . ? 0.2775 0.2204 0.2775 -0.0160 0.0258 -0.0160 758 HOH A O 3372 O O . HOH N . ? 0.2934 0.2591 0.2938 -0.0055 0.0323 0.0194 759 HOH A O 3373 O O . HOH N . ? 0.2184 0.2057 0.1855 -0.0004 0.0011 0.0003 760 HOH A O 3374 O O . HOH N . ? 0.2207 0.2118 0.1780 -0.0015 0.0123 0.0077 761 HOH A O 3375 O O . HOH N . ? 0.2390 0.2056 0.2474 0.0089 0.0024 0.0255 762 HOH A O 3376 O O . HOH N . ? 0.2609 0.2583 0.2633 -0.0067 0.0010 -0.0090 763 HOH A O 3377 O O . HOH N . ? 0.2010 0.1942 0.1864 -0.0059 -0.0008 -0.0128 764 HOH A O 3378 O O . HOH N . ? 0.2322 0.2226 0.2138 -0.0022 0.0082 0.0150 765 HOH A O 3379 O O . HOH N . ? 0.2586 0.2402 0.2048 0.0005 0.0126 -0.0053 766 HOH A O 3380 O O . HOH N . ? 0.3065 0.2810 0.2577 -0.0025 0.0367 0.0064 767 HOH A O 3381 O O . HOH N . ? 0.2097 0.1796 0.2687 -0.0108 0.0260 -0.0120 768 HOH A O 3382 O O . HOH N . ? 0.1897 0.1833 0.1856 0.0000 0.0055 0.0061 769 HOH A O 3383 O O . HOH N . ? 0.1992 0.1882 0.1887 -0.0022 0.0315 -0.0106 770 HOH A O 3384 O O . HOH N . ? 0.1992 0.2084 0.2273 -0.0010 -0.0143 -0.0068 771 HOH A O 3385 O O . HOH N . ? 0.2311 0.2477 0.3206 0.0022 0.0026 -0.0156 772 HOH A O 3386 O O . HOH N . ? 0.1927 0.1802 0.1672 0.0017 -0.0059 0.0080 773 HOH A O 3387 O O . HOH N . ? 0.1797 0.1685 0.1610 -0.0020 0.0137 -0.0047 774 HOH A O 3388 O O . HOH N . ? 0.2253 0.1993 0.2119 -0.0063 0.0419 0.0109 775 HOH A O 3389 O O . HOH N . ? 0.2510 0.2204 0.2777 -0.0093 0.0401 0.0120 776 HOH A O 3390 O O . HOH N . ? 0.2368 0.2183 0.2458 -0.0089 0.0104 -0.0224 777 HOH A O 3391 O O . HOH N . ? 0.1654 0.1592 0.1559 -0.0016 -0.0012 0.0044 778 HOH A O 3392 O O . HOH N . ? 0.2298 0.2413 0.3029 -0.0108 0.0073 -0.0183 779 HOH A O 3393 O O . HOH N . ? 0.2351 0.2259 0.2155 -0.0011 0.0053 -0.0036 780 HOH A O 3394 O O . HOH N . ? 0.2346 0.2222 0.2177 0.0002 0.0145 -0.0150 781 HOH A O 3395 O O . HOH N . ? 0.2218 0.2066 0.1820 -0.0002 0.0039 -0.0033 782 HOH A O 3396 O O . HOH N . ? 0.2616 0.2564 0.2553 -0.0011 -0.0022 0.0054 783 HOH A O 3397 O O . HOH N . ? 0.3038 0.2752 0.2837 -0.0061 0.0479 0.0116 784 HOH A O 3398 O O . HOH N . ? 0.2305 0.2198 0.2640 -0.0135 0.0039 -0.0269 785 HOH A O 3399 O O . HOH N . ? 0.2820 0.2805 0.2807 -0.0044 0.0022 -0.0037 786 HOH A O 3400 O O . HOH N . ? 0.2942 0.2603 0.2540 0.0015 0.0106 0.0282 787 HOH A O 3401 O O . HOH N . ? 0.2664 0.2517 0.2562 -0.0015 0.0179 -0.0089 788 HOH A O 3402 O O . HOH N . ? 0.2321 0.2204 0.2119 -0.0029 0.0117 -0.0073 789 HOH A O 3403 O O . HOH N . ? 0.2079 0.2128 0.2200 -0.0012 -0.0110 -0.0040 790 HOH A O 3404 O O . HOH N . ? 0.2039 0.1732 0.2262 0.0063 0.0113 0.0159 791 HOH A O 3405 O O . HOH N . ? 0.1804 0.1454 0.1724 0.0007 0.0155 0.0229 792 HOH A O 3406 O O . HOH N . ? 0.2500 0.2308 0.2169 0.0031 -0.0026 0.0145 793 HOH A O 3407 O O . HOH N . ? 0.3116 0.2784 0.3591 -0.0103 0.0396 0.0088 794 HOH A O 3408 O O . HOH N . ? 0.2380 0.2103 0.2997 -0.0124 0.0384 0.0011 795 HOH A O 3409 O O . HOH N . ? 0.1643 0.1769 0.2070 -0.0012 -0.0139 -0.0094 796 HOH A O 3410 O O . HOH N . ? 0.2746 0.2888 0.3474 -0.0093 0.0027 -0.0183 797 HOH A O 3411 O O . HOH N . ? 0.2604 0.2460 0.2304 -0.0001 0.0025 -0.0109 798 HOH A O 3412 O O . HOH N . ? 0.2612 0.2571 0.3343 -0.0141 0.0254 -0.0138 799 HOH A O 3413 O O . HOH N . ? 0.2216 0.1873 0.2242 -0.0026 0.0224 0.0182 800 HOH A O 3414 O O . HOH N . ? 0.2847 0.2874 0.3485 -0.0113 0.0252 -0.0122 801 HOH A O 3415 O O . HOH N . ? 0.2479 0.2479 0.2935 -0.0085 0.0324 -0.0094 802 HOH A O 3416 O O . HOH N . ? 0.2091 0.2087 0.2085 -0.0039 -0.0001 -0.0038 803 HOH A O 3417 O O . HOH N . ? 0.1957 0.1877 0.1546 -0.0012 0.0044 0.0048 804 HOH A O 3418 O O . HOH N . ? 0.2979 0.2795 0.3603 -0.0140 0.0274 -0.0101 805 HOH A O 3419 O O . HOH N . ? 0.2037 0.2028 0.1938 -0.0017 -0.0072 -0.0002 806 HOH A O 3420 O O . HOH N . ? 0.1939 0.1980 0.2341 -0.0044 0.0266 -0.0122 807 HOH A O 3421 O O . HOH N . ? 0.3615 0.3339 0.4039 -0.0102 0.0234 -0.0088 808 HOH A O 3422 O O . HOH N . ? 0.2704 0.2302 0.2565 -0.0020 0.0252 0.0281 809 HOH A O 3423 O O . HOH N . ? 0.3093 0.2991 0.3836 -0.0147 0.0291 -0.0121 810 HOH A O 3424 O O . HOH N . ? 0.2314 0.2211 0.2071 -0.0012 0.0056 -0.0021 811 HOH A O 3425 O O . HOH N . ? 0.2906 0.2963 0.3475 -0.0130 -0.0023 -0.0237 812 HOH A O 3426 O O . HOH N . ? 0.2966 0.2599 0.2723 0.0010 0.0140 0.0280 813 HOH A O 3427 O O . HOH N . ? 0.2562 0.2555 0.3277 -0.0139 0.0209 -0.0155 814 HOH A O 3428 O O . HOH N . ? 0.2068 0.1917 0.1876 -0.0042 0.0208 0.0044 815 HOH A O 3429 O O . HOH N . ? 0.3156 0.3034 0.2888 -0.0030 0.0116 -0.0094 816 HOH A O 3430 O O . HOH N . ? 0.3265 0.3219 0.3161 -0.0061 -0.0029 -0.0121 817 HOH A O 3431 O O . HOH N . ? 0.2755 0.2658 0.2286 0.0018 -0.0046 0.0185 818 HOH A O 3432 O O . HOH N . ? 0.3437 0.3181 0.3181 -0.0033 0.0238 0.0151 819 HOH A O 3433 O O . HOH N . ? 0.2533 0.2252 0.2291 0.0044 0.0014 0.0232 820 HOH A O 3434 O O . HOH N . ? 0.3208 0.2849 0.2673 0.0022 0.0096 0.0318 821 HOH A O 3435 O O . HOH N . ? 0.5314 0.5080 0.5342 -0.0079 0.0493 0.0062 822 HOH A O 3436 O O . HOH N . ? 0.2741 0.2538 0.2776 -0.0076 0.0444 0.0044 823 HOH A O 3437 O O . HOH N . ? 0.2210 0.2155 0.2286 -0.0014 0.0277 -0.0137 824 HOH A O 3438 O O . HOH N . ? 0.2503 0.2344 0.2062 0.0005 0.0001 -0.0015 825 HOH A O 3439 O O . HOH N . ? 0.1964 0.1885 0.1842 -0.0010 -0.0006 -0.0021 826 HOH A O 3440 O O . HOH N . ? 0.3145 0.3198 0.3361 -0.0063 -0.0055 -0.0117 827 HOH A O 3441 O O . HOH N . ? 0.3048 0.3048 0.3008 0.0000 0.0000 0.0000 828 HOH A O 3442 O O . HOH N . ? 0.2878 0.2643 0.2148 0.0014 0.0129 0.0032 829 HOH A O 3443 O O . HOH N . ? 0.2735 0.2564 0.2439 0.0025 -0.0029 0.0123 830 HOH A O 3444 O O . HOH N . ? 0.3132 0.2904 0.2751 0.0064 -0.0087 0.0218 831 HOH A O 3445 O O . HOH N . ? 0.3288 0.3277 0.3246 0.0022 -0.0173 0.0059 832 HOH A O 3446 O O . HOH N . ? 0.3015 0.2648 0.3220 -0.0056 0.0305 0.0161 833 HOH A O 3447 O O . HOH N . ? 0.2365 0.2488 0.2887 -0.0080 -0.0063 -0.0170 834 HOH A O 3448 O O . HOH N . ? 0.3260 0.3114 0.3918 -0.0138 0.0344 -0.0067 835 HOH A O 3449 O O . HOH N . ? 0.2893 0.3042 0.3621 -0.0078 0.0073 -0.0163 836 HOH A O 3450 O O . HOH N . ? 0.3328 0.3242 0.3058 -0.0022 0.0177 0.0097 837 HOH A O 3451 O O . HOH N . ? 0.3046 0.2850 0.3164 0.0013 0.0177 -0.0020 838 HOH A O 3452 O O . HOH N . ? 0.3306 0.3070 0.3625 -0.0105 0.0422 0.0061 839 HOH A O 3453 O O . HOH N . ? 0.3317 0.3295 0.3423 -0.0080 0.0017 -0.0113 840 HOH A O 3454 O O . HOH N . ? 0.2950 0.2791 0.2601 -0.0002 0.0145 -0.0118 841 HOH A O 3455 O O . HOH N . ? 0.2704 0.2483 0.2964 -0.0100 0.0413 0.0058 842 HOH A O 3456 O O . HOH N . ? 0.4266 0.3640 0.4266 -0.0149 0.0336 -0.0149 843 HOH A O 3457 O O . HOH N . ? 0.3666 0.3492 0.3255 0.0003 0.0109 -0.0130 844 HOH A O 3458 O O . HOH N . ? 0.2062 0.2056 0.2683 -0.0126 0.0244 -0.0118 845 HOH A O 3459 O O . HOH N . ? 0.2935 0.2570 0.3091 -0.0069 0.0366 0.0186 846 HOH A O 3460 O O . HOH N . ? 0.3569 0.3260 0.3456 -0.0047 0.0296 0.0183 847 HOH A O 3461 O O . HOH N . ? 0.3326 0.3066 0.2759 -0.0015 0.0306 0.0083 848 HOH A O 3462 O O . HOH N . ? 0.2733 0.2665 0.3133 -0.0087 0.0423 -0.0074 849 HOH A O 3463 O O . HOH N . ? 0.2498 0.2642 0.3172 -0.0084 0.0022 -0.0167 850 HOH A O 3464 O O . HOH N . ? 0.3493 0.3630 0.4357 0.0011 0.0134 -0.0178 851 HOH A O 3465 O O . HOH N . ? 0.3555 0.3713 0.4159 0.0017 -0.0170 -0.0090 852 HOH A O 3466 O O . HOH N . ? 0.3036 0.2762 0.2895 -0.0046 0.0272 0.0155 853 HOH A O 3467 O O . HOH N . ? 0.3036 0.2781 0.3523 -0.0118 0.0406 0.0041 854 HOH A O 3468 O O . HOH N . ? 0.2573 0.2669 0.3288 0.0066 -0.0078 -0.0080 855 HOH A O 3469 O O . HOH N . ? 0.3269 0.3319 0.3359 -0.0019 -0.0135 -0.0053 856 HOH A O 3470 O O . HOH N . ? 0.3810 0.3784 0.4560 -0.0133 0.0293 -0.0126 857 HOH A O 3471 O O . HOH N . ? 0.3172 0.2979 0.3380 -0.0109 0.0101 -0.0260 858 HOH A O 3472 O O . HOH N . ? 0.3389 0.3319 0.3012 -0.0040 -0.0105 -0.0143 859 HOH A O 3473 O O . HOH N . ? 0.3128 0.3030 0.2657 -0.0012 0.0159 0.0037 860 HOH A O 3474 O O . HOH N . ? 0.3643 0.3565 0.3544 -0.0076 -0.0029 -0.0202 861 HOH A O 3475 O O . HOH N . ? 0.3247 0.3371 0.4302 0.0083 -0.0121 -0.0106 862 HOH A O 3476 O O . HOH N . ? 0.3296 0.3098 0.3236 -0.0044 0.0164 -0.0201 863 HOH A O 3477 O O . HOH N . ? 0.3142 0.3064 0.2987 -0.0007 -0.0053 0.0022 864 HOH A O 3478 O O . HOH N . ? 0.2525 0.2439 0.2586 -0.0101 -0.0018 -0.0248 865 HOH A O 3479 O O . HOH N . ? 0.3680 0.3777 0.4275 -0.0029 0.0215 -0.0149 866 HOH A O 3480 O O . HOH N . ? 0.3677 0.3449 0.3746 -0.0080 0.0357 0.0085 867 HOH A O 3481 O O . HOH N . ? 0.2950 0.2846 0.2476 -0.0023 0.0029 -0.0095 868 HOH A O 3482 O O . HOH N . ? 0.3204 0.2885 0.2880 0.0048 -0.0004 0.0288 869 HOH A O 3483 O O . HOH N . ? 0.4012 0.3744 0.3778 -0.0048 0.0343 0.0139 870 HOH A O 3484 O O . HOH N . ? 0.2801 0.2677 0.2412 -0.0030 0.0093 -0.0108 871 HOH A O 3485 O O . HOH N . ? 0.3706 0.3636 0.3468 -0.0059 -0.0065 -0.0180 872 HOH A O 3486 O O . HOH N . ? 