data_4MX0 # _entry.id 4MX0 # _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 4MX0 RCSB RCSB082471 WWPDB D_1000082471 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MWJ . unspecified PDB 4MWL . unspecified PDB 4MWQ . unspecified PDB 4MWR . unspecified PDB 4MWU . unspecified PDB 4MWV . unspecified PDB 4MWW . unspecified PDB 4MWX . unspecified PDB 4MXY . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MX0 _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 4MX0 _cell.length_a 181.809 _cell.length_b 181.809 _cell.length_c 181.809 _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 4MX0 _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 non-polymer syn '3-(1-ACETYLAMINO-2-ETHYL-BUTYL)-4-GUANIDINO-2-HYDROXY-CYCLOPENTANECARBOXYLIC ACID' 328.407 1 ? ? ? ? 7 water nat water 18.015 366 ? ? ? ? # _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 4MX0 _struct_ref.pdbx_db_accession 4MX0 _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 4MX0 _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 4MX0 _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 BCZ non-polymer . '3-(1-ACETYLAMINO-2-ETHYL-BUTYL)-4-GUANIDINO-2-HYDROXY-CYCLOPENTANECARBOXYLIC ACID' BCX-1812 'C15 H28 N4 O4' 328.407 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 4MX0 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.83 _exptl_crystal.density_percent_sol 56.54 _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 4MX0 _reflns.observed_criterion_sigma_I 3.0 _reflns.observed_criterion_sigma_F 2.0 _reflns.d_resolution_low 50 _reflns.d_resolution_high 2.1 _reflns.number_obs 29084 _reflns.number_all 29156 _reflns.percent_possible_obs 96.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 22.380 _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 # _refine.entry_id 4MX0 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_d_res_high 2.1010 _refine.ls_d_res_low 42.8530 _refine.pdbx_ls_sigma_F 1.330 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 96.6300 _refine.ls_number_reflns_obs 29084 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method ? _refine.ls_matrix_type ? _refine.pdbx_R_Free_selection_details ? _refine.details ? _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1686 _refine.ls_R_factor_R_work 0.1667 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.2058 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 5.0900 _refine.ls_number_reflns_R_free 1481 _refine.ls_number_reflns_R_work 27603 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 24.4370 _refine.solvent_model_param_bsol 19.0160 _refine.solvent_model_param_ksol 0.3080 _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] -0.0000 _refine.aniso_B[2][2] 0.0000 _refine.aniso_B[3][3] 0.0000 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] -0.0000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.1800 _refine.overall_SU_B ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.pdbx_solvent_vdw_probe_radii 1.2000 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.9800 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set 0.8707 _refine.B_iso_max 75.970 _refine.B_iso_min 9.890 _refine.pdbx_overall_phase_error 18.9500 _refine.occupancy_max 1.000 _refine.occupancy_min 0.270 _refine.pdbx_diffrn_id 1 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_TLS_residual_ADP_flag ? # _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 157 _refine_hist.number_atoms_solvent 366 _refine_hist.number_atoms_total 3576 _refine_hist.d_res_high 2.1010 _refine_hist.d_res_low 42.8530 # 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 3332 0.006 ? ? ? 'X-RAY DIFFRACTION' f_angle_d 4547 1.092 ? ? ? 'X-RAY DIFFRACTION' f_chiral_restr 510 0.071 ? ? ? 'X-RAY DIFFRACTION' f_plane_restr 570 0.005 ? ? ? 'X-RAY DIFFRACTION' f_dihedral_angle_d 1249 22.895 ? ? ? # 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 2.1007 2.1686 11 100.0000 2545 . 0.1833 0.2603 . 143 . 2688 . 'X-RAY DIFFRACTION' . 2.1686 2.2461 11 88.0000 2216 . 0.2876 0.3368 . 136 . 2352 . 'X-RAY DIFFRACTION' . 2.2461 2.3360 11 88.0000 2243 . 0.3199 0.4235 . 120 . 2363 . 'X-RAY DIFFRACTION' . 2.3360 2.4423 11 100.0000 2547 . 0.1855 0.2292 . 143 . 2690 . 'X-RAY DIFFRACTION' . 2.4423 2.5710 11 100.0000 2556 . 0.1645 0.2354 . 143 . 2699 . 'X-RAY DIFFRACTION' . 2.5710 2.7321 11 100.0000 2555 . 0.1643 0.2064 . 157 . 2712 . 'X-RAY DIFFRACTION' . 2.7321 2.9430 11 100.0000 2593 . 0.1558 0.2059 . 109 . 2702 . 'X-RAY DIFFRACTION' . 2.9430 3.2391 11 100.0000 2585 . 0.1532 0.1830 . 146 . 2731 . 'X-RAY DIFFRACTION' . 3.2391 3.7075 11 91.0000 2388 . 0.1589 0.1955 . 125 . 2513 . 'X-RAY DIFFRACTION' . 3.7075 4.6702 11 99.0000 2622 . 0.1251 0.1407 . 134 . 2756 . 'X-RAY DIFFRACTION' . 4.6702 42.8617 11 98.0000 2753 . 0.1453 0.1539 . 125 . 2878 . 'X-RAY DIFFRACTION' . # _struct.entry_id 4MX0 _struct.title 'Shanghai N9-peramivir' _struct.pdbx_descriptor Neuraminidase _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MX0 _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 ? O N N 7 ? # _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 ? ? ? ? ? ? ? 2.043 ? disulf2 disulf ? ? A CYS 43 SG ? ? ? 1_555 A CYS 48 SG ? ? A CYS 125 A CYS 130 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 95 SG ? ? ? 1_555 A CYS 113 SG ? ? A CYS 177 A CYS 195 1_555 ? ? ? ? ? ? ? 2.037 ? disulf4 disulf ? ? A CYS 103 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 185 A CYS 232 1_555 ? ? ? ? ? ? ? 2.040 ? disulf5 disulf ? ? A CYS 152 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 234 A CYS 239 1_555 ? ? ? ? ? ? ? 2.034 ? disulf6 disulf ? ? A CYS 198 SG ? ? ? 1_555 A CYS 211 SG ? ? A CYS 280 A CYS 293 1_555 ? ? ? ? ? ? ? 2.043 ? disulf7 disulf ? ? A CYS 200 SG ? ? ? 1_555 A CYS 209 SG ? ? A CYS 282 A CYS 291 1_555 ? ? ? ? ? ? ? 2.043 ? disulf8 disulf ? ? A CYS 238 SG ? ? ? 1_555 A CYS 256 SG ? ? A CYS 320 A CYS 338 1_555 ? ? ? ? ? ? ? 2.031 ? disulf9 disulf ? ? A CYS 341 SG ? ? ? 1_555 A CYS 367 SG ? ? A CYS 423 A CYS 449 1_555 ? ? ? ? ? ? ? 2.036 ? covale1 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 504 A BMA 505 1_555 ? ? ? ? ? ? ? 1.437 ? covale2 covale ? ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 505 A MAN 506 1_555 ? ? ? ? ? ? ? 1.439 ? covale3 covale ? ? H MAN . O2 ? ? ? 1_555 I MAN . C1 ? ? A MAN 507 A MAN 508 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? F BMA . O6 ? ? ? 1_555 J MAN . C1 ? ? A BMA 505 A MAN 509 1_555 ? ? ? ? ? ? ? 1.441 ? covale5 covale ? ? J MAN . O6 ? ? ? 1_555 K MAN . C1 ? ? A MAN 509 A MAN 510 1_555 ? ? ? ? ? ? ? 1.441 ? covale6 covale ? ? G MAN . O2 ? ? ? 1_555 H MAN . C1 ? ? A MAN 506 A MAN 507 1_555 ? ? ? ? ? ? ? 1.442 ? 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 ? ? ? ? ? ? ? 1.447 ? covale9 covale ? ? J MAN . O3 ? ? ? 1_555 L MAN . C1 ? ? A MAN 509 A MAN 511 1_555 ? ? ? ? ? ? ? 1.448 ? covale10 covale ? ? A ASN 120 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 202 A NAG 503 1_555 ? ? ? ? ? ? ? 1.449 ? covale11 covale ? ? A ASN 65 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 147 A NAG 502 1_555 ? ? ? ? ? ? ? 1.451 ? metalc1 metalc ? ? M CA . CA ? ? ? 1_555 O HOH . O ? ? A CA 512 A HOH 615 1_555 ? ? ? ? ? ? ? 2.520 ? metalc2 metalc ? ? A ASP 244 OD2 ? ? ? 1_555 M CA . CA ? ? A ASP 326 A CA 512 1_555 ? ? ? ? ? ? ? 2.568 ? metalc3 metalc ? ? M CA . CA ? ? ? 1_555 O HOH . O ? ? A CA 512 A HOH 708 1_555 ? ? ? ? ? ? ? 2.597 ? metalc4 metalc ? ? A ASP 213 O ? ? ? 1_555 M CA . CA ? ? A ASP 295 A CA 512 1_555 ? ? ? ? ? ? ? 2.757 ? metalc5 metalc ? ? A ASN 266 O ? ? ? 1_555 M CA . CA ? ? A ASN 348 A CA 512 1_555 ? ? ? ? ? ? ? 2.798 ? metalc6 metalc ? ? A GLY 217 O ? ? ? 1_555 M CA . CA ? ? A GLY 299 A CA 512 1_555 ? ? ? ? ? ? ? 2.844 ? # 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 -3.11 2 ARG 350 A . ? ARG 432 A PRO 351 A ? PRO 433 A 1 3.64 # 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 CYS A 341 ? GLY A 349 ? CYS A 423 GLY A 431 B 4 SER A 325 ? PHE A 328 ? SER A 407 PHE A 410 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 VAL A 156 ? GLY A 164 ? VAL A 238 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 SER A 199 ? N SER A 281 O THR A 210 ? O THR A 292 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 ARG A 283 ? N ARG A 365 O GLU A 294 ? O GLU A 376 G 3 4 N LYS A 297 ? N LYS A 379 O GLN A 311 ? O GLN A 393 # 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 ? ? ? ? 15 'BINDING SITE FOR RESIDUE BCZ A 513' AC3 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG A 501 BOUND TO ASN A 87' AC4 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 502 BOUND TO ASN A 147' AC5 Software ? ? ? ? 35 '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 O . ? HOH A 615 . ? 1_555 ? 6 AC1 6 HOH O . ? HOH A 708 . ? 1_555 ? 7 AC2 15 ARG A 37 ? ARG A 119 . ? 1_555 ? 8 AC2 15 GLU A 38 ? GLU A 120 . ? 1_555 ? 9 AC2 15 LEU A 53 ? LEU A 135 . ? 1_555 ? 10 AC2 15 ASP A 70 ? ASP A 152 . ? 1_555 ? 11 AC2 15 ARG A 71 ? ARG A 153 . ? 1_555 ? 12 AC2 15 ARG A 75 ? ARG A 157 . ? 1_555 ? 13 AC2 15 TRP A 98 ? TRP A 180 . ? 1_555 ? 14 AC2 15 ARG A 144 ? ARG A 226 . ? 1_555 ? 15 AC2 15 GLU A 147 ? GLU A 229 . ? 1_555 ? 16 AC2 15 GLU A 197 ? GLU A 279 . ? 1_555 ? 17 AC2 15 ARG A 290 ? ARG A 372 . ? 1_555 ? 18 AC2 15 TYR A 324 ? TYR A 406 . ? 1_555 ? 19 AC2 15 HOH O . ? HOH A 601 . ? 1_555 ? 20 AC2 15 HOH O . ? HOH A 766 . ? 1_555 ? 21 AC2 15 HOH O . ? HOH A 818 . ? 1_555 ? 22 AC3 6 ASN A 2 ? ASN A 84 . ? 1_555 ? 23 AC3 6 PHE A 3 ? PHE A 85 . ? 1_555 ? 24 AC3 6 ASN A 5 ? ASN A 87 . ? 1_555 ? 25 AC3 6 ASN A 154 ? ASN A 236 . ? 1_555 ? 26 AC3 6 HOH O . ? HOH A 823 . ? 1_555 ? 27 AC3 6 HOH O . ? HOH A 903 . ? 1_555 ? 28 AC4 2 ASN A 65 ? ASN A 147 . ? 1_555 ? 29 AC4 2 TRP A 357 ? TRP A 439 . ? 1_555 ? 30 AC5 35 ASN A 119 ? ASN A 201 . ? 1_555 ? 31 AC5 35 ASN A 120 ? ASN A 202 . ? 1_555 ? 32 AC5 35 ARG A 247 ? ARG A 329 . ? 21_555 ? 33 AC5 35 ASN A 249 ? ASN A 331 . ? 21_555 ? 34 AC5 35 ASP A 250 ? ASP A 332 . ? 21_555 ? 35 AC5 35 ARG A 283 ? ARG A 365 . ? 21_555 ? 36 AC5 35 ILE A 285 ? ILE A 367 . ? 21_555 ? 37 AC5 35 THR A 287 ? THR A 369 . ? 21_555 ? 38 AC5 35 GLU A 294 ? GLU A 376 . ? 21_555 ? 39 AC5 35 LEU A 296 ? LEU A 378 . ? 21_555 ? 40 AC5 35 PRO A 309 ? PRO A 391 . ? 21_555 ? 41 AC5 35 ILE A 310 ? ILE A 392 . ? 21_555 ? 42 AC5 35 GLN A 311 ? GLN A 393 . ? 21_555 ? 43 AC5 35 GLY A 312 ? GLY A 394 . ? 21_555 ? 44 AC5 35 LEU A 373 ? LEU A 455 . ? 21_555 ? 45 AC5 35 GLY A 374 ? GLY A 456 . ? 21_555 ? 46 AC5 35 GLN A 375 ? GLN A 457 . ? 21_555 ? 47 AC5 35 HOH O . ? HOH A 627 . ? 21_555 ? 48 AC5 35 HOH O . ? HOH A 648 . ? 21_555 ? 49 AC5 35 HOH O . ? HOH A 679 . ? 21_555 ? 50 AC5 35 HOH O . ? HOH A 686 . ? 1_555 ? 51 AC5 35 HOH O . ? HOH A 719 . ? 1_555 ? 52 AC5 35 HOH O . ? HOH A 770 . ? 1_555 ? 53 AC5 35 HOH O . ? HOH A 791 . ? 1_555 ? 54 AC5 35 HOH O . ? HOH A 850 . ? 1_555 ? 55 AC5 35 HOH O . ? HOH A 860 . ? 1_555 ? 56 AC5 35 HOH O . ? HOH A 881 . ? 1_555 ? 57 AC5 35 HOH O . ? HOH A 890 . ? 1_555 ? 58 AC5 35 HOH O . ? HOH A 900 . ? 1_555 ? 59 AC5 35 HOH O . ? HOH A 904 . ? 1_555 ? 60 AC5 35 HOH O . ? HOH A 910 . ? 21_555 ? 61 AC5 35 HOH O . ? HOH A 924 . ? 21_555 ? 62 AC5 35 HOH O . ? HOH A 931 . ? 1_555 ? 63 AC5 35 HOH O . ? HOH A 939 . ? 1_555 ? 64 AC5 35 HOH O . ? HOH A 949 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MX0 _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 4MX0 _atom_sites.fract_transf_matrix[1][1] 0.005500 _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] 0.005500 _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] 0.005500 _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 ? 10.200 -29.936 8.318 1.00 57.50 ? 83 ARG A N 1 ATOM 2 C CA . ARG A 1 1 ? 10.723 -30.925 9.260 1.00 51.49 ? 83 ARG A CA 1 ATOM 3 C C . ARG A 1 1 ? 12.051 -30.506 9.900 1.00 47.99 ? 83 ARG A C 1 ATOM 4 O O . ARG A 1 1 ? 12.959 -30.012 9.226 1.00 41.03 ? 83 ARG A O 1 ATOM 5 C CB . ARG A 1 1 ? 10.872 -32.293 8.589 1.00 49.16 ? 83 ARG A CB 1 ATOM 6 C CG . ARG A 1 1 ? 9.799 -33.303 8.987 1.00 57.16 ? 83 ARG A CG 1 ATOM 7 C CD . ARG A 1 1 ? 10.118 -34.686 8.426 1.00 62.41 ? 83 ARG A CD 1 ATOM 8 N NE . ARG A 1 1 ? 9.064 -35.665 8.696 1.00 61.06 ? 83 ARG A NE 1 ATOM 9 C CZ . ARG A 1 1 ? 9.103 -36.935 8.300 1.00 63.18 ? 83 ARG A CZ 1 ATOM 10 N NH1 . ARG A 1 1 ? 10.146 -37.388 7.614 1.00 62.47 ? 83 ARG A NH1 1 ATOM 11 N NH2 . ARG A 1 1 ? 8.099 -37.757 8.585 1.00 54.62 ? 83 ARG A NH2 1 ATOM 12 N N . ASN A 1 2 ? 12.149 -30.706 11.210 1.00 45.21 ? 84 ASN A N 1 ATOM 13 C CA . ASN A 1 2 ? 13.370 -30.404 11.944 1.00 41.09 ? 84 ASN A CA 1 ATOM 14 C C . ASN A 1 2 ? 13.991 -31.664 12.541 1.00 36.62 ? 84 ASN A C 1 ATOM 15 O O . ASN A 1 2 ? 13.283 -32.639 12.820 1.00 31.50 ? 84 ASN A O 1 ATOM 16 C CB . ASN A 1 2 ? 13.086 -29.407 13.071 1.00 44.30 ? 84 ASN A CB 1 ATOM 17 C CG . ASN A 1 2 ? 12.435 -28.129 12.577 1.00 54.27 ? 84 ASN A CG 1 ATOM 18 O OD1 . ASN A 1 2 ? 13.091 -27.271 11.984 1.00 53.18 ? 84 ASN A OD1 1 ATOM 19 N ND2 . ASN A 1 2 ? 11.138 -27.988 12.837 1.00 46.20 ? 84 ASN A ND2 1 ATOM 20 N N . PHE A 1 3 ? 15.309 -31.642 12.732 1.00 27.43 ? 85 PHE A N 1 ATOM 21 C CA . PHE A 1 3 ? 15.995 -32.699 13.465 1.00 23.97 ? 85 PHE A CA 1 ATOM 22 C C . PHE A 1 3 ? 15.393 -32.775 14.866 1.00 26.34 ? 85 PHE A C 1 ATOM 23 O O . PHE A 1 3 ? 15.112 -31.745 15.475 1.00 27.83 ? 85 PHE A O 1 ATOM 24 C CB . PHE A 1 3 ? 17.487 -32.386 13.592 1.00 22.91 ? 85 PHE A CB 1 ATOM 25 C CG . PHE A 1 3 ? 18.270 -32.566 12.315 1.00 30.14 ? 85 PHE A CG 1 ATOM 26 C CD1 . PHE A 1 3 ? 18.147 -33.731 11.564 1.00 25.01 ? 85 PHE A CD1 1 ATOM 27 C CD2 . PHE A 1 3 ? 19.138 -31.569 11.870 1.00 28.23 ? 85 PHE A CD2 1 ATOM 28 C CE1 . PHE A 1 3 ? 18.870 -33.898 10.391 1.00 23.96 ? 85 PHE A CE1 1 ATOM 29 C CE2 . PHE A 1 3 ? 19.865 -31.730 10.692 1.00 31.39 ? 85 PHE A CE2 1 ATOM 30 C CZ . PHE A 1 3 ? 19.730 -32.896 9.954 1.00 24.18 ? 85 PHE A CZ 1 ATOM 31 N N . ASN A 1 4 ? 15.192 -33.982 15.383 1.00 25.96 ? 86 ASN A N 1 ATOM 32 C CA . ASN A 1 4 ? 14.711 -34.123 16.755 1.00 24.99 ? 86 ASN A CA 1 ATOM 33 C C . ASN A 1 4 ? 15.801 -33.855 17.793 1.00 25.14 ? 86 ASN A C 1 ATOM 34 O O . ASN A 1 4 ? 16.946 -34.292 17.629 1.00 21.04 ? 86 ASN A O 1 ATOM 35 C CB . ASN A 1 4 ? 14.121 -35.510 16.987 1.00 22.19 ? 86 ASN A CB 1 ATOM 36 C CG . ASN A 1 4 ? 13.659 -35.704 18.418 1.00 26.82 ? 86 ASN A CG 1 ATOM 37 O OD1 . ASN A 1 4 ? 14.195 -36.540 19.152 1.00 30.00 ? 86 ASN A OD1 1 ATOM 38 N ND2 . ASN A 1 4 ? 12.672 -34.912 18.832 1.00 20.05 ? 86 ASN A ND2 1 ATOM 39 N N . ASN A 1 5 ? 15.444 -33.136 18.857 1.00 21.11 ? 87 ASN A N 1 ATOM 40 C CA . ASN A 1 5 ? 16.359 -32.911 19.975 1.00 20.24 ? 87 ASN A CA 1 ATOM 41 C C . ASN A 1 5 ? 15.901 -33.661 21.227 1.00 20.82 ? 87 ASN A C 1 ATOM 42 O O . ASN A 1 5 ? 14.704 -33.722 21.525 1.00 24.79 ? 87 ASN A O 1 ATOM 43 C CB . ASN A 1 5 ? 16.484 -31.411 20.285 1.00 28.86 ? 87 ASN A CB 1 ATOM 44 C CG . ASN A 1 5 ? 16.987 -30.596 19.096 1.00 33.51 ? 87 ASN A CG 1 ATOM 45 O OD1 . ASN A 1 5 ? 17.896 -31.017 18.371 1.00 31.61 ? 87 ASN A OD1 1 ATOM 46 N ND2 . ASN A 1 5 ? 16.388 -29.415 18.896 1.00 36.67 ? 87 ASN A ND2 1 ATOM 47 N N . LEU A 1 6 ? 16.852 -34.234 21.958 1.00 22.72 ? 88 LEU A N 1 ATOM 48 C CA . LEU A 1 6 ? 16.545 -34.933 23.207 1.00 24.47 ? 88 LEU A CA 1 ATOM 49 C C . LEU A 1 6 ? 16.318 -33.937 24.342 1.00 24.62 ? 88 LEU A C 1 ATOM 50 O O . LEU A 1 6 ? 17.244 -33.617 25.092 1.00 26.86 ? 88 LEU A O 1 ATOM 51 C CB . LEU A 1 6 ? 17.685 -35.886 23.578 1.00 20.31 ? 88 LEU A CB 1 ATOM 52 C CG . LEU A 1 6 ? 18.076 -36.853 22.465 1.00 27.24 ? 88 LEU A CG 1 ATOM 53 C CD1 . LEU A 1 6 ? 19.306 -37.668 22.860 1.00 15.16 ? 88 LEU A CD1 1 ATOM 54 C CD2 . LEU A 1 6 ? 16.883 -37.757 22.125 1.00 21.41 ? 88 LEU A CD2 1 ATOM 55 N N . THR A 1 7 ? 15.083 -33.463 24.477 1.00 25.58 ? 89 THR A N 1 ATOM 56 C CA . THR A 1 7 ? 14.779 -32.387 25.419 1.00 30.71 ? 89 THR A CA 1 ATOM 57 C C . THR A 1 7 ? 13.991 -32.823 26.648 1.00 32.31 ? 89 THR A C 1 ATOM 58 O O . THR A 1 7 ? 13.742 -32.007 27.535 1.00 28.34 ? 89 THR A O 1 ATOM 59 C CB . THR A 1 7 ? 13.971 -31.278 24.744 1.00 30.52 ? 89 THR A CB 1 ATOM 60 O OG1 . THR A 1 7 ? 12.749 -31.830 24.233 1.00 31.49 ? 89 THR A OG1 1 ATOM 61 C CG2 . THR A 1 7 ? 14.765 -30.658 23.608 1.00 26.47 ? 89 THR A CG2 1 ATOM 62 N N . LYS A 1 8 ? 13.590 -34.092 26.700 1.00 20.77 ? 90 LYS A N 1 ATOM 63 C CA . LYS A 1 8 ? 12.740 -34.567 27.788 1.00 21.30 ? 90 LYS A CA 1 ATOM 64 C C . LYS A 1 8 ? 13.465 -35.570 28.682 1.00 24.07 ? 90 LYS A C 1 ATOM 65 O O . LYS A 1 8 ? 14.452 -36.188 28.265 1.00 26.99 ? 90 LYS A O 1 ATOM 66 C CB . LYS A 1 8 ? 11.457 -35.194 27.224 1.00 26.31 ? 90 LYS A CB 1 ATOM 67 C CG . LYS A 1 8 ? 10.652 -34.267 26.311 1.00 22.01 ? 90 LYS A CG 1 ATOM 68 C CD . LYS A 1 8 ? 9.511 -35.017 25.604 1.00 29.20 ? 90 LYS A CD 1 ATOM 69 C CE . LYS A 1 8 ? 8.674 -34.060 24.762 1.00 32.65 ? 90 LYS A CE 1 ATOM 70 N NZ . LYS A 1 8 ? 7.656 -34.756 23.927 1.00 28.53 ? 90 LYS A NZ 1 ATOM 71 N N . GLY A 1 9 ? 12.983 -35.717 29.913 1.00 23.70 ? 91 GLY A N 1 ATOM 72 C CA . GLY A 1 9 ? 13.440 -36.786 30.787 1.00 26.32 ? 91 GLY A CA 1 ATOM 73 C C . GLY A 1 9 ? 12.542 -37.994 30.582 1.00 25.54 ? 91 GLY A C 1 ATOM 74 O O . GLY A 1 9 ? 11.522 -37.897 29.893 1.00 25.85 ? 91 GLY A O 1 ATOM 75 N N . LEU A 1 10 ? 12.913 -39.131 31.161 1.00 19.90 ? 92 LEU A N 1 ATOM 76 C CA . LEU A 1 10 ? 12.071 -40.323 31.081 1.00 24.08 ? 92 LEU A CA 1 ATOM 77 C C . LEU A 1 10 ? 10.799 -40.143 31.904 1.00 26.05 ? 92 LEU A C 1 ATOM 78 O O . LEU A 1 10 ? 10.810 -39.471 32.940 1.00 24.15 ? 92 LEU A O 1 ATOM 79 C CB . LEU A 1 10 ? 12.825 -41.552 31.587 1.00 22.68 ? 92 LEU A CB 1 ATOM 80 C CG . LEU A 1 10 ? 14.132 -41.921 30.893 1.00 22.51 ? 92 LEU A CG 1 ATOM 81 C CD1 . LEU A 1 10 ? 14.777 -43.085 31.615 1.00 24.47 ? 92 LEU A CD1 1 ATOM 82 C CD2 . LEU A 1 10 ? 13.875 -42.272 29.434 1.00 21.27 ? 92 LEU A CD2 1 ATOM 83 N N . CYS A 1 11 ? 9.697 -40.729 31.445 1.00 19.06 ? 93 CYS A N 1 ATOM 84 C CA . CYS A 1 11 ? 8.499 -40.777 32.274 1.00 18.56 ? 93 CYS A CA 1 ATOM 85 C C . CYS A 1 11 ? 8.792 -41.668 33.476 1.00 23.40 ? 93 CYS A C 1 ATOM 86 O O . CYS A 1 11 ? 9.649 -42.563 33.407 1.00 17.70 ? 93 CYS A O 1 ATOM 87 C CB . CYS A 1 11 ? 7.307 -41.338 31.489 1.00 27.97 ? 93 CYS A CB 1 ATOM 88 S SG . CYS A 1 11 ? 6.841 -40.372 30.022 1.00 26.59 ? 93 CYS A SG 1 ATOM 89 N N . THR A 1 12 ? 8.093 -41.417 34.579 1.00 24.32 ? 94 THR A N 1 ATOM 90 C CA . THR A 1 12 ? 8.199 -42.270 35.754 1.00 21.99 ? 94 THR A CA 1 ATOM 91 C C . THR A 1 12 ? 7.678 -43.651 35.393 1.00 22.82 ? 94 THR A C 1 ATOM 92 O O . THR A 1 12 ? 