0.2948 0.2702 0.2300 0.0017 0.0083 0.0135 873 HOH A O 3487 O O . HOH N . ? 0.3335 0.3409 0.3509 -0.0026 -0.0155 -0.0084 874 HOH A O 3488 O O . HOH N . ? 0.3485 0.3240 0.3627 -0.0088 0.0392 0.0090 875 HOH A O 3489 O O . HOH N . ? 0.2944 0.2926 0.3301 -0.0131 -0.0046 -0.0272 876 HOH A O 3490 O O . HOH N . ? 0.3883 0.3801 0.3363 -0.0006 0.0015 0.0025 877 HOH A O 3491 O O . HOH N . ? 0.2427 0.2315 0.2264 -0.0003 0.0029 -0.0096 878 HOH A O 3492 O O . HOH N . ? 0.3127 0.2935 0.2545 0.0020 0.0000 0.0048 879 HOH A O 3493 O O . HOH N . ? 0.3674 0.3632 0.4280 -0.0121 0.0319 -0.0091 880 HOH A O 3494 O O . HOH N . ? 0.4081 0.3824 0.3455 0.0020 0.0073 0.0169 881 HOH A O 3495 O O . HOH N . ? 0.4968 0.4684 0.4537 0.0060 -0.0048 0.0285 882 HOH A O 3496 O O . HOH N . ? 0.3308 0.2996 0.3498 0.0089 0.0049 0.0220 883 HOH A O 3497 O O . HOH N . ? 0.4070 0.3777 0.3430 -0.0009 0.0276 0.0143 884 HOH A O 3498 O O . HOH N . ? 0.3288 0.3329 0.4109 -0.0130 0.0204 -0.0173 885 HOH A O 3499 O O . HOH N . ? 0.2769 0.2907 0.3284 -0.0043 -0.0076 -0.0132 886 HOH A O 3500 O O . HOH N . ? 0.3786 0.3705 0.3622 0.0000 -0.0071 0.0033 887 HOH A O 3501 O O . HOH N . ? 0.3113 0.3132 0.3088 -0.0034 -0.0107 -0.0065 888 HOH A O 3502 O O . HOH N . ? 0.4311 0.4491 0.5108 -0.0001 -0.0002 -0.0144 889 HOH A O 3503 O O . HOH N . ? 0.3308 0.3030 0.3086 -0.0029 0.0223 0.0174 890 HOH A O 3504 O O . HOH N . ? 0.3091 0.2985 0.2919 -0.0010 0.0201 -0.0029 891 HOH A O 3505 O O . HOH N . ? 0.3404 0.3528 0.4076 -0.0106 -0.0018 -0.0204 892 HOH A O 3506 O O . HOH N . ? 0.3898 0.3816 0.3503 -0.0012 0.0058 0.0095 893 HOH A O 3507 O O . HOH N . ? 0.3623 0.3456 0.3155 0.0005 0.0018 -0.0047 894 HOH A O 3508 O O . HOH N . ? 0.4009 0.3954 0.3945 -0.0004 -0.0035 0.0056 895 HOH A O 3509 O O . HOH N . ? 0.3070 0.3077 0.3798 0.0126 -0.0299 0.0088 896 HOH A O 3510 O O . HOH N . ? 0.3173 0.3033 0.3938 -0.0150 0.0293 -0.0125 897 HOH A O 3511 O O . HOH N . ? 0.3796 0.3505 0.3346 -0.0029 0.0328 0.0155 898 HOH A O 3512 O O . HOH N . ? 0.3157 0.3186 0.3218 -0.0047 -0.0078 -0.0086 899 HOH A O 3513 O O . HOH N . ? 0.2888 0.2896 0.3247 -0.0052 0.0322 -0.0115 900 HOH A O 3514 O O . HOH N . ? 0.3598 0.3333 0.3758 -0.0010 0.0185 -0.0015 901 HOH A O 3515 O O . HOH N . ? 0.4352 0.4427 0.5052 -0.0132 0.0007 -0.0240 902 HOH A O 3516 O O . HOH N . ? 0.3515 0.3355 0.3148 -0.0002 0.0192 -0.0109 903 HOH A O 3517 O O . HOH N . ? 0.3210 0.3143 0.3206 -0.0085 -0.0018 -0.0192 904 HOH A O 3518 O O . HOH N . ? 0.3809 0.3397 0.3890 -0.0016 0.0246 0.0240 905 HOH A O 3519 O O . HOH N . ? 0.4622 0.4500 0.4402 -0.0013 0.0203 -0.0063 906 HOH A O 3520 O O . HOH N . ? 0.4356 0.4480 0.4755 -0.0037 -0.0142 -0.0123 907 HOH A O 3521 O O . HOH N . ? 0.4698 0.4524 0.4771 -0.0097 0.0073 -0.0273 908 HOH A O 3522 O O . HOH N . ? 0.4352 0.4108 0.3886 0.0034 0.0001 0.0205 909 HOH A O 3523 O O . HOH N . ? 0.5020 0.4932 0.4446 -0.0004 0.0044 0.0037 910 HOH A O 3524 O O . HOH N . ? 0.3991 0.4084 0.4287 0.0008 -0.0178 -0.0049 911 HOH A O 3525 O O . HOH N . ? 0.4194 0.3843 0.3811 0.0031 0.0054 0.0307 912 HOH A O 3526 O O . HOH N . ? 0.3361 0.3282 0.3383 -0.0024 0.0328 -0.0122 913 HOH A O 3527 O O . HOH N . ? 0.3525 0.3341 0.3007 0.0032 -0.0071 0.0083 914 HOH A O 3528 O O . HOH N . ? 0.3236 0.2999 0.3653 -0.0116 0.0182 -0.0186 915 HOH A O 3529 O O . HOH N . ? 0.4727 0.4849 0.6180 0.0077 -0.0001 -0.0198 916 HOH A O 3530 O O . HOH N . ? 0.3863 0.3596 0.3815 -0.0073 0.0466 0.0107 917 HOH A O 3531 O O . HOH N . ? 0.3869 0.3777 0.4615 -0.0140 0.0337 -0.0100 918 HOH A O 3532 O O . HOH N . ? 0.4472 0.4173 0.4210 -0.0053 0.0426 0.0149 919 HOH A O 3533 O O . HOH N . ? 0.3937 0.4027 0.4354 -0.0082 -0.0043 -0.0156 920 HOH A O 3534 O O . HOH N . ? 0.5449 0.5169 0.4700 0.0019 0.0114 0.0159 921 HOH A O 3535 O O . HOH N . ? 0.4068 0.4190 0.4817 0.0076 -0.0186 -0.0048 922 HOH A O 3536 O O . HOH N . ? 0.3264 0.3211 0.2875 -0.0003 -0.0154 0.0009 923 HOH A O 3537 O O . HOH N . ? 0.3465 0.3081 0.3387 0.0012 0.0159 0.0262 924 HOH A O 3538 O O . HOH N . ? 0.3634 0.3496 0.3874 -0.0089 0.0440 -0.0014 925 HOH A O 3539 O O . HOH N . ? 0.3376 0.3503 0.4035 -0.0040 0.0155 -0.0145 926 HOH A O 3540 O O . HOH N . ? 0.4137 0.4235 0.5244 0.0098 -0.0145 -0.0088 927 HOH A O 3541 O O . HOH N . ? 0.4310 0.4121 0.4250 -0.0022 0.0198 -0.0157 928 HOH A O 3542 O O . HOH N . ? 0.3149 0.3323 0.3848 -0.0050 -0.0039 -0.0157 929 HOH A O 3543 O O . HOH N . ? 0.3191 0.3145 0.3462 -0.0117 0.0031 -0.0188 930 HOH A O 3544 O O . HOH N . ? 0.5190 0.5134 0.5265 -0.0100 -0.0051 -0.0243 931 HOH A O 3545 O O . HOH N . ? 0.5520 0.5287 0.4768 0.0014 0.0152 -0.0009 932 HOH A O 3546 O O . HOH N . ? 0.3417 0.3350 0.3311 -0.0007 -0.0069 0.0028 933 HOH A O 3547 O O . HOH N . ? 0.3833 0.3718 0.3376 -0.0022 0.0074 -0.0102 934 HOH A O 3548 O O . HOH N . ? 0.2933 0.2675 0.2714 -0.0045 0.0304 0.0137 935 HOH A O 3549 O O . HOH N . ? 0.3860 0.3997 0.5055 0.0073 -0.0066 -0.0149 936 HOH A O 3550 O O . HOH N . ? 0.3996 0.4129 0.4759 0.0001 0.0150 -0.0167 937 HOH A O 3551 O O . HOH N . ? 0.3650 0.3418 0.3426 -0.0052 0.0469 0.0034 938 HOH A O 3552 O O . HOH N . ? 0.3409 0.3254 0.3544 0.0024 0.0206 -0.0034 939 HOH A O 3553 O O . HOH N . ? 0.3148 0.2802 0.3728 -0.0102 0.0354 0.0037 940 HOH A O 3554 O O . HOH N . ? 0.3135 0.3068 0.3266 -0.0046 0.0366 -0.0096 941 HOH A O 3555 O O . HOH N . ? 0.4712 0.4554 0.5337 -0.0131 0.0404 -0.0035 942 HOH A O 3556 O O . HOH N . ? 0.4275 0.3956 0.3673 0.0030 0.0058 0.0281 943 HOH A O 3557 O O . HOH N . ? 0.5065 0.4780 0.4979 -0.0072 0.0510 0.0111 944 HOH A O 3558 O O . HOH N . ? 0.3301 0.3223 0.2931 -0.0012 0.0041 0.0071 945 HOH A O 3559 O O . HOH N . ? 0.3811 0.3670 0.4067 -0.0125 0.0057 -0.0267 946 HOH A O 3560 O O . HOH N . ? 0.3588 0.3457 0.3302 0.0024 -0.0103 0.0072 947 HOH A O 3561 O O . HOH N . ? 0.5474 0.5116 0.5889 -0.0075 0.0309 0.0074 948 HOH A O 3562 O O . HOH N . ? 0.3697 0.3846 0.4418 -0.0020 0.0098 -0.0149 949 HOH A O 3563 O O . HOH N . ? 0.4175 0.4090 0.3582 -0.0005 0.0003 -0.0020 950 HOH A O 3564 O O . HOH N . ? 0.4696 0.4410 0.5171 -0.0113 0.0403 0.0062 951 HOH A O 3565 O O . HOH N . ? 0.4593 0.4555 0.4280 0.0000 -0.0176 0.0014 952 HOH A O 3566 O O . HOH N . ? 0.2587 0.2543 0.2565 -0.0008 0.0037 -0.0038 953 HOH A O 3567 O O . HOH N . ? 0.3818 0.3726 0.3653 -0.0008 0.0029 -0.0049 954 HOH A O 3568 O O . HOH N . ? 0.3405 0.3125 0.3635 -0.0093 0.0390 0.0104 955 HOH A O 3569 O O . HOH N . ? 0.3379 0.3283 0.3235 -0.0007 0.0225 -0.0009 956 HOH A O 3570 O O . HOH N . ? 0.4277 0.3960 0.3873 0.0052 -0.0020 0.0307 957 HOH A O 3571 O O . HOH N . ? 0.3998 0.3907 0.3902 -0.0027 0.0081 0.0151 958 HOH A O 3572 O O . HOH N . ? 0.3916 0.3705 0.4583 -0.0137 0.0349 -0.0049 959 HOH A O 3573 O O . HOH N . ? 0.3474 0.3346 0.3149 -0.0005 0.0017 -0.0022 960 HOH A O 3574 O O . HOH N . ? 0.4502 0.4143 0.4217 -0.0014 0.0218 0.0265 961 HOH A O 3575 O O . HOH N . ? 0.3663 0.3571 0.3512 -0.0008 0.0000 -0.0044 962 HOH A O 3576 O O . HOH N . ? 0.4132 0.4263 0.5056 0.0080 -0.0168 -0.0078 963 HOH A O 3577 O O . HOH N . ? 0.2696 0.2869 0.3595 0.0036 -0.0055 -0.0135 964 HOH A O 3578 O O . HOH N . ? 0.4587 0.4589 0.4999 -0.0055 0.0355 -0.0125 965 HOH A O 3579 O O . HOH N . ? 0.4709 0.4419 0.4795 -0.0078 0.0382 0.0135 966 HOH A O 3580 O O . HOH N . ? 0.5275 0.5154 0.4818 -0.0009 0.0030 0.0219 967 HOH A O 3581 O O . HOH N . ? 0.5861 0.5713 0.5780 -0.0043 0.0438 -0.0072 968 HOH A O 3582 O O . HOH N . ? 0.4565 0.4331 0.4631 -0.0082 0.0465 0.0072 969 HOH A O 3583 O O . HOH N . ? 0.3827 0.3973 0.4324 -0.0026 -0.0141 -0.0122 970 HOH A O 3584 O O . HOH N . ? 0.3130 0.3043 0.2665 0.0013 -0.0048 0.0142 971 HOH A O 3585 O O . HOH N . ? 0.5254 0.5149 0.4800 -0.0034 -0.0019 -0.0145 972 HOH A O 3586 O O . HOH N . ? 0.4801 0.4461 0.4415 -0.0012 0.0213 0.0255 973 HOH A O 3587 O O . HOH N . ? 0.4062 0.4039 0.3909 -0.0051 -0.0106 -0.0131 974 HOH A O 3588 O O . HOH N . ? 0.4027 0.3663 0.4416 -0.0086 0.0377 0.0129 975 HOH A O 3589 O O . HOH N . ? 0.5091 0.4715 0.5575 -0.0085 0.0358 0.0097 976 HOH A O 3590 O O . HOH N . ? 0.3548 0.3577 0.4053 -0.0063 0.0328 -0.0126 977 HOH A O 3591 O O . HOH N . ? 0.4439 0.4380 0.4897 -0.0145 -0.0004 -0.0304 978 HOH A O 3592 O O . HOH N . ? 0.4492 0.4366 0.4325 -0.0003 0.0253 -0.0156 979 HOH A O 3593 O O . HOH N . ? 0.2905 0.2667 0.3015 -0.0036 0.0174 -0.0056 980 HOH A O 3594 O O . HOH N . ? 0.4781 0.4577 0.4156 0.0009 0.0166 -0.0054 981 HOH A O 3595 O O . HOH N . ? 0.4225 0.3844 0.3946 0.0048 0.0025 0.0321 982 HOH A O 3596 O O . HOH N . ? 0.3486 0.3335 0.3083 0.0007 -0.0040 0.0005 983 HOH A O 3597 O O . HOH N . ? 0.5090 0.4794 0.4431 0.0027 0.0067 0.0234 984 HOH A O 3598 O O . HOH N . ? 0.4571 0.4594 0.4785 -0.0086 -0.0038 -0.0152 985 HOH A O 3599 O O . HOH N . ? 0.4186 0.4276 0.5246 0.0090 -0.0084 -0.0109 986 HOH A O 3600 O O . HOH N . ? 0.3856 0.3626 0.3321 0.0027 0.0017 0.0163 987 HOH A O 3601 O O . HOH N . ? 0.3834 0.3902 0.4428 -0.0056 0.0283 -0.0142 988 HOH A O 3602 O O . HOH N . ? 0.4464 0.4289 0.4872 -0.0135 0.0086 -0.0313 989 HOH A O 3603 O O . HOH N . ? 0.3396 0.3495 0.4112 -0.0122 0.0008 -0.0224 990 HOH A O 3604 O O . HOH N . ? 0.3910 0.3855 0.3853 -0.0012 -0.0047 0.0040 991 HOH A O 3605 O O . HOH N . ? 0.4147 0.3833 0.3711 -0.0038 0.0409 0.0157 992 HOH A O 3606 O O . HOH N . ? 0.3965 0.4053 0.4621 -0.0080 0.0229 -0.0138 993 HOH A O 3607 O O . HOH N . ? 0.3170 0.3051 0.2887 -0.0010 0.0073 -0.0038 994 HOH A O 3608 O O . HOH N . ? 0.3764 0.3686 0.3646 -0.0029 0.0175 0.0132 995 HOH A O 3609 O O . HOH N . ? 0.3183 0.3146 0.3437 -0.0118 -0.0018 -0.0231 996 HOH A O 3610 O O . HOH N . ? 0.4448 0.4289 0.4870 -0.0110 0.0449 -0.0004 997 HOH A O 3611 O O . HOH N . ? 0.3996 0.4089 0.4665 -0.0062 0.0248 -0.0147 998 HOH A O 3612 O O . HOH N . ? 0.4173 0.4145 0.4047 -0.0053 -0.0065 -0.0110 999 HOH A O 3613 O O . HOH N . ? 0.4093 0.3820 0.4013 -0.0066 0.0393 0.0131 1000 HOH A O 3614 O O . HOH N . ? 0.4398 0.4107 0.4184 -0.0062 0.0524 0.0102 1001 HOH A O 3615 O O . HOH N . ? 0.3438 0.3359 0.3011 -0.0001 -0.0019 0.0091 1002 HOH A O 3616 O O . HOH N . ? 0.5102 0.5011 0.5616 -0.0112 0.0401 -0.0054 1003 HOH A O 3617 O O . HOH N . ? 0.5263 0.5189 0.4686 -0.0011 -0.0068 -0.0066 1004 HOH A O 3618 O O . HOH N . ? 0.3518 0.3390 0.3166 -0.0038 0.0080 -0.0143 1005 HOH A O 3619 O O . HOH N . ? 0.4761 0.4677 0.4555 -0.0025 0.0178 0.0117 1006 HOH A O 3620 O O . HOH N . ? 0.4494 0.4075 0.4544 -0.0027 0.0279 0.0256 1007 HOH A O 3621 O O . HOH N . ? 0.3845 0.3576 0.3987 -0.0033 0.0184 -0.0007 1008 HOH A O 3622 O O . HOH N . ? 0.2702 0.2494 0.2792 0.0003 0.0161 -0.0004 1009 HOH A O 3623 O O . HOH N . ? 0.3776 0.3968 0.4540 -0.0024 -0.0058 -0.0149 1010 HOH A O 3624 O O . HOH N . ? 0.4895 0.5069 0.5605 -0.0067 -0.0049 -0.0174 1011 HOH A O 3625 O O . HOH N . ? 0.5161 0.4850 0.5145 -0.0066 0.0369 0.0167 1012 HOH A O 3626 O O . HOH N . ? 0.3769 0.3667 0.3530 -0.0002 -0.0062 0.0007 1013 HOH A O 3627 O O . HOH N . ? 0.3206 0.2826 0.3153 0.0080 0.0019 0.0295 1014 HOH A O 3628 O O . HOH N . ? 0.3599 0.3380 0.3570 -0.0071 0.0502 0.0033 1015 HOH A O 3629 O O . HOH N . ? 0.4730 0.4715 0.4639 -0.0044 -0.0050 -0.0067 1016 HOH A O 3630 O O . HOH N . ? 0.4545 0.4230 0.4306 -0.0028 0.0245 0.0210 1017 HOH A O 3631 O O . HOH N . ? 0.4798 0.4708 0.4312 0.0003 -0.0002 0.0141 1018 HOH A O 3632 O O . HOH N . ? 0.5272 0.4903 0.4927 -0.0001 0.0175 0.0289 1019 HOH A O 3633 O O . HOH N . ? 0.4115 0.4119 0.4668 -0.0101 0.0307 -0.0100 1020 HOH A O 3634 O O . HOH N . ? 0.2462 0.2579 0.3378 0.0034 0.0123 -0.0187 1021 HOH A O 3635 O O . HOH N . ? 0.3637 0.3250 0.3841 0.0010 0.0197 0.0179 1022 HOH A O 3636 O O . HOH N . ? 0.2759 0.2304 0.2759 -0.0193 0.0148 -0.0193 1023 HOH A O 3637 O O . HOH N . ? 0.3616 0.3314 0.3092 -0.0015 0.0262 0.0188 1024 HOH A O 3638 O O . HOH N . ? 0.3961 0.3853 0.3839 -0.0025 0.0080 0.0175 1025 HOH A O 3639 O O . HOH N . ? 0.2771 0.2378 0.2799 -0.0009 0.0217 0.0236 1026 HOH A O 3640 O O . HOH N . ? 0.3281 0.3259 0.3249 -0.0051 0.0004 -0.0055 1027 HOH A O 3641 O O . HOH N . ? 0.4638 0.4385 0.4475 -0.0050 0.0295 0.0132 1028 HOH A O 3642 O O . HOH N . ? 0.4071 0.4131 0.4240 -0.0049 -0.0102 -0.0107 1029 HOH A O 3643 O O . HOH N . ? 0.3721 0.3824 0.4676 0.0101 -0.0224 -0.0041 1030 HOH A O 3644 O O . HOH N . ? 0.3610 0.3581 0.3769 -0.0105 -0.0053 -0.0229 1031 HOH A O 3645 O O . HOH N . ? 0.4142 0.4095 0.4300 -0.0033 0.0343 -0.0124 1032 HOH A O 3646 O O . HOH N . ? 0.4898 0.4612 0.5352 -0.0099 0.0231 -0.0116 1033 HOH A O 3647 O O . HOH N . ? 0.4351 0.4061 0.4045 0.0049 -0.0011 0.0260 1034 HOH A O 3648 O O . HOH N . ? 0.3827 0.3502 0.4398 -0.0102 0.0315 -0.0010 1035 HOH A O 3649 O O . HOH N . ? 0.5062 0.4832 0.4677 0.0080 -0.0123 0.0237 1036 HOH A O 3650 O O . HOH N . ? 0.4155 0.3795 0.4503 -0.0049 0.0261 0.0066 1037 HOH A O 3651 O O . HOH N . ? 0.3474 0.3354 0.3168 0.0000 -0.0034 0.0013 1038 HOH A O 3652 O O . HOH N . ? 0.4110 0.4028 0.4140 -0.0003 0.0294 -0.0173 1039 HOH A O 3653 O O . HOH N . ? 0.4479 0.4435 0.4761 -0.0055 0.0393 -0.0111 1040 HOH A O 3654 O O . HOH N . ? 0.4040 0.3963 0.4097 -0.0018 0.0347 -0.0149 1041 HOH A O 3655 O O . HOH N . ? 0.3701 0.3637 0.4347 -0.0125 0.0349 -0.0086 1042 HOH A O 3656 O O . HOH N . ? 0.4298 0.4413 0.4708 -0.0053 -0.0098 -0.0135 1043 HOH A O 3657 O O . HOH N . ? 0.3681 0.3594 0.3542 -0.0011 -0.0023 -0.0026 1044 HOH A O 3658 O O . HOH N . ? 0.3966 0.3881 0.3710 -0.0023 0.0132 0.0116 1045 HOH A O 3659 O O . HOH N . ? 0.4285 0.4107 0.3771 0.0006 0.0082 -0.0075 1046 HOH A O 3660 O O . HOH N . ? 0.4586 0.4479 0.4093 -0.0025 0.0004 -0.0136 1047 HOH A O 3661 O O . HOH N . ? 0.5123 0.5226 0.5944 -0.0123 0.0060 -0.0221 1048 HOH A O 3662 O O . HOH N . ? 0.4130 0.4116 0.4782 -0.0149 0.0087 -0.0227 1049 HOH A O 3663 O O . HOH N . ? 0.3582 0.3753 0.4571 0.0015 0.0041 -0.0173 1050 HOH A O 3664 O O . HOH N . ? 0.4760 0.4476 0.4427 -0.0039 0.0335 0.0156 1051 HOH A O 3665 O O . HOH N . ? 0.4779 0.4601 0.4779 -0.0075 0.0102 -0.0221 1052 HOH A O 3666 O O . HOH N . ? 0.4048 0.4046 0.3963 -0.0040 -0.0088 -0.0073 1053 HOH A O 3667 O O . HOH N . ? 0.4752 0.4679 0.4715 -0.0033 0.0187 0.0144 1054 HOH A O 3668 O O . HOH N . ? 0.3692 0.3584 0.4250 -0.0123 0.0377 -0.0051 1055 HOH A O 3669 O O . HOH N . ? 0.4375 0.4487 0.5065 -0.0092 0.0144 -0.0151 1056 HOH A O 3670 O O . HOH N . ? 0.4384 0.4144 0.4500 -0.0036 0.0182 -0.0098 1057 HOH A O 3671 O O . HOH N . ? 0.4316 0.4188 0.3937 -0.0024 0.0133 -0.0103 1058 HOH A O 3672 O O . HOH N . ? 0.4850 0.4865 0.4949 -0.0061 -0.0021 -0.0092 1059 HOH A O 3673 O O . HOH N . ? 0.5369 0.5492 0.6313 0.0018 0.0161 -0.0199 1060 HOH A O 3674 O O . HOH N . ? 0.4551 0.4135 0.4557 0.0034 0.0136 0.0282 1061 HOH A O 3675 O O . HOH N . ? 0.4195 0.3983 0.4778 -0.0128 0.0408 -0.0001 1062 HOH A O 3676 O O . HOH N . ? 0.4339 0.4508 0.5172 0.0005 0.0056 -0.0156 1063 HOH A O 3677 O O . HOH N . ? 0.4789 0.4748 0.4758 -0.0070 -0.0023 -0.0134 1064 HOH A O 3678 O O . HOH N . ? 0.5158 0.5197 0.5731 -0.0082 0.0302 -0.0120 1065 HOH A O 3679 O O . HOH N . ? 0.5214 0.4815 0.5063 0.0008 0.0167 0.0288 1066 HOH A O 3680 O O . HOH N . ? 0.4485 0.4421 0.5246 -0.0150 0.0232 -0.0162 1067 HOH A O 3681 O O . HOH N . ? 0.4496 0.4391 0.3974 -0.0009 0.0161 -0.0009 1068 HOH A O 3682 O O . HOH N . ? 0.3638 0.3734 0.4855 0.0064 0.0096 -0.0216 1069 HOH A O 3683 O O . HOH N . ? 0.4679 0.4390 0.4945 0.0018 0.0207 -0.0017 1070 HOH A O 3684 O O . HOH N . ? 0.5035 0.4748 0.4317 0.0003 0.0222 0.0133 1071 HOH A O 3685 O O . HOH N . ? 0.5110 0.5019 0.5047 -0.0001 0.0225 -0.0009 1072 HOH A O 3686 O O . HOH N . ? 0.4869 0.4462 0.4605 0.0035 0.0077 0.0330 1073 HOH A O 3687 O O . HOH N . ? 0.4794 0.4411 0.5216 -0.0081 0.0370 0.0132 1074 HOH A O 3688 O O . HOH N . ? 0.4833 0.4802 0.4523 -0.0020 -0.0172 -0.0062 1075 HOH A O 3689 O O . HOH N . ? 0.4611 0.4222 0.4792 -0.0061 0.0350 0.0200 1076 HOH A O 3690 O O . HOH N . ? 0.4575 0.4665 0.5177 -0.0120 -0.0056 -0.0239 1077 HOH A O 3691 O O . HOH N . ? 0.4881 0.4711 0.4792 -0.0017 0.0200 -0.0132 1078 HOH A O 3692 O O . HOH N . ? 0.5708 0.5531 0.6359 -0.0133 0.0405 -0.0031 1079 HOH A O 3693 O O . HOH N . ? 0.4370 0.4322 0.3900 -0.0013 -0.0169 -0.0063 1080 HOH A O 3694 O O . HOH N . ? 0.4596 0.4337 0.4224 -0.0040 0.0443 0.0060 1081 HOH A O 3695 O O . HOH N . ? 0.5063 0.5123 0.5609 -0.0128 -0.0079 -0.0271 1082 HOH A O 3696 O O . HOH N . ? 0.5235 0.4987 0.4628 0.0044 -0.0032 0.0195 1083 HOH A O 3697 O O . HOH N . ? 0.5183 0.5053 0.5042 -0.0013 0.0182 -0.0071 1084 HOH A O 3698 O O . HOH N . ? 0.3787 0.3952 0.4482 -0.0016 -0.0015 -0.0135 1085 HOH A O 3699 O O . HOH N . ? 0.5225 0.5039 0.5891 -0.0138 0.0359 -0.0050 1086 HOH A O 3700 O O . HOH N . ? 0.3780 0.3798 0.4704 0.0142 -0.0333 0.0081 1087 HOH A O 3701 O O . HOH N . ? 0.5290 0.5203 0.4953 -0.0053 -0.0070 -0.0192 1088 HOH A O 3702 O O . HOH N . ? 0.4967 0.4774 0.4386 0.0028 -0.0045 0.0061 1089 HOH A O 3703 O O . HOH N . ? 0.4148 0.4037 0.3858 -0.0009 0.0272 -0.0022 1090 HOH A O 3704 O O . HOH N . ? 0.4638 0.4597 0.4233 -0.0001 -0.0193 -0.0015 1091 HOH A O 3705 O O . HOH N . ? 0.4941 0.4794 0.5094 -0.0114 0.0045 -0.0280 1092 HOH A O 3706 O O . HOH N . ? 0.3821 0.3973 0.4776 0.0004 0.0123 -0.0186 1093 HOH A O 3707 O O . HOH N . ? 0.5070 0.4822 0.4348 0.0007 0.0201 0.0040 1094 HOH A O 3708 O O . HOH N . ? 0.4171 0.4315 0.4825 -0.0019 0.0045 -0.0133 1095 HOH A O 3709 O O . HOH N . ? 0.5283 0.5052 0.4845 -0.0026 0.0361 0.0032 1096 HOH A O 3710 O O . HOH N . ? 0.5522 0.5243 0.4678 0.0011 0.0234 0.0049 1097 HOH A O 3711 O O . HOH N . ? 0.5023 0.4851 0.4692 -0.0016 0.0338 -0.0082 1098 HOH A O 3712 O O . HOH N . ? 0.4384 0.4169 0.4422 -0.0027 0.0192 -0.0147 1099 HOH A O 3713 O O . HOH N . ? 0.4078 0.4213 0.5306 0.0033 0.0125 -0.0223 1100 HOH A O 3714 O O . HOH N . ? 0.5040 0.4639 0.5197 -0.0044 0.0308 0.0211 1101 HOH A O 3715 O O . HOH N . ? 