6.578 -43.789 34.849 1.00 20.21 ? 94 THR A O 1 ATOM 93 C CB . THR A 1 12 ? 7.408 -41.692 36.939 1.00 26.32 ? 94 THR A CB 1 ATOM 94 O OG1 . THR A 1 12 ? 7.992 -40.440 37.315 1.00 26.67 ? 94 THR A OG1 1 ATOM 95 C CG2 . THR A 1 12 ? 7.441 -42.643 38.139 1.00 22.27 ? 94 THR A CG2 1 ATOM 96 N N . ILE A 1 13 ? 8.487 -44.668 35.670 1.00 24.63 ? 95 ILE A N 1 ATOM 97 C CA . ILE A 1 13 ? 8.136 -46.045 35.351 1.00 18.93 ? 95 ILE A CA 1 ATOM 98 C C . ILE A 1 13 ? 7.568 -46.756 36.578 1.00 17.61 ? 95 ILE A C 1 ATOM 99 O O . ILE A 1 13 ? 8.323 -47.166 37.467 1.00 21.72 ? 95 ILE A O 1 ATOM 100 C CB . ILE A 1 13 ? 9.374 -46.819 34.843 1.00 20.98 ? 95 ILE A CB 1 ATOM 101 C CG1 . ILE A 1 13 ? 10.005 -46.103 33.642 1.00 17.65 ? 95 ILE A CG1 1 ATOM 102 C CG2 . ILE A 1 13 ? 9.004 -48.247 34.479 1.00 21.71 ? 95 ILE A CG2 1 ATOM 103 C CD1 . ILE A 1 13 ? 11.500 -46.437 33.446 1.00 18.52 ? 95 ILE A CD1 1 ATOM 104 N N . ASN A 1 14 ? 6.245 -46.915 36.630 1.00 20.59 ? 96 ASN A N 1 ATOM 105 C CA . ASN A 1 14 ? 5.623 -47.633 37.743 1.00 24.53 ? 96 ASN A CA 1 ATOM 106 C C . ASN A 1 14 ? 5.197 -49.052 37.367 1.00 25.61 ? 96 ASN A C 1 ATOM 107 O O . ASN A 1 14 ? 4.974 -49.891 38.245 1.00 23.30 ? 96 ASN A O 1 ATOM 108 C CB . ASN A 1 14 ? 4.442 -46.847 38.330 1.00 21.18 ? 96 ASN A CB 1 ATOM 109 C CG . ASN A 1 14 ? 4.883 -45.588 39.064 1.00 24.58 ? 96 ASN A CG 1 ATOM 110 O OD1 . ASN A 1 14 ? 5.933 -45.569 39.710 1.00 23.83 ? 96 ASN A OD1 1 ATOM 111 N ND2 . ASN A 1 14 ? 4.082 -44.527 38.960 1.00 20.87 ? 96 ASN A ND2 1 ATOM 112 N N . SER A 1 15 ? 5.086 -49.308 36.064 1.00 27.19 ? 97 SER A N 1 ATOM 113 C CA . SER A 1 15 ? 4.821 -50.652 35.541 1.00 23.69 ? 97 SER A CA 1 ATOM 114 C C . SER A 1 15 ? 5.046 -50.684 34.031 1.00 21.79 ? 97 SER A C 1 ATOM 115 O O . SER A 1 15 ? 5.448 -49.681 33.437 1.00 20.25 ? 97 SER A O 1 ATOM 116 C CB . SER A 1 15 ? 3.398 -51.124 35.879 1.00 19.71 ? 97 SER A CB 1 ATOM 117 O OG . SER A 1 15 ? 2.414 -50.217 35.403 1.00 23.08 ? 97 SER A OG 1 ATOM 118 N N . TRP A 1 16 ? 4.804 -51.834 33.408 1.00 18.14 ? 98 TRP A N 1 ATOM 119 C CA . TRP A 1 16 ? 4.948 -51.931 31.956 1.00 17.15 ? 98 TRP A CA 1 ATOM 120 C C . TRP A 1 16 ? 3.656 -52.434 31.314 1.00 23.79 ? 98 TRP A C 1 ATOM 121 O O . TRP A 1 16 ? 3.043 -53.396 31.799 1.00 20.74 ? 98 TRP A O 1 ATOM 122 C CB . TRP A 1 16 ? 6.149 -52.824 31.587 1.00 17.75 ? 98 TRP A CB 1 ATOM 123 C CG . TRP A 1 16 ? 7.462 -52.339 32.192 1.00 23.91 ? 98 TRP A CG 1 ATOM 124 C CD1 . TRP A 1 16 ? 7.977 -52.669 33.422 1.00 20.30 ? 98 TRP A CD1 1 ATOM 125 C CD2 . TRP A 1 16 ? 8.408 -51.434 31.594 1.00 18.19 ? 98 TRP A CD2 1 ATOM 126 N NE1 . TRP A 1 16 ? 9.181 -52.029 33.619 1.00 20.66 ? 98 TRP A NE1 1 ATOM 127 C CE2 . TRP A 1 16 ? 9.467 -51.264 32.515 1.00 22.54 ? 98 TRP A CE2 1 ATOM 128 C CE3 . TRP A 1 16 ? 8.462 -50.754 30.371 1.00 20.41 ? 98 TRP A CE3 1 ATOM 129 C CZ2 . TRP A 1 16 ? 10.569 -50.438 32.248 1.00 18.33 ? 98 TRP A CZ2 1 ATOM 130 C CZ3 . TRP A 1 16 ? 9.557 -49.925 30.111 1.00 20.50 ? 98 TRP A CZ3 1 ATOM 131 C CH2 . TRP A 1 16 ? 10.593 -49.777 31.045 1.00 14.82 ? 98 TRP A CH2 1 ATOM 132 N N . HIS A 1 17 ? 3.234 -51.775 30.235 1.00 16.33 ? 99 HIS A N 1 ATOM 133 C CA . HIS A 1 17 ? 2.042 -52.210 29.508 1.00 17.87 ? 99 HIS A CA 1 ATOM 134 C C . HIS A 1 17 ? 2.414 -52.834 28.160 1.00 16.52 ? 99 HIS A C 1 ATOM 135 O O . HIS A 1 17 ? 3.470 -52.527 27.594 1.00 16.92 ? 99 HIS A O 1 ATOM 136 C CB . HIS A 1 17 ? 1.058 -51.048 29.314 1.00 15.62 ? 99 HIS A CB 1 ATOM 137 C CG . HIS A 1 17 ? 1.499 -50.026 28.305 1.00 19.83 ? 99 HIS A CG 1 ATOM 138 N ND1 . HIS A 1 17 ? 1.314 -50.195 26.952 1.00 20.96 ? 99 HIS A ND1 1 ATOM 139 C CD2 . HIS A 1 17 ? 2.090 -48.815 28.459 1.00 22.49 ? 99 HIS A CD2 1 ATOM 140 C CE1 . HIS A 1 17 ? 1.785 -49.136 26.308 1.00 20.97 ? 99 HIS A CE1 1 ATOM 141 N NE2 . HIS A 1 17 ? 2.261 -48.288 27.199 1.00 25.46 ? 99 HIS A NE2 1 ATOM 142 N N . ILE A 1 18 ? 1.561 -53.726 27.660 1.00 18.11 ? 100 ILE A N 1 ATOM 143 C CA . ILE A 1 18 ? 1.801 -54.328 26.353 1.00 20.95 ? 100 ILE A CA 1 ATOM 144 C C . ILE A 1 18 ? 1.777 -53.245 25.270 1.00 20.10 ? 100 ILE A C 1 ATOM 145 O O . ILE A 1 18 ? 0.922 -52.348 25.295 1.00 19.16 ? 100 ILE A O 1 ATOM 146 C CB . ILE A 1 18 ? 0.783 -55.451 26.039 1.00 19.87 ? 100 ILE A CB 1 ATOM 147 C CG1 . ILE A 1 18 ? 1.145 -56.150 24.727 1.00 16.64 ? 100 ILE A CG1 1 ATOM 148 C CG2 . ILE A 1 18 ? -0.642 -54.925 26.020 1.00 15.63 ? 100 ILE A CG2 1 ATOM 149 C CD1 . ILE A 1 18 ? 2.503 -56.859 24.771 1.00 14.60 ? 100 ILE A CD1 1 ATOM 150 N N . TYR A 1 19 ? 2.736 -53.307 24.347 1.00 18.42 ? 101 TYR A N 1 ATOM 151 C CA . TYR A 1 19 ? 2.833 -52.322 23.266 1.00 14.37 ? 101 TYR A CA 1 ATOM 152 C C . TYR A 1 19 ? 2.672 -52.980 21.902 1.00 18.70 ? 101 TYR A C 1 ATOM 153 O O . TYR A 1 19 ? 1.906 -52.505 21.053 1.00 17.33 ? 101 TYR A O 1 ATOM 154 C CB . TYR A 1 19 ? 4.178 -51.596 23.346 1.00 13.96 ? 101 TYR A CB 1 ATOM 155 C CG . TYR A 1 19 ? 4.455 -50.622 22.223 1.00 13.95 ? 101 TYR A CG 1 ATOM 156 C CD1 . TYR A 1 19 ? 3.819 -49.386 22.170 1.00 22.94 ? 101 TYR A CD1 1 ATOM 157 C CD2 . TYR A 1 19 ? 5.388 -50.919 21.239 1.00 18.90 ? 101 TYR A CD2 1 ATOM 158 C CE1 . TYR A 1 19 ? 4.086 -48.482 21.152 1.00 21.43 ? 101 TYR A CE1 1 ATOM 159 C CE2 . TYR A 1 19 ? 5.664 -50.022 20.216 1.00 16.50 ? 101 TYR A CE2 1 ATOM 160 C CZ . TYR A 1 19 ? 5.011 -48.810 20.178 1.00 18.44 ? 101 TYR A CZ 1 ATOM 161 O OH . TYR A 1 19 ? 5.282 -47.924 19.165 1.00 20.65 ? 101 TYR A OH 1 ATOM 162 N N . GLY A 1 20 ? 3.398 -54.078 21.692 1.00 16.22 ? 102 GLY A N 1 ATOM 163 C CA . GLY A 1 20 ? 3.332 -54.787 20.428 1.00 16.33 ? 102 GLY A CA 1 ATOM 164 C C . GLY A 1 20 ? 3.735 -56.240 20.548 1.00 22.32 ? 102 GLY A C 1 ATOM 165 O O . GLY A 1 20 ? 4.564 -56.604 21.387 1.00 20.94 ? 102 GLY A O 1 ATOM 166 N N . LYS A 1 21 ? 3.145 -57.074 19.698 1.00 21.36 ? 103 LYS A N 1 ATOM 167 C CA . LYS A 1 21 ? 3.455 -58.496 19.660 1.00 17.14 ? 103 LYS A CA 1 ATOM 168 C C . LYS A 1 21 ? 3.022 -58.985 18.287 1.00 20.78 ? 103 LYS A C 1 ATOM 169 O O . LYS A 1 21 ? 1.902 -58.703 17.863 1.00 21.16 ? 103 LYS A O 1 ATOM 170 C CB . LYS A 1 21 ? 2.681 -59.232 20.755 1.00 14.82 ? 103 LYS A CB 1 ATOM 171 C CG . LYS A 1 21 ? 3.076 -60.693 20.923 1.00 15.68 ? 103 LYS A CG 1 ATOM 172 C CD . LYS A 1 21 ? 2.142 -61.411 21.889 1.00 20.28 ? 103 LYS A CD 1 ATOM 173 C CE . LYS A 1 21 ? 2.747 -62.724 22.376 1.00 22.34 ? 103 LYS A CE 1 ATOM 174 N NZ . LYS A 1 21 ? 3.153 -63.638 21.266 1.00 17.39 ? 103 LYS A NZ 1 ATOM 175 N N . ASP A 1 22 ? 3.889 -59.698 17.573 1.00 18.60 ? 104 ASP A N 1 ATOM 176 C CA . ASP A 1 22 ? 3.516 -60.092 16.212 1.00 16.33 ? 104 ASP A CA 1 ATOM 177 C C . ASP A 1 22 ? 3.056 -61.536 16.041 1.00 16.49 ? 104 ASP A C 1 ATOM 178 O O . ASP A 1 22 ? 2.441 -61.858 15.022 1.00 15.73 ? 104 ASP A O 1 ATOM 179 C CB . ASP A 1 22 ? 4.603 -59.745 15.186 1.00 18.88 ? 104 ASP A CB 1 ATOM 180 C CG . ASP A 1 22 ? 5.939 -60.388 15.491 1.00 17.59 ? 104 ASP A CG 1 ATOM 181 O OD1 . ASP A 1 22 ? 6.038 -61.198 16.444 1.00 18.57 ? 104 ASP A OD1 1 ATOM 182 O OD2 . ASP A 1 22 ? 6.902 -60.088 14.751 1.00 19.02 ? 104 ASP A OD2 1 ATOM 183 N N . ASN A 1 23 ? 3.338 -62.393 17.023 1.00 13.79 ? 105 ASN A N 1 ATOM 184 C CA . ASN A 1 23 ? 2.957 -63.803 16.928 1.00 18.93 ? 105 ASN A CA 1 ATOM 185 C C . ASN A 1 23 ? 3.475 -64.456 15.638 1.00 17.12 ? 105 ASN A C 1 ATOM 186 O O . ASN A 1 23 ? 2.799 -65.295 15.045 1.00 16.60 ? 105 ASN A O 1 ATOM 187 C CB . ASN A 1 23 ? 1.428 -63.944 17.013 1.00 14.46 ? 105 ASN A CB 1 ATOM 188 C CG . ASN A 1 23 ? 0.864 -63.417 18.325 1.00 20.99 ? 105 ASN A CG 1 ATOM 189 O OD1 . ASN A 1 23 ? 1.070 -64.016 19.379 1.00 17.94 ? 105 ASN A OD1 1 ATOM 190 N ND2 . ASN A 1 23 ? 0.141 -62.296 18.264 1.00 16.94 ? 105 ASN A ND2 1 ATOM 191 N N . ALA A 1 24 ? 4.673 -64.062 15.207 1.00 18.00 ? 106 ALA A N 1 ATOM 192 C CA . ALA A 1 24 ? 5.180 -64.425 13.878 1.00 18.54 ? 106 ALA A CA 1 ATOM 193 C C . ALA A 1 24 ? 5.304 -65.930 13.631 1.00 20.45 ? 106 ALA A C 1 ATOM 194 O O . ALA A 1 24 ? 5.030 -66.406 12.525 1.00 18.19 ? 106 ALA A O 1 ATOM 195 C CB . ALA A 1 24 ? 6.518 -63.735 13.609 1.00 18.14 ? 106 ALA A CB 1 ATOM 196 N N . VAL A 1 25 ? 5.730 -66.676 14.646 1.00 15.61 ? 107 VAL A N 1 ATOM 197 C CA . VAL A 1 25 ? 5.965 -68.109 14.467 1.00 21.38 ? 107 VAL A CA 1 ATOM 198 C C . VAL A 1 25 ? 4.641 -68.870 14.381 1.00 19.65 ? 107 VAL A C 1 ATOM 199 O O . VAL A 1 25 ? 4.512 -69.800 13.572 1.00 22.39 ? 107 VAL A O 1 ATOM 200 C CB . VAL A 1 25 ? 6.878 -68.681 15.572 1.00 20.32 ? 107 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 25 ? 7.254 -70.138 15.272 1.00 17.59 ? 107 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 25 ? 8.137 -67.831 15.691 1.00 16.96 ? 107 VAL A CG2 1 ATOM 203 N N . ARG A 1 26 ? 3.661 -68.470 15.199 1.00 19.71 ? 108 ARG A N 1 ATOM 204 C CA . ARG A 1 26 ? 2.311 -69.047 15.133 1.00 18.97 ? 108 ARG A CA 1 ATOM 205 C C . ARG A 1 26 ? 1.738 -68.852 13.732 1.00 21.76 ? 108 ARG A C 1 ATOM 206 O O . ARG A 1 26 ? 1.241 -69.789 13.103 1.00 21.22 ? 108 ARG A O 1 ATOM 207 C CB . ARG A 1 26 ? 1.367 -68.368 16.141 1.00 18.15 ? 108 ARG A CB 1 ATOM 208 C CG . ARG A 1 26 ? 1.598 -68.709 17.615 1.00 19.39 ? 108 ARG A CG 1 ATOM 209 C CD . ARG A 1 26 ? 0.723 -67.834 18.530 1.00 17.89 ? 108 ARG A CD 1 ATOM 210 N NE . ARG A 1 26 ? -0.695 -67.894 18.166 1.00 15.10 ? 108 ARG A NE 1 ATOM 211 C CZ . ARG A 1 26 ? -1.533 -68.832 18.594 1.00 19.58 ? 108 ARG A CZ 1 ATOM 212 N NH1 . ARG A 1 26 ? -1.100 -69.789 19.413 1.00 19.97 ? 108 ARG A NH1 1 ATOM 213 N NH2 . ARG A 1 26 ? -2.803 -68.817 18.210 1.00 20.30 ? 108 ARG A NH2 1 ATOM 214 N N . ILE A 1 27 ? 1.812 -67.618 13.248 1.00 17.60 ? 109 ILE A N 1 ATOM 215 C CA . ILE A 1 27 ? 1.229 -67.269 11.958 1.00 18.65 ? 109 ILE A CA 1 ATOM 216 C C . ILE A 1 27 ? 2.024 -67.894 10.808 1.00 23.75 ? 109 ILE A C 1 ATOM 217 O O . ILE A 1 27 ? 1.446 -68.352 9.811 1.00 21.36 ? 109 ILE A O 1 ATOM 218 C CB . ILE A 1 27 ? 1.123 -65.736 11.820 1.00 19.37 ? 109 ILE A CB 1 ATOM 219 C CG1 . ILE A 1 27 ? 0.154 -65.198 12.881 1.00 19.83 ? 109 ILE A CG1 1 ATOM 220 C CG2 . ILE A 1 27 ? 0.679 -65.333 10.416 1.00 19.94 ? 109 ILE A CG2 1 ATOM 221 C CD1 . ILE A 1 27 ? 0.140 -63.684 13.027 1.00 14.55 ? 109 ILE A CD1 1 ATOM 222 N N . GLY A 1 28 ? 3.345 -67.939 10.968 1.00 17.02 ? 110 GLY A N 1 ATOM 223 C CA . GLY A 1 28 ? 4.225 -68.492 9.955 1.00 18.06 ? 110 GLY A CA 1 ATOM 224 C C . GLY A 1 28 ? 4.165 -70.002 9.797 1.00 23.51 ? 110 GLY A C 1 ATOM 225 O O . GLY A 1 28 ? 4.778 -70.546 8.871 1.00 18.79 ? 110 GLY A O 1 ATOM 226 N N . GLU A 1 29 ? 3.434 -70.689 10.679 1.00 16.96 ? 111 GLU A N 1 ATOM 227 C CA . GLU A 1 29 ? 3.173 -72.121 10.486 1.00 18.88 ? 111 GLU A CA 1 ATOM 228 C C . GLU A 1 29 ? 2.375 -72.333 9.197 1.00 20.46 ? 111 GLU A C 1 ATOM 229 O O . GLU A 1 29 ? 2.440 -73.402 8.558 1.00 17.79 ? 111 GLU A O 1 ATOM 230 C CB . GLU A 1 29 ? 2.415 -72.706 11.684 1.00 19.33 ? 111 GLU A CB 1 ATOM 231 C CG . GLU A 1 29 ? 2.242 -74.234 11.656 1.00 19.66 ? 111 GLU A CG 1 ATOM 232 C CD . GLU A 1 29 ? 1.031 -74.688 10.855 1.00 20.63 ? 111 GLU A CD 1 ATOM 233 O OE1 . GLU A 1 29 ? 0.035 -73.934 10.814 1.00 22.76 ? 111 GLU A OE1 1 ATOM 234 O OE2 . GLU A 1 29 ? 1.076 -75.794 10.268 1.00 18.61 ? 111 GLU A OE2 1 ATOM 235 N N . SER A 1 30 ? 1.638 -71.297 8.806 1.00 17.02 ? 112 SER A N 1 ATOM 236 C CA . SER A 1 30 ? 0.764 -71.383 7.643 1.00 22.45 ? 112 SER A CA 1 ATOM 237 C C . SER A 1 30 ? 0.593 -70.009 7.007 1.00 23.70 ? 112 SER A C 1 ATOM 238 O O . SER A 1 30 ? -0.521 -69.488 6.911 1.00 28.46 ? 112 SER A O 1 ATOM 239 C CB . SER A 1 30 ? -0.591 -71.954 8.051 1.00 23.80 ? 112 SER A CB 1 ATOM 240 O OG . SER A 1 30 ? -1.384 -72.249 6.915 1.00 37.04 ? 112 SER A OG 1 ATOM 241 N N A SER A 1 31 ? 1.716 -69.434 6.587 0.27 23.72 ? 113 SER A N 1 ATOM 242 N N B SER A 1 31 ? 1.716 -69.427 6.592 0.73 23.78 ? 113 SER A N 1 ATOM 243 C CA A SER A 1 31 ? 1.755 -68.155 5.890 0.27 22.11 ? 113 SER A CA 1 ATOM 244 C CA B SER A 1 31 ? 1.760 -68.132 5.917 0.73 22.11 ? 113 SER A CA 1 ATOM 245 C C A SER A 1 31 ? 3.180 -67.912 5.423 0.27 20.92 ? 113 SER A C 1 ATOM 246 C C B SER A 1 31 ? 3.185 -67.884 5.452 0.73 20.92 ? 113 SER A C 1 ATOM 247 O O A SER A 1 31 ? 4.116 -68.545 5.917 0.27 19.82 ? 113 SER A O 1 ATOM 248 O O B SER A 1 31 ? 4.126 -68.482 5.982 0.73 19.77 ? 113 SER A O 1 ATOM 249 C CB A SER A 1 31 ? 1.307 -67.013 6.801 0.27 20.49 ? 113 SER A CB 1 ATOM 250 C CB B SER A 1 31 ? 1.334 -67.000 6.850 0.73 20.43 ? 113 SER A CB 1 ATOM 251 O OG A SER A 1 31 ? -0.082 -67.088 7.057 0.27 25.68 ? 113 SER A OG 1 ATOM 252 O OG B SER A 1 31 ? -0.077 -66.921 6.932 0.73 26.12 ? 113 SER A OG 1 ATOM 253 N N . ASP A 1 32 ? 3.347 -66.998 4.477 1.00 14.21 ? 114 ASP A N 1 ATOM 254 C CA . ASP A 1 32 ? 4.669 -66.690 3.952 1.00 17.91 ? 114 ASP A CA 1 ATOM 255 C C . ASP A 1 32 ? 5.395 -65.684 4.844 1.00 15.58 ? 114 ASP A C 1 ATOM 256 O O . ASP A 1 32 ? 5.586 -64.524 4.476 1.00 15.82 ? 114 ASP A O 1 ATOM 257 C CB . ASP A 1 32 ? 4.558 -66.224 2.503 1.00 14.05 ? 114 ASP A CB 1 ATOM 258 C CG . ASP A 1 32 ? 3.959 -67.294 1.612 1.00 20.73 ? 114 ASP A CG 1 ATOM 259 O OD1 . ASP A 1 32 ? 4.157 -68.496 1.924 1.00 18.60 ? 114 ASP A OD1 1 ATOM 260 O OD2 . ASP A 1 32 ? 3.293 -66.951 0.608 1.00 23.35 ? 114 ASP A OD2 1 ATOM 261 N N . VAL A 1 33 ? 5.783 -66.155 6.031 1.00 18.94 ? 115 VAL A N 1 ATOM 262 C CA . VAL A 1 33 ? 6.459 -65.336 7.035 1.00 20.07 ? 115 VAL A CA 1 ATOM 263 C C . VAL A 1 33 ? 7.967 -65.586 6.964 1.00 18.40 ? 115 VAL A C 1 ATOM 264 O O . VAL A 1 33 ? 8.415 -66.737 7.007 1.00 18.59 ? 115 VAL A O 1 ATOM 265 C CB . VAL A 1 33 ? 5.932 -65.659 8.454 1.00 22.56 ? 115 VAL A CB 1 ATOM 266 C CG1 . VAL A 1 33 ? 6.848 -65.086 9.533 1.00 18.42 ? 115 VAL A CG1 1 ATOM 267 C CG2 . VAL A 1 33 ? 4.493 -65.152 8.624 1.00 13.14 ? 115 VAL A CG2 1 ATOM 268 N N . LEU A 1 34 ? 8.745 -64.514 6.848 1.00 12.97 ? 116 LEU A N 1 ATOM 269 C CA . LEU A 1 34 ? 10.190 -64.639 6.696 1.00 16.09 ? 116 LEU A CA 1 ATOM 270 C C . LEU A 1 34 ? 10.836 -65.154 7.982 1.00 15.68 ? 116 LEU A C 1 ATOM 271 O O . LEU A 1 34 ? 10.428 -64.780 9.086 1.00 19.39 ? 116 LEU A O 1 ATOM 272 C CB . LEU A 1 34 ? 10.794 -63.288 6.299 1.00 19.04 ? 116 LEU A CB 1 ATOM 273 C CG . LEU A 1 34 ? 10.498 -62.829 4.869 1.00 17.71 ? 116 LEU A CG 1 ATOM 274 C CD1 . LEU A 1 34 ? 10.836 -61.352 4.656 1.00 13.31 ? 116 LEU A CD1 1 ATOM 275 C CD2 . LEU A 1 34 ? 11.256 -63.697 3.883 1.00 14.19 ? 116 LEU A CD2 1 ATOM 276 N N . VAL A 1 35 ? 11.829 -66.027 7.847 1.00 14.62 ? 117 VAL A N 1 ATOM 277 C CA . VAL A 1 35 ? 12.655 -66.394 8.992 1.00 12.96 ? 117 VAL A CA 1 ATOM 278 C C . VAL A 1 35 ? 13.502 -65.176 9.378 1.00 11.89 ? 117 VAL A C 1 ATOM 279 O O . VAL A 1 35 ? 14.113 -64.537 8.508 1.00 19.02 ? 117 VAL A O 1 ATOM 280 C CB . VAL A 1 35 ? 13.566 -67.602 8.678 1.00 18.11 ? 117 VAL A CB 1 ATOM 281 C CG1 . VAL A 1 35 ? 14.560 -67.836 9.805 1.00 15.69 ? 117 VAL A CG1 1 ATOM 282 C CG2 . VAL A 1 35 ? 12.727 -68.854 8.457 1.00 16.49 ? 117 VAL A CG2 1 ATOM 283 N N . THR A 1 36 ? 13.517 -64.828 10.663 1.00 14.81 ? 118 THR A N 1 ATOM 284 C CA . THR A 1 36 ? 14.330 -63.705 11.129 1.00 15.94 ? 118 THR A CA 1 ATOM 285 C C . THR A 1 36 ? 15.118 -64.072 12.367 1.00 16.33 ? 118 THR A C 1 ATOM 286 O O . THR A 1 36 ? 14.986 -65.178 12.896 1.00 18.21 ? 118 THR A O 1 ATOM 287 C CB . THR A 1 36 ? 13.472 -62.466 11.504 1.00 18.80 ? 118 THR A CB 1 ATOM 288 O OG1 . THR A 1 36 ? 12.568 -62.805 12.568 1.00 15.30 ? 118 THR A OG1 1 ATOM 289 C CG2 . THR A 1 36 ? 12.686 -61.953 10.307 1.00 14.89 ? 118 THR A CG2 1 ATOM 290 N N . ARG A 1 37 ? 15.949 -63.133 12.807 1.00 14.41 ? 119 ARG A N 1 ATOM 291 C CA . ARG A 1 37 ? 16.428 -63.080 14.185 1.00 13.80 ? 119 ARG A CA 1 ATOM 292 C C . ARG A 1 37 ? 16.984 -61.681 14.428 1.00 16.46 ? 119 ARG A C 1 ATOM 293 O O . ARG A 1 37 ? 16.963 -60.827 13.523 1.00 11.45 ? 119 ARG A O 1 ATOM 294 C CB . ARG A 1 37 ? 17.463 -64.175 14.504 1.00 13.33 ? 119 ARG A CB 1 ATOM 295 C CG . ARG A 1 37 ? 16.915 -65.325 15.388 1.00 14.45 ? 119 ARG A CG 1 ATOM 296 C CD . ARG A 1 37 ? 17.974 -65.873 16.364 1.00 20.34 ? 119 ARG A CD 1 ATOM 297 N NE . ARG A 1 37 ? 18.316 -64.875 17.383 1.00 19.67 ? 119 ARG A NE 1 ATOM 298 C CZ . ARG A 1 37 ? 19.492 -64.788 17.999 1.00 19.96 ? 119 ARG A CZ 1 ATOM 299 N NH1 . ARG A 1 37 ? 20.471 -65.644 17.712 1.00 14.35 ? 119 ARG A NH1 1 ATOM 300 N NH2 . ARG A 1 37 ? 19.693 -63.837 18.902 1.00 17.86 ? 119 ARG A NH2 1 ATOM 301 N N . GLU A 1 38 ? 17.463 -61.439 15.644 1.00 13.19 ? 120 GLU A N 1 ATOM 302 C CA . GLU A 1 38 ? 17.978 -60.121 16.008 1.00 14.17 ? 120 GLU A CA 1 ATOM 303 C C . GLU A 1 38 ? 16.999 -58.982 15.675 1.00 17.22 ? 120 GLU A C 1 ATOM 304 O O . GLU A 1 38 ? 17.354 -58.051 14.950 1.00 16.39 ? 120 GLU A O 1 ATOM 305 C CB . GLU A 1 38 ? 19.343 -59.876 15.334 1.00 14.71 ? 120 GLU A CB 1 ATOM 306 C CG . GLU A 1 38 ? 20.442 -60.893 15.731 1.00 16.20 ? 120 GLU A CG 1 ATOM 307 C CD . GLU A 1 38 ? 20.418 -62.177 14.902 1.00 14.69 ? 120 GLU A CD 1 ATOM 308 O OE1 . GLU A 1 38 ? 20.020 -62.119 13.718 1.00 14.45 ? 120 GLU A OE1 1 ATOM 309 O OE2 . GLU A 1 38 ? 20.802 -63.254 15.432 1.00 15.64 ? 120 GLU A OE2 1 ATOM 310 N N . PRO A 1 39 ? 15.765 -59.047 16.212 1.00 16.59 ? 121 PRO A N 1 ATOM 311 C CA . PRO A 1 39 ? 14.776 -58.010 15.900 1.00 15.96 ? 121 PRO A CA 1 ATOM 312 C C . PRO A 1 39 ? 14.934 -56.774 16.769 1.00 18.09 ? 121 PRO A C 1 ATOM 313 O O . PRO A 1 39 ? 15.656 -56.805 17.775 1.00 17.82 ? 121 PRO A O 1 ATOM 314 C CB . PRO A 1 39 ? 13.455 -58.687 16.261 1.00 19.48 ? 121 PRO A CB 1 ATOM 315 C CG . PRO A 1 39 ? 13.818 -59.533 17.459 1.00 17.13 ? 121 PRO A CG 1 ATOM 316 C CD . PRO A 1 39 ? 15.218 -60.053 17.146 1.00 16.67 ? 121 PRO A CD 1 ATOM 317 N N . TYR A 1 40 ? 14.282 -55.689 16.365 1.00 13.29 ? 122 TYR A N 1 ATOM 318 C CA . TYR A 1 40 ? 14.109 -54.529 17.234 1.00 13.82 ? 122 TYR A CA 1 ATOM 319 C C . TYR A 1 40 ? 12.907 -53.708 16.812 1.00 16.94 ? 122 TYR A C 1 ATOM 320 O O . TYR A 1 40 ? 12.129 -54.123 15.943 1.00 17.88 ? 122 TYR A O 1 ATOM 321 C CB . TYR A 1 40 ? 15.374 -53.656 17.350 1.00 14.91 ? 122 TYR A CB 1 ATOM 322 C CG . TYR A 1 40 ? 16.075 -53.252 16.062 1.00 16.72 ? 122 TYR A CG 1 ATOM 323 C CD1 . TYR A 1 40 ? 16.825 -54.170 15.347 1.00 16.88 ? 122 TYR A CD1 1 ATOM 324 C CD2 . TYR A 1 40 ? 16.047 -51.933 15.607 1.00 15.86 ? 122 TYR A CD2 1 ATOM 325 C CE1 . TYR A 1 40 ? 17.496 -53.805 14.193 1.00 16.18 ? 122 TYR A CE1 1 ATOM 326 C CE2 . TYR A 1 40 ? 16.728 -51.555 14.455 1.00 15.96 ? 122 TYR A CE2 1 ATOM 327 C CZ . TYR A 1 40 ? 17.449 -52.502 13.754 1.00 16.39 ? 122 TYR A CZ 1 ATOM 328 O OH . TYR A 1 40 ? 18.137 -52.160 12.608 1.00 17.50 ? 122 TYR A OH 1 ATOM 329 N N . VAL A 1 41 ? 