0.4457 0.4569 0.5288 0.0009 0.0193 -0.0192 1102 HOH A O 3716 O O . HOH N . ? 0.4120 0.4279 0.5361 0.0045 0.0011 -0.0191 1103 HOH A O 3717 O O . HOH N . ? 0.4738 0.4714 0.5275 -0.0146 0.0019 -0.0266 1104 HOH A O 3718 O O . HOH N . ? 0.4804 0.4853 0.5782 0.0135 -0.0327 0.0045 1105 HOH A O 3719 O O . HOH N . ? 0.5054 0.4962 0.4428 -0.0004 0.0052 -0.0001 1106 HOH A O 3720 O O . HOH N . ? 0.5170 0.5289 0.5791 -0.0107 -0.0079 -0.0228 1107 HOH A O 3721 O O . HOH N . ? 0.5351 0.5327 0.5945 -0.0150 0.0017 -0.0287 1108 HOH A O 3722 O O . HOH N . ? 0.4709 0.4868 0.5305 -0.0055 -0.0098 -0.0159 1109 HOH A O 3723 O O . HOH N . ? 0.5206 0.4852 0.4594 0.0034 0.0054 0.0328 1110 HOH A O 3724 O O . HOH N . ? 0.4580 0.4740 0.5688 0.0060 -0.0083 -0.0144 1111 HOH A O 3725 O O . HOH N . ? 0.5673 0.5644 0.5489 -0.0005 -0.0101 0.0036 1112 HOH A O 3726 O O . HOH N . ? 0.4955 0.4912 0.5294 -0.0133 -0.0041 -0.0293 1113 HOH A O 3727 O O . HOH N . ? 0.5666 0.5537 0.6286 -0.0127 0.0411 -0.0046 1114 HOH A O 3728 O O . HOH N . ? 0.5165 0.5118 0.5954 -0.0139 0.0306 -0.0128 1115 HOH A O 3729 O O . HOH N . ? 0.5310 0.5450 0.5778 0.0004 -0.0193 -0.0086 1116 HOH A O 3730 O O . HOH N . ? 0.5369 0.5278 0.6234 -0.0151 0.0310 -0.0139 1117 HOH A O 3731 O O . HOH N . ? 0.5446 0.5148 0.5360 -0.0068 0.0441 0.0147 1118 HOH A O 3732 O O . HOH N . ? 0.5211 0.5200 0.5083 -0.0006 -0.0117 0.0016 1119 HOH A O 3733 O O . HOH N . ? 0.5585 0.5480 0.5771 -0.0066 0.0452 -0.0072 1120 HOH A O 3734 O O . HOH N . ? 0.5625 0.5561 0.6190 -0.0153 0.0023 -0.0313 1121 HOH A O 3735 O O . HOH N . ? 0.5222 0.5152 0.5899 -0.0149 0.0203 -0.0162 1122 HOH A O 3736 O O . HOH N . ? 0.5238 0.5144 0.5185 -0.0011 0.0288 -0.0142 1123 HOH A O 3737 O O . HOH N . ? 0.6006 0.5777 0.5495 -0.0016 0.0330 0.0013 1124 HOH A O 3738 O O . HOH N . ? 0.5772 0.5843 0.6505 -0.0095 0.0251 -0.0145 1125 HOH A O 3739 O O . HOH N . ? 0.6230 0.5990 0.5663 -0.0012 0.0304 0.0037 1126 HOH A O 3740 O O . HOH N . ? 0.5050 0.4676 0.5392 -0.0070 0.0331 0.0132 1127 HOH A O 3741 O O . HOH N . ? 0.4663 0.4571 0.4389 -0.0023 0.0217 0.0103 1128 HOH A O 3742 O O . HOH N . ? 0.4945 0.5095 0.6227 0.0032 0.0093 -0.0220 1129 HOH A O 3743 O O . HOH N . ? 0.6026 0.5881 0.5831 -0.0024 0.0167 -0.0119 1130 HOH A O 3744 O O . HOH N . ? 0.4832 0.4862 0.5656 -0.0139 0.0175 -0.0191 1131 HOH A O 3745 O O . HOH N . ? 0.5306 0.5429 0.6058 -0.0110 0.0023 -0.0206 1132 HOH A O 3746 O O . HOH N . ? 0.5444 0.5081 0.5720 -0.0082 0.0395 0.0162 1133 HOH A O 3747 O O . HOH N . ? 0.5183 0.5328 0.6239 0.0000 0.0162 -0.0207 1134 HOH A O 3748 O O . HOH N . ? 0.4889 0.4758 0.5021 0.0025 0.0220 -0.0032 1135 HOH A O 3749 O O . HOH N . ? 0.5632 0.5573 0.5008 0.0007 -0.0153 0.0005 1136 HOH A O 3750 O O . HOH N . ? 0.4343 0.4066 0.3883 -0.0019 0.0252 0.0164 1137 HOH A O 3751 O O . HOH N . ? 0.4384 0.4369 0.4356 -0.0044 0.0005 -0.0042 1138 HOH A O 3752 O O . HOH N . ? 0.4308 0.4029 0.3890 -0.0027 0.0289 0.0157 1139 HOH A O 3753 O O . HOH N . ? 0.4713 0.4557 0.4664 -0.0076 0.0074 -0.0225 1140 HOH A O 3754 O O . HOH N . ? 0.3455 0.3478 0.3627 -0.0073 -0.0018 -0.0116 1141 HOH A O 3755 O O . HOH N . ? 0.4515 0.4472 0.3988 0.0007 -0.0209 -0.0007 1142 HOH A O 3756 O O . HOH N . ? 0.5333 0.5285 0.4781 0.0017 -0.0211 0.0029 1143 HOH A O 3757 O O . HOH N . ? 0.3710 0.3766 0.4764 0.0147 -0.0375 0.0055 1144 HOH A O 3758 O O . HOH N . ? 0.4546 0.4320 0.4111 0.0025 0.0020 0.0174 1145 HOH A O 3759 O O . HOH N . ? 0.5392 0.5470 0.5929 -0.0043 0.0251 -0.0138 1146 HOH A O 3760 O O . HOH N . ? 0.4942 0.5059 0.6280 0.0082 -0.0037 -0.0169 1147 HOH A O 3761 O O . HOH N . ? 0.4414 0.4242 0.4023 0.0003 0.0013 -0.0135 1148 HOH A O 3762 O O . HOH N . ? 0.5217 0.5203 0.5809 -0.0109 0.0326 -0.0098 1149 HOH A O 3763 O O . HOH N . ? 0.6009 0.5809 0.5542 -0.0010 0.0314 -0.0051 1150 HOH A O 3764 O O . HOH N . ? 0.5016 0.4954 0.4466 -0.0011 -0.0120 -0.0063 1151 HOH A O 3765 O O . HOH N . ? 0.5100 0.4790 0.5608 -0.0094 0.0256 -0.0086 1152 HOH A O 3766 O O . HOH N . ? 0.4994 0.5100 0.6414 0.0078 0.0026 -0.0204 1153 HOH A O 3767 O O . HOH N . ? 0.4426 0.4401 0.4297 0.0016 -0.0166 0.0065 1154 HOH A O 3768 O O . HOH N . ? 0.5645 0.5232 0.5665 0.0009 0.0188 0.0262 1155 HOH A O 3769 O O . HOH N . ? 0.5418 0.5073 0.5836 -0.0065 0.0264 0.0007 1156 HOH A O 3770 O O . HOH N . ? 0.4724 0.4633 0.5167 -0.0103 0.0408 -0.0050 1157 HOH A O 3771 O O . HOH N . ? 0.5012 0.5087 0.5870 -0.0128 0.0140 -0.0202 1158 HOH A O 3772 O O . HOH N . ? 0.5413 0.5134 0.5483 -0.0081 0.0422 0.0125 1159 HOH A O 3773 O O . HOH N . ? 0.5371 0.5211 0.5166 -0.0030 0.0397 -0.0073 1160 HOH A O 3774 O O . HOH N . ? 0.5811 0.5437 0.5865 0.0093 0.0020 0.0286 1161 HOH A O 3775 O O . HOH N . ? 0.5706 0.5641 0.5064 -0.0002 -0.0116 -0.0033 1162 HOH A O 3776 O O . HOH N . ? 0.5759 0.5641 0.5525 -0.0019 0.0160 -0.0060 1163 HOH A O 3777 O O . HOH N . ? 0.5273 0.5375 0.5652 0.0017 -0.0169 -0.0049 1164 HOH A O 3778 O O . HOH N . ? 0.5577 0.5552 0.6296 -0.0151 0.0142 -0.0206 1165 HOH A O 3779 O O . HOH N . ? 0.6068 0.5857 0.5393 0.0027 -0.0011 0.0049 1166 HOH A O 3780 O O . HOH N . ? 0.5705 0.5281 0.5557 0.0040 0.0096 0.0321 1167 HOH A O 3781 O O . HOH N . ? 0.5143 0.4714 0.5262 0.0011 0.0202 0.0253 1168 HOH A O 3782 O O . HOH N . ? 0.5130 0.5030 0.4610 -0.0013 0.0144 0.0084 1169 HOH A O 3783 O O . HOH N . ? 0.5432 0.5354 0.4832 0.0000 -0.0033 0.0020 1170 HOH A O 3784 O O . HOH N . ? 0.5971 0.6038 0.6631 -0.0050 0.0306 -0.0159 1171 HOH A O 3785 O O . HOH N . ? 0.4846 0.4938 0.5148 -0.0054 -0.0116 -0.0132 1172 HOH A O 3786 O O . HOH N . ? 0.5637 0.5506 0.5478 -0.0019 0.0348 -0.0118 1173 HOH A O 3787 O O . HOH N . ? 0.5374 0.5443 0.6114 -0.0108 0.0215 -0.0150 1174 HOH A O 3788 O O . HOH N . ? 0.5875 0.5751 0.5566 0.0011 -0.0104 0.0016 1175 HOH A O # 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 ARG 1 83 83 ARG ARG A . n A 1 2 ASN 2 84 84 ASN ASN A . n A 1 3 PHE 3 85 85 PHE PHE A . n A 1 4 ASN 4 86 86 ASN ASN A . n A 1 5 ASN 5 87 87 ASN ASN A . n A 1 6 LEU 6 88 88 LEU LEU A . n A 1 7 THR 7 89 89 THR THR A . n A 1 8 LYS 8 90 90 LYS LYS A . n A 1 9 GLY 9 91 91 GLY GLY A . n A 1 10 LEU 10 92 92 LEU LEU A . n A 1 11 CYS 11 93 93 CYS CYS A . n A 1 12 THR 12 94 94 THR THR A . n A 1 13 ILE 13 95 95 ILE ILE A . n A 1 14 ASN 14 96 96 ASN ASN A . n A 1 15 SER 15 97 97 SER SER A . n A 1 16 TRP 16 98 98 TRP TRP A . n A 1 17 HIS 17 99 99 HIS HIS A . n A 1 18 ILE 18 100 100 ILE ILE A . n A 1 19 TYR 19 101 101 TYR TYR A . n A 1 20 GLY 20 102 102 GLY GLY A . n A 1 21 LYS 21 103 103 LYS LYS A . n A 1 22 ASP 22 104 104 ASP ASP A . n A 1 23 ASN 23 105 105 ASN ASN A . n A 1 24 ALA 24 106 106 ALA ALA A . n A 1 25 VAL 25 107 107 VAL VAL A . n A 1 26 ARG 26 108 108 ARG ARG A . n A 1 27 ILE 27 109 109 ILE ILE A . n A 1 28 GLY 28 110 110 GLY GLY A . n A 1 29 GLU 29 111 111 GLU GLU A . n A 1 30 SER 30 112 112 SER SER A . n A 1 31 SER 31 113 113 SER SER A . n A 1 32 ASP 32 114 114 ASP ASP A . n A 1 33 VAL 33 115 115 VAL VAL A . n A 1 34 LEU 34 116 116 LEU LEU A . n A 1 35 VAL 35 117 117 VAL VAL A . n A 1 36 THR 36 118 118 THR THR A . n A 1 37 ARG 37 119 119 ARG ARG A . n A 1 38 GLU 38 120 120 GLU GLU A . n A 1 39 PRO 39 121 121 PRO PRO A . n A 1 40 TYR 40 122 122 TYR TYR A . n A 1 41 VAL 41 123 123 VAL VAL A . n A 1 42 SER 42 124 124 SER SER A . n A 1 43 CYS 43 125 125 CYS CYS A . n A 1 44 ASP 44 126 126 ASP ASP A . n A 1 45 PRO 45 127 127 PRO PRO A . n A 1 46 ASP 46 128 128 ASP ASP A . n A 1 47 GLU 47 129 129 GLU GLU A . n A 1 48 CYS 48 130 130 CYS CYS A . n A 1 49 ARG 49 131 131 ARG ARG A . n A 1 50 PHE 50 132 132 PHE PHE A . n A 1 51 TYR 51 133 133 TYR TYR A . n A 1 52 ALA 52 134 134 ALA ALA A . n A 1 53 LEU 53 135 135 LEU LEU A . n A 1 54 SER 54 136 136 SER SER A . n A 1 55 GLN 55 137 137 GLN GLN A . n A 1 56 GLY 56 138 138 GLY GLY A . n A 1 57 THR 57 139 139 THR THR A . n A 1 58 THR 58 140 140 THR THR A . n A 1 59 ILE 59 141 141 ILE ILE A . n A 1 60 ARG 60 142 142 ARG ARG A . n A 1 61 GLY 61 143 143 GLY GLY A . n A 1 62 LYS 62 144 144 LYS LYS A . n A 1 63 HIS 63 145 145 HIS HIS A . n A 1 64 SER 64 146 146 SER SER A . n A 1 65 ASN 65 147 147 ASN ASN A . n A 1 66 GLY 66 148 148 GLY GLY A . n A 1 67 THR 67 149 149 THR THR A . n A 1 68 ILE 68 150 150 ILE ILE A . n A 1 69 HIS 69 151 151 HIS HIS A . n A 1 70 ASP 70 152 152 ASP ASP A . n A 1 71 ARG 71 153 153 ARG ARG A . n A 1 72 SER 72 154 154 SER SER A . n A 1 73 GLN 73 155 155 GLN GLN A . n A 1 74 TYR 74 156 156 TYR TYR A . n A 1 75 ARG 75 157 157 ARG ARG A . n A 1 76 ALA 76 158 158 ALA ALA A . n A 1 77 LEU 77 159 159 LEU LEU A . n A 1 78 ILE 78 160 160 ILE ILE A . n A 1 79 SER 79 161 161 SER SER A . n A 1 80 TRP 80 162 162 TRP TRP A . n A 1 81 PRO 81 163 163 PRO PRO A . n A 1 82 LEU 82 164 164 LEU LEU A . n A 1 83 SER 83 165 165 SER SER A . n A 1 84 SER 84 166 166 SER SER A . n A 1 85 PRO 85 167 167 PRO PRO A . n A 1 86 PRO 86 168 168 PRO PRO A . n A 1 87 THR 87 169 169 THR THR A . n A 1 88 VAL 88 170 170 VAL VAL A . n A 1 89 TYR 89 171 171 TYR TYR A . n A 1 90 ASN 90 172 172 ASN ASN A . n A 1 91 SER 91 173 173 SER SER A . n A 1 92 ARG 92 174 174 ARG ARG A . n A 1 93 VAL 93 175 175 VAL VAL A . n A 1 94 GLU 94 176 176 GLU GLU A . n A 1 95 CYS 95 177 177 CYS CYS A . n A 1 96 ILE 96 178 178 ILE ILE A . n A 1 97 GLY 97 179 179 GLY GLY A . n A 1 98 TRP 98 180 180 TRP TRP A . n A 1 99 SER 99 181 181 SER SER A . n A 1 100 SER 100 182 182 SER SER A . n A 1 101 THR 101 183 183 THR THR A . n A 1 102 SER 102 184 184 SER SER A . n A 1 103 CYS 103 185 185 CYS CYS A . n A 1 104 HIS 104 186 186 HIS HIS A . n A 1 105 ASP 105 187 187 ASP ASP A . n A 1 106 GLY 106 188 188 GLY GLY A . n A 1 107 LYS 107 189 189 LYS LYS A . n A 1 108 SER 108 190 190 SER SER A . n A 1 109 ARG 109 191 191 ARG ARG A . n A 1 110 MET 110 192 192 MET MET A . n A 1 111 SER 111 193 193 SER SER A . n A 1 112 ILE 112 194 194 ILE ILE A . n A 1 113 CYS 113 195 195 CYS CYS A . n A 1 114 ILE 114 196 196 ILE ILE A . n A 1 115 SER 115 197 197 SER SER A . n A 1 116 GLY 116 198 198 GLY GLY A . n A 1 117 PRO 117 199 199 PRO PRO A . n A 1 118 ASN 118 200 200 ASN ASN A . n A 1 119 ASN 119 201 201 ASN ASN A . n A 1 120 ASN 120 202 202 ASN ASN A . n A 1 121 ALA 121 203 203 ALA ALA A . n A 1 122 SER 122 204 204 SER SER A . n A 1 123 ALA 123 205 205 ALA ALA A . n A 1 124 VAL 124 206 206 VAL VAL A . n A 1 125 VAL 125 207 207 VAL VAL A . n A 1 126 TRP 126 208 208 TRP TRP A . n A 1 127 TYR 127 209 209 TYR TYR A . n A 1 128 ASN 128 210 210 ASN ASN A . n A 1 129 ARG 129 211 211 ARG ARG A . n A 1 130 ARG 130 212 212 ARG ARG A . n A 1 131 PRO 131 213 213 PRO PRO A . n A 1 132 VAL 132 214 214 VAL VAL A . n A 1 133 ALA 133 215 215 ALA ALA A . n A 1 134 GLU 134 216 216 GLU GLU A . n A 1 135 ILE 135 217 217 ILE ILE A . n A 1 136 ASN 136 218 218 ASN ASN A . n A 1 137 THR 137 219 219 THR THR A . n A 1 138 TRP 138 220 220 TRP TRP A . n A 1 139 ALA 139 221 221 ALA ALA A . n A 1 140 ARG 140 222 222 ARG ARG A . n A 1 141 ASN 141 223 223 ASN ASN A . n A 1 142 ILE 142 224 224 ILE ILE A . n A 1 143 LEU 143 225 225 LEU LEU A . n A 1 144 ARG 144 226 226 ARG ARG A . n A 1 145 THR 145 227 227 THR THR A . n A 1 146 GLN 146 228 228 GLN GLN A . n A 1 147 GLU 147 229 229 GLU GLU A . n A 1 148 SER 148 230 230 SER SER A . n A 1 149 GLU 149 231 231 GLU GLU A . n A 1 150 CYS 150 232 232 CYS CYS A . n A 1 151 VAL 151 233 233 VAL VAL A . n A 1 152 CYS 152 234 234 CYS CYS A . n A 1 153 HIS 153 235 235 HIS HIS A . n A 1 154 ASN 154 236 236 ASN ASN A . n A 1 155 GLY 155 237 237 GLY GLY A . n A 1 156 VAL 156 238 238 VAL VAL A . n A 1 157 CYS 157 239 239 CYS CYS A . n A 1 158 PRO 158 240 240 PRO PRO A . n A 1 159 VAL 159 241 241 VAL VAL A . n A 1 160 VAL 160 242 242 VAL VAL A . n A 1 161 PHE 161 243 243 PHE PHE A . n A 1 162 THR 162 244 244 THR THR A . n A 1 163 ASP 163 245 245 ASP ASP A . n A 1 164 GLY 164 246 246 GLY GLY A . n A 1 165 SER 165 247 247 SER SER A . n A 1 166 ALA 166 248 248 ALA ALA A . n A 1 167 THR 167 249 249 THR THR A . n A 1 168 GLY 168 250 250 GLY GLY A . n A 1 169 PRO 169 251 251 PRO PRO A . n A 1 170 ALA 170 252 252 ALA ALA A . n A 1 171 ASP 171 253 253 ASP ASP A . n A 1 172 THR 172 254 254 THR THR A . n A 1 173 ARG 173 255 255 ARG ARG A . n A 1 174 ILE 174 256 256 ILE ILE A . n A 1 175 TYR 175 257 257 TYR TYR A . n A 1 176 TYR 176 258 258 TYR TYR A . n A 1 177 PHE 177 259 259 PHE PHE A . n A 1 178 LYS 178 260 260 LYS LYS A . n A 1 179 GLU 179 261 261 GLU GLU A . n A 1 180 GLY 180 262 262 GLY GLY A . n A 1 181 LYS 181 263 263 LYS LYS A . n A 1 182 ILE 182 264 264 ILE ILE A . n A 1 183 LEU 183 265 265 LEU LEU A . n A 1 184 LYS 184 266 266 LYS LYS A . n A 1 185 TRP 185 267 267 TRP TRP A . n A 1 186 GLU 186 268 268 GLU GLU A . n A 1 187 SER 187 269 269 SER SER A . n A 1 188 LEU 188 270 270 LEU LEU A . n A 1 189 THR 189 271 271 THR THR A . n A 1 190 GLY 190 272 272 GLY GLY A . n A 1 191 THR 191 273 273 THR THR A . n A 1 192 ALA 192 274 274 ALA ALA A . n A 1 193 LYS 193 275 275 LYS LYS A . n A 1 194 HIS 194 276 276 HIS HIS A . n A 1 195 ILE 195 277 277 ILE ILE A . n A 1 196 GLU 196 278 278 GLU GLU A . n A 1 197 GLU 197 279 279 GLU GLU A . n A 1 198 CYS 198 280 280 CYS CYS A . n A 1 199 SER 199 281 281 SER SER A . n A 1 200 CYS 200 282 282 CYS CYS A . n A 1 201 TYR 201 283 283 TYR TYR A . n A 1 202 GLY 202 284 284 GLY GLY A . n A 1 203 GLU 203 285 285 GLU GLU A . n A 1 204 ARG 204 286 286 ARG ARG A . n A 1 205 THR 205 287 287 THR THR A . n A 1 206 GLY 206 288 288 GLY GLY A . n A 1 207 ILE 207 289 289 ILE ILE A . n A 1 208 THR 208 290 290 THR THR A . n A 1 209 CYS 209 291 291 CYS CYS A . n A 1 210 THR 210 292 292 THR THR A . n A 1 211 CYS 211 293 293 CYS CYS A . n A 1 212 LYS 212 294 294 LYS LYS A . n A 1 213 ASP 213 295 295 ASP ASP A . n A 1 214 ASN 214 296 296 ASN ASN A . n A 1 215 TRP 215 297 297 TRP TRP A . n A 1 216 GLN 216 298 298 GLN GLN A . n A 1 217 GLY 217 299 299 GLY GLY A . n A 1 218 SER 218 300 300 SER SER A . n A 1 219 ASN 219 301 301 ASN ASN A . n A 1 220 ARG 220 302 302 ARG ARG A . n A 1 221 PRO 221 303 303 PRO PRO A . n A 1 222 VAL 222 304 304 VAL VAL A . n A 1 223 ILE 223 305 305 ILE ILE A . n A 1 224 GLN 224 306 306 GLN GLN A . n A 1 225 ILE 225 307 307 ILE ILE A . n A 1 226 ASP 226 308 308 ASP ASP A . n A 1 227 PRO 227 309 309 PRO PRO A . n A 1 228 VAL 228 310 310 VAL VAL A . n A 1 229 ALA 229 311 311 ALA ALA A . n A 1 230 MET 230 312 312 MET MET A . n A 1 231 THR 231 313 313 THR THR A . n A 1 232 HIS 232 314 314 HIS HIS A . n A 1 233 THR 233 315 315 THR THR A . n A 1 234 SER 234 316 316 SER SER A . n A 1 235 GLN 235 317 317 GLN GLN A . n A 1 236 TYR 236 318 318 TYR TYR A . n A 1 237 ILE 237 319 319 ILE ILE A . n A 1 238 CYS 238 320 320 CYS CYS A . n A 1 239 SER 239 321 321 SER SER A . n A 1 240 PRO 240 322 322 PRO PRO A . n A 1 241 VAL 241 323 323 VAL VAL A . n A 1 242 LEU 242 324 324 LEU LEU A . n A 1 243 THR 243 325 325 THR THR A . n A 1 244 ASP 244 326 326 ASP ASP A . n A 1 245 ASN 245 327 327 ASN ASN A . n A 1 246 PRO 246 328 328 PRO PRO A . n A 1 247 ARG 247 329 329 ARG ARG A . n A 1 248 PRO 248 330 330 PRO PRO A . n A 1 249 ASN 249 331 331 ASN ASN A . n A 1 250 ASP 250 332 332 ASP ASP A . n A 1 251 PRO 251 333 333 PRO PRO A . n A 1 252 ASN 252 334 334 ASN ASN A . n A 1 253 ILE 253 335 335 ILE ILE A . n A 1 254 GLY 254 336 336 GLY GLY A . n A 1 255 LYS 255 337 337 LYS LYS A . n A 1 256 CYS 256 338 338 CYS CYS A . n A 1 257 ASN 257 339 339 ASN ASN A . n A 1 258 ASP 258 340 340 ASP ASP A . n A 1 259 PRO 259 341 341 PRO PRO A . n A 1 260 TYR 260 342 342 TYR TYR A . n A 1 261 PRO 261 343 343 PRO PRO A . n A 1 262 GLY 262 344 344 GLY GLY A . n A 1 263 ASN 263 345 345 ASN ASN A . n A 1 264 ASN 264 346 346 ASN ASN A . n A 1 265 ASN 265 347 347 ASN ASN A . n A 1 266 ASN 266 348 348 ASN ASN A . n A 1 267 GLY 267 349 349 GLY GLY A . n A 1 268 VAL 268 350 350 VAL VAL A . n A 1 269 LYS 269 351 351 LYS LYS A . n A 1 270 GLY 270 352 352 GLY GLY A . n A 1 271 PHE 271 353 353 PHE PHE A . n A 1 272 SER 272 354 354 SER SER A . n A 1 273 TYR 273 355 355 TYR TYR A . n A 1 274 LEU 274 356 356 LEU LEU A . n A 1 275 ASP 275 357 357 ASP ASP A . n A 1 276 GLY 276 358 358 GLY GLY A . n A 1 277 ALA 277 359 359 ALA ALA A . n A 1 278 ASN 278 360 360 ASN ASN A . n A 1 279 THR 279 361 361 THR THR A . n A 1 280 TRP 280 362 362 TRP TRP A . n A 1 281 LEU 281 363 363 LEU LEU A . n A 1 282 GLY 282 364 364 GLY GLY A . n A 1 283 ARG 283 365 365 ARG ARG A . n A 1 284 THR 284 366 366 THR THR A . n A 1 285 ILE 285 367 367 ILE ILE A . n A 1 286 SER 286 368 368 SER SER A . n A 1 287 THR 287 369 369 THR THR A . n A 1 288 ALA 288 370 370 ALA ALA A . n A 1 289 SER 289 371 371 SER SER A . n A 1 290 ARG 290 372 372 ARG ARG A . n A 1 291 SER 291 373 373 SER SER A . n A 1 292 GLY 292 374 374 GLY GLY A . n A 1 293 TYR 293 375 375 TYR TYR A . n A 1 294 GLU 294 376 376 GLU GLU A . n A 1 295 MET 295 377 377 MET MET A . n A 1 296 LEU 296 378 378 LEU LEU A . n A 1 297 LYS 297 379 379 LYS LYS A . n A 1 298 VAL 298 380 380 VAL VAL A . n A 1 299 PRO 299 381 381 PRO PRO A . n A 1 300 ASN 300 382 382 ASN ASN A . n A 1 301 ALA 301 383 383 ALA ALA A . n A 1 302 LEU 302 384 384 LEU LEU A . n A 1 303 THR 303 385 385 THR THR A . n A 1 304 ASP 304 386 386 ASP ASP A . n A 1 305 ASP 305 387 387 ASP ASP A . n A 1 306 ARG 306 388 388 ARG ARG A . n A 1 307 SER 307 389 389 SER SER A . n A 1 308 LYS 308 390 390 LYS LYS A . n A 1 309 PRO 309 391 391 PRO PRO A . n A 1 310 ILE 310 392 392 ILE ILE A . n A 1 311 GLN 311 393 393 GLN GLN A . n A 1 312 GLY 312 394 394 GLY GLY A . n A 1 313 GLN 313 395 395 GLN GLN A . n A 1 314 THR 314 396 396 THR THR A . n A 1 315 ILE 315 397 397 ILE ILE A . n A 1 316 VAL 316 398 398 VAL VAL A . n A 1 317 LEU 317 399 399 LEU LEU A . n A 1 318 ASN 318 400 400 ASN ASN A . n A 1 319 ALA 319 401 401 ALA ALA A . n A 1 320 ASP 320 402 402 ASP ASP A . n A 1 321 