12.727 -52.568 17.465 1.00 18.36 ? 123 VAL A N 1 ATOM 330 C CA . VAL A 1 41 ? 11.632 -51.667 17.129 1.00 13.59 ? 123 VAL A CA 1 ATOM 331 C C . VAL A 1 41 ? 12.251 -50.285 17.001 1.00 20.11 ? 123 VAL A C 1 ATOM 332 O O . VAL A 1 41 ? 13.182 -49.945 17.744 1.00 18.30 ? 123 VAL A O 1 ATOM 333 C CB . VAL A 1 41 ? 10.549 -51.650 18.236 1.00 23.26 ? 123 VAL A CB 1 ATOM 334 C CG1 . VAL A 1 41 ? 9.291 -50.950 17.752 1.00 19.98 ? 123 VAL A CG1 1 ATOM 335 C CG2 . VAL A 1 41 ? 10.214 -53.075 18.691 1.00 18.20 ? 123 VAL A CG2 1 ATOM 336 N N . SER A 1 42 ? 11.759 -49.499 16.051 1.00 19.35 ? 124 SER A N 1 ATOM 337 C CA . SER A 1 42 ? 12.237 -48.134 15.883 1.00 20.98 ? 124 SER A CA 1 ATOM 338 C C . SER A 1 42 ? 11.120 -47.269 15.311 1.00 22.14 ? 124 SER A C 1 ATOM 339 O O . SER A 1 42 ? 10.337 -47.731 14.469 1.00 19.57 ? 124 SER A O 1 ATOM 340 C CB . SER A 1 42 ? 13.462 -48.101 14.971 1.00 21.33 ? 124 SER A CB 1 ATOM 341 O OG . SER A 1 42 ? 13.964 -46.784 14.832 1.00 17.95 ? 124 SER A OG 1 ATOM 342 N N . CYS A 1 43 ? 11.044 -46.022 15.766 1.00 13.36 ? 125 CYS A N 1 ATOM 343 C CA . CYS A 1 43 ? 9.978 -45.116 15.333 1.00 20.80 ? 125 CYS A CA 1 ATOM 344 C C . CYS A 1 43 ? 10.442 -44.050 14.348 1.00 20.00 ? 125 CYS A C 1 ATOM 345 O O . CYS A 1 43 ? 11.562 -43.534 14.453 1.00 20.43 ? 125 CYS A O 1 ATOM 346 C CB . CYS A 1 43 ? 9.352 -44.417 16.538 1.00 16.64 ? 125 CYS A CB 1 ATOM 347 S SG . CYS A 1 43 ? 8.500 -45.532 17.674 1.00 22.00 ? 125 CYS A SG 1 ATOM 348 N N . ASP A 1 44 ? 9.572 -43.751 13.386 1.00 19.62 ? 126 ASP A N 1 ATOM 349 C CA . ASP A 1 44 ? 9.654 -42.543 12.576 1.00 20.34 ? 126 ASP A CA 1 ATOM 350 C C . ASP A 1 44 ? 8.738 -41.523 13.261 1.00 22.12 ? 126 ASP A C 1 ATOM 351 O O . ASP A 1 44 ? 8.075 -41.860 14.249 1.00 27.23 ? 126 ASP A O 1 ATOM 352 C CB . ASP A 1 44 ? 9.187 -42.833 11.141 1.00 23.75 ? 126 ASP A CB 1 ATOM 353 C CG . ASP A 1 44 ? 10.155 -43.720 10.382 1.00 27.98 ? 126 ASP A CG 1 ATOM 354 O OD1 . ASP A 1 44 ? 11.071 -44.284 11.025 1.00 22.99 ? 126 ASP A OD1 1 ATOM 355 O OD2 . ASP A 1 44 ? 9.998 -43.857 9.147 1.00 25.40 ? 126 ASP A OD2 1 ATOM 356 N N . PRO A 1 45 ? 8.719 -40.266 12.780 1.00 25.27 ? 127 PRO A N 1 ATOM 357 C CA . PRO A 1 45 ? 7.824 -39.304 13.436 1.00 22.10 ? 127 PRO A CA 1 ATOM 358 C C . PRO A 1 45 ? 6.339 -39.593 13.218 1.00 28.19 ? 127 PRO A C 1 ATOM 359 O O . PRO A 1 45 ? 5.517 -39.078 13.988 1.00 22.45 ? 127 PRO A O 1 ATOM 360 C CB . PRO A 1 45 ? 8.195 -37.970 12.771 1.00 25.36 ? 127 PRO A CB 1 ATOM 361 C CG . PRO A 1 45 ? 9.601 -38.147 12.324 1.00 23.08 ? 127 PRO A CG 1 ATOM 362 C CD . PRO A 1 45 ? 9.685 -39.595 11.891 1.00 20.48 ? 127 PRO A CD 1 ATOM 363 N N . ASP A 1 46 ? 5.999 -40.385 12.200 1.00 24.92 ? 128 ASP A N 1 ATOM 364 C CA . ASP A 1 46 ? 4.593 -40.665 11.896 1.00 29.43 ? 128 ASP A CA 1 ATOM 365 C C . ASP A 1 46 ? 4.215 -42.145 12.032 1.00 32.84 ? 128 ASP A C 1 ATOM 366 O O . ASP A 1 46 ? 3.064 -42.526 11.775 1.00 31.21 ? 128 ASP A O 1 ATOM 367 C CB . ASP A 1 46 ? 4.227 -40.157 10.492 1.00 30.73 ? 128 ASP A CB 1 ATOM 368 C CG . ASP A 1 46 ? 5.184 -40.657 9.417 1.00 44.03 ? 128 ASP A CG 1 ATOM 369 O OD1 . ASP A 1 46 ? 6.040 -41.520 9.725 1.00 38.38 ? 128 ASP A OD1 1 ATOM 370 O OD2 . ASP A 1 46 ? 5.079 -40.190 8.259 1.00 52.59 ? 128 ASP A OD2 1 ATOM 371 N N . GLU A 1 47 ? 5.176 -42.976 12.438 1.00 22.97 ? 129 GLU A N 1 ATOM 372 C CA . GLU A 1 47 ? 4.966 -44.423 12.446 1.00 30.77 ? 129 GLU A CA 1 ATOM 373 C C . GLU A 1 47 ? 6.046 -45.139 13.249 1.00 28.15 ? 129 GLU A C 1 ATOM 374 O O . GLU A 1 47 ? 7.210 -44.741 13.228 1.00 25.45 ? 129 GLU A O 1 ATOM 375 C CB . GLU A 1 47 ? 4.964 -44.956 11.004 1.00 25.86 ? 129 GLU A CB 1 ATOM 376 C CG . GLU A 1 47 ? 4.646 -46.444 10.878 1.00 38.04 ? 129 GLU A CG 1 ATOM 377 C CD . GLU A 1 47 ? 4.879 -46.989 9.474 1.00 38.59 ? 129 GLU A CD 1 ATOM 378 O OE1 . GLU A 1 47 ? 5.405 -46.242 8.618 1.00 35.79 ? 129 GLU A OE1 1 ATOM 379 O OE2 . GLU A 1 47 ? 4.541 -48.173 9.234 1.00 37.84 ? 129 GLU A OE2 1 ATOM 380 N N . CYS A 1 48 ? 5.658 -46.197 13.952 1.00 22.15 ? 130 CYS A N 1 ATOM 381 C CA . CYS A 1 48 ? 6.628 -47.078 14.603 1.00 22.69 ? 130 CYS A CA 1 ATOM 382 C C . CYS A 1 48 ? 6.602 -48.432 13.915 1.00 25.38 ? 130 CYS A C 1 ATOM 383 O O . CYS A 1 48 ? 5.532 -48.917 13.524 1.00 18.62 ? 130 CYS A O 1 ATOM 384 C CB . CYS A 1 48 ? 6.319 -47.229 16.092 1.00 20.80 ? 130 CYS A CB 1 ATOM 385 S SG . CYS A 1 48 ? 6.570 -45.690 17.021 1.00 24.86 ? 130 CYS A SG 1 ATOM 386 N N . ARG A 1 49 ? 7.778 -49.038 13.753 1.00 17.60 ? 131 ARG A N 1 ATOM 387 C CA . ARG A 1 49 ? 7.881 -50.284 13.002 1.00 18.02 ? 131 ARG A CA 1 ATOM 388 C C . ARG A 1 49 ? 8.767 -51.333 13.671 1.00 19.72 ? 131 ARG A C 1 ATOM 389 O O . ARG A 1 49 ? 9.669 -50.997 14.463 1.00 17.44 ? 131 ARG A O 1 ATOM 390 C CB . ARG A 1 49 ? 8.372 -49.997 11.575 1.00 18.04 ? 131 ARG A CB 1 ATOM 391 C CG . ARG A 1 49 ? 7.350 -49.261 10.716 1.00 21.44 ? 131 ARG A CG 1 ATOM 392 C CD . ARG A 1 49 ? 7.970 -48.663 9.458 1.00 21.85 ? 131 ARG A CD 1 ATOM 393 N NE . ARG A 1 49 ? 8.397 -49.671 8.486 1.00 23.41 ? 131 ARG A NE 1 ATOM 394 C CZ . ARG A 1 49 ? 7.597 -50.216 7.574 1.00 26.22 ? 131 ARG A CZ 1 ATOM 395 N NH1 . ARG A 1 49 ? 6.318 -49.864 7.517 1.00 25.46 ? 131 ARG A NH1 1 ATOM 396 N NH2 . ARG A 1 49 ? 8.076 -51.113 6.714 1.00 26.09 ? 131 ARG A NH2 1 ATOM 397 N N . PHE A 1 50 ? 8.489 -52.601 13.358 1.00 19.98 ? 132 PHE A N 1 ATOM 398 C CA . PHE A 1 50 ? 9.333 -53.726 13.772 1.00 16.30 ? 132 PHE A CA 1 ATOM 399 C C . PHE A 1 50 ? 10.474 -53.898 12.766 1.00 17.88 ? 132 PHE A C 1 ATOM 400 O O . PHE A 1 50 ? 10.274 -53.712 11.561 1.00 13.21 ? 132 PHE A O 1 ATOM 401 C CB . PHE A 1 50 ? 8.515 -55.023 13.843 1.00 11.44 ? 132 PHE A CB 1 ATOM 402 C CG . PHE A 1 50 ? 7.677 -55.174 15.103 1.00 17.22 ? 132 PHE A CG 1 ATOM 403 C CD1 . PHE A 1 50 ? 7.668 -54.192 16.092 1.00 13.08 ? 132 PHE A CD1 1 ATOM 404 C CD2 . PHE A 1 50 ? 6.915 -56.322 15.301 1.00 17.36 ? 132 PHE A CD2 1 ATOM 405 C CE1 . PHE A 1 50 ? 6.905 -54.351 17.248 1.00 13.92 ? 132 PHE A CE1 1 ATOM 406 C CE2 . PHE A 1 50 ? 6.157 -56.495 16.456 1.00 18.38 ? 132 PHE A CE2 1 ATOM 407 C CZ . PHE A 1 50 ? 6.146 -55.515 17.429 1.00 14.97 ? 132 PHE A CZ 1 ATOM 408 N N . TYR A 1 51 ? 11.663 -54.242 13.266 1.00 17.43 ? 133 TYR A N 1 ATOM 409 C CA . TYR A 1 51 ? 12.853 -54.442 12.443 1.00 17.61 ? 133 TYR A CA 1 ATOM 410 C C . TYR A 1 51 ? 13.458 -55.790 12.813 1.00 22.29 ? 133 TYR A C 1 ATOM 411 O O . TYR A 1 51 ? 13.294 -56.256 13.944 1.00 11.94 ? 133 TYR A O 1 ATOM 412 C CB . TYR A 1 51 ? 13.885 -53.329 12.694 1.00 17.55 ? 133 TYR A CB 1 ATOM 413 C CG . TYR A 1 51 ? 13.468 -51.971 12.175 1.00 17.08 ? 133 TYR A CG 1 ATOM 414 C CD1 . TYR A 1 51 ? 12.472 -51.241 12.812 1.00 13.81 ? 133 TYR A CD1 1 ATOM 415 C CD2 . TYR A 1 51 ? 14.073 -51.418 11.049 1.00 14.18 ? 133 TYR A CD2 1 ATOM 416 C CE1 . TYR A 1 51 ? 12.076 -50.001 12.338 1.00 14.18 ? 133 TYR A CE1 1 ATOM 417 C CE2 . TYR A 1 51 ? 13.688 -50.177 10.570 1.00 16.82 ? 133 TYR A CE2 1 ATOM 418 C CZ . TYR A 1 51 ? 12.686 -49.473 11.216 1.00 18.41 ? 133 TYR A CZ 1 ATOM 419 O OH . TYR A 1 51 ? 12.295 -48.233 10.746 1.00 16.80 ? 133 TYR A OH 1 ATOM 420 N N . ALA A 1 52 ? 14.145 -56.422 11.865 1.00 20.36 ? 134 ALA A N 1 ATOM 421 C CA . ALA A 1 52 ? 14.853 -57.678 12.139 1.00 20.53 ? 134 ALA A CA 1 ATOM 422 C C . ALA A 1 52 ? 15.744 -58.054 10.965 1.00 19.16 ? 134 ALA A C 1 ATOM 423 O O . ALA A 1 52 ? 15.612 -57.499 9.868 1.00 20.67 ? 134 ALA A O 1 ATOM 424 C CB . ALA A 1 52 ? 13.868 -58.823 12.446 1.00 15.30 ? 134 ALA A CB 1 ATOM 425 N N . LEU A 1 53 ? 16.647 -59.001 11.196 1.00 16.65 ? 135 LEU A N 1 ATOM 426 C CA . LEU A 1 53 ? 17.467 -59.527 10.116 1.00 20.46 ? 135 LEU A CA 1 ATOM 427 C C . LEU A 1 53 ? 16.821 -60.776 9.526 1.00 15.18 ? 135 LEU A C 1 ATOM 428 O O . LEU A 1 53 ? 16.763 -61.824 10.180 1.00 17.97 ? 135 LEU A O 1 ATOM 429 C CB . LEU A 1 53 ? 18.874 -59.848 10.608 1.00 16.10 ? 135 LEU A CB 1 ATOM 430 C CG . LEU A 1 53 ? 19.746 -58.665 11.035 1.00 18.69 ? 135 LEU A CG 1 ATOM 431 C CD1 . LEU A 1 53 ? 21.067 -59.177 11.582 1.00 11.83 ? 135 LEU A CD1 1 ATOM 432 C CD2 . LEU A 1 53 ? 19.981 -57.723 9.864 1.00 18.61 ? 135 LEU A CD2 1 ATOM 433 N N . SER A 1 54 ? 16.333 -60.659 8.295 1.00 13.69 ? 136 SER A N 1 ATOM 434 C CA . SER A 1 54 ? 15.763 -61.803 7.584 1.00 15.89 ? 136 SER A CA 1 ATOM 435 C C . SER A 1 54 ? 16.856 -62.814 7.256 1.00 12.62 ? 136 SER A C 1 ATOM 436 O O . SER A 1 54 ? 18.051 -62.484 7.268 1.00 18.88 ? 136 SER A O 1 ATOM 437 C CB . SER A 1 54 ? 15.062 -61.349 6.297 1.00 14.28 ? 136 SER A CB 1 ATOM 438 O OG . SER A 1 54 ? 14.711 -62.456 5.475 1.00 14.68 ? 136 SER A OG 1 ATOM 439 N N . GLN A 1 55 ? 16.443 -64.046 6.980 1.00 14.69 ? 137 GLN A N 1 ATOM 440 C CA . GLN A 1 55 ? 17.360 -65.099 6.554 1.00 14.13 ? 137 GLN A CA 1 ATOM 441 C C . GLN A 1 55 ? 17.122 -65.439 5.080 1.00 17.88 ? 137 GLN A C 1 ATOM 442 O O . GLN A 1 55 ? 17.683 -66.402 4.549 1.00 18.07 ? 137 GLN A O 1 ATOM 443 C CB . GLN A 1 55 ? 17.180 -66.344 7.431 1.00 15.42 ? 137 GLN A CB 1 ATOM 444 C CG . GLN A 1 55 ? 17.703 -66.186 8.871 1.00 13.71 ? 137 GLN A CG 1 ATOM 445 C CD . GLN A 1 55 ? 19.213 -66.421 8.984 1.00 16.07 ? 137 GLN A CD 1 ATOM 446 O OE1 . GLN A 1 55 ? 19.947 -66.345 7.991 1.00 20.95 ? 137 GLN A OE1 1 ATOM 447 N NE2 . GLN A 1 55 ? 19.679 -66.714 10.197 1.00 15.72 ? 137 GLN A NE2 1 ATOM 448 N N . GLY A 1 56 ? 16.288 -64.639 4.424 1.00 14.08 ? 138 GLY A N 1 ATOM 449 C CA . GLY A 1 56 ? 16.024 -64.812 3.005 1.00 17.61 ? 138 GLY A CA 1 ATOM 450 C C . GLY A 1 56 ? 15.311 -66.111 2.680 1.00 19.30 ? 138 GLY A C 1 ATOM 451 O O . GLY A 1 56 ? 15.681 -66.808 1.728 1.00 16.90 ? 138 GLY A O 1 ATOM 452 N N . THR A 1 57 ? 14.285 -66.425 3.470 1.00 16.28 ? 139 THR A N 1 ATOM 453 C CA . THR A 1 57 ? 13.485 -67.637 3.300 1.00 18.96 ? 139 THR A CA 1 ATOM 454 C C . THR A 1 57 ? 12.292 -67.558 4.251 1.00 19.77 ? 139 THR A C 1 ATOM 455 O O . THR A 1 57 ? 12.361 -66.854 5.266 1.00 18.93 ? 139 THR A O 1 ATOM 456 C CB . THR A 1 57 ? 14.317 -68.902 3.625 1.00 22.36 ? 139 THR A CB 1 ATOM 457 O OG1 . THR A 1 57 ? 13.503 -70.068 3.476 1.00 18.53 ? 139 THR A OG1 1 ATOM 458 C CG2 . THR A 1 57 ? 14.873 -68.849 5.061 1.00 20.28 ? 139 THR A CG2 1 ATOM 459 N N . THR A 1 58 ? 11.196 -68.248 3.938 1.00 15.77 ? 140 THR A N 1 ATOM 460 C CA . THR A 1 58 ? 10.101 -68.356 4.908 1.00 17.72 ? 140 THR A CA 1 ATOM 461 C C . THR A 1 58 ? 10.350 -69.546 5.827 1.00 14.79 ? 140 THR A C 1 ATOM 462 O O . THR A 1 58 ? 11.228 -70.366 5.549 1.00 15.19 ? 140 THR A O 1 ATOM 463 C CB . THR A 1 58 ? 8.710 -68.498 4.258 1.00 14.20 ? 140 THR A CB 1 ATOM 464 O OG1 . THR A 1 58 ? 8.649 -69.717 3.510 1.00 18.30 ? 140 THR A OG1 1 ATOM 465 C CG2 . THR A 1 58 ? 8.401 -67.312 3.348 1.00 15.09 ? 140 THR A CG2 1 ATOM 466 N N . ILE A 1 59 ? 9.576 -69.637 6.910 1.00 20.55 ? 141 ILE A N 1 ATOM 467 C CA . ILE A 1 59 ? 9.732 -70.716 7.884 1.00 22.55 ? 141 ILE A CA 1 ATOM 468 C C . ILE A 1 59 ? 9.359 -72.079 7.306 1.00 20.71 ? 141 ILE A C 1 ATOM 469 O O . ILE A 1 59 ? 10.061 -73.066 7.543 1.00 21.64 ? 141 ILE A O 1 ATOM 470 C CB . ILE A 1 59 ? 8.881 -70.480 9.150 1.00 27.21 ? 141 ILE A CB 1 ATOM 471 C CG1 . ILE A 1 59 ? 8.929 -69.013 9.575 1.00 26.60 ? 141 ILE A CG1 1 ATOM 472 C CG2 . ILE A 1 59 ? 9.354 -71.385 10.283 1.00 25.26 ? 141 ILE A CG2 1 ATOM 473 C CD1 . ILE A 1 59 ? 8.095 -68.706 10.824 1.00 29.01 ? 141 ILE A CD1 1 ATOM 474 N N . ARG A 1 60 ? 8.254 -72.140 6.563 1.00 15.78 ? 142 ARG A N 1 ATOM 475 C CA . ARG A 1 60 ? 7.834 -73.403 5.949 1.00 21.90 ? 142 ARG A CA 1 ATOM 476 C C . ARG A 1 60 ? 8.704 -73.757 4.743 1.00 21.76 ? 142 ARG A C 1 ATOM 477 O O . ARG A 1 60 ? 8.769 -74.921 4.341 1.00 26.50 ? 142 ARG A O 1 ATOM 478 C CB . ARG A 1 60 ? 6.352 -73.369 5.542 1.00 17.41 ? 142 ARG A CB 1 ATOM 479 C CG . ARG A 1 60 ? 5.379 -73.588 6.694 1.00 21.77 ? 142 ARG A CG 1 ATOM 480 C CD . ARG A 1 60 ? 5.679 -74.896 7.428 1.00 23.44 ? 142 ARG A CD 1 ATOM 481 N NE . ARG A 1 60 ? 4.535 -75.385 8.206 1.00 21.59 ? 142 ARG A NE 1 ATOM 482 C CZ . ARG A 1 60 ? 4.526 -76.545 8.857 1.00 26.87 ? 142 ARG A CZ 1 ATOM 483 N NH1 . ARG A 1 60 ? 5.596 -77.330 8.818 1.00 23.49 ? 142 ARG A NH1 1 ATOM 484 N NH2 . ARG A 1 60 ? 3.451 -76.928 9.538 1.00 23.99 ? 142 ARG A NH2 1 ATOM 485 N N . GLY A 1 61 ? 9.368 -72.750 4.172 1.00 23.02 ? 143 GLY A N 1 ATOM 486 C CA . GLY A 1 61 ? 10.266 -72.970 3.051 1.00 17.23 ? 143 GLY A CA 1 ATOM 487 C C . GLY A 1 61 ? 11.384 -73.922 3.421 1.00 22.59 ? 143 GLY A C 1 ATOM 488 O O . GLY A 1 61 ? 11.866 -73.898 4.557 1.00 18.40 ? 143 GLY A O 1 ATOM 489 N N . LYS A 1 62 ? 11.798 -74.764 2.476 1.00 19.70 ? 144 LYS A N 1 ATOM 490 C CA . LYS A 1 62 ? 12.861 -75.725 2.750 1.00 20.30 ? 144 LYS A CA 1 ATOM 491 C C . LYS A 1 62 ? 14.197 -75.044 3.051 1.00 18.15 ? 144 LYS A C 1 ATOM 492 O O . LYS A 1 62 ? 15.050 -75.629 3.718 1.00 17.32 ? 144 LYS A O 1 ATOM 493 C CB . LYS A 1 62 ? 13.023 -76.714 1.588 1.00 20.03 ? 144 LYS A CB 1 ATOM 494 C CG . LYS A 1 62 ? 11.883 -77.728 1.448 1.00 23.45 ? 144 LYS A CG 1 ATOM 495 C CD . LYS A 1 62 ? 12.105 -78.601 0.211 1.00 19.43 ? 144 LYS A CD 1 ATOM 496 C CE . LYS A 1 62 ? 10.902 -79.489 -0.080 1.00 25.45 ? 144 LYS A CE 1 ATOM 497 N NZ . LYS A 1 62 ? 11.065 -80.196 -1.388 1.00 22.16 ? 144 LYS A NZ 1 ATOM 498 N N . HIS A 1 63 ? 14.379 -73.818 2.560 1.00 15.63 ? 145 HIS A N 1 ATOM 499 C CA . HIS A 1 63 ? 15.610 -73.065 2.823 1.00 18.06 ? 145 HIS A CA 1 ATOM 500 C C . HIS A 1 63 ? 15.712 -72.570 4.276 1.00 20.42 ? 145 HIS A C 1 ATOM 501 O O . HIS A 1 63 ? 16.733 -71.990 4.670 1.00 19.40 ? 145 HIS A O 1 ATOM 502 C CB . HIS A 1 63 ? 15.765 -71.888 1.846 1.00 15.97 ? 145 HIS A CB 1 ATOM 503 C CG . HIS A 1 63 ? 15.957 -72.300 0.416 1.00 18.93 ? 145 HIS A CG 1 ATOM 504 N ND1 . HIS A 1 63 ? 14.944 -72.244 -0.518 1.00 22.20 ? 145 HIS A ND1 1 ATOM 505 C CD2 . HIS A 1 63 ? 17.048 -72.765 -0.241 1.00 18.30 ? 145 HIS A CD2 1 ATOM 506 C CE1 . HIS A 1 63 ? 15.402 -72.661 -1.688 1.00 16.62 ? 145 HIS A CE1 1 ATOM 507 N NE2 . HIS A 1 63 ? 16.676 -72.979 -1.547 1.00 17.71 ? 145 HIS A NE2 1 ATOM 508 N N . SER A 1 64 ? 14.664 -72.793 5.071 1.00 17.46 ? 146 SER A N 1 ATOM 509 C CA . SER A 1 64 ? 14.734 -72.491 6.500 1.00 21.56 ? 146 SER A CA 1 ATOM 510 C C . SER A 1 64 ? 15.683 -73.466 7.210 1.00 19.11 ? 146 SER A C 1 ATOM 511 O O . SER A 1 64 ? 16.170 -73.178 8.307 1.00 19.75 ? 146 SER A O 1 ATOM 512 C CB . SER A 1 64 ? 13.346 -72.525 7.152 1.00 21.28 ? 146 SER A CB 1 ATOM 513 O OG . SER A 1 64 ? 12.827 -73.844 7.190 1.00 19.30 ? 146 SER A OG 1 ATOM 514 N N . ASN A 1 65 ? 15.936 -74.613 6.578 1.00 13.21 ? 147 ASN A N 1 ATOM 515 C CA . ASN A 1 65 ? 16.905 -75.592 7.075 1.00 17.64 ? 147 ASN A CA 1 ATOM 516 C C . ASN A 1 65 ? 18.287 -74.948 7.216 1.00 17.30 ? 147 ASN A C 1 ATOM 517 O O . ASN A 1 65 ? 18.885 -74.539 6.225 1.00 20.40 ? 147 ASN A O 1 ATOM 518 C CB . ASN A 1 65 ? 16.965 -76.790 6.112 1.00 17.71 ? 147 ASN A CB 1 ATOM 519 C CG . ASN A 1 65 ? 17.617 -78.027 6.727 1.00 24.95 ? 147 ASN A CG 1 ATOM 520 O OD1 . ASN A 1 65 ? 18.451 -77.927 7.633 1.00 23.64 ? 147 ASN A OD1 1 ATOM 521 N ND2 . ASN A 1 65 ? 17.241 -79.209 6.218 1.00 33.53 ? 147 ASN A ND2 1 ATOM 522 N N . GLY A 1 66 ? 18.791 -74.833 8.442 1.00 18.28 ? 148 GLY A N 1 ATOM 523 C CA . GLY A 1 66 ? 20.132 -74.306 8.635 1.00 17.57 ? 148 GLY A CA 1 ATOM 524 C C . GLY A 1 66 ? 20.192 -72.837 9.036 1.00 22.11 ? 148 GLY A C 1 ATOM 525 O O . GLY A 1 66 ? 21.274 -72.251 9.079 1.00 20.99 ? 148 GLY A O 1 ATOM 526 N N . THR A 1 67 ? 19.039 -72.246 9.351 1.00 14.45 ? 149 THR A N 1 ATOM 527 C CA . THR A 1 67 ? 18.974 -70.822 9.695 1.00 21.83 ? 149 THR A CA 1 ATOM 528 C C . THR A 1 67 ? 19.476 -70.486 11.097 1.00 19.80 ? 149 THR A C 1 ATOM 529 O O . THR A 1 67 ? 19.315 -69.353 11.555 1.00 17.68 ? 149 THR A O 1 ATOM 530 C CB . THR A 1 67 ? 17.555 -70.257 9.541 1.00 21.25 ? 149 THR A CB 1 ATOM 531 O OG1 . THR A 1 67 ? 16.601 -71.215 10.024 1.00 19.92 ? 149 THR A OG1 1 ATOM 532 C CG2 . THR A 1 67 ? 17.268 -69.939 8.081 1.00 20.46 ? 149 THR A CG2 1 ATOM 533 N N . ILE A 1 68 ? 20.082 -71.453 11.785 1.00 22.54 ? 150 ILE A N 1 ATOM 534 C CA . ILE A 1 68 ? 20.823 -71.121 13.004 1.00 21.76 ? 150 ILE A CA 1 ATOM 535 C C . ILE A 1 68 ? 22.059 -70.296 12.622 1.00 18.93 ? 150 ILE A C 1 ATOM 536 O O . ILE A 1 68 ? 22.603 -69.542 13.441 1.00 24.78 ? 150 ILE A O 1 ATOM 537 C CB . ILE A 1 68 ? 21.232 -72.376 13.825 1.00 17.30 ? 150 ILE A CB 1 ATOM 538 C CG1 . ILE A 1 68 ? 21.659 -71.964 15.244 1.00 19.16 ? 150 ILE A CG1 1 ATOM 539 C CG2 . ILE A 1 68 ? 22.348 -73.174 13.117 1.00 17.76 ? 150 ILE A CG2 1 ATOM 540 C CD1 . ILE A 1 68 ? 22.162 -73.114 16.109 1.00 30.01 ? 150 ILE A CD1 1 ATOM 541 N N . HIS A 1 69 ? 22.478 -70.436 11.365 1.00 23.94 ? 151 HIS A N 1 ATOM 542 C CA . HIS A 1 69 ? 23.636 -69.721 10.821 1.00 28.40 ? 151 HIS A CA 1 ATOM 543 C C . HIS A 1 69 ? 23.499 -68.194 10.956 1.00 21.45 ? 151 HIS A C 1 ATOM 544 O O . HIS A 1 69 ? 22.463 -67.622 10.599 1.00 23.56 ? 151 HIS A O 1 ATOM 545 C CB . HIS A 1 69 ? 23.822 -70.119 9.351 1.00 24.87 ? 151 HIS A CB 1 ATOM 546 C CG . HIS A 1 69 ? 25.151 -69.742 8.779 1.00 38.92 ? 151 HIS A CG 1 ATOM 547 N ND1 . HIS A 1 69 ? 25.293 -68.795 7.784 1.00 39.61 ? 151 HIS A ND1 1 ATOM 548 C CD2 . HIS A 1 69 ? 26.400 -70.196 9.042 1.00 42.55 ? 151 HIS A CD2 1 ATOM 549 C CE1 . HIS A 1 69 ? 26.569 -68.677 7.468 1.00 31.81 ? 151 HIS A CE1 1 ATOM 550 N NE2 . HIS A 1 69 ? 27.264 -69.515 8.219 1.00 39.37 ? 151 HIS A NE2 1 ATOM 551 N N . ASP A 1 70 ? 24.548 -67.541 11.458 1.00 23.87 ? 152 ASP A N 1 ATOM 552 C CA . ASP A 1 70 ? 24.509 -66.103 11.756 1.00 21.47 ? 152 ASP A CA 1 ATOM 553 C C . ASP A 1 70 ? 24.710 -65.148 10.563 1.00 17.58 ? 152 ASP A C 1 ATOM 554 O O . ASP A 1 70 ? 24.063 -64.101 10.484 1.00 16.75 ? 152 ASP A O 1 ATOM 555 C CB . ASP A 1 70 ? 25.552 -65.762 12.828 1.00 22.74 ? 152 ASP A CB 1 ATOM 556 C CG . ASP A 1 70 ? 25.042 -65.982 14.238 1.00 24.68 ? 152 ASP A CG 1 ATOM 557 O OD1 . ASP A 1 70 ? 23.816 -65.855 14.460 1.00 18.07 ? 152 ASP A OD1 1 ATOM 558 O OD2 . ASP A 1 70 ? 25.876 -66.267 15.131 1.00 18.20 ? 152 ASP A OD2 1 ATOM 559 N N . ARG A 1 71 ? 25.617 -65.493 9.654 1.00 18.07 ? 153 ARG A N 1 ATOM 560 C CA . ARG A 1 71 ? 26.076 -64.538 8.643 1.00 20.99 ? 153 ARG A CA 1 ATOM 561 C C . ARG A 1 71 ? 26.156 -65.125 7.235 1.00 20.56 ? 153 ARG A C 1 ATOM 562 O O . ARG A 1 71 ? 27.183 -65.683 6.848 1.00 36.58 ? 153 ARG A O 1 ATOM 563 C CB . ARG A 1 71 ? 27.453 -63.979 9.033 1.00 15.53 ? 153 ARG A CB 1 ATOM 564 C CG . ARG A 1 71 ? 27.471 -63.193 10.338 1.00 16.53 ? 153 ARG A CG 1 ATOM 565 C CD . ARG A 1 71 ? 28.885 -62.740 10.671 1.00 17.95 ? 