TRP 321 403 403 TRP TRP A . n A 1 322 SER 322 404 404 SER SER A . n A 1 323 GLY 323 405 405 GLY GLY A . n A 1 324 TYR 324 406 406 TYR TYR A . n A 1 325 SER 325 407 407 SER SER A . n A 1 326 GLY 326 408 408 GLY GLY A . n A 1 327 SER 327 409 409 SER SER A . n A 1 328 PHE 328 410 410 PHE PHE A . n A 1 329 MET 329 411 411 MET MET A . n A 1 330 ASP 330 412 412 ASP ASP A . n A 1 331 TYR 331 413 413 TYR TYR A . n A 1 332 TRP 332 414 414 TRP TRP A . n A 1 333 ALA 333 415 415 ALA ALA A . n A 1 334 GLU 334 416 416 GLU GLU A . n A 1 335 GLY 335 417 417 GLY GLY A . n A 1 336 ASP 336 418 418 ASP ASP A . n A 1 337 CYS 337 419 419 CYS CYS A . n A 1 338 TYR 338 420 420 TYR TYR A . n A 1 339 ARG 339 421 421 ARG ARG A . n A 1 340 ALA 340 422 422 ALA ALA A . n A 1 341 CYS 341 423 423 CYS CYS A . n A 1 342 PHE 342 424 424 PHE PHE A . n A 1 343 TYR 343 425 425 TYR TYR A . n A 1 344 VAL 344 426 426 VAL VAL A . n A 1 345 GLU 345 427 427 GLU GLU A . n A 1 346 LEU 346 428 428 LEU LEU A . n A 1 347 ILE 347 429 429 ILE ILE A . n A 1 348 ARG 348 430 430 ARG ARG A . n A 1 349 GLY 349 431 431 GLY GLY A . n A 1 350 ARG 350 432 432 ARG ARG A . n A 1 351 PRO 351 433 433 PRO PRO A . n A 1 352 LYS 352 434 434 LYS LYS A . n A 1 353 GLU 353 435 435 GLU GLU A . n A 1 354 ASP 354 436 436 ASP ASP A . n A 1 355 LYS 355 437 437 LYS LYS A . n A 1 356 VAL 356 438 438 VAL VAL A . n A 1 357 TRP 357 439 439 TRP TRP A . n A 1 358 TRP 358 440 440 TRP TRP A . n A 1 359 THR 359 441 441 THR THR A . n A 1 360 SER 360 442 442 SER SER A . n A 1 361 ASN 361 443 443 ASN ASN A . n A 1 362 SER 362 444 444 SER SER A . n A 1 363 ILE 363 445 445 ILE ILE A . n A 1 364 VAL 364 446 446 VAL VAL A . n A 1 365 SER 365 447 447 SER SER A . n A 1 366 MET 366 448 448 MET MET A . n A 1 367 CYS 367 449 449 CYS CYS A . n A 1 368 SER 368 450 450 SER SER A . n A 1 369 SER 369 451 451 SER SER A . n A 1 370 THR 370 452 452 THR THR A . n A 1 371 GLU 371 453 453 GLU GLU A . n A 1 372 PHE 372 454 454 PHE PHE A . n A 1 373 LEU 373 455 455 LEU LEU A . n A 1 374 GLY 374 456 456 GLY GLY A . n A 1 375 GLN 375 457 457 GLN GLN A . n A 1 376 TRP 376 458 458 TRP TRP A . n A 1 377 ASN 377 459 459 ASN ASN A . n A 1 378 TRP 378 460 460 TRP TRP A . n A 1 379 PRO 379 461 461 PRO PRO A . n A 1 380 ASP 380 462 462 ASP ASP A . n A 1 381 GLY 381 463 463 GLY GLY A . n A 1 382 ALA 382 464 464 ALA ALA A . n A 1 383 LYS 383 465 465 LYS LYS A . n A 1 384 ILE 384 466 466 ILE ILE A . n A 1 385 GLU 385 467 467 GLU GLU A . n A 1 386 TYR 386 468 468 TYR TYR A . n A 1 387 PHE 387 469 469 PHE PHE A . n A 1 388 LEU 388 470 470 LEU LEU A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 501 501 NAG NAG A . C 2 NAG 1 502 502 NAG NAG A . D 2 NAG 1 503 503 NAG NAG A . E 2 NAG 2 504 504 NAG NAG A . F 3 BMA 3 505 505 BMA BMA A . G 4 MAN 4 506 506 MAN MAN A . H 4 MAN 5 507 507 MAN MAN A . I 4 MAN 6 508 508 MAN MAN A . J 4 MAN 7 509 509 MAN MAN A . K 4 MAN 8 510 510 MAN MAN A . L 4 MAN 9 511 511 MAN MAN A . M 5 CA 1 512 601 CA CA A . N 6 HOH 1 601 1 HOH HOH A . N 6 HOH 2 602 2 HOH HOH A . N 6 HOH 3 603 3 HOH HOH A . N 6 HOH 4 604 4 HOH HOH A . N 6 HOH 5 605 5 HOH HOH A . N 6 HOH 6 606 6 HOH HOH A . N 6 HOH 7 607 7 HOH HOH A . N 6 HOH 8 608 8 HOH HOH A . N 6 HOH 9 609 9 HOH HOH A . N 6 HOH 10 610 10 HOH HOH A . N 6 HOH 11 611 11 HOH HOH A . N 6 HOH 12 612 12 HOH HOH A . N 6 HOH 13 613 13 HOH HOH A . N 6 HOH 14 614 14 HOH HOH A . N 6 HOH 15 615 15 HOH HOH A . N 6 HOH 16 616 16 HOH HOH A . N 6 HOH 17 617 17 HOH HOH A . N 6 HOH 18 618 18 HOH HOH A . N 6 HOH 19 619 19 HOH HOH A . N 6 HOH 20 620 20 HOH HOH A . N 6 HOH 21 621 21 HOH HOH A . N 6 HOH 22 622 22 HOH HOH A . N 6 HOH 23 623 23 HOH HOH A . N 6 HOH 24 624 24 HOH HOH A . N 6 HOH 25 625 25 HOH HOH A . N 6 HOH 26 626 26 HOH HOH A . N 6 HOH 27 627 27 HOH HOH A . N 6 HOH 28 628 28 HOH HOH A . N 6 HOH 29 629 29 HOH HOH A . N 6 HOH 30 630 30 HOH HOH A . N 6 HOH 31 631 31 HOH HOH A . N 6 HOH 32 632 32 HOH HOH A . N 6 HOH 33 633 33 HOH HOH A . N 6 HOH 34 634 34 HOH HOH A . N 6 HOH 35 635 35 HOH HOH A . N 6 HOH 36 636 36 HOH HOH A . N 6 HOH 37 637 37 HOH HOH A . N 6 HOH 38 638 38 HOH HOH A . N 6 HOH 39 639 39 HOH HOH A . N 6 HOH 40 640 40 HOH HOH A . N 6 HOH 41 641 41 HOH HOH A . N 6 HOH 42 642 42 HOH HOH A . N 6 HOH 43 643 43 HOH HOH A . N 6 HOH 44 644 44 HOH HOH A . N 6 HOH 45 645 45 HOH HOH A . N 6 HOH 46 646 46 HOH HOH A . N 6 HOH 47 647 47 HOH HOH A . N 6 HOH 48 648 48 HOH HOH A . N 6 HOH 49 649 49 HOH HOH A . N 6 HOH 50 650 50 HOH HOH A . N 6 HOH 51 651 51 HOH HOH A . N 6 HOH 52 652 52 HOH HOH A . N 6 HOH 53 653 53 HOH HOH A . N 6 HOH 54 654 54 HOH HOH A . N 6 HOH 55 655 55 HOH HOH A . N 6 HOH 56 656 56 HOH HOH A . N 6 HOH 57 657 57 HOH HOH A . N 6 HOH 58 658 58 HOH HOH A . N 6 HOH 59 659 59 HOH HOH A . N 6 HOH 60 660 60 HOH HOH A . N 6 HOH 61 661 61 HOH HOH A . N 6 HOH 62 662 62 HOH HOH A . N 6 HOH 63 663 63 HOH HOH A . N 6 HOH 64 664 64 HOH HOH A . N 6 HOH 65 665 65 HOH HOH A . N 6 HOH 66 666 66 HOH HOH A . N 6 HOH 67 667 67 HOH HOH A . N 6 HOH 68 668 68 HOH HOH A . N 6 HOH 69 669 69 HOH HOH A . N 6 HOH 70 670 70 HOH HOH A . N 6 HOH 71 671 71 HOH HOH A . N 6 HOH 72 672 72 HOH HOH A . N 6 HOH 73 673 73 HOH HOH A . N 6 HOH 74 674 74 HOH HOH A . N 6 HOH 75 675 75 HOH HOH A . N 6 HOH 76 676 76 HOH HOH A . N 6 HOH 77 677 77 HOH HOH A . N 6 HOH 78 678 78 HOH HOH A . N 6 HOH 79 679 79 HOH HOH A . N 6 HOH 80 680 80 HOH HOH A . N 6 HOH 81 681 81 HOH HOH A . N 6 HOH 82 682 82 HOH HOH A . N 6 HOH 83 683 83 HOH HOH A . N 6 HOH 84 684 84 HOH HOH A . N 6 HOH 85 685 85 HOH HOH A . N 6 HOH 86 686 86 HOH HOH A . N 6 HOH 87 687 87 HOH HOH A . N 6 HOH 88 688 88 HOH HOH A . N 6 HOH 89 689 89 HOH HOH A . N 6 HOH 90 690 90 HOH HOH A . N 6 HOH 91 691 91 HOH HOH A . N 6 HOH 92 692 92 HOH HOH A . N 6 HOH 93 693 93 HOH HOH A . N 6 HOH 94 694 94 HOH HOH A . N 6 HOH 95 695 95 HOH HOH A . N 6 HOH 96 696 96 HOH HOH A . N 6 HOH 97 697 97 HOH HOH A . N 6 HOH 98 698 98 HOH HOH A . N 6 HOH 99 699 99 HOH HOH A . N 6 HOH 100 700 100 HOH HOH A . N 6 HOH 101 701 101 HOH HOH A . N 6 HOH 102 702 102 HOH HOH A . N 6 HOH 103 703 103 HOH HOH A . N 6 HOH 104 704 104 HOH HOH A . N 6 HOH 105 705 105 HOH HOH A . N 6 HOH 106 706 106 HOH HOH A . N 6 HOH 107 707 107 HOH HOH A . N 6 HOH 108 708 108 HOH HOH A . N 6 HOH 109 709 109 HOH HOH A . N 6 HOH 110 710 110 HOH HOH A . N 6 HOH 111 711 111 HOH HOH A . N 6 HOH 112 712 112 HOH HOH A . N 6 HOH 113 713 113 HOH HOH A . N 6 HOH 114 714 114 HOH HOH A . N 6 HOH 115 715 115 HOH HOH A . N 6 HOH 116 716 116 HOH HOH A . N 6 HOH 117 717 117 HOH HOH A . N 6 HOH 118 718 118 HOH HOH A . N 6 HOH 119 719 119 HOH HOH A . N 6 HOH 120 720 120 HOH HOH A . N 6 HOH 121 721 121 HOH HOH A . N 6 HOH 122 722 122 HOH HOH A . N 6 HOH 123 723 123 HOH HOH A . N 6 HOH 124 724 124 HOH HOH A . N 6 HOH 125 725 125 HOH HOH A . N 6 HOH 126 726 126 HOH HOH A . N 6 HOH 127 727 127 HOH HOH A . N 6 HOH 128 728 128 HOH HOH A . N 6 HOH 129 729 129 HOH HOH A . N 6 HOH 130 730 130 HOH HOH A . N 6 HOH 131 731 131 HOH HOH A . N 6 HOH 132 732 132 HOH HOH A . N 6 HOH 133 733 133 HOH HOH A . N 6 HOH 134 734 134 HOH HOH A . N 6 HOH 135 735 135 HOH HOH A . N 6 HOH 136 736 136 HOH HOH A . N 6 HOH 137 737 137 HOH HOH A . N 6 HOH 138 738 138 HOH HOH A . N 6 HOH 139 739 139 HOH HOH A . N 6 HOH 140 740 140 HOH HOH A . N 6 HOH 141 741 141 HOH HOH A . N 6 HOH 142 742 142 HOH HOH A . N 6 HOH 143 743 143 HOH HOH A . N 6 HOH 144 744 144 HOH HOH A . N 6 HOH 145 745 145 HOH HOH A . N 6 HOH 146 746 146 HOH HOH A . N 6 HOH 147 747 147 HOH HOH A . N 6 HOH 148 748 148 HOH HOH A . N 6 HOH 149 749 149 HOH HOH A . N 6 HOH 150 750 150 HOH HOH A . N 6 HOH 151 751 151 HOH HOH A . N 6 HOH 152 752 152 HOH HOH A . N 6 HOH 153 753 153 HOH HOH A . N 6 HOH 154 754 154 HOH HOH A . N 6 HOH 155 755 155 HOH HOH A . N 6 HOH 156 756 156 HOH HOH A . N 6 HOH 157 757 157 HOH HOH A . N 6 HOH 158 758 158 HOH HOH A . N 6 HOH 159 759 159 HOH HOH A . N 6 HOH 160 760 160 HOH HOH A . N 6 HOH 161 761 161 HOH HOH A . N 6 HOH 162 762 162 HOH HOH A . N 6 HOH 163 763 163 HOH HOH A . N 6 HOH 164 764 164 HOH HOH A . N 6 HOH 165 765 165 HOH HOH A . N 6 HOH 166 766 166 HOH HOH A . N 6 HOH 167 767 167 HOH HOH A . N 6 HOH 168 768 168 HOH HOH A . N 6 HOH 169 769 169 HOH HOH A . N 6 HOH 170 770 170 HOH HOH A . N 6 HOH 171 771 171 HOH HOH A . N 6 HOH 172 772 172 HOH HOH A . N 6 HOH 173 773 173 HOH HOH A . N 6 HOH 174 774 174 HOH HOH A . N 6 HOH 175 775 175 HOH HOH A . N 6 HOH 176 776 176 HOH HOH A . N 6 HOH 177 777 177 HOH HOH A . N 6 HOH 178 778 178 HOH HOH A . N 6 HOH 179 779 179 HOH HOH A . N 6 HOH 180 780 180 HOH HOH A . N 6 HOH 181 781 181 HOH HOH A . N 6 HOH 182 782 182 HOH HOH A . N 6 HOH 183 783 183 HOH HOH A . N 6 HOH 184 784 184 HOH HOH A . N 6 HOH 185 785 185 HOH HOH A . N 6 HOH 186 786 186 HOH HOH A . N 6 HOH 187 787 187 HOH HOH A . N 6 HOH 188 788 188 HOH HOH A . N 6 HOH 189 789 189 HOH HOH A . N 6 HOH 190 790 190 HOH HOH