153 ARG A CD 1 ATOM 566 N NE . ARG A 1 71 ? 29.822 -63.862 10.643 1.00 16.27 ? 153 ARG A NE 1 ATOM 567 C CZ . ARG A 1 71 ? 30.003 -64.705 11.656 1.00 18.81 ? 153 ARG A CZ 1 ATOM 568 N NH1 . ARG A 1 71 ? 29.300 -64.556 12.775 1.00 17.33 ? 153 ARG A NH1 1 ATOM 569 N NH2 . ARG A 1 71 ? 30.882 -65.699 11.556 1.00 17.90 ? 153 ARG A NH2 1 ATOM 570 N N . SER A 1 72 ? 25.081 -64.988 6.469 1.00 22.62 ? 154 SER A N 1 ATOM 571 C CA . SER A 1 72 ? 25.052 -65.479 5.094 1.00 24.03 ? 154 SER A CA 1 ATOM 572 C C . SER A 1 72 ? 24.772 -64.307 4.167 1.00 26.36 ? 154 SER A C 1 ATOM 573 O O . SER A 1 72 ? 24.439 -63.213 4.631 1.00 21.31 ? 154 SER A O 1 ATOM 574 C CB . SER A 1 72 ? 23.944 -66.512 4.915 1.00 19.80 ? 154 SER A CB 1 ATOM 575 O OG . SER A 1 72 ? 22.685 -65.861 4.806 1.00 18.86 ? 154 SER A OG 1 ATOM 576 N N . GLN A 1 73 ? 24.882 -64.542 2.860 1.00 22.04 ? 155 GLN A N 1 ATOM 577 C CA . GLN A 1 73 ? 24.641 -63.499 1.865 1.00 19.70 ? 155 GLN A CA 1 ATOM 578 C C . GLN A 1 73 ? 23.152 -63.290 1.610 1.00 18.92 ? 155 GLN A C 1 ATOM 579 O O . GLN A 1 73 ? 22.762 -62.474 0.763 1.00 17.50 ? 155 GLN A O 1 ATOM 580 C CB . GLN A 1 73 ? 25.340 -63.853 0.545 1.00 18.90 ? 155 GLN A CB 1 ATOM 581 C CG . GLN A 1 73 ? 26.867 -63.934 0.637 1.00 17.11 ? 155 GLN A CG 1 ATOM 582 C CD . GLN A 1 73 ? 27.369 -65.340 0.885 1.00 21.66 ? 155 GLN A CD 1 ATOM 583 O OE1 . GLN A 1 73 ? 26.759 -66.109 1.634 1.00 19.22 ? 155 GLN A OE1 1 ATOM 584 N NE2 . GLN A 1 73 ? 28.487 -65.692 0.246 1.00 24.77 ? 155 GLN A NE2 1 ATOM 585 N N . TYR A 1 74 ? 22.322 -64.022 2.350 1.00 17.27 ? 156 TYR A N 1 ATOM 586 C CA . TYR A 1 74 ? 20.885 -64.041 2.097 1.00 20.58 ? 156 TYR A CA 1 ATOM 587 C C . TYR A 1 74 ? 20.148 -63.298 3.195 1.00 21.56 ? 156 TYR A C 1 ATOM 588 O O . TYR A 1 74 ? 18.913 -63.275 3.228 1.00 22.75 ? 156 TYR A O 1 ATOM 589 C CB . TYR A 1 74 ? 20.405 -65.491 1.975 1.00 18.35 ? 156 TYR A CB 1 ATOM 590 C CG . TYR A 1 74 ? 21.418 -66.327 1.231 1.00 20.22 ? 156 TYR A CG 1 ATOM 591 C CD1 . TYR A 1 74 ? 21.784 -65.999 -0.071 1.00 22.88 ? 156 TYR A CD1 1 ATOM 592 C CD2 . TYR A 1 74 ? 22.039 -67.412 1.835 1.00 19.12 ? 156 TYR A CD2 1 ATOM 593 C CE1 . TYR A 1 74 ? 22.732 -66.733 -0.753 1.00 15.78 ? 156 TYR A CE1 1 ATOM 594 C CE2 . TYR A 1 74 ? 22.980 -68.164 1.155 1.00 18.12 ? 156 TYR A CE2 1 ATOM 595 C CZ . TYR A 1 74 ? 23.323 -67.816 -0.139 1.00 21.32 ? 156 TYR A CZ 1 ATOM 596 O OH . TYR A 1 74 ? 24.264 -68.553 -0.823 1.00 24.27 ? 156 TYR A OH 1 ATOM 597 N N . ARG A 1 75 ? 20.914 -62.678 4.091 1.00 15.49 ? 157 ARG A N 1 ATOM 598 C CA . ARG A 1 75 ? 20.319 -61.873 5.152 1.00 14.59 ? 157 ARG A CA 1 ATOM 599 C C . ARG A 1 75 ? 20.167 -60.417 4.723 1.00 15.46 ? 157 ARG A C 1 ATOM 600 O O . ARG A 1 75 ? 20.911 -59.919 3.866 1.00 14.67 ? 157 ARG A O 1 ATOM 601 C CB . ARG A 1 75 ? 21.139 -61.959 6.450 1.00 17.30 ? 157 ARG A CB 1 ATOM 602 C CG . ARG A 1 75 ? 21.366 -63.388 6.963 1.00 16.37 ? 157 ARG A CG 1 ATOM 603 C CD . ARG A 1 75 ? 21.561 -63.419 8.484 1.00 22.54 ? 157 ARG A CD 1 ATOM 604 N NE . ARG A 1 75 ? 20.302 -63.238 9.217 1.00 18.98 ? 157 ARG A NE 1 ATOM 605 C CZ . ARG A 1 75 ? 20.170 -63.376 10.536 1.00 23.01 ? 157 ARG A CZ 1 ATOM 606 N NH1 . ARG A 1 75 ? 18.979 -63.211 11.112 1.00 15.52 ? 157 ARG A NH1 1 ATOM 607 N NH2 . ARG A 1 75 ? 21.227 -63.691 11.282 1.00 18.08 ? 157 ARG A NH2 1 ATOM 608 N N . ALA A 1 76 ? 19.187 -59.748 5.321 1.00 15.74 ? 158 ALA A N 1 ATOM 609 C CA . ALA A 1 76 ? 18.952 -58.333 5.086 1.00 15.66 ? 158 ALA A CA 1 ATOM 610 C C . ALA A 1 76 ? 18.184 -57.766 6.271 1.00 18.31 ? 158 ALA A C 1 ATOM 611 O O . ALA A 1 76 ? 17.385 -58.475 6.897 1.00 12.53 ? 158 ALA A O 1 ATOM 612 C CB . ALA A 1 76 ? 18.155 -58.128 3.799 1.00 18.35 ? 158 ALA A CB 1 ATOM 613 N N . LEU A 1 77 ? 18.437 -56.501 6.591 1.00 17.75 ? 159 LEU A N 1 ATOM 614 C CA . LEU A 1 77 ? 17.597 -55.783 7.544 1.00 21.11 ? 159 LEU A CA 1 ATOM 615 C C . LEU A 1 77 ? 16.266 -55.465 6.873 1.00 21.80 ? 159 LEU A C 1 ATOM 616 O O . LEU A 1 77 ? 16.234 -54.795 5.837 1.00 18.06 ? 159 LEU A O 1 ATOM 617 C CB . LEU A 1 77 ? 18.270 -54.481 7.979 1.00 18.61 ? 159 LEU A CB 1 ATOM 618 C CG . LEU A 1 77 ? 17.401 -53.518 8.785 1.00 17.13 ? 159 LEU A CG 1 ATOM 619 C CD1 . LEU A 1 77 ? 17.004 -54.152 10.112 1.00 14.31 ? 159 LEU A CD1 1 ATOM 620 C CD2 . LEU A 1 77 ? 18.107 -52.174 8.994 1.00 13.49 ? 159 LEU A CD2 1 ATOM 621 N N . ILE A 1 78 ? 15.173 -55.962 7.444 1.00 19.08 ? 160 ILE A N 1 ATOM 622 C CA . ILE A 1 78 ? 13.838 -55.614 6.963 1.00 19.37 ? 160 ILE A CA 1 ATOM 623 C C . ILE A 1 78 ? 13.075 -54.855 8.044 1.00 19.03 ? 160 ILE A C 1 ATOM 624 O O . ILE A 1 78 ? 13.394 -54.967 9.235 1.00 14.28 ? 160 ILE A O 1 ATOM 625 C CB . ILE A 1 78 ? 13.028 -56.863 6.570 1.00 15.06 ? 160 ILE A CB 1 ATOM 626 C CG1 . ILE A 1 78 ? 13.007 -57.878 7.718 1.00 15.28 ? 160 ILE A CG1 1 ATOM 627 C CG2 . ILE A 1 78 ? 13.596 -57.489 5.292 1.00 16.10 ? 160 ILE A CG2 1 ATOM 628 C CD1 . ILE A 1 78 ? 12.038 -59.063 7.482 1.00 11.05 ? 160 ILE A CD1 1 ATOM 629 N N . SER A 1 79 ? 12.077 -54.077 7.633 1.00 14.47 ? 161 SER A N 1 ATOM 630 C CA . SER A 1 79 ? 11.165 -53.457 8.588 1.00 14.31 ? 161 SER A CA 1 ATOM 631 C C . SER A 1 79 ? 9.746 -53.734 8.140 1.00 18.86 ? 161 SER A C 1 ATOM 632 O O . SER A 1 79 ? 9.500 -53.944 6.948 1.00 19.53 ? 161 SER A O 1 ATOM 633 C CB . SER A 1 79 ? 11.395 -51.949 8.677 1.00 16.66 ? 161 SER A CB 1 ATOM 634 O OG . SER A 1 79 ? 10.979 -51.290 7.494 1.00 18.34 ? 161 SER A OG 1 ATOM 635 N N . TRP A 1 80 ? 8.810 -53.740 9.087 1.00 22.77 ? 162 TRP A N 1 ATOM 636 C CA . TRP A 1 80 ? 7.420 -54.020 8.748 1.00 20.75 ? 162 TRP A CA 1 ATOM 637 C C . TRP A 1 80 ? 6.466 -53.390 9.765 1.00 19.62 ? 162 TRP A C 1 ATOM 638 O O . TRP A 1 80 ? 6.906 -52.987 10.848 1.00 19.65 ? 162 TRP A O 1 ATOM 639 C CB . TRP A 1 80 ? 7.206 -55.530 8.594 1.00 18.69 ? 162 TRP A CB 1 ATOM 640 C CG . TRP A 1 80 ? 7.342 -56.324 9.848 1.00 17.68 ? 162 TRP A CG 1 ATOM 641 C CD1 . TRP A 1 80 ? 6.330 -56.722 10.673 1.00 16.32 ? 162 TRP A CD1 1 ATOM 642 C CD2 . TRP A 1 80 ? 8.555 -56.846 10.415 1.00 15.06 ? 162 TRP A CD2 1 ATOM 643 N NE1 . TRP A 1 80 ? 6.834 -57.462 11.716 1.00 16.42 ? 162 TRP A NE1 1 ATOM 644 C CE2 . TRP A 1 80 ? 8.197 -57.552 11.582 1.00 17.83 ? 162 TRP A CE2 1 ATOM 645 C CE3 . TRP A 1 80 ? 9.908 -56.787 10.046 1.00 17.12 ? 162 TRP A CE3 1 ATOM 646 C CZ2 . TRP A 1 80 ? 9.142 -58.189 12.391 1.00 12.90 ? 162 TRP A CZ2 1 ATOM 647 C CZ3 . TRP A 1 80 ? 10.844 -57.423 10.844 1.00 16.11 ? 162 TRP A CZ3 1 ATOM 648 C CH2 . TRP A 1 80 ? 10.456 -58.118 12.005 1.00 19.32 ? 162 TRP A CH2 1 ATOM 649 N N . PRO A 1 81 ? 5.171 -53.262 9.409 1.00 21.15 ? 163 PRO A N 1 ATOM 650 C CA . PRO A 1 81 ? 4.244 -52.539 10.298 1.00 23.25 ? 163 PRO A CA 1 ATOM 651 C C . PRO A 1 81 ? 4.124 -53.142 11.695 1.00 21.34 ? 163 PRO A C 1 ATOM 652 O O . PRO A 1 81 ? 4.166 -54.368 11.839 1.00 18.56 ? 163 PRO A O 1 ATOM 653 C CB . PRO A 1 81 ? 2.902 -52.631 9.560 1.00 26.23 ? 163 PRO A CB 1 ATOM 654 C CG . PRO A 1 81 ? 3.288 -52.719 8.102 1.00 20.97 ? 163 PRO A CG 1 ATOM 655 C CD . PRO A 1 81 ? 4.563 -53.545 8.091 1.00 19.24 ? 163 PRO A CD 1 ATOM 656 N N . LEU A 1 82 ? 3.985 -52.271 12.698 1.00 23.56 ? 164 LEU A N 1 ATOM 657 C CA . LEU A 1 82 ? 3.940 -52.665 14.108 1.00 20.51 ? 164 LEU A CA 1 ATOM 658 C C . LEU A 1 82 ? 2.968 -53.819 14.342 1.00 18.51 ? 164 LEU A C 1 ATOM 659 O O . LEU A 1 82 ? 1.819 -53.767 13.897 1.00 17.68 ? 164 LEU A O 1 ATOM 660 C CB . LEU A 1 82 ? 3.539 -51.464 14.978 1.00 23.46 ? 164 LEU A CB 1 ATOM 661 C CG . LEU A 1 82 ? 3.899 -51.522 16.468 1.00 24.71 ? 164 LEU A CG 1 ATOM 662 C CD1 . LEU A 1 82 ? 5.376 -51.235 16.635 1.00 25.37 ? 164 LEU A CD1 1 ATOM 663 C CD2 . LEU A 1 82 ? 3.073 -50.530 17.263 1.00 26.44 ? 164 LEU A CD2 1 ATOM 664 N N . SER A 1 83 ? 3.458 -54.870 15.001 1.00 20.05 ? 165 SER A N 1 ATOM 665 C CA . SER A 1 83 ? 2.643 -56.021 15.413 1.00 18.49 ? 165 SER A CA 1 ATOM 666 C C . SER A 1 83 ? 2.133 -56.954 14.306 1.00 17.93 ? 165 SER A C 1 ATOM 667 O O . SER A 1 83 ? 1.518 -57.984 14.601 1.00 17.09 ? 165 SER A O 1 ATOM 668 C CB . SER A 1 83 ? 1.499 -55.592 16.332 1.00 20.66 ? 165 SER A CB 1 ATOM 669 O OG . SER A 1 83 ? 2.013 -55.051 17.532 1.00 17.20 ? 165 SER A OG 1 ATOM 670 N N A SER A 1 84 ? 2.384 -56.588 13.051 0.55 15.75 ? 166 SER A N 1 ATOM 671 N N B SER A 1 84 ? 2.362 -56.604 13.046 0.45 15.85 ? 166 SER A N 1 ATOM 672 C CA A SER A 1 84 ? 2.217 -57.520 11.946 0.55 17.39 ? 166 SER A CA 1 ATOM 673 C CA B SER A 1 84 ? 2.136 -57.570 11.983 0.45 17.39 ? 166 SER A CA 1 ATOM 674 C C A SER A 1 84 ? 3.430 -58.439 11.968 0.55 15.50 ? 166 SER A C 1 ATOM 675 C C B SER A 1 84 ? 3.400 -58.422 11.940 0.45 15.36 ? 166 SER A C 1 ATOM 676 O O A SER A 1 84 ? 4.452 -58.092 12.565 0.55 14.20 ? 166 SER A O 1 ATOM 677 O O B SER A 1 84 ? 4.430 -58.015 12.480 0.45 14.24 ? 166 SER A O 1 ATOM 678 C CB A SER A 1 84 ? 2.124 -56.773 10.610 0.55 17.58 ? 166 SER A CB 1 ATOM 679 C CB B SER A 1 84 ? 1.878 -56.871 10.646 0.45 17.58 ? 166 SER A CB 1 ATOM 680 O OG A SER A 1 84 ? 0.845 -56.190 10.427 0.55 13.82 ? 166 SER A OG 1 ATOM 681 O OG B SER A 1 84 ? 3.059 -56.285 10.133 0.45 17.04 ? 166 SER A OG 1 ATOM 682 N N . PRO A 1 85 ? 3.329 -59.620 11.335 1.00 17.40 ? 167 PRO A N 1 ATOM 683 C CA . PRO A 1 85 ? 4.531 -60.460 11.273 1.00 14.59 ? 167 PRO A CA 1 ATOM 684 C C . PRO A 1 85 ? 5.387 -60.077 10.060 1.00 15.65 ? 167 PRO A C 1 ATOM 685 O O . PRO A 1 85 ? 4.878 -59.437 9.131 1.00 13.21 ? 167 PRO A O 1 ATOM 686 C CB . PRO A 1 85 ? 3.951 -61.865 11.105 1.00 15.85 ? 167 PRO A CB 1 ATOM 687 C CG . PRO A 1 85 ? 2.704 -61.629 10.280 1.00 18.21 ? 167 PRO A CG 1 ATOM 688 C CD . PRO A 1 85 ? 2.151 -60.296 10.749 1.00 17.50 ? 167 PRO A CD 1 ATOM 689 N N . PRO A 1 86 ? 6.682 -60.440 10.069 1.00 20.19 ? 168 PRO A N 1 ATOM 690 C CA . PRO A 1 86 ? 7.485 -60.106 8.884 1.00 16.35 ? 168 PRO A CA 1 ATOM 691 C C . PRO A 1 86 ? 7.172 -61.047 7.721 1.00 18.97 ? 168 PRO A C 1 ATOM 692 O O . PRO A 1 86 ? 7.693 -62.161 7.681 1.00 23.06 ? 168 PRO A O 1 ATOM 693 C CB . PRO A 1 86 ? 8.927 -60.309 9.366 1.00 21.63 ? 168 PRO A CB 1 ATOM 694 C CG . PRO A 1 86 ? 8.823 -61.310 10.504 1.00 16.66 ? 168 PRO A CG 1 ATOM 695 C CD . PRO A 1 86 ? 7.478 -61.064 11.146 1.00 20.27 ? 168 PRO A CD 1 ATOM 696 N N . THR A 1 87 ? 6.329 -60.611 6.789 1.00 20.15 ? 169 THR A N 1 ATOM 697 C CA . THR A 1 87 ? 5.976 -61.450 5.648 1.00 20.48 ? 169 THR A CA 1 ATOM 698 C C . THR A 1 87 ? 6.742 -61.036 4.394 1.00 18.79 ? 169 THR A C 1 ATOM 699 O O . THR A 1 87 ? 7.296 -59.937 4.322 1.00 15.96 ? 169 THR A O 1 ATOM 700 C CB . THR A 1 87 ? 4.467 -61.399 5.353 1.00 24.23 ? 169 THR A CB 1 ATOM 701 O OG1 . THR A 1 87 ? 4.146 -60.159 4.707 1.00 18.24 ? 169 THR A OG1 1 ATOM 702 C CG2 . THR A 1 87 ? 3.667 -61.514 6.650 1.00 19.36 ? 169 THR A CG2 1 ATOM 703 N N . VAL A 1 88 ? 6.768 -61.926 3.410 1.00 18.68 ? 170 VAL A N 1 ATOM 704 C CA . VAL A 1 88 ? 7.399 -61.651 2.124 1.00 19.37 ? 170 VAL A CA 1 ATOM 705 C C . VAL A 1 88 ? 6.783 -60.420 1.447 1.00 19.52 ? 170 VAL A C 1 ATOM 706 O O . VAL A 1 88 ? 7.476 -59.658 0.771 1.00 24.61 ? 170 VAL A O 1 ATOM 707 C CB . VAL A 1 88 ? 7.283 -62.890 1.202 1.00 23.24 ? 170 VAL A CB 1 ATOM 708 C CG1 . VAL A 1 88 ? 7.796 -62.598 -0.210 1.00 19.24 ? 170 VAL A CG1 1 ATOM 709 C CG2 . VAL A 1 88 ? 8.037 -64.075 1.813 1.00 14.65 ? 170 VAL A CG2 1 ATOM 710 N N . TYR A 1 89 ? 5.488 -60.210 1.671 1.00 18.05 ? 171 TYR A N 1 ATOM 711 C CA . TYR A 1 89 ? 4.725 -59.193 0.939 1.00 19.16 ? 171 TYR A CA 1 ATOM 712 C C . TYR A 1 89 ? 4.569 -57.851 1.667 1.00 23.93 ? 171 TYR A C 1 ATOM 713 O O . TYR A 1 89 ? 4.158 -56.864 1.060 1.00 28.15 ? 171 TYR A O 1 ATOM 714 C CB . TYR A 1 89 ? 3.342 -59.756 0.563 1.00 17.79 ? 171 TYR A CB 1 ATOM 715 C CG . TYR A 1 89 ? 3.393 -61.215 0.152 1.00 18.29 ? 171 TYR A CG 1 ATOM 716 C CD1 . TYR A 1 89 ? 4.138 -61.618 -0.950 1.00 17.85 ? 171 TYR A CD1 1 ATOM 717 C CD2 . TYR A 1 89 ? 2.718 -62.190 0.882 1.00 15.22 ? 171 TYR A CD2 1 ATOM 718 C CE1 . TYR A 1 89 ? 4.204 -62.951 -1.326 1.00 17.37 ? 171 TYR A CE1 1 ATOM 719 C CE2 . TYR A 1 89 ? 2.771 -63.522 0.511 1.00 16.29 ? 171 TYR A CE2 1 ATOM 720 C CZ . TYR A 1 89 ? 3.521 -63.895 -0.593 1.00 17.53 ? 171 TYR A CZ 1 ATOM 721 O OH . TYR A 1 89 ? 3.589 -65.216 -0.976 1.00 18.90 ? 171 TYR A OH 1 ATOM 722 N N . ASN A 1 90 ? 4.894 -57.807 2.959 1.00 24.34 ? 172 ASN A N 1 ATOM 723 C CA . ASN A 1 90 ? 4.735 -56.573 3.736 1.00 27.66 ? 172 ASN A CA 1 ATOM 724 C C . ASN A 1 90 ? 6.051 -56.041 4.312 1.00 30.26 ? 172 ASN A C 1 ATOM 725 O O . ASN A 1 90 ? 6.070 -54.983 4.953 1.00 36.96 ? 172 ASN A O 1 ATOM 726 C CB . ASN A 1 90 ? 3.722 -56.776 4.876 1.00 28.63 ? 172 ASN A CB 1 ATOM 727 C CG . ASN A 1 90 ? 4.311 -57.562 6.052 1.00 37.95 ? 172 ASN A CG 1 ATOM 728 O OD1 . ASN A 1 90 ? 5.219 -58.380 5.868 1.00 34.27 ? 172 ASN A OD1 1 ATOM 729 N ND2 . ASN A 1 90 ? 3.789 -57.327 7.259 1.00 24.29 ? 172 ASN A ND2 1 ATOM 730 N N . SER A 1 91 ? 7.139 -56.783 4.104 1.00 15.62 ? 173 SER A N 1 ATOM 731 C CA . SER A 1 91 ? 8.450 -56.404 4.635 1.00 21.12 ? 173 SER A CA 1 ATOM 732 C C . SER A 1 91 ? 9.236 -55.533 3.656 1.00 29.44 ? 173 SER A C 1 ATOM 733 O O . SER A 1 91 ? 9.391 -55.883 2.489 1.00 29.49 ? 173 SER A O 1 ATOM 734 C CB . SER A 1 91 ? 9.273 -57.643 4.992 1.00 21.05 ? 173 SER A CB 1 ATOM 735 O OG . SER A 1 91 ? 8.649 -58.412 6.011 1.00 21.55 ? 173 SER A OG 1 ATOM 736 N N . ARG A 1 92 ? 9.734 -54.401 4.147 1.00 14.03 ? 174 ARG A N 1 ATOM 737 C CA . ARG A 1 92 ? 10.539 -53.483 3.344 1.00 20.81 ? 174 ARG A CA 1 ATOM 738 C C . ARG A 1 92 ? 12.019 -53.685 3.657 1.00 17.65 ? 174 ARG A C 1 ATOM 739 O O . ARG A 1 92 ? 12.410 -53.657 4.828 1.00 20.70 ? 174 ARG A O 1 ATOM 740 C CB . ARG A 1 92 ? 10.137 -52.042 3.667 1.00 18.47 ? 174 ARG A CB 1 ATOM 741 C CG . ARG A 1 92 ? 10.918 -50.959 2.943 1.00 27.79 ? 174 ARG A CG 1 ATOM 742 C CD . ARG A 1 92 ? 10.253 -49.601 3.159 1.00 34.55 ? 174 ARG A CD 1 ATOM 743 N NE . ARG A 1 92 ? 10.430 -49.110 4.526 1.00 32.56 ? 174 ARG A NE 1 ATOM 744 C CZ . ARG A 1 92 ? 9.564 -48.324 5.161 1.00 37.26 ? 174 ARG A CZ 1 ATOM 745 N NH1 . ARG A 1 92 ? 8.442 -47.942 4.558 1.00 30.09 ? 174 ARG A NH1 1 ATOM 746 N NH2 . ARG A 1 92 ? 9.814 -47.926 6.405 1.00 24.82 ? 174 ARG A NH2 1 ATOM 747 N N . VAL A 1 93 ? 12.846 -53.896 2.629 1.00 21.13 ? 175 VAL A N 1 ATOM 748 C CA . VAL A 1 93 ? 14.284 -54.081 2.865 1.00 18.20 ? 175 VAL A CA 1 ATOM 749 C C . VAL A 1 93 ? 14.984 -52.740 3.065 1.00 22.64 ? 175 VAL A C 1 ATOM 750 O O . VAL A 1 93 ? 14.925 -51.868 2.193 1.00 19.29 ? 175 VAL A O 1 ATOM 751 C CB . VAL A 1 93 ? 14.973 -54.869 1.736 1.00 19.94 ? 175 VAL A CB 1 ATOM 752 C CG1 . VAL A 1 93 ? 16.480 -54.980 2.007 1.00 17.67 ? 175 VAL A CG1 1 ATOM 753 C CG2 . VAL A 1 93 ? 14.375 -56.255 1.622 1.00 14.57 ? 175 VAL A CG2 1 ATOM 754 N N . GLU A 1 94 ? 15.632 -52.565 4.215 1.00 21.54 ? 176 GLU A N 1 ATOM 755 C CA . GLU A 1 94 ? 16.367 -51.326 4.481 1.00 18.56 ? 176 GLU A CA 1 ATOM 756 C C . GLU A 1 94 ? 17.781 -51.377 3.882 1.00 20.21 ? 176 GLU A C 1 ATOM 757 O O . GLU A 1 94 ? 18.259 -50.396 3.312 1.00 21.25 ? 176 GLU A O 1 ATOM 758 C CB . GLU A 1 94 ? 16.432 -51.041 5.987 1.00 24.55 ? 176 GLU A CB 1 ATOM 759 C CG . GLU A 1 94 ? 15.071 -51.043 6.704 1.00 23.30 ? 176 GLU A CG 1 ATOM 760 C CD . GLU A 1 94 ? 14.205 -49.834 6.365 1.00 31.07 ? 176 GLU A CD 1 ATOM 761 O OE1 . GLU A 1 94 ? 14.768 -48.751 6.088 1.00 31.47 ? 176 GLU A OE1 1 ATOM 762 O OE2 . GLU A 1 94 ? 12.958 -49.963 6.385 1.00 25.03 ? 176 GLU A OE2 1 ATOM 763 N N . CYS A 1 95 ? 18.442 -52.525 4.018 1.00 17.45 ? 177 CYS A N 1 ATOM 764 C CA . CYS A 1 95 ? 19.771 -52.745 3.432 1.00 17.33 ? 177 CYS A CA 1 ATOM 765 C C . CYS A 1 95 ? 20.156 -54.209 3.580 1.00 19.62 ? 177 CYS A C 1 ATOM 766 O O . CYS A 1 95 ? 19.483 -54.964 4.295 1.00 19.13 ? 177 CYS A O 1 ATOM 767 C CB . CYS A 1 95 ? 20.842 -51.830 4.057 1.00 16.80 ? 177 CYS A CB 1 ATOM 768 S SG . CYS A 1 95 ? 20.775 -51.651 5.867 1.00 27.36 ? 177 CYS A SG 1 ATOM 769 N N . ILE A 1 96 ? 21.236 -54.605 2.908 1.00 17.24 ? 178 ILE A N 1 ATOM 770 C CA . ILE A 1 96 ? 21.677 -55.999 2.883 1.00 13.98 ? 178 ILE A CA 1 ATOM 771 C C . ILE A 1 96 ? 22.831 -56.239 3.857 1.00 21.55 ? 178 ILE A C 1 ATOM 772 O O . ILE A 1 96 ? 23.808 -55.487 3.867 1.00 14.61 ? 178 ILE A O 1 ATOM 773 C CB . ILE A 1 96 ? 22.142 -56.405 1.468 1.00 13.92 ? 178 ILE A CB 1 ATOM 774 C CG1 . ILE A 1 96 ? 21.069 -56.060 0.434 1.00 15.14 ? 178 ILE A CG1 1 ATOM 775 C CG2 . ILE A 1 96 ? 22.501 -57.901 1.424 1.00 14.63 ? 178 ILE A CG2 1 ATOM 776 C CD1 . ILE A 1 96 ? 19.815 -56.911 0.552 1.00 13.06 ? 178 ILE A CD1 1 ATOM 777 N N . GLY A 1 97 ? 22.727 -57.291 4.667 1.00 18.88 ? 179 GLY A N 1 ATOM 778 C CA . GLY A 1 97 ? 23.766 -57.589 5.635 1.00 19.39 ? 179 GLY A CA 1 ATOM 779 C C . GLY A 1 97 ? 23.297 -58.459 6.784 1.00 18.08 ? 179 GLY A C 1 ATOM 780 O O . GLY A 1 97 ? 22.123 -58.852 6.849 1.00 17.82 ? 179 GLY A O 1 ATOM 781 N N . TRP A 1 98 ? 24.214 -58.749 7.700 1.00 18.19 ? 180 TRP A N 1 ATOM 782 C CA . TRP A 1 98 ? 23.928 -59.682 8.785 1.00 17.61 ? 180 TRP A CA 1 ATOM 783 C C . TRP A 1 98 ? 24.171 -59.090 10.174 1.00 20.28 ? 180 TRP A C 1 ATOM 784 O O . TRP A 1 98 ? 24.261 -59.828 11.163 1.00 17.93 ? 180 TRP A O 1 ATOM 785 C CB . TRP A 1 98 ? 24.712 -60.987 8.602 1.00 21.02 ? 180 TRP A CB 1 ATOM 786 C CG . TRP A 1 98 ? 26.109 -60.826 8.053 1.00 23.34 ? 180 TRP A CG 1 ATOM 787 C CD1 . TRP A 1 98 ? 26.569 -61.273 6.846 1.00 21.82 ? 180 TRP A CD1 1 ATOM 788 C CD2 . TRP A 1 98 ? 27.228 -60.204 8.703 1.00 20.90 ? 180 TRP A CD2 1 ATOM 789 N NE1 . TRP A 1 98 ? 27.903 -60.959 6.700 1.00 21.25 ? 180 TRP A NE1 1 ATOM 790 C CE2 . TRP A 1 98 ? 28.330 -60.302 7.825 1.00 21.81 ? 180 TRP A CE2 1 ATOM 791 C CE3 . TRP A 1 98 ? 27.403 -59.568 9.937 1.00 18.47 ? 180 TRP A CE3 1 ATOM 792 C CZ2 . TRP A 1 98 ? 29.592 -59.787 8.146 1.00 20.40 ? 180 TRP A CZ2 1 ATOM 793 C CZ3 . TRP A 1 98 ? 28.652 -59.053 10.253 1.00 20.01 ? 180 TRP A CZ3 1 ATOM 794 C CH2 . TRP A 1 98 ? 29.731 -59.168 9.363 1.00 20.31 ? 180 TRP A CH2 1 ATOM 795 N N . SER A 1 99 ? 24.287 -57.762 10.231 1.00 17.25 ? 181 SER A N 1 ATOM 796 C CA . SER A 1 99 ? 24.349 -57.015 11.489 1.00 15.85 ? 181 SER A CA 1 ATOM 797 C C . SER A 1 99 ? 23.879 -55.604 11.168 1.00 17.11 ? 181 SER A C 1 ATOM 798 O O . SER A 1 99 ? 24.211 -55.072 10.099 1.00 17.47 ? 181 SER A O 1 ATOM 799 C CB . SER A 1 99 ? 25.770 -56.976 12.042 1.00 13.71 ? 181 SER A CB 1 ATOM 800 O OG . SER A 1 99 ? 25.793 -56.427 13.356 1.00 14.44 ? 181 SER A OG 1 ATOM 801 N N . SER A 1 100 ? 23.108 -54.989 12.066 1.00 16.97 ? 182 SER A N 1 ATOM 802 C CA . SER A 1 100 ? 22.477 -53.716 11.712 1.00 14.51 ? 182 SER A CA 1 ATOM 803 C C . SER A 1 100 ? 