A . N 6 HOH 191 791 191 HOH HOH A . N 6 HOH 192 792 192 HOH HOH A . N 6 HOH 193 793 193 HOH HOH A . N 6 HOH 194 794 194 HOH HOH A . N 6 HOH 195 795 195 HOH HOH A . N 6 HOH 196 796 196 HOH HOH A . N 6 HOH 197 797 197 HOH HOH A . N 6 HOH 198 798 198 HOH HOH A . N 6 HOH 199 799 199 HOH HOH A . N 6 HOH 200 800 200 HOH HOH A . N 6 HOH 201 801 201 HOH HOH A . N 6 HOH 202 802 202 HOH HOH A . N 6 HOH 203 803 203 HOH HOH A . N 6 HOH 204 804 204 HOH HOH A . N 6 HOH 205 805 205 HOH HOH A . N 6 HOH 206 806 206 HOH HOH A . N 6 HOH 207 807 207 HOH HOH A . N 6 HOH 208 808 208 HOH HOH A . N 6 HOH 209 809 209 HOH HOH A . N 6 HOH 210 810 210 HOH HOH A . N 6 HOH 211 811 211 HOH HOH A . N 6 HOH 212 812 212 HOH HOH A . N 6 HOH 213 813 213 HOH HOH A . N 6 HOH 214 814 214 HOH HOH A . N 6 HOH 215 815 215 HOH HOH A . N 6 HOH 216 816 216 HOH HOH A . N 6 HOH 217 817 217 HOH HOH A . N 6 HOH 218 818 218 HOH HOH A . N 6 HOH 219 819 219 HOH HOH A . N 6 HOH 220 820 220 HOH HOH A . N 6 HOH 221 821 221 HOH HOH A . N 6 HOH 222 822 222 HOH HOH A . N 6 HOH 223 823 223 HOH HOH A . N 6 HOH 224 824 224 HOH HOH A . N 6 HOH 225 825 225 HOH HOH A . N 6 HOH 226 826 226 HOH HOH A . N 6 HOH 227 827 227 HOH HOH A . N 6 HOH 228 828 228 HOH HOH A . N 6 HOH 229 829 229 HOH HOH A . N 6 HOH 230 830 230 HOH HOH A . N 6 HOH 231 831 231 HOH HOH A . N 6 HOH 232 832 232 HOH HOH A . N 6 HOH 233 833 233 HOH HOH A . N 6 HOH 234 834 234 HOH HOH A . N 6 HOH 235 835 235 HOH HOH A . N 6 HOH 236 836 236 HOH HOH A . N 6 HOH 237 837 237 HOH HOH A . N 6 HOH 238 838 238 HOH HOH A . N 6 HOH 239 839 239 HOH HOH A . N 6 HOH 240 840 240 HOH HOH A . N 6 HOH 241 841 241 HOH HOH A . N 6 HOH 242 842 242 HOH HOH A . N 6 HOH 243 843 243 HOH HOH A . N 6 HOH 244 844 244 HOH HOH A . N 6 HOH 245 845 245 HOH HOH A . N 6 HOH 246 846 246 HOH HOH A . N 6 HOH 247 847 247 HOH HOH A . N 6 HOH 248 848 248 HOH HOH A . N 6 HOH 249 849 249 HOH HOH A . N 6 HOH 250 850 250 HOH HOH A . N 6 HOH 251 851 251 HOH HOH A . N 6 HOH 252 852 252 HOH HOH A . N 6 HOH 253 853 253 HOH HOH A . N 6 HOH 254 854 254 HOH HOH A . N 6 HOH 255 855 255 HOH HOH A . N 6 HOH 256 856 256 HOH HOH A . N 6 HOH 257 857 257 HOH HOH A . N 6 HOH 258 858 258 HOH HOH A . N 6 HOH 259 859 259 HOH HOH A . N 6 HOH 260 860 260 HOH HOH A . N 6 HOH 261 861 261 HOH HOH A . N 6 HOH 262 862 262 HOH HOH A . N 6 HOH 263 863 263 HOH HOH A . N 6 HOH 264 864 264 HOH HOH A . N 6 HOH 265 865 265 HOH HOH A . N 6 HOH 266 866 266 HOH HOH A . N 6 HOH 267 867 267 HOH HOH A . N 6 HOH 268 868 268 HOH HOH A . N 6 HOH 269 869 269 HOH HOH A . N 6 HOH 270 870 270 HOH HOH A . N 6 HOH 271 871 271 HOH HOH A . N 6 HOH 272 872 272 HOH HOH A . N 6 HOH 273 873 273 HOH HOH A . N 6 HOH 274 874 274 HOH HOH A . N 6 HOH 275 875 275 HOH HOH A . N 6 HOH 276 876 276 HOH HOH A . N 6 HOH 277 877 277 HOH HOH A . N 6 HOH 278 878 278 HOH HOH A . N 6 HOH 279 879 279 HOH HOH A . N 6 HOH 280 880 280 HOH HOH A . N 6 HOH 281 881 281 HOH HOH A . N 6 HOH 282 882 282 HOH HOH A . N 6 HOH 283 883 283 HOH HOH A . N 6 HOH 284 884 284 HOH HOH A . N 6 HOH 285 885 285 HOH HOH A . N 6 HOH 286 886 286 HOH HOH A . N 6 HOH 287 887 287 HOH HOH A . N 6 HOH 288 888 288 HOH HOH A . N 6 HOH 289 889 289 HOH HOH A . N 6 HOH 290 890 290 HOH HOH A . N 6 HOH 291 891 291 HOH HOH A . N 6 HOH 292 892 292 HOH HOH A . N 6 HOH 293 893 293 HOH HOH A . N 6 HOH 294 894 294 HOH HOH A . N 6 HOH 295 895 295 HOH HOH A . N 6 HOH 296 896 296 HOH HOH A . N 6 HOH 297 897 297 HOH HOH A . N 6 HOH 298 898 298 HOH HOH A . N 6 HOH 299 899 299 HOH HOH A . N 6 HOH 300 900 300 HOH HOH A . N 6 HOH 301 901 301 HOH HOH A . N 6 HOH 302 902 302 HOH HOH A . N 6 HOH 303 903 303 HOH HOH A . N 6 HOH 304 904 304 HOH HOH A . N 6 HOH 305 905 305 HOH HOH A . N 6 HOH 306 906 306 HOH HOH A . N 6 HOH 307 907 307 HOH HOH A . N 6 HOH 308 908 308 HOH HOH A . N 6 HOH 309 909 309 HOH HOH A . N 6 HOH 310 910 310 HOH HOH A . N 6 HOH 311 911 311 HOH HOH A . N 6 HOH 312 912 312 HOH HOH A . N 6 HOH 313 913 313 HOH HOH A . N 6 HOH 314 914 314 HOH HOH A . N 6 HOH 315 915 315 HOH HOH A . N 6 HOH 316 916 316 HOH HOH A . N 6 HOH 317 917 317 HOH HOH A . N 6 HOH 318 918 318 HOH HOH A . N 6 HOH 319 919 319 HOH HOH A . N 6 HOH 320 920 320 HOH HOH A . N 6 HOH 321 921 321 HOH HOH A . N 6 HOH 322 922 322 HOH HOH A . N 6 HOH 323 923 323 HOH HOH A . N 6 HOH 324 924 324 HOH HOH A . N 6 HOH 325 925 325 HOH HOH A . N 6 HOH 326 926 326 HOH HOH A . N 6 HOH 327 927 327 HOH HOH A . N 6 HOH 328 928 328 HOH HOH A . N 6 HOH 329 929 329 HOH HOH A . N 6 HOH 330 930 330 HOH HOH A . N 6 HOH 331 931 331 HOH HOH A . N 6 HOH 332 932 332 HOH HOH A . N 6 HOH 333 933 333 HOH HOH A . N 6 HOH 334 934 334 HOH HOH A . N 6 HOH 335 935 335 HOH HOH A . N 6 HOH 336 936 336 HOH HOH A . N 6 HOH 337 937 337 HOH HOH A . N 6 HOH 338 938 338 HOH HOH A . N 6 HOH 339 939 339 HOH HOH A . N 6 HOH 340 940 340 HOH HOH A . N 6 HOH 341 941 341 HOH HOH A . N 6 HOH 342 942 342 HOH HOH A . N 6 HOH 343 943 343 HOH HOH A . N 6 HOH 344 944 344 HOH HOH A . N 6 HOH 345 945 345 HOH HOH A . N 6 HOH 346 946 346 HOH HOH A . N 6 HOH 347 947 347 HOH HOH A . N 6 HOH 348 948 348 HOH HOH A . N 6 HOH 349 949 349 HOH HOH A . N 6 HOH 350 950 350 HOH HOH A . N 6 HOH 351 951 351 HOH HOH A . N 6 HOH 352 952 352 HOH HOH A . N 6 HOH 353 953 353 HOH HOH A . N 6 HOH 354 954 354 HOH HOH A . N 6 HOH 355 955 355 HOH HOH A . N 6 HOH 356 956 356 HOH HOH A . N 6 HOH 357 957 357 HOH HOH A . N 6 HOH 358 958 358 HOH HOH A . N 6 HOH 359 959 359 HOH HOH A . N 6 HOH 360 960 360 HOH HOH A . N 6 HOH 361 961 361 HOH HOH A . N 6 HOH 362 962 362 HOH HOH A . N 6 HOH 363 963 363 HOH HOH A . N 6 HOH 364 964 364 HOH HOH A . N 6 HOH 365 965 365 HOH HOH A . N 6 HOH 366 966 366 HOH HOH A . N 6 HOH 367 967 367 HOH HOH A . N 6 HOH 368 968 368 HOH HOH A . N 6 HOH 369 969 369 HOH HOH A . N 6 HOH 370 970 370 HOH HOH A . N 6 HOH 371 971 371 HOH HOH A . N 6 HOH 372 972 372 HOH HOH A . N 6 HOH 373 973 373 HOH HOH A . N 6 HOH 374 974 374 HOH HOH A . N 6 HOH 375 975 375 HOH HOH A . N 6 HOH 376 976 376 HOH HOH A . N 6 HOH 377 977 377 HOH HOH A . N 6 HOH 378 978 378 HOH HOH A . N 6 HOH 379 979 379 HOH HOH A . N 6 HOH 380 980 380 HOH HOH A . N 6 HOH 381 981 381 HOH HOH A . N 6 HOH 382 982 382 HOH HOH A . N 6 HOH 383 983 383 HOH HOH A . N 6 HOH 384 984 384 HOH HOH A . N 6 HOH 385 985 385 HOH HOH A . N 6 HOH 386 986 386 HOH HOH A . N 6 HOH 387 987 387 HOH HOH A . N 6 HOH 388 988 388 HOH HOH A . N 6 HOH 389 989 389 HOH HOH A . N 6 HOH 390 990 390 HOH HOH A . N 6 HOH 391 991 391 HOH HOH A . N 6 HOH 392 992 392 HOH HOH A . N 6 HOH 393 993 393 HOH HOH A . N 6 HOH 394 994 394 HOH HOH A . N 6 HOH 395 995 395 HOH HOH A . N 6 HOH 396 996 396 HOH HOH A . N 6 HOH 397 997 397 HOH HOH A . N 6 HOH 398 998 398 HOH HOH A . N 6 HOH 399 999 399 HOH HOH A . N 6 HOH 400 1000 400 HOH HOH A . N 6 HOH 401 1001 401 HOH HOH A . N 6 HOH 402 1002 402 HOH HOH A . N 6 HOH 403 1003 403 HOH HOH A . N 6 HOH 404 1004 404 HOH HOH A . N 6 HOH 405 1005 405 HOH HOH A . N 6 HOH 406 1006 406 HOH HOH A . N 6 HOH 407 1007 407 HOH HOH A . N 6 HOH 408 1008 408 HOH HOH A . N 6 HOH 409 1009 409 HOH HOH A . N 6 HOH 410 1010 410 HOH HOH A . N 6 HOH 411 1011 411 HOH HOH A . N 6 HOH 412 1012 412 HOH HOH A . N 6 HOH 413 1013 413 HOH HOH A . N 6 HOH 414 1014 414 HOH HOH A . N 6 HOH 415 1015 415 HOH HOH A . N 6 HOH 416 1016 416 HOH HOH A . N 6 HOH 417 1017 417 HOH HOH A . N 6 HOH 418 1018 418 HOH HOH A . N 6 HOH 419 1019 419 HOH HOH A . N 6 HOH 420 1020 420 HOH HOH A . N 6 HOH 421 1021 421 HOH HOH A . N 6 HOH 422 1022 422 HOH HOH A . N 6 HOH 423 1023 423 HOH HOH A . N 6 HOH 424 1024 424 HOH HOH A . N 6 HOH 425 1025 425 HOH HOH A . N 6 HOH 426 1026 426 HOH HOH A . N 6 HOH 427 1027 427 HOH HOH A . N 6 HOH 428 1028 428 HOH HOH A . N 6 HOH 429 1029 429 HOH HOH A . N 6 HOH 430 1030 430 HOH HOH A . N 6 HOH 431 1031 431 HOH HOH A . N 6 HOH 432 1032 432 HOH HOH A . N 6 HOH 433 1033 433 HOH HOH A . N 6 HOH 434 1034 434 HOH HOH A . N 6 HOH 435 1035 435 HOH HOH A . N 6 HOH 436 1036 436 HOH HOH A . N 6 HOH 437 1037 437 HOH HOH A . N 6 HOH 438 1038 438 HOH HOH A . N 6 HOH 439 1039 439 HOH HOH A . N 6 HOH 440 1040 440 HOH HOH A . N 6 HOH 441 1041 441 HOH HOH A . N 6 HOH 442 1042 442 HOH HOH A . N 6 HOH 443 1043 443 HOH HOH A . N 6 HOH 444 1044 444 HOH HOH A . N 6 HOH 445 1045 445 HOH HOH A . N 6 HOH 446 1046 446 HOH HOH A . N 6 HOH 447 1047 447 HOH HOH A . N 6 HOH 448 1048 448 HOH HOH A . N 6 HOH 449 1049 449 HOH HOH A . N 6 HOH 450 1050 450 HOH HOH A . N 6 HOH 451 1051 451 HOH HOH A . N 6 HOH 452 1052 452 HOH HOH A . N 6 HOH 453 1053 453 HOH HOH A . N 6 HOH 454 1054 454 HOH HOH A . N 6 HOH 455 1055 455 HOH HOH A . N 6 HOH 456 1056 456 HOH HOH A . N 6 HOH 457 1057 457 HOH HOH A . N 6 HOH 458 1058 458 HOH HOH A . N 6 HOH 459 1059 459 HOH HOH A . N 6 HOH 460 1060 460 HOH HOH A . N 6 HOH 461 1061 461 HOH HOH A . N 6 HOH 462 1062 462 HOH HOH A . N 6 HOH 463 1063 463 HOH HOH A . N 6 HOH 464 1064 464 HOH