22.157 -52.774 12.871 1.00 17.48 ? 182 SER A C 1 ATOM 804 O O . SER A 1 100 ? 22.180 -53.160 14.045 1.00 16.02 ? 182 SER A O 1 ATOM 805 C CB . SER A 1 100 ? 21.180 -53.975 10.941 1.00 17.60 ? 182 SER A CB 1 ATOM 806 O OG . SER A 1 100 ? 20.121 -54.305 11.832 1.00 19.27 ? 182 SER A OG 1 ATOM 807 N N . THR A 1 101 ? 21.877 -51.524 12.510 1.00 14.45 ? 183 THR A N 1 ATOM 808 C CA . THR A 1 101 ? 21.239 -50.564 13.399 1.00 14.79 ? 183 THR A CA 1 ATOM 809 C C . THR A 1 101 ? 20.434 -49.626 12.508 1.00 17.78 ? 183 THR A C 1 ATOM 810 O O . THR A 1 101 ? 20.637 -49.591 11.289 1.00 17.01 ? 183 THR A O 1 ATOM 811 C CB . THR A 1 101 ? 22.264 -49.766 14.255 1.00 21.15 ? 183 THR A CB 1 ATOM 812 O OG1 . THR A 1 101 ? 21.570 -49.002 15.252 1.00 19.64 ? 183 THR A OG1 1 ATOM 813 C CG2 . THR A 1 101 ? 23.089 -48.819 13.386 1.00 19.53 ? 183 THR A CG2 1 ATOM 814 N N . SER A 1 102 ? 19.510 -48.883 13.101 1.00 21.00 ? 184 SER A N 1 ATOM 815 C CA . SER A 1 102 ? 18.688 -47.952 12.339 1.00 15.96 ? 184 SER A CA 1 ATOM 816 C C . SER A 1 102 ? 18.090 -46.931 13.293 1.00 20.64 ? 184 SER A C 1 ATOM 817 O O . SER A 1 102 ? 17.761 -47.265 14.436 1.00 21.58 ? 184 SER A O 1 ATOM 818 C CB . SER A 1 102 ? 17.575 -48.704 11.590 1.00 15.43 ? 184 SER A CB 1 ATOM 819 O OG . SER A 1 102 ? 16.916 -47.874 10.640 1.00 14.71 ? 184 SER A OG 1 ATOM 820 N N . CYS A 1 103 ? 17.956 -45.689 12.837 1.00 21.85 ? 185 CYS A N 1 ATOM 821 C CA . CYS A 1 103 ? 17.274 -44.668 13.626 1.00 17.38 ? 185 CYS A CA 1 ATOM 822 C C . CYS A 1 103 ? 16.835 -43.501 12.746 1.00 16.38 ? 185 CYS A C 1 ATOM 823 O O . CYS A 1 103 ? 17.462 -43.215 11.725 1.00 20.27 ? 185 CYS A O 1 ATOM 824 C CB . CYS A 1 103 ? 18.163 -44.169 14.771 1.00 18.86 ? 185 CYS A CB 1 ATOM 825 S SG . CYS A 1 103 ? 19.874 -43.748 14.309 1.00 20.41 ? 185 CYS A SG 1 ATOM 826 N N . HIS A 1 104 ? 15.753 -42.836 13.143 1.00 20.09 ? 186 HIS A N 1 ATOM 827 C CA . HIS A 1 104 ? 15.290 -41.636 12.450 1.00 16.48 ? 186 HIS A CA 1 ATOM 828 C C . HIS A 1 104 ? 15.812 -40.406 13.188 1.00 20.76 ? 186 HIS A C 1 ATOM 829 O O . HIS A 1 104 ? 15.807 -40.381 14.423 1.00 18.16 ? 186 HIS A O 1 ATOM 830 C CB . HIS A 1 104 ? 13.763 -41.618 12.407 1.00 17.98 ? 186 HIS A CB 1 ATOM 831 C CG . HIS A 1 104 ? 13.194 -40.797 11.291 1.00 21.73 ? 186 HIS A CG 1 ATOM 832 N ND1 . HIS A 1 104 ? 13.111 -39.422 11.346 1.00 23.55 ? 186 HIS A ND1 1 ATOM 833 C CD2 . HIS A 1 104 ? 12.670 -41.157 10.093 1.00 23.47 ? 186 HIS A CD2 1 ATOM 834 C CE1 . HIS A 1 104 ? 12.563 -38.970 10.231 1.00 21.54 ? 186 HIS A CE1 1 ATOM 835 N NE2 . HIS A 1 104 ? 12.289 -40.003 9.454 1.00 20.83 ? 186 HIS A NE2 1 ATOM 836 N N . ASP A 1 105 ? 16.268 -39.391 12.448 1.00 22.30 ? 187 ASP A N 1 ATOM 837 C CA . ASP A 1 105 ? 16.781 -38.172 13.083 1.00 18.24 ? 187 ASP A CA 1 ATOM 838 C C . ASP A 1 105 ? 15.740 -37.054 13.186 1.00 21.69 ? 187 ASP A C 1 ATOM 839 O O . ASP A 1 105 ? 16.054 -35.944 13.625 1.00 22.46 ? 187 ASP A O 1 ATOM 840 C CB . ASP A 1 105 ? 18.060 -37.663 12.384 1.00 18.29 ? 187 ASP A CB 1 ATOM 841 C CG . ASP A 1 105 ? 17.844 -37.305 10.914 1.00 19.19 ? 187 ASP A CG 1 ATOM 842 O OD1 . ASP A 1 105 ? 16.684 -37.134 10.473 1.00 18.59 ? 187 ASP A OD1 1 ATOM 843 O OD2 . ASP A 1 105 ? 18.858 -37.182 10.188 1.00 22.17 ? 187 ASP A OD2 1 ATOM 844 N N . GLY A 1 106 ? 14.507 -37.350 12.780 1.00 21.89 ? 188 GLY A N 1 ATOM 845 C CA . GLY A 1 106 ? 13.438 -36.366 12.791 1.00 16.86 ? 188 GLY A CA 1 ATOM 846 C C . GLY A 1 106 ? 13.146 -35.883 11.381 1.00 22.73 ? 188 GLY A C 1 ATOM 847 O O . GLY A 1 106 ? 12.013 -35.499 11.069 1.00 25.37 ? 188 GLY A O 1 ATOM 848 N N . LYS A 1 107 ? 14.175 -35.892 10.533 1.00 25.26 ? 189 LYS A N 1 ATOM 849 C CA . LYS A 1 107 ? 14.016 -35.568 9.113 1.00 29.73 ? 189 LYS A CA 1 ATOM 850 C C . LYS A 1 107 ? 13.983 -36.837 8.261 1.00 26.46 ? 189 LYS A C 1 ATOM 851 O O . LYS A 1 107 ? 13.063 -37.040 7.461 1.00 23.64 ? 189 LYS A O 1 ATOM 852 C CB . LYS A 1 107 ? 15.150 -34.660 8.633 1.00 22.38 ? 189 LYS A CB 1 ATOM 853 C CG . LYS A 1 107 ? 15.114 -33.236 9.179 1.00 24.98 ? 189 LYS A CG 1 ATOM 854 C CD . LYS A 1 107 ? 16.230 -32.409 8.552 1.00 32.74 ? 189 LYS A CD 1 ATOM 855 C CE . LYS A 1 107 ? 16.217 -30.966 9.028 1.00 36.65 ? 189 LYS A CE 1 ATOM 856 N NZ . LYS A 1 107 ? 17.338 -30.171 8.428 1.00 32.81 ? 189 LYS A NZ 1 ATOM 857 N N . SER A 1 108 ? 14.994 -37.688 8.428 1.00 22.06 ? 190 SER A N 1 ATOM 858 C CA . SER A 1 108 ? 15.051 -38.952 7.693 1.00 22.67 ? 190 SER A CA 1 ATOM 859 C C . SER A 1 108 ? 15.683 -40.076 8.507 1.00 21.70 ? 190 SER A C 1 ATOM 860 O O . SER A 1 108 ? 16.294 -39.839 9.556 1.00 19.78 ? 190 SER A O 1 ATOM 861 C CB . SER A 1 108 ? 15.799 -38.787 6.368 1.00 21.47 ? 190 SER A CB 1 ATOM 862 O OG . SER A 1 108 ? 14.979 -38.168 5.400 1.00 32.86 ? 190 SER A OG 1 ATOM 863 N N . ARG A 1 109 ? 15.536 -41.299 8.009 1.00 23.16 ? 191 ARG A N 1 ATOM 864 C CA . ARG A 1 109 ? 16.054 -42.470 8.699 1.00 18.88 ? 191 ARG A CA 1 ATOM 865 C C . ARG A 1 109 ? 17.442 -42.861 8.203 1.00 22.49 ? 191 ARG A C 1 ATOM 866 O O . ARG A 1 109 ? 17.706 -42.886 6.990 1.00 18.87 ? 191 ARG A O 1 ATOM 867 C CB . ARG A 1 109 ? 15.090 -43.646 8.538 1.00 17.42 ? 191 ARG A CB 1 ATOM 868 C CG . ARG A 1 109 ? 15.621 -44.973 9.077 1.00 20.27 ? 191 ARG A CG 1 ATOM 869 C CD . ARG A 1 109 ? 14.480 -45.938 9.338 1.00 17.65 ? 191 ARG A CD 1 ATOM 870 N NE . ARG A 1 109 ? 13.637 -45.465 10.435 1.00 16.51 ? 191 ARG A NE 1 ATOM 871 C CZ . ARG A 1 109 ? 13.861 -45.754 11.716 1.00 19.16 ? 191 ARG A CZ 1 ATOM 872 N NH1 . ARG A 1 109 ? 14.896 -46.516 12.056 1.00 14.81 ? 191 ARG A NH1 1 ATOM 873 N NH2 . ARG A 1 109 ? 13.050 -45.293 12.657 1.00 20.50 ? 191 ARG A NH2 1 ATOM 874 N N . MET A 1 110 ? 18.332 -43.156 9.144 1.00 15.41 ? 192 MET A N 1 ATOM 875 C CA . MET A 1 110 ? 19.613 -43.765 8.802 1.00 18.98 ? 192 MET A CA 1 ATOM 876 C C . MET A 1 110 ? 19.533 -45.267 9.094 1.00 19.69 ? 192 MET A C 1 ATOM 877 O O . MET A 1 110 ? 19.057 -45.674 10.161 1.00 19.01 ? 192 MET A O 1 ATOM 878 C CB . MET A 1 110 ? 20.754 -43.122 9.604 1.00 16.84 ? 192 MET A CB 1 ATOM 879 C CG . MET A 1 110 ? 22.101 -43.794 9.385 1.00 18.84 ? 192 MET A CG 1 ATOM 880 S SD . MET A 1 110 ? 23.413 -43.178 10.463 1.00 20.66 ? 192 MET A SD 1 ATOM 881 C CE . MET A 1 110 ? 22.847 -43.786 12.072 1.00 18.49 ? 192 MET A CE 1 ATOM 882 N N . SER A 1 111 ? 19.965 -46.088 8.140 1.00 21.70 ? 193 SER A N 1 ATOM 883 C CA . SER A 1 111 ? 20.098 -47.524 8.375 1.00 18.86 ? 193 SER A CA 1 ATOM 884 C C . SER A 1 111 ? 21.503 -47.977 8.018 1.00 20.28 ? 193 SER A C 1 ATOM 885 O O . SER A 1 111 ? 22.077 -47.527 7.019 1.00 22.14 ? 193 SER A O 1 ATOM 886 C CB . SER A 1 111 ? 19.053 -48.324 7.588 1.00 17.29 ? 193 SER A CB 1 ATOM 887 O OG . SER A 1 111 ? 17.753 -48.055 8.074 1.00 18.98 ? 193 SER A OG 1 ATOM 888 N N . ILE A 1 112 ? 22.066 -48.853 8.846 1.00 21.83 ? 194 ILE A N 1 ATOM 889 C CA . ILE A 1 112 ? 23.409 -49.374 8.606 1.00 18.08 ? 194 ILE A CA 1 ATOM 890 C C . ILE A 1 112 ? 23.382 -50.901 8.632 1.00 21.51 ? 194 ILE A C 1 ATOM 891 O O . ILE A 1 112 ? 22.892 -51.502 9.599 1.00 22.92 ? 194 ILE A O 1 ATOM 892 C CB . ILE A 1 112 ? 24.423 -48.867 9.662 1.00 20.70 ? 194 ILE A CB 1 ATOM 893 C CG1 . ILE A 1 112 ? 24.396 -47.342 9.767 1.00 23.10 ? 194 ILE A CG1 1 ATOM 894 C CG2 . ILE A 1 112 ? 25.832 -49.332 9.329 1.00 18.67 ? 194 ILE A CG2 1 ATOM 895 C CD1 . ILE A 1 112 ? 25.376 -46.778 10.797 1.00 11.85 ? 194 ILE A CD1 1 ATOM 896 N N . CYS A 1 113 ? 23.893 -51.516 7.564 1.00 15.55 ? 195 CYS A N 1 ATOM 897 C CA . CYS A 1 113 ? 24.020 -52.970 7.470 1.00 19.60 ? 195 CYS A CA 1 ATOM 898 C C . CYS A 1 113 ? 25.466 -53.318 7.216 1.00 22.36 ? 195 CYS A C 1 ATOM 899 O O . CYS A 1 113 ? 26.140 -52.657 6.419 1.00 16.79 ? 195 CYS A O 1 ATOM 900 C CB . CYS A 1 113 ? 23.185 -53.522 6.311 1.00 20.37 ? 195 CYS A CB 1 ATOM 901 S SG . CYS A 1 113 ? 21.416 -53.447 6.584 1.00 29.06 ? 195 CYS A SG 1 ATOM 902 N N . ILE A 1 114 ? 25.943 -54.360 7.884 1.00 16.94 ? 196 ILE A N 1 ATOM 903 C CA . ILE A 1 114 ? 27.296 -54.848 7.654 1.00 16.46 ? 196 ILE A CA 1 ATOM 904 C C . ILE A 1 114 ? 27.209 -56.168 6.895 1.00 16.37 ? 196 ILE A C 1 ATOM 905 O O . ILE A 1 114 ? 26.328 -56.976 7.180 1.00 19.67 ? 196 ILE A O 1 ATOM 906 C CB . ILE A 1 114 ? 28.036 -55.022 8.996 1.00 15.05 ? 196 ILE A CB 1 ATOM 907 C CG1 . ILE A 1 114 ? 28.165 -53.658 9.678 1.00 15.36 ? 196 ILE A CG1 1 ATOM 908 C CG2 . ILE A 1 114 ? 29.416 -55.643 8.793 1.00 16.33 ? 196 ILE A CG2 1 ATOM 909 C CD1 . ILE A 1 114 ? 28.534 -53.720 11.144 1.00 16.33 ? 196 ILE A CD1 1 ATOM 910 N N . SER A 1 115 ? 28.091 -56.382 5.916 1.00 17.03 ? 197 SER A N 1 ATOM 911 C CA . SER A 1 115 ? 28.148 -57.669 5.218 1.00 17.20 ? 197 SER A CA 1 ATOM 912 C C . SER A 1 115 ? 29.594 -58.027 4.907 1.00 18.74 ? 197 SER A C 1 ATOM 913 O O . SER A 1 115 ? 30.499 -57.226 5.150 1.00 22.16 ? 197 SER A O 1 ATOM 914 C CB . SER A 1 115 ? 27.327 -57.647 3.917 1.00 16.47 ? 197 SER A CB 1 ATOM 915 O OG . SER A 1 115 ? 28.045 -57.032 2.858 1.00 19.38 ? 197 SER A OG 1 ATOM 916 N N . GLY A 1 116 ? 29.805 -59.225 4.365 1.00 16.32 ? 198 GLY A N 1 ATOM 917 C CA . GLY A 1 116 ? 31.133 -59.672 3.986 1.00 22.02 ? 198 GLY A CA 1 ATOM 918 C C . GLY A 1 116 ? 31.538 -60.931 4.726 1.00 21.92 ? 198 GLY A C 1 ATOM 919 O O . GLY A 1 116 ? 30.790 -61.428 5.574 1.00 22.03 ? 198 GLY A O 1 ATOM 920 N N . PRO A 1 117 ? 32.726 -61.461 4.406 1.00 19.93 ? 199 PRO A N 1 ATOM 921 C CA . PRO A 1 117 ? 33.272 -62.601 5.149 1.00 19.32 ? 199 PRO A CA 1 ATOM 922 C C . PRO A 1 117 ? 33.890 -62.090 6.449 1.00 22.75 ? 199 PRO A C 1 ATOM 923 O O . PRO A 1 117 ? 34.065 -60.867 6.588 1.00 16.49 ? 199 PRO A O 1 ATOM 924 C CB . PRO A 1 117 ? 34.359 -63.131 4.212 1.00 24.42 ? 199 PRO A CB 1 ATOM 925 C CG . PRO A 1 117 ? 34.857 -61.903 3.506 1.00 17.45 ? 199 PRO A CG 1 ATOM 926 C CD . PRO A 1 117 ? 33.636 -61.003 3.340 1.00 16.20 ? 199 PRO A CD 1 ATOM 927 N N . ASN A 1 118 ? 34.210 -62.995 7.373 1.00 21.76 ? 200 ASN A N 1 ATOM 928 C CA . ASN A 1 118 ? 34.714 -62.610 8.690 1.00 23.51 ? 200 ASN A CA 1 ATOM 929 C C . ASN A 1 118 ? 35.900 -61.648 8.651 1.00 22.63 ? 200 ASN A C 1 ATOM 930 O O . ASN A 1 118 ? 35.998 -60.741 9.484 1.00 24.61 ? 200 ASN A O 1 ATOM 931 C CB . ASN A 1 118 ? 35.064 -63.859 9.516 1.00 22.57 ? 200 ASN A CB 1 ATOM 932 C CG . ASN A 1 118 ? 33.833 -64.680 9.885 1.00 25.74 ? 200 ASN A CG 1 ATOM 933 O OD1 . ASN A 1 118 ? 32.735 -64.426 9.391 1.00 24.50 ? 200 ASN A OD1 1 ATOM 934 N ND2 . ASN A 1 118 ? 34.013 -65.664 10.761 1.00 33.59 ? 200 ASN A ND2 1 ATOM 935 N N . ASN A 1 119 ? 36.788 -61.834 7.677 1.00 17.54 ? 201 ASN A N 1 ATOM 936 C CA . ASN A 1 119 ? 38.022 -61.051 7.612 1.00 21.64 ? 201 ASN A CA 1 ATOM 937 C C . ASN A 1 119 ? 37.990 -59.868 6.641 1.00 21.89 ? 201 ASN A C 1 ATOM 938 O O . ASN A 1 119 ? 39.005 -59.206 6.433 1.00 22.87 ? 201 ASN A O 1 ATOM 939 C CB . ASN A 1 119 ? 39.222 -61.960 7.293 1.00 26.05 ? 201 ASN A CB 1 ATOM 940 C CG . ASN A 1 119 ? 39.132 -62.600 5.908 1.00 32.99 ? 201 ASN A CG 1 ATOM 941 O OD1 . ASN A 1 119 ? 38.230 -62.302 5.117 1.00 21.77 ? 201 ASN A OD1 1 ATOM 942 N ND2 . ASN A 1 119 ? 40.081 -63.485 5.609 1.00 23.15 ? 201 ASN A ND2 1 ATOM 943 N N . ASN A 1 120 ? 36.833 -59.601 6.043 1.00 22.65 ? 202 ASN A N 1 ATOM 944 C CA . ASN A 1 120 ? 36.744 -58.536 5.040 1.00 17.43 ? 202 ASN A CA 1 ATOM 945 C C . ASN A 1 120 ? 35.358 -57.884 5.014 1.00 23.45 ? 202 ASN A C 1 ATOM 946 O O . ASN A 1 120 ? 34.853 -57.526 3.948 1.00 21.97 ? 202 ASN A O 1 ATOM 947 C CB . ASN A 1 120 ? 37.103 -59.086 3.649 1.00 19.05 ? 202 ASN A CB 1 ATOM 948 C CG . ASN A 1 120 ? 38.345 -58.425 3.042 1.00 21.16 ? 202 ASN A CG 1 ATOM 949 O OD1 . ASN A 1 120 ? 38.783 -57.361 3.493 1.00 25.06 ? 202 ASN A OD1 1 ATOM 950 N ND2 . ASN A 1 120 ? 38.910 -59.060 2.003 1.00 24.05 ? 202 ASN A ND2 1 ATOM 951 N N . ALA A 1 121 ? 34.753 -57.723 6.192 1.00 20.90 ? 203 ALA A N 1 ATOM 952 C CA . ALA A 1 121 ? 33.410 -57.147 6.296 1.00 18.46 ? 203 ALA A CA 1 ATOM 953 C C . ALA A 1 121 ? 33.408 -55.629 6.138 1.00 20.34 ? 203 ALA A C 1 ATOM 954 O O . ALA A 1 121 ? 34.416 -54.966 6.402 1.00 20.39 ? 203 ALA A O 1 ATOM 955 C CB . ALA A 1 121 ? 32.756 -57.538 7.618 1.00 15.59 ? 203 ALA A CB 1 ATOM 956 N N . SER A 1 122 ? 32.268 -55.080 5.725 1.00 18.74 ? 204 SER A N 1 ATOM 957 C CA . SER A 1 122 ? 32.135 -53.639 5.559 1.00 20.00 ? 204 SER A CA 1 ATOM 958 C C . SER A 1 122 ? 30.727 -53.172 5.901 1.00 21.80 ? 204 SER A C 1 ATOM 959 O O . SER A 1 122 ? 29.745 -53.879 5.658 1.00 20.72 ? 204 SER A O 1 ATOM 960 C CB . SER A 1 122 ? 32.473 -53.228 4.128 1.00 17.93 ? 204 SER A CB 1 ATOM 961 O OG . SER A 1 122 ? 31.547 -53.795 3.214 1.00 20.56 ? 204 SER A OG 1 ATOM 962 N N . ALA A 1 123 ? 30.638 -51.970 6.456 1.00 17.02 ? 205 ALA A N 1 ATOM 963 C CA . ALA A 1 123 ? 29.354 -51.367 6.781 1.00 17.94 ? 205 ALA A CA 1 ATOM 964 C C . ALA A 1 123 ? 28.966 -50.406 5.673 1.00 23.61 ? 205 ALA A C 1 ATOM 965 O O . ALA A 1 123 ? 29.814 -49.667 5.166 1.00 20.77 ? 205 ALA A O 1 ATOM 966 C CB . ALA A 1 123 ? 29.445 -50.621 8.112 1.00 17.56 ? 205 ALA A CB 1 ATOM 967 N N . VAL A 1 124 ? 27.693 -50.418 5.289 1.00 14.60 ? 206 VAL A N 1 ATOM 968 C CA . VAL A 1 124 ? 27.182 -49.401 4.383 1.00 15.75 ? 206 VAL A CA 1 ATOM 969 C C . VAL A 1 124 ? 26.142 -48.577 5.127 1.00 18.65 ? 206 VAL A C 1 ATOM 970 O O . VAL A 1 124 ? 25.204 -49.126 5.717 1.00 15.64 ? 206 VAL A O 1 ATOM 971 C CB . VAL A 1 124 ? 26.579 -50.002 3.101 1.00 18.86 ? 206 VAL A CB 1 ATOM 972 C CG1 . VAL A 1 124 ? 26.122 -48.888 2.170 1.00 16.98 ? 206 VAL A CG1 1 ATOM 973 C CG2 . VAL A 1 124 ? 27.600 -50.882 2.401 1.00 12.26 ? 206 VAL A CG2 1 ATOM 974 N N . VAL A 1 125 ? 26.331 -47.261 5.126 1.00 20.21 ? 207 VAL A N 1 ATOM 975 C CA . VAL A 1 125 ? 25.413 -46.359 5.809 1.00 20.68 ? 207 VAL A CA 1 ATOM 976 C C . VAL A 1 125 ? 24.398 -45.785 4.820 1.00 21.92 ? 207 VAL A C 1 ATOM 977 O O . VAL A 1 125 ? 24.769 -45.072 3.883 1.00 22.27 ? 207 VAL A O 1 ATOM 978 C CB . VAL A 1 125 ? 26.164 -45.207 6.519 1.00 19.85 ? 207 VAL A CB 1 ATOM 979 C CG1 . VAL A 1 125 ? 25.184 -44.296 7.245 1.00 22.96 ? 207 VAL A CG1 1 ATOM 980 C CG2 . VAL A 1 125 ? 27.197 -45.763 7.509 1.00 20.87 ? 207 VAL A CG2 1 ATOM 981 N N . TRP A 1 126 ? 23.123 -46.107 5.028 1.00 20.45 ? 208 TRP A N 1 ATOM 982 C CA . TRP A 1 126 ? 22.034 -45.563 4.220 1.00 17.56 ? 208 TRP A CA 1 ATOM 983 C C . TRP A 1 126 ? 21.374 -44.396 4.938 1.00 20.28 ? 208 TRP A C 1 ATOM 984 O O . TRP A 1 126 ? 21.138 -44.470 6.143 1.00 19.63 ? 208 TRP A O 1 ATOM 985 C CB . TRP A 1 126 ? 20.988 -46.649 3.969 1.00 20.80 ? 208 TRP A CB 1 ATOM 986 C CG . TRP A 1 126 ? 21.512 -47.765 3.128 1.00 19.83 ? 208 TRP A CG 1 ATOM 987 C CD1 . TRP A 1 126 ? 22.520 -48.635 3.447 1.00 18.27 ? 208 TRP A CD1 1 ATOM 988 C CD2 . TRP A 1 126 ? 21.062 -48.135 1.821 1.00 22.23 ? 208 TRP A CD2 1 ATOM 989 N NE1 . TRP A 1 126 ? 22.723 -49.519 2.416 1.00 18.48 ? 208 TRP A NE1 1 ATOM 990 C CE2 . TRP A 1 126 ? 21.839 -49.237 1.407 1.00 22.13 ? 208 TRP A CE2 1 ATOM 991 C CE3 . TRP A 1 126 ? 20.077 -47.642 0.960 1.00 25.41 ? 208 TRP A CE3 1 ATOM 992 C CZ2 . TRP A 1 126 ? 21.662 -49.850 0.163 1.00 19.06 ? 208 TRP A CZ2 1 ATOM 993 C CZ3 . TRP A 1 126 ? 19.902 -48.255 -0.276 1.00 18.23 ? 208 TRP A CZ3 1 ATOM 994 C CH2 . TRP A 1 126 ? 20.691 -49.345 -0.659 1.00 18.16 ? 208 TRP A CH2 1 ATOM 995 N N . TYR A 1 127 ? 21.078 -43.327 4.199 1.00 21.47 ? 209 TYR A N 1 ATOM 996 C CA . TYR A 1 127 ? 20.300 -42.204 4.719 1.00 19.38 ? 209 TYR A CA 1 ATOM 997 C C . TYR A 1 127 ? 19.198 -41.844 3.722 1.00 22.64 ? 209 TYR A C 1 ATOM 998 O O . TYR A 1 127 ? 19.476 -41.640 2.534 1.00 16.82 ? 209 TYR A O 1 ATOM 999 C CB . TYR A 1 127 ? 21.191 -40.984 4.985 1.00 24.22 ? 209 TYR A CB 1 ATOM 1000 C CG . TYR A 1 127 ? 20.471 -39.877 5.722 1.00 24.83 ? 209 TYR A CG 1 ATOM 1001 C CD1 . TYR A 1 127 ? 20.158 -40.014 7.068 1.00 17.15 ? 209 TYR A CD1 1 ATOM 1002 C CD2 . TYR A 1 127 ? 20.094 -38.702 5.072 1.00 20.25 ? 209 TYR A CD2 1 ATOM 1003 C CE1 . TYR A 1 127 ? 19.499 -39.018 7.748 1.00 21.49 ? 209 TYR A CE1 1 ATOM 1004 C CE2 . TYR A 1 127 ? 19.427 -37.691 5.750 1.00 17.87 ? 209 TYR A CE2 1 ATOM 1005 C CZ . TYR A 1 127 ? 19.133 -37.860 7.088 1.00 20.44 ? 209 TYR A CZ 1 ATOM 1006 O OH . TYR A 1 127 ? 18.474 -36.874 7.787 1.00 22.85 ? 209 TYR A OH 1 ATOM 1007 N N . ASN A 1 128 ? 17.957 -41.768 4.208 1.00 19.31 ? 210 ASN A N 1 ATOM 1008 C CA . ASN A 1 128 ? 16.799 -41.511 3.350 1.00 22.47 ? 210 ASN A CA 1 ATOM 1009 C C . ASN A 1 128 ? 16.760 -42.502 2.189 1.00 22.74 ? 210 ASN A C 1 ATOM 1010 O O . ASN A 1 128 ? 16.598 -42.114 1.028 1.00 23.16 ? 210 ASN A O 1 ATOM 1011 C CB . ASN A 1 128 ? 16.793 -40.062 2.841 1.00 20.19 ? 210 ASN A CB 1 ATOM 1012 C CG . ASN A 1 128 ? 15.453 -39.650 2.229 1.00 27.79 ? 210 ASN A CG 1 ATOM 1013 O OD1 . ASN A 1 128 ? 14.394 -40.158 2.608 1.00 29.21 ? 210 ASN A OD1 1 ATOM 1014 N ND2 . ASN A 1 128 ? 15.501 -38.718 1.279 1.00 28.39 ? 210 ASN A ND2 1 ATOM 1015 N N . ARG A 1 129 ? 16.944 -43.780 2.526 1.00 24.27 ? 211 ARG A N 1 ATOM 1016 C CA . ARG A 1 129 ? 16.845 -44.902 1.583 1.00 28.24 ? 211 ARG A CA 1 ATOM 1017 C C . ARG A 1 129 ? 17.877 -44.897 0.440 1.00 27.02 ? 211 ARG A C 1 ATOM 1018 O O . ARG A 1 129 ? 17.662 -45.536 -0.593 1.00 26.63 ? 211 ARG A O 1 ATOM 1019 C CB . ARG A 1 129 ? 15.416 -45.030 1.025 1.00 31.12 ? 211 ARG A CB 1 ATOM 1020 C CG . ARG A 1 129 ? 14.308 -44.722 2.050 1.00 42.91 ? 211 ARG A CG 1 ATOM 1021 C CD . ARG A 1 129 ? 13.042 -45.551 1.823 1.00 39.31 ? 211 ARG A CD 1 ATOM 1022 N NE . ARG A 1 129 ? 12.906 -46.578 2.854 1.00 52.23 ? 211 ARG A NE 1 ATOM 1023 C CZ . ARG A 1 129 ? 13.388 -47.815 2.754 1.00 48.43 ? 211 ARG A CZ 1 ATOM 1024 N NH1 . ARG A 1 129 ? 14.031 -48.202 1.660 1.00 50.74 ? 211 ARG A NH1 1 ATOM 1025 N NH2 . ARG A 1 129 ? 13.228 -48.671 3.751 1.00 40.55 ? 211 ARG A NH2 1 ATOM 1026 N N . ARG A 1 130 ? 18.995 -44.196 0.635 1.00 20.19 ? 212 ARG A N 1 ATOM 1027 C CA . ARG A 1 130 ? 20.106 -44.218 -0.318 1.00 18.62 ? 212 ARG A CA 1 ATOM 1028 C C . ARG A 1 130 ? 21.427 -44.453 0.406 1.00 20.36 ? 212 ARG A C 1 ATOM 1029 O O . ARG A 1 130 ? 21.644 -43.914 1.493 1.00 19.55 ? 212 ARG A O 1 ATOM 1030 C CB . ARG A 1 130 ? 20.213 -42.885 -1.066 1.00 22.78 ? 212 ARG A CB 1 ATOM 1031 C CG . ARG A 1 130 ? 18.978 -42.458 -1.833 1.00 23.55 ? 212 ARG A CG 1 ATOM 1032 C CD . ARG A 1 130 ? 19.250 -41.138 -2.552 1.00 19.60 ? 212 ARG A CD 1 ATOM 1033 N NE . ARG A 1 130 ? 18.193 -40.794 -3.499 1.00 23.01 ? 212 ARG A NE 1 ATOM 1034 C CZ . ARG A 1 130 ? 17.192 -39.965 -3.227 1.00 29.84 ? 212 ARG A CZ 1 ATOM 1035 N NH1 . ARG A 1 130 ? 17.115 -39.393 -2.031 1.00 20.47 ? 212 ARG A NH1 1 ATOM 1036 N NH2 . ARG A 1 130 ? 16.272 -39.706 -4.149 1.00 25.02 ? 212 ARG A NH2 1 ATOM 1037 N N . PRO A 1 131 ? 22.332 -45.228 -0.211 1.00 24.77 ? 213 PRO A N 1 ATOM 1038 C CA . PRO A 1 131 ? 23.651 -45.457 0.392 1.00 20.68 ? 213 PRO A CA 1 ATOM 1039 C C . PRO A 1 131 ? 24.481 -44.175 0.352 1.00 24.35 ? 213 PRO A C 1 ATOM 1040 O O . PRO A 1 131 ? 24.544 -43.525 -0.699 1.00 20.13 ? 213 PRO A O 1 ATOM 1041 C CB . PRO A 1 131 ? 24.269 -46.529 -0.518 1.00 20.60 ? 213 PRO A CB 1 ATOM 1042 C CG . PRO A 1 131 ? 23.620 -46.300 -1.866 1.00 22.46 ? 213 PRO A CG 1 ATOM 1043 C CD . PRO A 1 131 ? 22.214 -45.830 -1.557 1.00 21.56 ? 213 PRO A CD 1 ATOM 1044 N N . VAL A 1 132 ? 25.101 -43.813 1.475 1.00 13.71 ? 214 VAL A N 1 ATOM 1045 C CA . VAL A 1 132 ? 25.811 -42.533 1.581 1.00 19.66 ? 214 VAL A CA 1 ATOM 1046 C C . VAL A 1 132 ? 27.294 -42.708 1.915 1.00 18.71 ? 214 VAL A C 1 ATOM 1047 O O . VAL A 1 132 ? 28.161 -42.109 1.273 1.00 24.18 ? 214 VAL A O 1 ATOM 1048 C CB . VAL A 1 132 ? 25.130 -41.587 2.610 1.00 17.05 ? 214 VAL A CB 1 ATOM 1049 C CG1 . VAL A 1 132 ? 26.031 -40.418 2.951 1.00 23.78 ? 214 VAL A CG1 1 ATOM 1050 C CG2 . VAL A 1 132 ? 23.814 -41.066 2.058 1.00 25.17 ? 214 VAL A CG2 1 ATOM 1051 N N . ALA A 1 133 ? 27.582 -43.537 2.914 1.00 20.68 ? 215 ALA A N 1 ATOM 1052 C CA . ALA A 1 133 ? 28.960 -43.775 3.337 1.00 19.73 ? 215 ALA A CA 1 ATOM 1053 C C . ALA A 1 133 ? 29.216 -45.262 3.581 1.00 24.60 ? 215 ALA A C 1 ATOM 1054 O O . ALA A 1 133 ? 28.272 -46.032 3.812 1.00 20.03 ? 215 ALA A O 1 ATOM 1055 C CB . ALA A 1 133 ? 29.281 -42.964 4.588 1.00 22.54 ? 215 ALA A CB 1 ATOM 1056 N N . GLU A 1 134 ? 30.492 -45.652 3.533 1.00 16.89 ? 216 GLU A N 1 ATOM 1057 C CA . GLU A 1 134 ? 30.901 -47.043 3.707 1.00 23.78 ? 216 GLU A CA 1 ATOM 1058 C C . GLU A 1 134 ? 32.096 -47.104 4.647 1.00 23.46 ? 216 GLU A C 1 ATOM 1059 O O . GLU A 1 134 ? 32.946 -46.207 4.639 1.00 20.98 ? 216 GLU A O 1 ATOM 1060 C CB . GLU A 1 134 ? 31.298 -47.677 2.368 1.00 20.47 ? 216 GLU A CB 1 ATOM 1061 C CG . GLU A 1 134 ? 30.295 -47.495 1.235 1.00 20.53 ? 216 GLU A CG 1 ATOM 1062 C CD . GLU A 1 134 ? 30.344 -46.102 0.634 1.00 23.87 ? 216 GLU A CD 1 ATOM 1063 O OE1 . GLU A 1 134 ? 31.466 -45.585 0.416 1.00 25.43 ? 216 GLU A OE1 1 ATOM 1064 O OE2 . GLU A 1 134 ? 29.260 -45.518 0.398 1.00 27.11 ? 216 GLU A OE2 1 ATOM 1065 N N . ILE A 1 135 ? 32.167 -48.166 5.447 1.00 21.07 ? 217 ILE A N 1 ATOM 1066 C CA . ILE A 1 135 ? 33.255 -48.333 6.409 1.00 21.96 ? 217 ILE A CA 1 ATOM 1067 C C . ILE A 1 135 ? 33.818 -49.746 6.315 1.00 23.37 ? 217 ILE A C 1 ATOM 1068 O O . ILE A 1 135 ? 33.083 -50.734 6.469 1.00 21.59 ? 217 ILE A O 1 ATOM 1069 C CB . ILE A 1 135 ? 32.784 -48.061 7.857 1.00 22.74 ? 217 ILE A CB 1 ATOM 1070 C CG1 . ILE A 1 135 ? 32.129 -46.680 7.954 1.00 23.85 ? 217 ILE A CG1 1 ATOM 1071 C CG2 . ILE A 1 135 ? 33.954 -48.162 8.837 1.00 20.17 ? 217 ILE A CG2 1 ATOM 1072 C CD1 . ILE A 1 135 ? 31.400 -46.428 9.256 1.00 26.19 ? 217 ILE A CD1 1 ATOM 1073 N N . ASN A 1 136 ? 35.116 -49.853 6.054 1.00 24.72 ? 218 ASN A N 1 ATOM 1074 C CA . ASN A 1 136 ? 35.738 -51.171 5.966 1.00 19.52 ? 218 ASN A CA 1 ATOM 1075 C C . ASN A 1 136 ? 36.146 -51.670 7.351 1.00 20.49 ? 218 ASN A C 1 ATOM 1076 O O . ASN A 1 136 ? 36.411 -50.870 8.253 1.00 19.02 ? 218 ASN A O 1 ATOM 1077 C CB . ASN A 1 136 ? 36.943 -51.146 5.023 1.00 15.95 ? 218 ASN A CB 1 ATOM 1078 C CG . ASN A 1 136 ? 37.319 -52.533 4.511 1.00 27.67 ? 218 ASN A CG 1 ATOM 1079 O OD1 . ASN A 1 136 ? 36.448 -53.356 4.206 1.00 24.57 ? 218 ASN A OD1 1 ATOM 1080 N ND2 . ASN A 1 136 ? 38.625 -52.800 4.419 1.00 25.23 ? 218 ASN A ND2 1 ATOM 1081 N N . THR A 1 137 ? 36.168 -52.990 7.518 1.00 18.98 ? 219 THR A N 1 ATOM 1082 C CA . THR A 1 137 ? 36.680 -53.616 8.739 1.00 21.04 ? 219 THR A CA 1 ATOM 1083 C C . THR A 1 137 ? 38.062 -53.056 9.124 1.00 21.00 ? 219 THR A C 1 ATOM 1084 O O . THR A 1 137 ? 38.920 -52.838 8.259 1.00 22.14 ? 219 THR A O 1 ATOM 1085 C CB . THR A 1 137 ? 36.721 -55.157 8.582 1.00 17.61 ? 219 THR A CB 1 ATOM 1086 O OG1 . THR A 1 137 ? 37.231 -55.767 9.774 1.00 19.47 ? 219 THR A OG1 1 ATOM 1087 C CG2 . THR A 1 137 ? 37.578 -55.562 7.386 1.00 19.00 ? 219 THR A CG2 1 ATOM 1088 N N . TRP A 1 138 ? 38.253 -52.787 10.417 1.00 24.45 ? 220 TRP A N 1 ATOM 1089 C CA . TRP A 1 138 ? 39.526 -52.268 10.917 1.00 25.01 ? 220 TRP A CA 1 ATOM 1090 C C . TRP A 1 138 ? 40.307 -53.308 11.731 1.00 25.71 ? 220 TRP A C 1 ATOM 1091 O O . TRP A 1 138 ? 41.503 -53.132 12.007 1.00 28.04 ? 220 TRP A O 1 ATOM 1092 C CB . TRP A 1 138 ? 39.325 -50.975 11.719 1.00 21.71 ? 220 TRP A CB 1 ATOM 1093 C CG . TRP A 1 138 ? 38.356 -51.085 12.854 1.00 23.83 ? 220 TRP A CG 1 ATOM 1094 C CD1 . TRP A 1 138 ? 38.610 -51.564 14.108 1.00 21.66 ? 220 TRP A CD1 1 ATOM 1095 C CD2 . TRP A 1 138 ? 36.976 -50.685 12.847 1.00 18.46 ? 220 TRP A CD2 1 ATOM 1096 N NE1 . TRP A 1 138 ? 37.471 -51.486 14.881 1.00 23.78 ? 220 TRP A NE1 1 ATOM 1097 C CE2 . TRP A 1 138 ? 36.453 -50.959 14.128 1.00 18.63 ? 220 TRP A CE2 1 ATOM 1098 C CE3 . TRP A 1 138 ? 36.135 -50.125 11.880 1.00 19.12 ? 220 TRP A CE3 1 ATOM 1099 C CZ2 . TRP A 1 138 ? 35.121 -50.689 14.468 1.00 16.32 ? 220 TRP A CZ2 1 ATOM 1100 C CZ3 . TRP A 1 138 ? 34.815 -49.857 12.214 1.00 15.31 ? 220 TRP A CZ3 1 ATOM 1101 C CH2 . TRP A 1 138 ? 34.322 -50.136 13.501 1.00 21.77 ? 220 TRP A CH2 1 ATOM 1102 N N . ALA A 1 139 ? 39.634 -54.400 12.087 1.00 21.19 ? 221 ALA A N 1 ATOM 1103 C CA . ALA A 1 139 ? 40.268 -55.479 12.843 1.00 26.49 ? 221 ALA A CA 1 ATOM 1104 C C . ALA A 1 139 ? 40.169 -56.829 12.125 1.00 26.71 ? 221 ALA A C 1 ATOM 1105 O O . ALA A 1 139 ? 40.743 -57.823 12.576 1.00 26.85 ? 221 ALA A O 1 ATOM 1106 C CB . ALA A 1 139 ? 39.665 -55.572 14.244 1.00 25.80 ? 221 ALA A CB 1 ATOM 1107 N N . ARG A 1 140 ? 39.425 -56.859 11.020 1.00 26.34 ? 222 ARG A N 1 ATOM 1108 C CA . ARG A 1 140 ? 39.311 -58.056 10.180 1.00 26.26 ? 222 ARG A CA 1 ATOM 1109 C C . ARG A 1 140 ? 38.788 -59.268 10.951 1.00 22.89 ? 222 ARG A C 1 ATOM 1110 O O . ARG A 1 140 ? 39.238 -60.398 10.746 1.00 22.21 ? 222 ARG A O 1 ATOM 1111 C CB . ARG A 1 140 ? 40.654 -58.371 9.500 1.00 25.40 ? 222 ARG A CB 1 ATOM 1112 C CG . ARG A 1 140 ? 41.371 -57.126 8.971 1.00 33.85 ? 222 ARG A CG 1 ATOM 1113 C CD . ARG A 1 140 ? 41.964 -57.345 7.593 1.00 42.36 ? 222 ARG A CD 1 ATOM 1114 N NE . ARG A 1 140 ? 41.592 -56.257 6.689 1.00 64.68 ? 222 ARG A NE 1 ATOM 1115 C CZ . ARG A 1 140 ? 42.129 -56.051 5.489 1.00 60.26 ? 222 ARG A CZ 1 ATOM 1116 N NH1 . ARG A 1 140 ? 43.079 -56.857 5.038 1.00 71.58 ? 222 ARG A NH1 1 ATOM 1117 N NH2 . ARG A 1 140 ? 41.723 -55.031 4.743 1.00 49.04 ? 222 ARG A NH2 1 ATOM 1118 N N . ASN A 1 141 ? 37.825 -59.033 11.833 1.00 17.24 ? 223 ASN A N 1 ATOM 1119 C CA . ASN A 1 141 ? 37.248 -60.122 12.610 1.00 19.35 ? 223 ASN A CA 1 ATOM 1120 C C . ASN A 1 141 ? 35.800 -59.812 12.962 1.00 23.47 ? 223 ASN A C 1 ATOM 1121 O O . ASN A 1 141 ? 35.494 -59.405 14.090 1.00 21.22 ? 223 ASN A O 1 ATOM 1122 C CB . ASN A 1 141 ? 38.085 -60.388 13.866 1.00 23.86 ? 223 ASN A CB 1 ATOM 1123 C CG . ASN A 1 141 ? 37.620 -61.612 14.635 1.00 27.22 ? 223 ASN A CG 1 ATOM 1124 O OD1 . ASN A 1 141 ? 36.705 -62.324 14.210 1.00 23.51 ? 223 ASN A OD1 1 ATOM 1125 N ND2 . ASN A 1 141 ? 38.259 -61.869 15.765 1.00 26.07 ? 223 ASN A ND2 1 ATOM 1126 N N . ILE A 1 142 ? 34.929 -60.009 11.973 1.00 22.67 ? 224 ILE A N 1 ATOM 1127 C CA . ILE A 1 142 ? 33.490 -59.792 12.098 1.00 25.92 ? 224 ILE A CA 1 ATOM 1128 C C . ILE A 1 142 ? 33.134 -58.388 12.583 1.00 20.38 ? 224 ILE A C 1 ATOM 1129 O O . ILE A 1 142 ? 32.683 -58.217 13.718 1.00 20.07 ? 224 ILE A O 1 ATOM 1130 C CB . ILE A 1 142 ? 32.817 -60.862 13.004 1.00 24.18 ? 224 ILE A CB 1 ATOM 1131 C CG1 . ILE A 1 142 ? 33.355 -62.258 12.670 1.00 26.78 ? 224 ILE A CG1 1 ATOM 1132 C CG2 . ILE A 1 142 ? 31.286 -60.803 12.869 1.00 14.75 ? 224 ILE A CG2 1 ATOM 1133 C CD1 . ILE A 1 142 ? 32.724 -63.385 13.483 1.00 24.08 ? 224 ILE A CD1 1 ATOM 1134 N N . LEU A 1 143 ? 33.352 -57.391 11.723 1.00 20.31 ? 225 LEU A N 1 ATOM 1135 C CA . LEU A 1 143 ? 32.852 -56.041 11.982 1.00 23.00 ? 225 LEU A CA 1 ATOM 1136 C C . LEU A 1 143 ? 31.352 -56.157 12.253 1.00 21.42 ? 225 LEU A C 1 ATOM 1137 O O . LEU A 1 143 ? 30.625 -56.790 11.483 1.00 15.62 ? 225 LEU A O 1 ATOM 1138 C CB . LEU A 1 143 ? 33.133 -55.123 10.785 1.00 19.89 ? 225 LEU A CB 1 ATOM 1139 C CG . LEU A 1 143 ? 32.442 -53.761 10.699 1.00 20.44 ? 225 LEU A CG 1 ATOM 1140 C CD1 . LEU A 1 143 ? 32.842 -52.869 11.855 1.00 18.06 ? 225 LEU A CD1 1 ATOM 1141 C CD2 . LEU A 1 143 ? 32.750 -53.080 9.366 1.00 22.12 ? 225 LEU A CD2 1 ATOM 1142 N N . ARG A 1 144 ? 30.895 -55.580 13.361 1.00 19.43 ? 226 ARG A N 1 ATOM 1143 C CA . ARG A 1 144 ? 29.524 -55.806 13.808 1.00 14.94 ? 226 ARG A CA 1 ATOM 1144 C C . ARG A 1 144 ? 29.005 -54.660 14.661 1.00 17.99 ? 226 ARG A C 1 ATOM 1145 O O . ARG A 1 144 ? 29.790 -53.879 15.208 1.00 21.72 ? 226 ARG A O 1 ATOM 1146 C CB . ARG A 1 144 ? 29.442 -57.125 14.578 1.00 17.05 ? 226 ARG A CB 1 ATOM 1147 C CG . ARG A 1 144 ? 30.366 -57.200 15.790 1.00 16.54 ? 226 ARG A CG 1 ATOM 1148 C CD . ARG A 1 144 ? 30.545 -58.651 16.237 1.00 18.30 ? 226 ARG A CD 1 ATOM 1149 N NE . ARG A 1 144 ? 31.372 -58.803 17.438 1.00 16.95 ? 226 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 144 ? 32.698 -58.936 17.432 1.00 23.86 ? 226 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 144 ? 33.375 -58.900 16.285 1.00 16.77 ? 226 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 144 ? 33.352 -59.093 18.579 1.00 19.88 ? 226 ARG A NH2 1 ATOM 1153 N N . THR A 1 145 ? 27.682 -54.563 14.783 1.00 18.50 ? 227 THR A N 1 ATOM 1154 C CA . THR A 1 145 ? 27.078 -53.426 15.470 1.00 15.10 ? 227 THR A CA 1 ATOM 1155 C C . THR A 1 145 ? 25.890 -53.793 16.380 1.00 14.16 ? 227 THR A C 1 ATOM 1156 O O . THR A 1 145 ? 25.760 -54.947 16.806 1.00 20.21 ? 227 THR A O 1 ATOM 1157 C CB . THR A 1 145 ? 26.741 -52.283 14.470 1.00 19.30 ? 227 THR A CB 1 ATOM 1158 O OG1 . THR A 1 145 ? 26.429 -51.081 15.185 1.00 17.37 ? 227 THR A OG1 1 ATOM 1159 C CG2 . THR A 1 145 ? 25.585 -52.670 13.530 1.00 16.05 ? 227 THR A CG2 1 ATOM 1160 N N . GLN A 1 146 ? 25.032 -52.815 16.665 1.00 18.17 ? 228 GLN A N 1 ATOM 1161 C CA . GLN A 1 146 ? 24.101 -52.877 17.801 1.00 14.58 ? 228 GLN A CA 1 ATOM 1162 C C . GLN A 1 146 ? 22.987 -53.938 17.802 1.00 17.23 ? 228 GLN A C 1 ATOM 1163 O O . GLN A 1 146 ? 22.712 -54.530 18.851 1.00 17.12 ? 228 GLN A O 1 ATOM 1164 C CB . GLN A 1 146 ? 23.490 -51.492 18.047 1.00 14.51 ? 228 GLN A CB 1 ATOM 1165 C CG . GLN A 1 146 ? 24.513 -50.437 18.459 1.00 16.93 ? 228 GLN A CG 1 ATOM 1166 C CD . GLN A 1 146 ? 23.886 -49.072 18.679 1.00 22.35 ? 228 GLN A CD 1 ATOM 1167 O OE1 . GLN A 1 146 ? 24.586 -48.059 18.750 1.00 23.06 ? 228 GLN A OE1 1 ATOM 1168 N NE2 . GLN A 1 146 ? 22.557 -49.038 18.790 1.00 20.04 ? 228 GLN A NE2 1 ATOM 1169 N N . GLU A 1 147 ? 22.351 -54.166 16.650 1.00 16.16 ? 229 GLU A N 1 ATOM 1170 C CA . GLU A 1 147 ? 21.151 -55.025 16.532 1.00 16.65 ? 229 GLU A CA 1 ATOM 1171 C C . GLU A 1 147 ? 19.935 -54.445 17.263 1.00 18.96 ? 229 GLU A C 1 ATOM 1172 O O . GLU A 1 147 ? 18.992 -55.173 17.595 1.00 20.90 ? 229 GLU A O 1 ATOM 1173 C CB . GLU A 1 147 ? 21.390 -56.484 16.982 1.00 18.61 ? 229 GLU A CB 1 ATOM 1174 C CG . GLU A 1 147 ? 22.776 -57.076 16.673 1.00 18.60 ? 229 GLU A CG 1 ATOM 1175 C CD . GLU A 1 147 ? 23.083 -57.235 15.183 1.00 18.79 ? 229 GLU A CD 1 ATOM 1176 O OE1 . GLU A 1 147 ? 22.263 -56.830 14.326 1.00 18.76 ? 229 GLU A OE1 1 ATOM 1177 O OE2 . GLU A 1 147 ? 24.173 -57.769 14.865 1.00 17.52 ? 229 GLU A OE2 1 ATOM 1178 N N . SER A 1 148 ? 19.973 -53.140 17.526 1.00 15.63 ? 230 SER A N 1 ATOM 1179 C CA . SER A 1 148 ? 18.787 -52.392 17.948 1.00 16.93 ? 230 SER A CA 1 ATOM 1180 C C . SER A 1 148 ? 18.961 -50.943 17.515 1.00 17.38 ? 230 SER A C 1 ATOM 1181 O O . SER A 1 148 ? 20.004 -50.588 16.961 1.00 15.38 ? 230 SER A O 1 ATOM 1182 C CB . SER A 1 148 ? 18.511 -52.516 19.456 1.00 15.10 ? 230 SER A CB 1 ATOM 1183 O OG . SER A 1 148 ? 19.589 -52.054 20.258 1.00 17.46 ? 230 SER A OG 1 ATOM 1184 N N . GLU A 1 149 ? 17.948 -50.110 17.743 1.00 17.69 ? 231 GLU A N 1 ATOM 1185 C CA . GLU A 1 149 ? 17.968 -48.757 17.186 1.00 17.44 ? 231 GLU A CA 1 ATOM 1186 C C . GLU A 1 149 ? 19.070 -47.876 17.770 1.00 22.54 ? 231 GLU A C 1 ATOM 1187 O O . GLU A 1 149 ? 19.477 -48.052 18.925 1.00 18.02 ? 231 GLU A O 1 ATOM 1188 C CB . GLU A 1 149 ? 16.602 -48.065 17.309 1.00 16.12 ? 231 GLU A CB 1 ATOM 1189 C CG . GLU A 1 149 ? 16.311 -47.431 18.668 1.00 17.09 ? 231 GLU A CG 1 ATOM 1190 C CD . GLU A 1 149 ? 15.073 -46.541 18.645 1.00 22.70 ? 231 GLU A CD 1 ATOM 1191 O OE1 . GLU A 1 149 ? 14.377 -46.511 17.602 1.00 19.34 ? 231 GLU A OE1 1 ATOM 1192 O OE2 . GLU A 1 149 ? 14.793 -45.870 19.670 1.00 19.98 ? 231 GLU A OE2 1 ATOM 1193 N N . CYS A 1 150 ? 19.573 -46.954 16.950 1.00 17.87 ? 232 CYS A N 1 ATOM 1194 C CA . CYS A 1 150 ? 20.468 -45.914 17.440 1.00 22.03 ? 232 CYS A CA 1 ATOM 1195 C C . CYS A 1 150 ? 19.596 -44.744 17.896 1.00 20.91 ? 232 CYS A C 1 ATOM 1196 O O . CYS A 1 150 ? 18.366 -44.845 17.886 1.00 19.29 ? 232 CYS A O 1 ATOM 1197 C CB . CYS A 1 150 ? 21.480 -45.492 16.362 1.00 22.36 ? 232 CYS A CB 1 ATOM 1198 S SG . CYS A 1 150 ? 20.876 -45.497 14.624 1.00 23.45 ? 232 CYS A SG 1 ATOM 1199 N N . VAL A 1 151 ? 20.218 -43.646 18.314 1.00 15.88 ? 233 VAL A N 1 ATOM 1200 C CA . VAL A 1 151 ? 19.466 -42.483 18.782 1.00 20.53 ? 233 VAL A CA 1 ATOM 1201 C C . VAL A 1 151 ? 20.119 -41.227 18.231 1.00 23.24 ? 233 VAL A C 1 ATOM 1202 O O . VAL A 1 151 ? 21.343 -41.169 18.112 1.00 24.61 ? 233 VAL A O 1 ATOM 1203 C CB . VAL A 1 151 ? 19.438 -42.389 20.331 1.00 21.88 ? 233 VAL A CB 1 ATOM 1204 C CG1 . VAL A 1 151 ? 18.542 -41.231 20.779 1.00 21.58 ? 233 VAL A CG1 1 ATOM 1205 C CG2 . VAL A 1 151 ? 18.940 -43.682 20.939 1.00 23.18 ? 233 VAL A CG2 1 ATOM 1206 N N . CYS A 1 152 ? 19.315 -40.220 17.901 1.00 18.32 ? 234 CYS A N 1 ATOM 1207 C CA . CYS A 1 152 ? 19.858 -39.008 17.308 1.00 20.42 ? 234 CYS A CA 1 ATOM 1208 C C . CYS A 1 152 ? 19.602 -37.781 18.177 1.00 25.56 ? 234 CYS A C 1 ATOM 1209 O O . CYS A 1 152 ? 18.642 -37.740 18.962 1.00 20.13 ? 234 CYS A O 1 ATOM 1210 C CB . CYS A 1 152 ? 19.280 -38.796 15.905 1.00 21.98 ? 234 CYS A CB 1 ATOM 1211 S SG . CYS A 1 152 ? 19.594 -40.187 14.790 1.00 22.93 ? 234 CYS A SG 1 ATOM 1212 N N . HIS A 1 153 ? 20.474 -36.788 18.045 1.00 18.86 ? 235 HIS A N 1 ATOM 1213 C CA . HIS A 1 153 ? 20.231 -35.484 18.664 1.00 21.66 ? 235 HIS A CA 1 ATOM 1214 C C . HIS A 1 153 ? 20.747 -34.365 17.759 1.00 19.41 ? 235 HIS A C 1 ATOM 1215 O O . HIS A 1 153 ? 21.946 -34.302 17.451 1.00 20.85 ? 235 HIS A O 1 ATOM 1216 C CB . HIS A 1 153 ? 20.879 -35.395 20.049 1.00 21.30 ? 235 HIS A CB 1 ATOM 1217 C CG . HIS A 1 153 ? 20.740 -34.051 20.686 1.00 24.66 ? 235 HIS A CG 1 ATOM 1218 N ND1 . HIS A 1 153 ? 19.589 -33.649 21.340 1.00 24.76 ? 235 HIS A ND1 1 ATOM 1219 C CD2 . HIS A 1 153 ? 21.591 -33.001 20.760 1.00 27.21 ? 235 HIS A CD2 1 ATOM 1220 C CE1 . HIS A 1 153 ? 19.745 -32.423 21.791 1.00 27.57 ? 235 HIS A CE1 1 ATOM 1221 N NE2 . HIS A 1 153 ? 20.955 -32.003 21.453 1.00 28.53 ? 235 HIS A NE2 1 ATOM 1222 N N . ASN A 1 154 ? 19.830 -33.498 17.334 1.00 20.89 ? 236 ASN A N 1 ATOM 1223 C CA . ASN A 1 154 ? 20.135 -32.423 16.395 1.00 24.73 ? 236 ASN A CA 1 ATOM 1224 C C . ASN A 1 154 ? 20.862 -32.912 15.139 1.00 25.11 ? 236 ASN A C 1 ATOM 1225 O O . ASN A 1 154 ? 21.800 -32.268 14.664 1.00 21.46 ? 236 ASN A O 1 ATOM 1226 C CB . ASN A 1 154 ? 20.938 -31.307 17.077 1.00 24.94 ? 236 ASN A CB 1 ATOM 1227 C CG . ASN A 1 154 ? 20.864 -29.994 16.317 1.00 32.98 ? 236 ASN A CG 1 ATOM 1228 O OD1 . ASN A 1 154 ? 19.933 -29.771 15.543 1.00 29.17 ? 236 ASN A OD1 1 ATOM 1229 N ND2 . ASN A 1 154 ? 21.847 -29.122 16.529 1.00 35.01 ? 236 ASN A ND2 1 ATOM 1230 N N . GLY A 1 155 ? 20.433 -34.055 14.610 1.00 26.22 ? 237 GLY A N 1 ATOM 1231 C CA . GLY A 1 155 ? 21.026 -34.597 13.395 1.00 25.58 ? 237 GLY A CA 1 ATOM 1232 C C . GLY A 1 155 ? 22.178 -35.565 13.620 1.00 25.09 ? 237 GLY A C 1 ATOM 1233 O O . GLY A 1 155 ? 22.559 -36.306 12.706 1.00 25.74 ? 237 GLY A O 1 ATOM 1234 N N . VAL A 1 156 ? 22.740 -35.564 14.828 1.00 20.37 ? 238 VAL A N 1 ATOM 1235 C CA . VAL A 1 156 ? 23.896 -36.409 15.120 1.00 23.30 ? 238 VAL A CA 1 ATOM 1236 C C . VAL A 1 156 ? 23.458 -37.739 15.714 1.00 20.04 ? 238 VAL A C 1 ATOM 1237 O O . VAL A 1 156 ? 22.863 -37.774 16.796 1.00 17.20 ? 238 VAL A O 1 ATOM 1238 C CB . VAL A 1 156 ? 24.870 -35.732 16.100 1.00 22.32 ? 238 VAL A CB 1 ATOM 1239 C CG1 . VAL A 1 156 ? 25.998 -36.695 16.466 1.00 16.63 ? 238 VAL A CG1 1 ATOM 1240 C CG2 . VAL A 1 156 ? 25.430 -34.452 15.490 1.00 25.49 ? 238 VAL A CG2 1 ATOM 1241 N N . CYS A 1 157 ? 23.763 -38.831 15.018 1.00 22.91 ? 239 CYS A N 1 ATOM 1242 C CA . CYS A 1 157 ? 23.349 -40.157 15.474 1.00 21.37 ? 239 CYS A CA 1 ATOM 1243 C C . CYS A 1 157 ? 24.553 -41.041 15.760 1.00 21.55 ? 239 CYS A C 1 ATOM 1244 O O . CYS A 1 157 ? 25.134 -41.615 14.840 1.00 19.74 ? 239 CYS A O 1 ATOM 1245 C CB . CYS A 1 157 ? 22.475 -40.840 14.420 1.00 19.93 ? 239 CYS A CB 1 ATOM 1246 S SG . CYS A 1 157 ? 21.244 -39.755 13.682 1.00 23.90 ? 239 CYS A SG 1 ATOM 1247 N N . PRO A 1 158 ? 24.928 -41.159 17.041 1.00 23.73 ? 240 PRO A N 1 ATOM 1248 C CA . PRO A 1 158 ? 26.038 -42.034 17.438 1.00 22.41 ? 240 PRO A CA 1 ATOM 1249 C C . PRO A 1 158 ? 25.693 -43.515 17.264 1.00 18.96 ? 240 PRO A C 1 ATOM 1250 O O . PRO A 1 158 ? 24.537 -43.899 17.475 1.00 19.33 ? 240 PRO A O 1 ATOM 1251 C CB . PRO A 1 158 ? 26.220 -41.711 18.929 1.00 18.73 ? 240 PRO A CB 1 ATOM 1252 C CG . PRO A 1 158 ? 25.554 -40.351 19.121 1.00 27.83 ? 240 PRO A CG 1 ATOM 1253 C CD . PRO A 1 158 ? 24.394 -40.389 18.177 1.00 24.17 ? 240 PRO A CD 1 ATOM 1254 N N . VAL A 1 159 ? 26.680 -44.325 16.876 1.00 19.49 ? 241 VAL A N 1 ATOM 1255 C CA . VAL A 1 159 ? 26.511 -45.775 16.736 1.00 20.01 ? 241 VAL A CA 1 ATOM 1256 C C . VAL A 1 159 ? 27.739 -46.503 17.292 1.00 19.78 ? 241 VAL A C 1 ATOM 1257 O O . VAL A 1 159 ? 28.878 -46.092 17.039 1.00 20.50 ? 241 VAL A O 1 ATOM 1258 C CB . VAL A 1 159 ? 26.344 -46.212 15.252 1.00 20.58 ? 241 VAL A CB 1 ATOM 1259 C CG1 . VAL A 1 159 ? 26.215 -47.733 15.156 1.00 15.35 ? 241 VAL A CG1 1 ATOM 1260 C CG2 . VAL A 1 159 ? 25.149 -45.537 14.597 1.00 15.29 ? 241 VAL A CG2 1 ATOM 1261 N N . VAL A 1 160 ? 27.523 -47.590 18.030 1.00 19.93 ? 242 VAL A N 1 ATOM 1262 C CA . VAL A 1 160 ? 28.650 -48.360 18.559 1.00 14.68 ? 242 VAL A CA 1 ATOM 1263 C C . VAL A 1 160 ? 28.955 -49.548 17.646 1.00 23.64 ? 242 VAL A C 1 ATOM 1264 O O . VAL A 1 160 ? 28.042 -50.280 17.255 1.00 19.55 ? 