HOH A . N 6 HOH 465 1065 465 HOH HOH A . N 6 HOH 466 1066 466 HOH HOH A . N 6 HOH 467 1067 467 HOH HOH A . N 6 HOH 468 1068 468 HOH HOH A . N 6 HOH 469 1069 469 HOH HOH A . N 6 HOH 470 1070 470 HOH HOH A . N 6 HOH 471 1071 471 HOH HOH A . N 6 HOH 472 1072 472 HOH HOH A . N 6 HOH 473 1073 473 HOH HOH A . N 6 HOH 474 1074 474 HOH HOH A . N 6 HOH 475 1075 475 HOH HOH A . N 6 HOH 476 1076 476 HOH HOH A . N 6 HOH 477 1077 477 HOH HOH A . N 6 HOH 478 1078 478 HOH HOH A . N 6 HOH 479 1079 479 HOH HOH A . N 6 HOH 480 1080 480 HOH HOH A . N 6 HOH 481 1081 481 HOH HOH A . N 6 HOH 482 1082 482 HOH HOH A . N 6 HOH 483 1083 483 HOH HOH A . N 6 HOH 484 1084 484 HOH HOH A . N 6 HOH 485 1085 485 HOH HOH A . N 6 HOH 486 1086 486 HOH HOH A . N 6 HOH 487 1087 487 HOH HOH A . N 6 HOH 488 1088 488 HOH HOH A . N 6 HOH 489 1089 489 HOH HOH A . N 6 HOH 490 1090 490 HOH HOH A . N 6 HOH 491 1091 491 HOH HOH A . N 6 HOH 492 1092 492 HOH HOH A . N 6 HOH 493 1093 493 HOH HOH A . N 6 HOH 494 1094 494 HOH HOH A . N 6 HOH 495 1095 495 HOH HOH A . N 6 HOH 496 1096 496 HOH HOH A . N 6 HOH 497 1097 497 HOH HOH A . N 6 HOH 498 1098 498 HOH HOH A . N 6 HOH 499 1099 499 HOH HOH A . N 6 HOH 500 1100 500 HOH HOH A . N 6 HOH 501 1101 501 HOH HOH A . N 6 HOH 502 1102 502 HOH HOH A . N 6 HOH 503 1103 503 HOH HOH A . N 6 HOH 504 1104 504 HOH HOH A . N 6 HOH 505 1105 505 HOH HOH A . N 6 HOH 506 1106 506 HOH HOH A . N 6 HOH 507 1107 507 HOH HOH A . N 6 HOH 508 1108 508 HOH HOH A . N 6 HOH 509 1109 509 HOH HOH A . N 6 HOH 510 1110 510 HOH HOH A . N 6 HOH 511 1111 511 HOH HOH A . N 6 HOH 512 1112 512 HOH HOH A . N 6 HOH 513 1113 513 HOH HOH A . N 6 HOH 514 1114 514 HOH HOH A . N 6 HOH 515 1115 515 HOH HOH A . N 6 HOH 516 1116 516 HOH HOH A . N 6 HOH 517 1117 517 HOH HOH A . N 6 HOH 518 1118 518 HOH HOH A . N 6 HOH 519 1119 519 HOH HOH A . N 6 HOH 520 1120 520 HOH HOH A . N 6 HOH 521 1121 521 HOH HOH A . N 6 HOH 522 1122 522 HOH HOH A . N 6 HOH 523 1123 523 HOH HOH A . N 6 HOH 524 1124 524 HOH HOH A . N 6 HOH 525 1125 525 HOH HOH A . N 6 HOH 526 1126 526 HOH HOH A . N 6 HOH 527 1127 527 HOH HOH A . N 6 HOH 528 1128 528 HOH HOH A . N 6 HOH 529 1129 529 HOH HOH A . N 6 HOH 530 1130 530 HOH HOH A . N 6 HOH 531 1131 531 HOH HOH A . N 6 HOH 532 1132 532 HOH HOH A . N 6 HOH 533 1133 533 HOH HOH A . N 6 HOH 534 1134 534 HOH HOH A . N 6 HOH 535 1135 535 HOH HOH A . N 6 HOH 536 1136 536 HOH HOH A . N 6 HOH 537 1137 537 HOH HOH A . N 6 HOH 538 1138 538 HOH HOH A . N 6 HOH 539 1139 539 HOH HOH A . N 6 HOH 540 1140 540 HOH HOH A . N 6 HOH 541 1141 541 HOH HOH A . N 6 HOH 542 1142 542 HOH HOH A . N 6 HOH 543 1143 543 HOH HOH A . N 6 HOH 544 1144 544 HOH HOH A . N 6 HOH 545 1145 545 HOH HOH A . N 6 HOH 546 1146 546 HOH HOH A . N 6 HOH 547 1147 547 HOH HOH A . N 6 HOH 548 1148 548 HOH HOH A . N 6 HOH 549 1149 549 HOH HOH A . N 6 HOH 550 1150 550 HOH HOH A . N 6 HOH 551 1151 551 HOH HOH A . N 6 HOH 552 1152 552 HOH HOH A . N 6 HOH 553 1153 553 HOH HOH A . N 6 HOH 554 1154 554 HOH HOH A . N 6 HOH 555 1155 555 HOH HOH A . N 6 HOH 556 1156 556 HOH HOH A . N 6 HOH 557 1157 557 HOH HOH A . N 6 HOH 558 1158 558 HOH HOH A . N 6 HOH 559 1159 559 HOH HOH A . N 6 HOH 560 1160 560 HOH HOH A . N 6 HOH 561 1161 561 HOH HOH A . N 6 HOH 562 1162 562 HOH HOH A . N 6 HOH 563 1163 563 HOH HOH A . N 6 HOH 564 1164 564 HOH HOH A . N 6 HOH 565 1165 565 HOH HOH A . N 6 HOH 566 1166 566 HOH HOH A . N 6 HOH 567 1167 567 HOH HOH A . N 6 HOH 568 1168 568 HOH HOH A . N 6 HOH 569 1169 569 HOH HOH A . N 6 HOH 570 1170 570 HOH HOH A . N 6 HOH 571 1171 571 HOH HOH A . N 6 HOH 572 1172 572 HOH HOH A . N 6 HOH 573 1173 573 HOH HOH A . N 6 HOH 574 1174 574 HOH HOH A . N 6 HOH 575 1175 575 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 5 A ASN 87 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 65 A ASN 147 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 120 A ASN 202 ? 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 tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3,4 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 25950 ? 1 MORE 86 ? 1 'SSA (A^2)' 46870 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 15_555 y,-x,z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 4 'crystal symmetry operation' 16_555 -y,x,z 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 758 ? N HOH . 2 1 A HOH 828 ? N HOH . 3 1 A HOH 843 ? N HOH . 4 1 A HOH 1023 ? N HOH . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A GLY 217 ? A GLY 299 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 89.7 ? 2 O ? A GLY 217 ? A GLY 299 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 639 ? 1_555 87.8 ? 3 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 639 ? 1_555 88.7 ? 4 O ? A GLY 217 ? A GLY 299 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASP 213 ? A ASP 295 ? 1_555 81.7 ? 5 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASP 213 ? A ASP 295 ? 1_555 93.9 ? 6 O ? N HOH . ? A HOH 639 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASP 213 ? A ASP 295 ? 1_555 169.2 ? 7 O ? A GLY 217 ? A GLY 299 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASN 266 ? A ASN 348 ? 1_555 161.9 ? 8 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASN 266 ? A ASN 348 ? 1_555 108.3 ? 9 O ? N HOH . ? A HOH 639 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASN 266 ? A ASN 348 ? 1_555 90.7 ? 10 O ? A ASP 213 ? A ASP 295 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASN 266 ? A ASN 348 ? 1_555 98.4 ? 11 O ? A GLY 217 ? A GLY 299 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 621 ? 1_555 86.7 ? 12 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 621 ? 1_555 174.7 ? 13 O ? N HOH . ? A HOH 639 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 621 ? 1_555 87.2 ? 14 O ? A ASP 213 ? A ASP 295 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 621 ? 1_555 89.5 ? 15 O ? A ASN 266 ? A ASN 348 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? N HOH . ? A HOH 621 ? 1_555 75.1 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-11-20 2 'Structure model' 1 1 2013-12-18 3 'Structure model' 1 2 2015-10-21 4 'Structure model' 1 3 2017-11-15 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Database references' 3 3 'Structure model' 'Source and taxonomy' 4 4 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 4 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 20.0524 _pdbx_refine_tls.origin_y 19.9516 _pdbx_refine_tls.origin_z 54.7118 _pdbx_refine_tls.T[1][1] 0.0348 _pdbx_refine_tls.T[2][2] 0.0253 _pdbx_refine_tls.T[3][3] 0.0254 _pdbx_refine_tls.T[1][2] -0.0048 _pdbx_refine_tls.T[1][3] 0.0111 _pdbx_refine_tls.T[2][3] 0.0010 _pdbx_refine_tls.L[1][1] 0.2236 _pdbx_refine_tls.L[2][2] 0.3057 _pdbx_refine_tls.L[3][3] 0.0659 _pdbx_refine_tls.L[1][2] -0.0159 _pdbx_refine_tls.L[1][3] -0.0189 _pdbx_refine_tls.L[2][3] 0.0259 _pdbx_refine_tls.S[1][1] 0.0134 _pdbx_refine_tls.S[1][2] 0.0084 _pdbx_refine_tls.S[1][3] 0.0368 _pdbx_refine_tls.S[2][1] -0.0278 _pdbx_refine_tls.S[2][2] 0.0087 _pdbx_refine_tls.S[2][3] -0.0494 _pdbx_refine_tls.S[3][1] -0.0183 _pdbx_refine_tls.S[3][2] 0.0121 _pdbx_refine_tls.S[3][3] 0.0012 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id ? _pdbx_refine_tls_group.beg_auth_seq_id ? _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ALL # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal HKL-2000 'data collection' . ? 1 PHENIX refinement '(phenix.refine: 1.8_1069)' ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 786 ? ? O A HOH 1138 ? ? 1.90 2 1 O A HOH 786 ? ? O A HOH 803 ? ? 1.97 3 1 O A HOH 1137 ? ? O A HOH 1139 ? ? 2.05 4 1 O A HOH 1104 ? ? O A HOH 1108 ? ? 2.09 5 1 O A HOH 972 ? ? O A HOH 1047 ? ? 2.16 6 1 O A HOH 1142 ? ? O A HOH 1143 ? ? 2.18 7 1 O A HOH 1100 ? ? O A HOH 1129 ? ? 2.18 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CB _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 SER _pdbx_validate_rmsd_bond.auth_seq_id_1 447 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 B _pdbx_validate_rmsd_bond.auth_atom_id_2 OG _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 SER _pdbx_validate_rmsd_bond.auth_seq_id_2 447 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 B _pdbx_validate_rmsd_bond.bond_value 1.323 _pdbx_validate_rmsd_bond.bond_target_value 1.418 _pdbx_validate_rmsd_bond.bond_deviation -0.095 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.013 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 SER A 97 ? ? -171.11 -178.05 2 1 SER A 112 ? ? -146.92 52.39 3 1 SER A 112 ? ? -146.92 50.16 4 1 SER A 165 ? ? 70.06 -3.02 5 1 ASN A 202 ? ? -154.63 36.85 6 1 ASN A 223 ? ? -150.45 77.06 7 1 THR A 227 ? ? -136.46 -153.34 8 1 CYS A 293 ? ? -117.21 -164.94 9 1 GLN A 317 ? ? -161.16 -157.84 10 1 ASP A 357 ? ? -151.57 54.41 11 1 SER A 404 ? ? -114.10 -134.16 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'CALCIUM ION' CA 6 water HOH #