242 VAL A O 1 ATOM 1265 C CB . VAL A 1 160 ? 28.365 -48.859 19.996 1.00 18.19 ? 242 VAL A CB 1 ATOM 1266 C CG1 . VAL A 1 160 ? 29.618 -49.494 20.613 1.00 19.35 ? 242 VAL A CG1 1 ATOM 1267 C CG2 . VAL A 1 160 ? 27.863 -47.707 20.859 1.00 15.04 ? 242 VAL A CG2 1 ATOM 1268 N N . PHE A 1 161 ? 30.232 -49.725 17.302 1.00 17.07 ? 243 PHE A N 1 ATOM 1269 C CA . PHE A 1 161 ? 30.679 -50.861 16.502 1.00 19.04 ? 243 PHE A CA 1 ATOM 1270 C C . PHE A 1 161 ? 31.751 -51.615 17.280 1.00 24.43 ? 243 PHE A C 1 ATOM 1271 O O . PHE A 1 161 ? 32.511 -51.018 18.047 1.00 26.02 ? 243 PHE A O 1 ATOM 1272 C CB . PHE A 1 161 ? 31.312 -50.405 15.182 1.00 19.88 ? 243 PHE A CB 1 ATOM 1273 C CG . PHE A 1 161 ? 30.371 -49.691 14.229 1.00 22.85 ? 243 PHE A CG 1 ATOM 1274 C CD1 . PHE A 1 161 ? 30.123 -48.330 14.362 1.00 24.77 ? 243 PHE A CD1 1 ATOM 1275 C CD2 . PHE A 1 161 ? 29.796 -50.371 13.158 1.00 23.10 ? 243 PHE A CD2 1 ATOM 1276 C CE1 . PHE A 1 161 ? 29.290 -47.663 13.471 1.00 18.85 ? 243 PHE A CE1 1 ATOM 1277 C CE2 . PHE A 1 161 ? 28.956 -49.714 12.256 1.00 27.27 ? 243 PHE A CE2 1 ATOM 1278 C CZ . PHE A 1 161 ? 28.701 -48.356 12.413 1.00 21.42 ? 243 PHE A CZ 1 ATOM 1279 N N . THR A 1 162 ? 31.829 -52.924 17.070 1.00 19.33 ? 244 THR A N 1 ATOM 1280 C CA . THR A 1 162 ? 32.964 -53.701 17.551 1.00 15.90 ? 244 THR A CA 1 ATOM 1281 C C . THR A 1 162 ? 33.559 -54.471 16.373 1.00 23.78 ? 244 THR A C 1 ATOM 1282 O O . THR A 1 162 ? 32.838 -54.904 15.472 1.00 22.75 ? 244 THR A O 1 ATOM 1283 C CB . THR A 1 162 ? 32.557 -54.672 18.689 1.00 19.23 ? 244 THR A CB 1 ATOM 1284 O OG1 . THR A 1 162 ? 32.058 -53.915 19.799 1.00 17.47 ? 244 THR A OG1 1 ATOM 1285 C CG2 . THR A 1 162 ? 33.750 -55.512 19.158 1.00 22.14 ? 244 THR A CG2 1 ATOM 1286 N N . ASP A 1 163 ? 34.879 -54.610 16.367 1.00 22.13 ? 245 ASP A N 1 ATOM 1287 C CA . ASP A 1 163 ? 35.555 -55.438 15.379 1.00 23.35 ? 245 ASP A CA 1 ATOM 1288 C C . ASP A 1 163 ? 36.712 -56.103 16.120 1.00 23.27 ? 245 ASP A C 1 ATOM 1289 O O . ASP A 1 163 ? 37.465 -55.427 16.832 1.00 23.71 ? 245 ASP A O 1 ATOM 1290 C CB . ASP A 1 163 ? 36.051 -54.578 14.209 1.00 16.26 ? 245 ASP A CB 1 ATOM 1291 C CG . ASP A 1 163 ? 36.442 -55.403 12.986 1.00 24.76 ? 245 ASP A CG 1 ATOM 1292 O OD1 . ASP A 1 163 ? 36.553 -56.645 13.096 1.00 23.49 ? 245 ASP A OD1 1 ATOM 1293 O OD2 . ASP A 1 163 ? 36.661 -54.801 11.909 1.00 20.62 ? 245 ASP A OD2 1 ATOM 1294 N N . GLY A 1 164 ? 36.827 -57.424 15.987 1.00 19.07 ? 246 GLY A N 1 ATOM 1295 C CA . GLY A 1 164 ? 37.837 -58.176 16.712 1.00 24.70 ? 246 GLY A CA 1 ATOM 1296 C C . GLY A 1 164 ? 37.252 -59.333 17.502 1.00 29.65 ? 246 GLY A C 1 ATOM 1297 O O . GLY A 1 164 ? 36.120 -59.774 17.251 1.00 20.24 ? 246 GLY A O 1 ATOM 1298 N N . SER A 1 165 ? 38.018 -59.826 18.470 1.00 22.84 ? 247 SER A N 1 ATOM 1299 C CA . SER A 1 165 ? 37.627 -61.028 19.207 1.00 26.58 ? 247 SER A CA 1 ATOM 1300 C C . SER A 1 165 ? 36.335 -60.883 20.031 1.00 27.26 ? 247 SER A C 1 ATOM 1301 O O . SER A 1 165 ? 35.992 -59.794 20.499 1.00 29.34 ? 247 SER A O 1 ATOM 1302 C CB . SER A 1 165 ? 38.779 -61.500 20.099 1.00 26.47 ? 247 SER A CB 1 ATOM 1303 O OG . SER A 1 165 ? 38.447 -62.701 20.769 1.00 31.69 ? 247 SER A OG 1 ATOM 1304 N N . ALA A 1 166 ? 35.626 -61.996 20.189 1.00 29.11 ? 248 ALA A N 1 ATOM 1305 C CA . ALA A 1 166 ? 34.458 -62.073 21.062 1.00 33.25 ? 248 ALA A CA 1 ATOM 1306 C C . ALA A 1 166 ? 34.848 -62.670 22.413 1.00 33.66 ? 248 ALA A C 1 ATOM 1307 O O . ALA A 1 166 ? 34.049 -62.686 23.358 1.00 30.07 ? 248 ALA A O 1 ATOM 1308 C CB . ALA A 1 166 ? 33.380 -62.922 20.418 1.00 24.98 ? 248 ALA A CB 1 ATOM 1309 N N . THR A 1 167 ? 36.074 -63.176 22.492 1.00 26.30 ? 249 THR A N 1 ATOM 1310 C CA . THR A 1 167 ? 36.541 -63.874 23.685 1.00 36.74 ? 249 THR A CA 1 ATOM 1311 C C . THR A 1 167 ? 37.853 -63.278 24.205 1.00 38.26 ? 249 THR A C 1 ATOM 1312 O O . THR A 1 167 ? 38.656 -63.973 24.832 1.00 37.16 ? 249 THR A O 1 ATOM 1313 C CB . THR A 1 167 ? 36.735 -65.379 23.403 1.00 30.74 ? 249 THR A CB 1 ATOM 1314 O OG1 . THR A 1 167 ? 37.779 -65.555 22.439 1.00 34.74 ? 249 THR A OG1 1 ATOM 1315 C CG2 . THR A 1 167 ? 35.449 -65.997 22.863 1.00 33.38 ? 249 THR A CG2 1 ATOM 1316 N N . GLY A 1 168 ? 38.054 -61.990 23.937 1.00 30.89 ? 250 GLY A N 1 ATOM 1317 C CA . GLY A 1 168 ? 39.252 -61.275 24.344 1.00 32.23 ? 250 GLY A CA 1 ATOM 1318 C C . GLY A 1 168 ? 39.112 -59.798 24.008 1.00 35.39 ? 250 GLY A C 1 ATOM 1319 O O . GLY A 1 168 ? 38.064 -59.369 23.512 1.00 34.00 ? 250 GLY A O 1 ATOM 1320 N N . PRO A 1 169 ? 40.161 -59.006 24.284 1.00 28.58 ? 251 PRO A N 1 ATOM 1321 C CA . PRO A 1 169 ? 40.147 -57.575 23.950 1.00 34.38 ? 251 PRO A CA 1 ATOM 1322 C C . PRO A 1 169 ? 39.846 -57.331 22.470 1.00 30.85 ? 251 PRO A C 1 ATOM 1323 O O . PRO A 1 169 ? 40.487 -57.938 21.608 1.00 22.16 ? 251 PRO A O 1 ATOM 1324 C CB . PRO A 1 169 ? 41.574 -57.134 24.277 1.00 26.83 ? 251 PRO A CB 1 ATOM 1325 C CG . PRO A 1 169 ? 41.993 -58.068 25.387 1.00 31.18 ? 251 PRO A CG 1 ATOM 1326 C CD . PRO A 1 169 ? 41.374 -59.392 25.031 1.00 27.39 ? 251 PRO A CD 1 ATOM 1327 N N . ALA A 1 170 ? 38.875 -56.461 22.191 1.00 29.52 ? 252 ALA A N 1 ATOM 1328 C CA . ALA A 1 170 ? 38.471 -56.149 20.816 1.00 29.36 ? 252 ALA A CA 1 ATOM 1329 C C . ALA A 1 170 ? 38.548 -54.649 20.544 1.00 24.46 ? 252 ALA A C 1 ATOM 1330 O O . ALA A 1 170 ? 38.733 -53.851 21.472 1.00 19.32 ? 252 ALA A O 1 ATOM 1331 C CB . ALA A 1 170 ? 37.055 -56.667 20.542 1.00 17.00 ? 252 ALA A CB 1 ATOM 1332 N N . ASP A 1 171 ? 38.382 -54.265 19.279 1.00 26.32 ? 253 ASP A N 1 ATOM 1333 C CA . ASP A 1 171 ? 38.465 -52.854 18.895 1.00 28.78 ? 253 ASP A CA 1 ATOM 1334 C C . ASP A 1 171 ? 37.078 -52.239 18.716 1.00 29.91 ? 253 ASP A C 1 ATOM 1335 O O . ASP A 1 171 ? 36.465 -52.343 17.648 1.00 25.21 ? 253 ASP A O 1 ATOM 1336 C CB . ASP A 1 171 ? 39.299 -52.675 17.618 1.00 26.37 ? 253 ASP A CB 1 ATOM 1337 C CG . ASP A 1 171 ? 40.714 -53.223 17.758 1.00 41.29 ? 253 ASP A CG 1 ATOM 1338 O OD1 . ASP A 1 171 ? 41.378 -52.917 18.770 1.00 42.18 ? 253 ASP A OD1 1 ATOM 1339 O OD2 . ASP A 1 171 ? 41.159 -53.970 16.861 1.00 56.59 ? 253 ASP A OD2 1 ATOM 1340 N N . THR A 1 172 ? 36.586 -51.599 19.771 1.00 23.67 ? 254 THR A N 1 ATOM 1341 C CA . THR A 1 172 ? 35.276 -50.965 19.737 1.00 20.26 ? 254 THR A CA 1 ATOM 1342 C C . THR A 1 172 ? 35.432 -49.489 19.372 1.00 20.67 ? 254 THR A C 1 ATOM 1343 O O . THR A 1 172 ? 36.362 -48.818 19.837 1.00 23.53 ? 254 THR A O 1 ATOM 1344 C CB . THR A 1 172 ? 34.543 -51.138 21.087 1.00 20.13 ? 254 THR A CB 1 ATOM 1345 O OG1 . THR A 1 172 ? 34.196 -52.518 21.257 1.00 21.17 ? 254 THR A OG1 1 ATOM 1346 C CG2 . THR A 1 172 ? 33.272 -50.296 21.147 1.00 15.45 ? 254 THR A CG2 1 ATOM 1347 N N . ARG A 1 173 ? 34.540 -49.002 18.512 1.00 18.29 ? 255 ARG A N 1 ATOM 1348 C CA . ARG A 1 173 ? 34.555 -47.609 18.080 1.00 24.65 ? 255 ARG A CA 1 ATOM 1349 C C . ARG A 1 173 ? 33.169 -46.997 18.229 1.00 23.57 ? 255 ARG A C 1 ATOM 1350 O O . ARG A 1 173 ? 32.154 -47.687 18.070 1.00 17.53 ? 255 ARG A O 1 ATOM 1351 C CB . ARG A 1 173 ? 34.990 -47.495 16.616 1.00 23.25 ? 255 ARG A CB 1 ATOM 1352 C CG . ARG A 1 173 ? 36.437 -47.882 16.329 1.00 21.85 ? 255 ARG A CG 1 ATOM 1353 C CD . ARG A 1 173 ? 36.798 -47.565 14.877 1.00 17.61 ? 255 ARG A CD 1 ATOM 1354 N NE . ARG A 1 173 ? 38.183 -47.906 14.556 1.00 19.96 ? 255 ARG A NE 1 ATOM 1355 C CZ . ARG A 1 173 ? 38.748 -47.693 13.372 1.00 24.66 ? 255 ARG A CZ 1 ATOM 1356 N NH1 . ARG A 1 173 ? 38.044 -47.144 12.391 1.00 18.49 ? 255 ARG A NH1 1 ATOM 1357 N NH2 . ARG A 1 173 ? 40.014 -48.034 13.169 1.00 22.47 ? 255 ARG A NH2 1 ATOM 1358 N N . ILE A 1 174 ? 33.126 -45.708 18.542 1.00 21.71 ? 256 ILE A N 1 ATOM 1359 C CA . ILE A 1 174 ? 31.864 -44.980 18.532 1.00 21.82 ? 256 ILE A CA 1 ATOM 1360 C C . ILE A 1 174 ? 31.884 -44.033 17.337 1.00 29.79 ? 256 ILE A C 1 ATOM 1361 O O . ILE A 1 174 ? 32.756 -43.161 17.249 1.00 26.89 ? 256 ILE A O 1 ATOM 1362 C CB . ILE A 1 174 ? 31.631 -44.175 19.830 1.00 25.32 ? 256 ILE A CB 1 ATOM 1363 C CG1 . ILE A 1 174 ? 31.379 -45.104 21.023 1.00 28.98 ? 256 ILE A CG1 1 ATOM 1364 C CG2 . ILE A 1 174 ? 30.433 -43.262 19.665 1.00 19.97 ? 256 ILE A CG2 1 ATOM 1365 C CD1 . ILE A 1 174 ? 32.636 -45.686 21.678 1.00 30.16 ? 256 ILE A CD1 1 ATOM 1366 N N . TYR A 1 175 ? 30.949 -44.222 16.405 1.00 27.35 ? 257 TYR A N 1 ATOM 1367 C CA . TYR A 1 175 ? 30.853 -43.354 15.231 1.00 24.81 ? 257 TYR A CA 1 ATOM 1368 C C . TYR A 1 175 ? 29.749 -42.327 15.417 1.00 24.80 ? 257 TYR A C 1 ATOM 1369 O O . TYR A 1 175 ? 28.731 -42.597 16.062 1.00 22.54 ? 257 TYR A O 1 ATOM 1370 C CB . TYR A 1 175 ? 30.587 -44.167 13.961 1.00 23.40 ? 257 TYR A CB 1 ATOM 1371 C CG . TYR A 1 175 ? 31.837 -44.694 13.292 1.00 23.09 ? 257 TYR A CG 1 ATOM 1372 C CD1 . TYR A 1 175 ? 32.524 -45.785 13.824 1.00 22.06 ? 257 TYR A CD1 1 ATOM 1373 C CD2 . TYR A 1 175 ? 32.321 -44.116 12.124 1.00 20.71 ? 257 TYR A CD2 1 ATOM 1374 C CE1 . TYR A 1 175 ? 33.664 -46.279 13.220 1.00 21.27 ? 257 TYR A CE1 1 ATOM 1375 C CE2 . TYR A 1 175 ? 33.470 -44.604 11.507 1.00 19.08 ? 257 TYR A CE2 1 ATOM 1376 C CZ . TYR A 1 175 ? 34.134 -45.683 12.062 1.00 25.05 ? 257 TYR A CZ 1 ATOM 1377 O OH . TYR A 1 175 ? 35.271 -46.185 11.460 1.00 25.29 ? 257 TYR A OH 1 ATOM 1378 N N . TYR A 1 176 ? 29.961 -41.144 14.858 1.00 23.17 ? 258 TYR A N 1 ATOM 1379 C CA . TYR A 1 176 ? 28.993 -40.072 14.956 1.00 16.64 ? 258 TYR A CA 1 ATOM 1380 C C . TYR A 1 176 ? 28.587 -39.697 13.546 1.00 26.75 ? 258 TYR A C 1 ATOM 1381 O O . TYR A 1 176 ? 29.390 -39.145 12.787 1.00 26.37 ? 258 TYR A O 1 ATOM 1382 C CB . TYR A 1 176 ? 29.606 -38.878 15.687 1.00 21.99 ? 258 TYR A CB 1 ATOM 1383 C CG . TYR A 1 176 ? 29.977 -39.185 17.117 1.00 16.79 ? 258 TYR A CG 1 ATOM 1384 C CD1 . TYR A 1 176 ? 31.241 -39.665 17.442 1.00 22.06 ? 258 TYR A CD1 1 ATOM 1385 C CD2 . TYR A 1 176 ? 29.057 -39.004 18.143 1.00 23.64 ? 258 TYR A CD2 1 ATOM 1386 C CE1 . TYR A 1 176 ? 31.578 -39.949 18.754 1.00 20.93 ? 258 TYR A CE1 1 ATOM 1387 C CE2 . TYR A 1 176 ? 29.383 -39.285 19.457 1.00 22.93 ? 258 TYR A CE2 1 ATOM 1388 C CZ . TYR A 1 176 ? 30.641 -39.755 19.755 1.00 18.30 ? 258 TYR A CZ 1 ATOM 1389 O OH . TYR A 1 176 ? 30.967 -40.030 21.063 1.00 22.81 ? 258 TYR A OH 1 ATOM 1390 N N . PHE A 1 177 ? 27.349 -40.025 13.186 1.00 24.36 ? 259 PHE A N 1 ATOM 1391 C CA . PHE A 1 177 ? 26.861 -39.771 11.833 1.00 20.65 ? 259 PHE A CA 1 ATOM 1392 C C . PHE A 1 177 ? 25.923 -38.574 11.778 1.00 22.46 ? 259 PHE A C 1 ATOM 1393 O O . PHE A 1 177 ? 25.200 -38.298 12.740 1.00 27.72 ? 259 PHE A O 1 ATOM 1394 C CB . PHE A 1 177 ? 26.116 -40.993 11.299 1.00 18.37 ? 259 PHE A CB 1 ATOM 1395 C CG . PHE A 1 177 ? 26.944 -42.248 11.254 1.00 18.90 ? 259 PHE A CG 1 ATOM 1396 C CD1 . PHE A 1 177 ? 27.805 -42.488 10.191 1.00 18.07 ? 259 PHE A CD1 1 ATOM 1397 C CD2 . PHE A 1 177 ? 26.836 -43.203 12.262 1.00 16.47 ? 259 PHE A CD2 1 ATOM 1398 C CE1 . PHE A 1 177 ? 28.559 -43.651 10.138 1.00 17.44 ? 259 PHE A CE1 1 ATOM 1399 C CE2 . PHE A 1 177 ? 27.583 -44.367 12.217 1.00 21.07 ? 259 PHE A CE2 1 ATOM 1400 C CZ . PHE A 1 177 ? 28.448 -44.594 11.152 1.00 19.88 ? 259 PHE A CZ 1 ATOM 1401 N N . LYS A 1 178 ? 25.936 -37.865 10.653 1.00 21.70 ? 260 LYS A N 1 ATOM 1402 C CA . LYS A 1 178 ? 24.893 -36.885 10.365 1.00 22.75 ? 260 LYS A CA 1 ATOM 1403 C C . LYS A 1 178 ? 24.497 -36.992 8.898 1.00 20.70 ? 260 LYS A C 1 ATOM 1404 O O . LYS A 1 178 ? 25.355 -36.922 8.006 1.00 26.77 ? 260 LYS A O 1 ATOM 1405 C CB . LYS A 1 178 ? 25.341 -35.464 10.692 1.00 25.40 ? 260 LYS A CB 1 ATOM 1406 C CG . LYS A 1 178 ? 24.276 -34.417 10.390 1.00 20.68 ? 260 LYS A CG 1 ATOM 1407 C CD . LYS A 1 178 ? 24.669 -33.067 10.985 1.00 28.11 ? 260 LYS A CD 1 ATOM 1408 C CE . LYS A 1 178 ? 23.563 -32.044 10.819 1.00 28.69 ? 260 LYS A CE 1 ATOM 1409 N NZ . LYS A 1 178 ? 23.703 -30.928 11.808 1.00 47.49 ? 260 LYS A NZ 1 ATOM 1410 N N . GLU A 1 179 ? 23.200 -37.181 8.656 1.00 27.12 ? 261 GLU A N 1 ATOM 1411 C CA . GLU A 1 179 ? 22.688 -37.443 7.312 1.00 24.55 ? 261 GLU A CA 1 ATOM 1412 C C . GLU A 1 179 ? 23.492 -38.548 6.622 1.00 20.29 ? 261 GLU A C 1 ATOM 1413 O O . GLU A 1 179 ? 23.708 -38.514 5.404 1.00 25.39 ? 261 GLU A O 1 ATOM 1414 C CB . GLU A 1 179 ? 22.662 -36.148 6.486 1.00 23.56 ? 261 GLU A CB 1 ATOM 1415 C CG . GLU A 1 179 ? 21.784 -35.072 7.120 1.00 26.16 ? 261 GLU A CG 1 ATOM 1416 C CD . GLU A 1 179 ? 21.687 -33.795 6.299 1.00 34.67 ? 261 GLU A CD 1 ATOM 1417 O OE1 . GLU A 1 179 ? 22.740 -33.243 5.914 1.00 42.11 ? 261 GLU A OE1 1 ATOM 1418 O OE2 . GLU A 1 179 ? 20.549 -33.343 6.046 1.00 48.63 ? 261 GLU A OE2 1 ATOM 1419 N N . GLY A 1 180 ? 23.950 -39.518 7.415 1.00 22.31 ? 262 GLY A N 1 ATOM 1420 C CA . GLY A 1 180 ? 24.687 -40.657 6.890 1.00 18.49 ? 262 GLY A CA 1 ATOM 1421 C C . GLY A 1 180 ? 26.180 -40.425 6.711 1.00 23.49 ? 262 GLY A C 1 ATOM 1422 O O . GLY A 1 180 ? 26.932 -41.369 6.441 1.00 20.91 ? 262 GLY A O 1 ATOM 1423 N N . LYS A 1 181 ? 26.616 -39.176 6.855 1.00 20.51 ? 263 LYS A N 1 ATOM 1424 C CA . LYS A 1 181 ? 28.036 -38.864 6.725 1.00 22.39 ? 263 LYS A CA 1 ATOM 1425 C C . LYS A 1 181 ? 28.764 -38.999 8.060 1.00 23.46 ? 263 LYS A C 1 ATOM 1426 O O . LYS A 1 181 ? 28.192 -38.722 9.122 1.00 19.90 ? 263 LYS A O 1 ATOM 1427 C CB . LYS A 1 181 ? 28.227 -37.462 6.131 1.00 30.10 ? 263 LYS A CB 1 ATOM 1428 C CG . LYS A 1 181 ? 27.616 -37.320 4.733 1.00 28.56 ? 263 LYS A CG 1 ATOM 1429 C CD . LYS A 1 181 ? 28.243 -36.181 3.937 1.00 50.59 ? 263 LYS A CD 1 ATOM 1430 C CE . LYS A 1 181 ? 27.618 -34.834 4.270 1.00 65.51 ? 263 LYS A CE 1 ATOM 1431 N NZ . LYS A 1 181 ? 28.153 -33.750 3.389 1.00 74.49 ? 263 LYS A NZ 1 ATOM 1432 N N . ILE A 1 182 ? 30.022 -39.436 8.001 1.00 24.35 ? 264 ILE A N 1 ATOM 1433 C CA . ILE A 1 182 ? 30.853 -39.590 9.194 1.00 22.68 ? 264 ILE A CA 1 ATOM 1434 C C . ILE A 1 182 ? 31.397 -38.240 9.661 1.00 29.27 ? 264 ILE A C 1 ATOM 1435 O O . ILE A 1 182 ? 32.208 -37.609 8.969 1.00 24.18 ? 264 ILE A O 1 ATOM 1436 C CB . ILE A 1 182 ? 32.032 -40.560 8.940 1.00 18.84 ? 264 ILE A CB 1 ATOM 1437 C CG1 . ILE A 1 182 ? 31.516 -41.939 8.515 1.00 16.11 ? 264 ILE A CG1 1 ATOM 1438 C CG2 . ILE A 1 182 ? 32.904 -40.683 10.181 1.00 16.62 ? 264 ILE A CG2 1 ATOM 1439 C CD1 . ILE A 1 182 ? 32.590 -42.843 7.937 1.00 22.34 ? 264 ILE A CD1 1 ATOM 1440 N N . LEU A 1 183 ? 30.946 -37.799 10.834 1.00 24.11 ? 265 LEU A N 1 ATOM 1441 C CA . LEU A 1 183 ? 31.434 -36.554 11.415 1.00 27.70 ? 265 LEU A CA 1 ATOM 1442 C C . LEU A 1 183 ? 32.726 -36.821 12.157 1.00 23.95 ? 265 LEU A C 1 ATOM 1443 O O . LEU A 1 183 ? 33.648 -36.000 12.144 1.00 29.58 ? 265 LEU A O 1 ATOM 1444 C CB . LEU A 1 183 ? 30.413 -35.969 12.391 1.00 25.51 ? 265 LEU A CB 1 ATOM 1445 C CG . LEU A 1 183 ? 29.085 -35.495 11.809 1.00 33.84 ? 265 LEU A CG 1 ATOM 1446 C CD1 . LEU A 1 183 ? 28.205 -34.883 12.897 1.00 27.21 ? 265 LEU A CD1 1 ATOM 1447 C CD2 . LEU A 1 183 ? 29.332 -34.502 10.681 1.00 31.42 ? 265 LEU A CD2 1 ATOM 1448 N N . LYS A 1 184 ? 32.785 -37.987 12.795 1.00 24.01 ? 266 LYS A N 1 ATOM 1449 C CA . LYS A 1 184 ? 33.839 -38.295 13.747 1.00 22.55 ? 266 LYS A CA 1 ATOM 1450 C C . LYS A 1 184 ? 33.661 -39.731 14.218 1.00 22.47 ? 266 LYS A C 1 ATOM 1451 O O . LYS A 1 184 ? 32.536 -40.243 14.263 1.00 21.35 ? 266 LYS A O 1 ATOM 1452 C CB . LYS A 1 184 ? 33.731 -37.341 14.946 1.00 22.12 ? 266 LYS A CB 1 ATOM 1453 C CG . LYS A 1 184 ? 34.672 -37.636 16.115 1.00 22.03 ? 266 LYS A CG 1 ATOM 1454 C CD . LYS A 1 184 ? 34.393 -36.688 17.277 1.00 25.32 ? 266 LYS A CD 1 ATOM 1455 C CE . LYS A 1 184 ? 35.319 -36.969 18.454 1.00 29.51 ? 266 LYS A CE 1 ATOM 1456 N NZ . LYS A 1 184 ? 35.080 -36.022 19.584 1.00 27.06 ? 266 LYS A NZ 1 ATOM 1457 N N . TRP A 1 185 ? 34.774 -40.384 14.538 1.00 17.35 ? 267 TRP A N 1 ATOM 1458 C CA . TRP A 1 185 ? 34.733 -41.639 15.276 1.00 26.30 ? 267 TRP A CA 1 ATOM 1459 C C . TRP A 1 185 ? 35.826 -41.620 16.334 1.00 26.57 ? 267 TRP A C 1 ATOM 1460 O O . TRP A 1 185 ? 36.806 -40.882 16.204 1.00 19.30 ? 267 TRP A O 1 ATOM 1461 C CB . TRP A 1 185 ? 34.872 -42.854 14.353 1.00 21.61 ? 267 TRP A CB 1 ATOM 1462 C CG . TRP A 1 185 ? 36.195 -42.992 13.651 1.00 24.75 ? 267 TRP A CG 1 ATOM 1463 C CD1 . TRP A 1 185 ? 36.496 -42.603 12.371 1.00 20.08 ? 267 TRP A CD1 1 ATOM 1464 C CD2 . TRP A 1 185 ? 37.385 -43.605 14.174 1.00 23.98 ? 267 TRP A CD2 1 ATOM 1465 N NE1 . TRP A 1 185 ? 37.807 -42.923 12.077 1.00 25.99 ? 267 TRP A NE1 1 ATOM 1466 C CE2 . TRP A 1 185 ? 38.372 -43.536 13.167 1.00 20.71 ? 267 TRP A CE2 1 ATOM 1467 C CE3 . TRP A 1 185 ? 37.712 -44.195 15.401 1.00 22.44 ? 267 TRP A CE3 1 ATOM 1468 C CZ2 . TRP A 1 185 ? 39.661 -44.046 13.349 1.00 19.62 ? 267 TRP A CZ2 1 ATOM 1469 C CZ3 . TRP A 1 185 ? 38.994 -44.698 15.581 1.00 25.36 ? 267 TRP A CZ3 1 ATOM 1470 C CH2 . TRP A 1 185 ? 39.953 -44.616 14.562 1.00 22.15 ? 267 TRP A CH2 1 ATOM 1471 N N . GLU A 1 186 ? 35.648 -42.417 17.383 1.00 20.76 ? 268 GLU A N 1 ATOM 1472 C CA . GLU A 1 186 ? 36.627 -42.488 18.456 1.00 26.68 ? 268 GLU A CA 1 ATOM 1473 C C . GLU A 1 186 ? 36.719 -43.909 18.999 1.00 26.09 ? 268 GLU A C 1 ATOM 1474 O O . GLU A 1 186 ? 35.738 -44.655 18.991 1.00 25.05 ? 268 GLU A O 1 ATOM 1475 C CB . GLU A 1 186 ? 36.275 -41.498 19.578 1.00 31.21 ? 268 GLU A CB 1 ATOM 1476 C CG . GLU A 1 186 ? 34.861 -41.650 20.138 1.00 33.58 ? 268 GLU A CG 1 ATOM 1477 C CD . GLU A 1 186 ? 34.505 -40.562 21.149 1.00 31.44 ? 268 GLU A CD 1 ATOM 1478 O OE1 . GLU A 1 186 ? 33.353 -40.558 21.637 1.00 31.76 ? 268 GLU A OE1 1 ATOM 1479 O OE2 . GLU A 1 186 ? 35.372 -39.711 21.455 1.00 31.66 ? 268 GLU A OE2 1 ATOM 1480 N N A SER A 1 187 ? 37.903 -44.300 19.450 0.37 23.30 ? 269 SER A N 1 ATOM 1481 N N B SER A 1 187 ? 37.908 -44.279 19.465 0.63 23.27 ? 269 SER A N 1 ATOM 1482 C CA A SER A 1 187 ? 38.060 -45.611 20.057 0.37 26.71 ? 269 SER A CA 1 ATOM 1483 C CA B SER A 1 187 ? 38.098 -45.569 20.109 0.63 26.75 ? 269 SER A CA 1 ATOM 1484 C C A SER A 1 187 ? 37.448 -45.605 21.452 0.37 24.56 ? 269 SER A C 1 ATOM 1485 C C B SER A 1 187 ? 37.386 -45.578 21.453 0.63 24.54 ? 269 SER A C 1 ATOM 1486 O O A SER A 1 187 ? 37.438 -44.575 22.131 0.37 25.61 ? 269 SER A O 1 ATOM 1487 O O B SER A 1 187 ? 37.243 -44.533 22.094 0.63 25.60 ? 269 SER A O 1 ATOM 1488 C CB A SER A 1 187 ? 39.532 -46.001 20.124 0.37 24.75 ? 269 SER A CB 1 ATOM 1489 C CB B SER A 1 187 ? 39.584 -45.872 20.294 0.63 24.77 ? 269 SER A CB 1 ATOM 1490 O OG A SER A 1 187 ? 40.296 -44.958 20.697 0.37 26.71 ? 269 SER A OG 1 ATOM 1491 O OG B SER A 1 187 ? 40.194 -46.187 19.057 0.63 22.46 ? 269 SER A OG 1 ATOM 1492 N N . LEU A 1 188 ? 36.925 -46.756 21.861 1.00 24.56 ? 270 LEU A N 1 ATOM 1493 C CA . LEU A 1 188 ? 36.282 -46.921 23.160 1.00 24.49 ? 270 LEU A CA 1 ATOM 1494 C C . LEU A 1 188 ? 37.212 -46.533 24.303 1.00 26.07 ? 270 LEU A C 1 ATOM 1495 O O . LEU A 1 188 ? 38.371 -46.956 24.346 1.00 21.22 ? 270 LEU A O 1 ATOM 1496 C CB . LEU A 1 188 ? 35.844 -48.373 23.346 1.00 18.51 ? 270 LEU A CB 1 ATOM 1497 C CG . LEU A 1 188 ? 35.401 -48.776 24.756 1.00 24.82 ? 270 LEU A CG 1 ATOM 1498 C CD1 . LEU A 1 188 ? 34.056 -48.154 25.104 1.00 14.93 ? 270 LEU A CD1 1 ATOM 1499 C CD2 . LEU A 1 188 ? 35.345 -50.294 24.889 1.00 19.28 ? 270 LEU A CD2 1 ATOM 1500 N N . THR A 1 189 ? 36.694 -45.729 25.225 1.00 27.25 ? 271 THR A N 1 ATOM 1501 C CA . THR A 1 189 ? 37.442 -45.350 26.422 1.00 31.76 ? 271 THR A CA 1 ATOM 1502 C C . THR A 1 189 ? 36.660 -45.738 27.682 1.00 32.33 ? 271 THR A C 1 ATOM 1503 O O . THR A 1 189 ? 35.517 -46.207 27.596 1.00 24.33 ? 271 THR A O 1 ATOM 1504 C CB . THR A 1 189 ? 37.748 -43.835 26.435 1.00 27.71 ? 271 THR A CB 1 ATOM 1505 O OG1 . THR A 1 189 ? 38.829 -43.564 27.335 1.00 46.74 ? 271 THR A OG1 1 ATOM 1506 C CG2 . THR A 1 189 ? 36.525 -43.041 26.861 1.00 32.42 ? 271 THR A CG2 1 ATOM 1507 N N . GLY A 1 190 ? 37.271 -45.553 28.850 1.00 25.30 ? 272 GLY A N 1 ATOM 1508 C CA . GLY A 1 190 ? 36.592 -45.855 30.099 1.00 23.84 ? 272 GLY A CA 1 ATOM 1509 C C . GLY A 1 190 ? 36.970 -47.220 30.637 1.00 22.56 ? 272 GLY A C 1 ATOM 1510 O O . GLY A 1 190 ? 38.014 -47.768 30.266 1.00 23.88 ? 272 GLY A O 1 ATOM 1511 N N . THR A 1 191 ? 36.119 -47.789 31.489 1.00 24.70 ? 273 THR A N 1 ATOM 1512 C CA . THR A 1 191 ? 36.502 -48.994 32.223 1.00 25.99 ? 273 THR A CA 1 ATOM 1513 C C . THR A 1 191 ? 35.833 -50.277 31.736 1.00 24.49 ? 273 THR A C 1 ATOM 1514 O O . THR A 1 191 ? 36.147 -51.364 32.227 1.00 24.40 ? 273 THR A O 1 ATOM 1515 C CB . THR A 1 191 ? 36.285 -48.829 33.744 1.00 26.10 ? 273 THR A CB 1 ATOM 1516 O OG1 . THR A 1 191 ? 34.887 -48.685 34.025 1.00 23.43 ? 273 THR A OG1 1 ATOM 1517 C CG2 . THR A 1 191 ? 37.021 -47.599 34.243 1.00 23.62 ? 273 THR A CG2 1 ATOM 1518 N N . ALA A 1 192 ? 34.922 -50.161 30.771 1.00 19.74 ? 274 ALA A N 1 ATOM 1519 C CA . ALA A 1 192 ? 34.322 -51.358 30.183 1.00 19.79 ? 274 ALA A CA 1 ATOM 1520 C C . ALA A 1 192 ? 35.415 -52.109 29.435 1.00 23.91 ? 274 ALA A C 1 ATOM 1521 O O . ALA A 1 192 ? 36.165 -51.500 28.666 1.00 22.24 ? 274 ALA A O 1 ATOM 1522 C CB . ALA A 1 192 ? 33.179 -50.990 29.244 1.00 19.11 ? 274 ALA A CB 1 ATOM 1523 N N . LYS A 1 193 ? 35.512 -53.417 29.675 1.00 18.80 ? 275 LYS A N 1 ATOM 1524 C CA . LYS A 1 193 ? 36.618 -54.220 29.146 1.00 23.32 ? 275 LYS A CA 1 ATOM 1525 C C . LYS A 1 193 ? 36.254 -54.975 27.865 1.00 28.89 ? 275 LYS A C 1 ATOM 1526 O O . LYS A 1 193 ? 37.140 -55.463 27.153 1.00 23.72 ? 275 LYS A O 1 ATOM 1527 C CB . LYS A 1 193 ? 37.142 -55.197 30.209 1.00 21.76 ? 275 LYS A CB 1 ATOM 1528 C CG . LYS A 1 193 ? 37.661 -54.524 31.491 1.00 24.40 ? 275 LYS A CG 1 ATOM 1529 C CD . LYS A 1 193 ? 38.657 -53.400 31.161 1.00 24.99 ? 275 LYS A CD 1 ATOM 1530 C CE . LYS A 1 193 ? 39.365 -52.875 32.410 1.00 18.48 ? 275 LYS A CE 1 ATOM 1531 N NZ . LYS A 1 193 ? 38.433 -52.232 33.390 1.00 19.61 ? 275 LYS A NZ 1 ATOM 1532 N N . HIS A 1 194 ? 34.957 -55.075 27.576 1.00 25.90 ? 276 HIS A N 1 ATOM 1533 C CA . HIS A 1 194 ? 34.498 -55.704 26.333 1.00 20.95 ? 276 HIS A CA 1 ATOM 1534 C C . HIS A 1 194 ? 33.088 -55.237 25.989 1.00 24.25 ? 276 HIS A C 1 ATOM 1535 O O . HIS A 1 194 ? 32.227 -55.172 26.869 1.00 22.94 ? 276 HIS A O 1 ATOM 1536 C CB . HIS A 1 194 ? 34.534 -57.226 26.449 1.00 19.25 ? 276 HIS A CB 1 ATOM 1537 C CG . HIS A 1 194 ? 34.476 -57.934 25.129 1.00 29.55 ? 276 HIS A CG 1 ATOM 1538 N ND1 . HIS A 1 194 ? 33.361 -58.622 24.700 1.00 22.51 ? 276 HIS A ND1 1 ATOM 1539 C CD2 . HIS A 1 194 ? 35.400 -58.069 24.148 1.00 25.08 ? 276 HIS A CD2 1 ATOM 1540 C CE1 . HIS A 1 194 ? 33.599 -59.142 23.510 1.00 28.27 ? 276 HIS A CE1 1 ATOM 1541 N NE2 . HIS A 1 194 ? 34.832 -58.827 23.155 1.00 24.69 ? 276 HIS A NE2 1 ATOM 1542 N N . ILE A 1 195 ? 32.856 -54.915 24.714 1.00 19.42 ? 277 ILE A N 1 ATOM 1543 C CA . ILE A 1 195 ? 31.587 -54.314 24.280 1.00 17.88 ? 277 ILE A CA 1 ATOM 1544 C C . ILE A 1 195 ? 30.959 -55.042 23.084 1.00 27.25 ? 277 ILE A C 1 ATOM 1545 O O . ILE A 1 195 ? 31.601 -55.195 22.041 1.00 21.27 ? 277 ILE A O 1 ATOM 1546 C CB . ILE A 1 195 ? 31.785 -52.834 23.884 1.00 21.42 ? 277 ILE A CB 1 ATOM 1547 C CG1 . ILE A 1 195 ? 32.243 -52.013 25.084 1.00 20.87 ? 277 ILE A CG1 1 ATOM 1548 C CG2 . ILE A 1 195 ? 30.501 -52.252 23.285 1.00 12.39 ? 277 ILE A CG2 1 ATOM 1549 C CD1 . ILE A 1 195 ? 31.198 -51.898 26.170 1.00 21.82 ? 277 ILE A CD1 1 ATOM 1550 N N . GLU A 1 196 ? 29.710 -55.483 23.238 1.00 23.00 ? 278 GLU A N 1 ATOM 1551 C CA . GLU A 1 196 ? 28.944 -56.059 22.134 1.00 15.62 ? 278 GLU A CA 1 ATOM 1552 C C . GLU A 1 196 ? 27.526 -55.518 22.153 1.00 23.64 ? 278 GLU A C 1 ATOM 1553 O O . GLU A 1 196 ? 26.967 -55.275 23.230 1.00 20.92 ? 278 GLU A O 1 ATOM 1554 C CB . GLU A 1 196 ? 28.853 -57.579 22.268 1.00 16.07 ? 278 GLU A CB 1 ATOM 1555 C CG . GLU A 1 196 ? 30.176 -58.306 22.316 1.00 18.46 ? 278 GLU A CG 1 ATOM 1556 C CD . GLU A 1 196 ? 30.784 -58.524 20.946 1.00 22.19 ? 278 GLU A CD 1 ATOM 1557 O OE1 . GLU A 1 196 ? 31.678 -59.393 20.831 1.00 24.07 ? 278 GLU A OE1 1 ATOM 1558 O OE2 . GLU A 1 196 ? 30.379 -57.830 19.988 1.00 24.22 ? 278 GLU A OE2 1 ATOM 1559 N N . GLU A 1 197 ? 26.952 -55.336 20.964 1.00 19.14 ? 279 GLU A N 1 ATOM 1560 C CA . GLU A 1 197 ? 25.504 -55.197 20.812 1.00 17.18 ? 279 GLU A CA 1 ATOM 1561 C C . GLU A 1 197 ? 24.849 -54.206 21.777 1.00 18.68 ? 279 GLU A C 1 ATOM 1562 O O . GLU A 1 197 ? 24.004 -54.586 22.598 1.00 13.38 ? 279 GLU A O 1 ATOM 1563 C CB . GLU A 1 197 ? 24.850 -56.582 20.950 1.00 16.36 ? 279 GLU A CB 1 ATOM 1564 C CG . GLU A 1 197 ? 25.349 -57.576 19.900 1.00 14.77 ? 279 GLU A CG 1 ATOM 1565 C CD . GLU A 1 197 ? 24.885 -59.003 20.140 1.00 23.50 ? 279 GLU A CD 1 ATOM 1566 O OE1 . GLU A 1 197 ? 24.861 -59.442 21.313 1.00 21.60 ? 279 GLU A OE1 1 ATOM 1567 O OE2 . GLU A 1 197 ? 24.566 -59.700 19.145 1.00 21.23 ? 279 GLU A OE2 1 ATOM 1568 N N . CYS A 1 198 ? 25.240 -52.941 21.684 1.00 18.85 ? 280 CYS A N 1 ATOM 1569 C CA . CYS A 1 198 ? 24.701 -51.932 22.592 1.00 19.49 ? 280 CYS A CA 1 ATOM 1570 C C . CYS A 1 198 ? 23.228 -51.644 22.316 1.00 20.56 ? 280 CYS A C 1 ATOM 1571 O O . CYS A 1 198 ? 22.813 -51.523 21.153 1.00 15.32 ? 280 CYS A O 1 ATOM 1572 C CB . CYS A 1 198 ? 25.521 -50.642 22.509 1.00 15.66 ? 280 CYS A CB 1 ATOM 1573 S SG . CYS A 1 198 ? 27.205 -50.822 23.170 1.00 29.25 ? 280 CYS A SG 1 ATOM 1574 N N . SER A 1 199 ? 22.444 -51.578 23.393 1.00 16.74 ? 281 SER A N 1 ATOM 1575 C CA . SER A 1 199 ? 21.062 -51.107 23.349 1.00 16.82 ? 281 SER A CA 1 ATOM 1576 C C . SER A 1 199 ? 21.028 -49.690 23.922 1.00 20.46 ? 281 SER A C 1 ATOM 1577 O O . SER A 1 199 ? 21.425 -49.478 25.074 1.00 21.75 ? 281 SER A O 1 ATOM 1578 C CB . SER A 1 199 ? 20.151 -52.010 24.184 1.00 18.33 ? 281 SER A CB 1 ATOM 1579 O OG . SER A 1 199 ? 20.180 -53.344 23.725 1.00 18.37 ? 281 SER A OG 1 ATOM 1580 N N . CYS A 1 200 ? 20.551 -48.724 23.135 1.00 17.56 ? 282 CYS A N 1 ATOM 1581 C CA . CYS A 1 200 ? 20.655 -47.321 23.538 1.00 20.74 ? 282 CYS A CA 1 ATOM 1582 C C . CYS A 1 200 ? 19.313 -46.609 23.589 1.00 19.61 ? 282 CYS A C 1 ATOM 1583 O O . CYS A 1 200 ? 18.336 -47.044 22.965 1.00 17.19 ? 282 CYS A O 1 ATOM 1584 C CB . CYS A 1 200 ? 21.599 -46.553 22.603 1.00 17.17 ? 282 CYS A CB 1 ATOM 1585 S SG . CYS A 1 200 ? 23.155 -47.402 22.261 1.00 22.06 ? 282 CYS A SG 1 ATOM 1586 N N . TYR A 1 201 ? 19.281 -45.511 24.344 1.00 14.66 ? 283 TYR A N 1 ATOM 1587 C CA . TYR A 1 201 ? 18.122 -44.623 24.399 1.00 18.69 ? 283 TYR A CA 1 ATOM 1588 C C . TYR A 1 201 ? 18.631 -43.224 24.725 1.00 22.00 ? 283 TYR A C 1 ATOM 1589 O O . TYR A 1 201 ? 19.742 -43.068 25.249 1.00 20.33 ? 283 TYR A O 1 ATOM 1590 C CB . TYR A 1 201 ? 17.101 -45.085 25.448 1.00 18.95 ? 283 TYR A CB 1 ATOM 1591 C CG . TYR A 1 201 ? 17.585 -44.966 26.878 1.00 18.48 ? 283 TYR A CG 1 ATOM 1592 C CD1 . TYR A 1 201 ? 18.292 -46.001 27.475 1.00 16.65 ? 283 TYR A CD1 1 ATOM 1593 C CD2 . TYR A 1 201 ? 17.327 -43.825 27.632 1.00 22.89 ? 283 TYR A CD2 1 ATOM 1594 C CE1 . TYR A 1 201 ? 18.733 -45.909 28.773 1.00 17.16 ? 283 TYR A CE1 1 ATOM 1595 C CE2 . TYR A 1 201 ? 17.770 -43.722 28.942 1.00 16.80 ? 283 TYR A CE2 1 ATOM 1596 C CZ . TYR A 1 201 ? 18.476 -44.770 29.501 1.00 17.74 ? 283 TYR A CZ 1 ATOM 1597 O OH . TYR A 1 201 ? 18.927 -44.694 30.799 1.00 24.50 ? 283 TYR A OH 1 ATOM 1598 N N . GLY A 1 202 ? 17.831 -42.208 24.409 1.00 16.87 ? 284 GLY A N 1 ATOM 1599 C CA . GLY A 1 202 ? 18.249 -40.837 24.637 1.00 19.84 ? 284 GLY A CA 1 ATOM 1600 C C . GLY A 1 202 ? 17.289 -40.071 25.527 1.00 25.18 ? 284 GLY A C 1 ATOM 1601 O O . GLY A 1 202 ? 16.079 -40.283 25.502 1.00 19.53 ? 284 GLY A O 1 ATOM 1602 N N . GLU A 1 203 ? 17.838 -39.176 26.331 1.00 26.82 ? 285 GLU A N 1 ATOM 1603 C CA . GLU A 1 203 ? 17.025 -38.230 27.077 1.00 26.04 ? 285 GLU A CA 1 ATOM 1604 C C . GLU A 1 203 ? 17.905 -37.016 27.332 1.00 27.30 ? 285 GLU A C 1 ATOM 1605 O O . GLU A 1 203 ? 19.064 -37.007 26.920 1.00 31.84 ? 285 GLU A O 1 ATOM 1606 C CB . GLU A 1 203 ? 16.479 -38.857 28.365 1.00 23.31 ? 285 GLU A CB 1 ATOM 1607 C CG . GLU A 1 203 ? 17.507 -39.613 29.190 1.00 28.74 ? 285 GLU A CG 1 ATOM 1608 C CD . GLU A 1 203 ? 17.709 -38.991 30.560 1.00 40.32 ? 285 GLU A CD 1 ATOM 1609 O OE1 . GLU A 1 203 ? 17.233 -37.854 30.771 1.00 36.59 ? 285 GLU A OE1 1 ATOM 1610 O OE2 . GLU A 1 203 ? 18.344 -39.636 31.423 1.00 56.41 ? 285 GLU A OE2 1 ATOM 1611 N N . ARG A 1 204 ? 17.361 -35.986 27.973 1.00 29.10 ? 286 ARG A N 1 ATOM 1612 C CA . ARG A 1 204 ? 18.080 -34.718 28.122 1.00 33.96 ? 286 ARG A CA 1 ATOM 1613 C C . ARG A 1 204 ? 19.497 -34.850 28.680 1.00 32.85 ? 286 ARG A C 1 ATOM 1614 O O . ARG A 1 204 ? 20.358 -34.026 28.383 1.00 33.70 ? 286 ARG A O 1 ATOM 1615 C CB . ARG A 1 204 ? 17.277 -33.749 28.981 1.00 31.69 ? 286 ARG A CB 1 ATOM 1616 C CG . ARG A 1 204 ? 16.809 -34.340 30.297 1.00 29.84 ? 286 ARG A CG 1 ATOM 1617 C CD . ARG A 1 204 ? 15.922 -33.356 31.040 1.00 30.07 ? 286 ARG A CD 1 ATOM 1618 N NE . ARG A 1 204 ? 15.264 -33.994 32.174 1.00 30.28 ? 286 ARG A NE 1 ATOM 1619 C CZ . ARG A 1 204 ? 14.071 -33.630 32.630 1.00 32.29 ? 286 ARG A CZ 1 ATOM 1620 N NH1 . ARG A 1 204 ? 13.419 -32.629 32.048 1.00 28.99 ? 286 ARG A NH1 1 ATOM 1621 N NH2 . ARG A 1 204 ? 13.529 -34.266 33.660 1.00 36.90 ? 286 ARG A NH2 1 ATOM 1622 N N . THR A 1 205 ? 19.736 -35.894 29.476 1.00 64.52 ? 287 THR A N 1 ATOM 1623 C CA . THR A 1 205 ? 21.054 -36.115 30.076 1.00 67.46 ? 287 THR A CA 1 ATOM 1624 C C . THR A 1 205 ? 22.077 -36.650 29.067 1.00 72.01 ? 287 THR A C 1 ATOM 1625 O O . THR A 1 205 ? 23.273 -36.732 29.372 1.00 69.62 ? 287 THR A O 1 ATOM 1626 C CB . THR A 1 205 ? 20.993 -37.068 31.302 1.00 75.97 ? 287 THR A CB 1 ATOM 1627 O OG1 . THR A 1 205 ? 20.746 -38.415 30.871 1.00 75.45 ? 287 THR A OG1 1 ATOM 1628 C CG2 . THR A 1 205 ? 19.907 -36.627 32.292 1.00 64.57 ? 287 THR A CG2 1 ATOM 1629 N N . GLY A 1 206 ? 21.603 -37.002 27.870 1.00 50.77 ? 288 GLY A N 1 ATOM 1630 C CA . GLY A 1 206 ? 22.458 -37.555 26.832 1.00 37.74 ? 288 GLY A CA 1 ATOM 1631 C C . GLY A 1 206 ? 21.943 -38.870 26.275 1.00 37.01 ? 288 GLY A C 1 ATOM 1632 O O . GLY A 1 206 ? 20.745 -39.153 26.330 1.00 34.15 ? 288 GLY A O 1 ATOM 1633 N N . ILE A 1 207 ? 22.848 -39.673 25.726 1.00 26.64 ? 289 ILE A N 1 ATOM 1634 C CA . ILE A 1 207 ? 22.486 -40.985 25.199 1.00 21.42 ? 289 ILE A CA 1 ATOM 1635 C C . ILE A 1 207 ? 23.106 -42.064 26.088 1.00 21.49 ? 289 ILE A C 1 ATOM 1636 O O . ILE A 1 207 ? 24.298 -41.998 26.412 1.00 22.92 ? 289 ILE A O 1 ATOM 1637 C CB . ILE A 1 207 ? 22.940 -41.129 23.728 1.00 18.13 ? 289 ILE A CB 1 ATOM 1638 C CG1 . ILE A 1 207 ? 22.195 -40.118 22.849 1.00 19.81 ? 289 ILE A CG1 1 ATOM 1639 C CG2 . ILE A 1 207 ? 22.713 -42.548 23.217 1.00 18.66 ? 289 ILE A CG2 1 ATOM 1640 C CD1 . ILE A 1 207 ? 22.597 -40.135 21.376 1.00 20.07 ? 289 ILE A CD1 1 ATOM 1641 N N . THR A 1 208 ? 22.294 -43.032 26.514 1.00 20.72 ? 290 THR A N 1 ATOM 1642 C CA . THR A 1 208 ? 22.786 -44.125 27.356 1.00 16.32 ? 290 THR A CA 1 ATOM 1643 C C . THR A 1 208 ? 22.679 -45.458 26.615 1.00 22.16 ? 290 THR A C 1 ATOM 1644 O O . THR A 1 208 ? 21.611 -45.803 26.092 1.00 21.64 ? 290 THR A O 1 ATOM 1645 C CB . THR A 1 208 ? 22.007 -44.228 28.694 1.00 18.26 ? 290 THR A CB 1 ATOM 1646 O OG1 . THR A 1 208 ? 22.039 -42.971 29.384 1.00 22.04 ? 290 THR A OG1 1 ATOM 1647 C CG2 . THR A 1 208 ? 22.614 -45.304 29.585 1.00 21.43 ? 290 THR A CG2 1 ATOM 1648 N N . CYS A 1 209 ? 23.784 -46.199 26.572 1.00 21.69 ? 291 CYS A N 1 ATOM 1649 C CA . CYS A 1 209 ? 23.819 -47.506 25.926 1.00 22.26 ? 291 CYS A CA 1 ATOM 1650 C C . CYS A 1 209 ? 24.172 -48.597 26.926 1.00 23.38 ? 291 CYS A C 1 ATOM 1651 O O . CYS A 1 209 ? 25.207 -48.526 27.592 1.00 25.24 ? 291 CYS A O 1 ATOM 1652 C CB . CYS A 1 209 ? 24.842 -47.516 24.788 1.00 21.27 ? 291 CYS A CB 1 ATOM 1653 S SG . CYS A 1 209 ? 24.459 -46.378 23.455 1.00 24.81 ? 291 CYS A SG 1 ATOM 1654 N N . THR A 1 210 ? 23.306 -49.600 27.038 1.00 18.70 ? 292 THR A N 1 ATOM 1655 C CA . THR A 1 210 ? 23.602 -50.773 27.860 1.00 19.50 ? 292 THR A CA 1 ATOM 1656 C C . THR A 1 210 ? 23.990 -51.917 26.933 1.00 18.25 ? 292 THR A C 1 ATOM 1657 O O . THR A 1 210 ? 23.204 -52.300 26.059 1.00 21.64 ? 292 THR A O 1 ATOM 1658 C CB . THR A 1 210 ? 22.387 -51.192 28.705 1.00 17.56 ? 292 THR A CB 1 ATOM 1659 O OG1 . THR A 1 210 ? 21.883 -50.053 29.418 1.00 21.85 ? 292 THR A OG1 1 ATOM 1660 C CG2 . THR A 1 210 ? 22.784 -52.280 29.692 1.00 17.09 ? 292 THR A CG2 1 ATOM 1661 N N . CYS A 1 211 ? 25.189 -52.462 27.112 1.00 20.52 ? 293 CYS A N 1 ATOM 1662 C CA . CYS A 1 211 ? 25.720 -53.442 26.163 1.00 15.82 ? 293 CYS A CA 1 ATOM 1663 C C . CYS A 1 211 ? 25.966 -54.827 26.759 1.00 19.21 ? 293 CYS A C 1 ATOM 1664 O O . CYS A 1 211 ? 25.361 -55.217 27.764 1.00 17.70 ? 293 CYS A O 1 ATOM 1665 C CB . CYS A 1 211 ? 27.010 -52.905 25.538 1.00 17.84 ? 293 CYS A CB 1 ATOM 1666 S SG . CYS A 1 211 ? 26.903 -51.138 25.166 1.00 21.79 ? 293 CYS A SG 1 ATOM 1667 N N . LYS A 1 212 ? 26.855 -55.572 26.111 1.00 19.18 ? 294 LYS A N 1 ATOM 1668 C CA . LYS A 1 212 ? 27.160 -56.934 26.513 1.00 16.89 ? 294 LYS A CA 1 ATOM 1669 C C . LYS A 1 212 ? 28.672 -57.115 26.529 1.00 20.44 ? 294 LYS A C 1 ATOM 1670 O O . LYS A 1 212 ? 29.353 -56.809 25.541 1.00 20.56 ? 294 LYS A O 1 ATOM 1671 C CB . LYS A 1 212 ? 26.547 -57.934 25.525 1.00 21.05 ? 294 LYS A CB 1 ATOM 1672 C CG . LYS A 1 212 ? 26.899 -59.388 25.825 1.00 18.35 ? 294 LYS A CG 1 ATOM 1673 C CD . LYS A 1 212 ? 26.386 -60.340 24.754 1.00 25.75 ? 294 LYS A CD 1 ATOM 1674 C CE . LYS A 1 212 ? 27.426 -60.569 23.672 1.00 25.18 ? 294 LYS A CE 1 ATOM 1675 N NZ . LYS A 1 212 ? 27.090 -61.742 22.813 1.00 28.48 ? 294 LYS A NZ 1 ATOM 1676 N N . ASP A 1 213 ? 29.195 -57.592 27.654 1.00 17.30 ? 295 ASP A N 1 ATOM 1677 C CA . ASP A 1 213 ? 30.593 -58.005 27.741 1.00 19.69 ? 295 ASP A CA 1 ATOM 1678 C C . ASP A 1 213 ? 30.571 -59.495 27.502 1.00 23.24 ? 295 ASP A C 1 ATOM 1679 O O . ASP A 1 213 ? 30.170 -60.232 28.377 1.00 21.02 ? 295 ASP A O 1 ATOM 1680 C CB . ASP A 1 213 ? 31.136 -57.710 29.150 1.00 24.08 ? 295 ASP A CB 1 ATOM 1681 C CG . ASP A 1 213 ? 32.560 -58.245 29.385 1.00 23.28 ? 295 ASP A CG 1 ATOM 1682 O OD1 . ASP A 1 213 ? 32.918 -59.353 28.912 1.00 19.07 ? 295 ASP A OD1 1 ATOM 1683 O OD2 . ASP A 1 213 ? 33.328 -57.554 30.087 1.00 24.39 ? 295 ASP A OD2 1 ATOM 1684 N N . ASN A 1 214 ? 31.009 -59.950 26.336 1.00 23.61 ? 296 ASN A N 1 ATOM 1685 C CA . ASN A 1 214 ? 30.962 -61.380 26.048 1.00 29.16 ? 296 ASN A CA 1 ATOM 1686 C C . ASN A 1 214 ? 32.158 -62.135 26.627 1.00 33.61 ? 296 ASN A C 1 ATOM 1687 O O . ASN A 1 214 ? 32.108 -63.350 26.821 1.00 32.00 ? 296 ASN A O 1 ATOM 1688 C CB . ASN A 1 214 ? 30.884 -61.618 24.543 1.00 20.99 ? 296 ASN A CB 1 ATOM 1689 C CG . ASN A 1 214 ? 30.480 -63.037 24.203 1.00 26.39 ? 296 ASN A CG 1 ATOM 1690 O OD1 . ASN A 1 214 ? 29.314 -63.411 24.351 1.00 22.78 ? 296 ASN A OD1 1 ATOM 1691 N ND2 . ASN A 1 214 ? 31.438 -63.832 23.735 1.00 24.48 ? 296 ASN A ND2 1 ATOM 1692 N N . TRP A 1 215 ? 33.223 -61.398 26.913 1.00 27.48 ? 297 TRP A N 1 ATOM 1693 C CA . TRP A 1 215 ? 34.494 -61.987 27.323 1.00 24.69 ? 297 TRP A CA 1 ATOM 1694 C C . TRP A 1 215 ? 34.488 -62.544 28.759 1.00 26.58 ? 297 TRP A C 1 ATOM 1695 O O . TRP A 1 215 ? 34.656 -63.755 28.952 1.00 25.29 ? 297 TRP A O 1 ATOM 1696 C CB . TRP A 1 215 ? 35.608 -60.960 27.090 1.00 26.99 ? 297 TRP A CB 1 ATOM 1697 C CG . TRP A 1 215 ? 36.986 -61.342 27.541 1.00 30.46 ? 297 TRP A CG 1 ATOM 1698 C CD1 . TRP A 1 215 ? 37.474 -62.600 27.777 1.00 30.75 ? 297 TRP A CD1 1 ATOM 1699 C CD2 . TRP A 1 215 ? 38.062 -60.434 27.818 1.00 28.24 ? 297 TRP A CD2 1 ATOM 1700 N NE1 . TRP A 1 215 ? 38.791 -62.523 28.183 1.00 25.25 ? 297 TRP A NE1 1 ATOM 1701 C CE2 . TRP A 1 215 ? 39.172 -61.205 28.220 1.00 32.59 ? 297 TRP A CE2 1 ATOM 1702 C CE3 . TRP A 1 215 ? 38.191 -59.039 27.761 1.00 27.37 ? 297 TRP A CE3 1 ATOM 1703 C CZ2 . TRP A 1 215 ? 40.398 -60.624 28.568 1.00 28.64 ? 297 TRP A CZ2 1 ATOM 1704 C CZ3 . TRP A 1 215 ? 39.405 -58.465 28.110 1.00 28.57 ? 297 TRP A CZ3 1 ATOM 1705 C CH2 . TRP A 1 215 ? 40.492 -59.256 28.506 1.00 32.70 ? 297 TRP A CH2 1 ATOM 1706 N N . GLN A 1 216 ? 34.281 -61.687 29.761 1.00 32.55 ? 298 GLN A N 1 ATOM 1707 C CA . GLN A 1 216 ? 34.403 -62.135 31.155 1.00 31.11 ? 298 GLN A CA 1 ATOM 1708 C C . GLN A 1 216 ? 33.264 -61.748 32.100 1.00 33.09 ? 298 GLN A C 1 ATOM 1709 O O . GLN A 1 216 ? 33.116 -62.346 33.170 1.00 31.28 ? 298 GLN A O 1 ATOM 1710 C CB . GLN A 1 216 ? 35.696 -61.598 31.766 1.00 36.80 ? 298 GLN A CB 1 ATOM 1711 C CG . GLN A 1 216 ? 36.967 -62.159 31.186 1.00 36.89 ? 298 GLN A CG 1 ATOM 1712 C CD . GLN A 1 216 ? 38.184 -61.461 31.746 1.00 47.00 ? 298 GLN A CD 1 ATOM 1713 O OE1 . GLN A 1 216 ? 39.068 -62.099 32.321 1.00 48.00 ? 298 GLN A OE1 1 ATOM 1714 N NE2 . GLN A 1 216 ? 38.236 -60.134 31.588 1.00 35.64 ? 298 GLN A NE2 1 ATOM 1715 N N . GLY A 1 217 ? 32.478 -60.743 31.738 1.00 25.36 ? 299 GLY A N 1 ATOM 1716 C CA . GLY A 1 217 ? 31.567 -60.167 32.712 1.00 28.73 ? 299 GLY A CA 1 ATOM 1717 C C . GLY A 1 217 ? 30.096 -60.468 32.584 1.00 28.70 ? 299 GLY A C 1 ATOM 1718 O O . GLY A 1 217 ? 29.506 -60.246 31.536 1.00 31.56 ? 299 GLY A O 1 ATOM 1719 N N . SER A 1 218 ? 29.491 -60.915 33.677 1.00 27.37 ? 300 SER A N 1 ATOM 1720 C CA . SER A 1 218 ? 28.052 -61.139 33.693 1.00 23.16 ? 300 SER A CA 1 ATOM 1721 C C . SER A 1 218 ? 27.281 -59.919 34.177 1.00 27.78 ? 300 SER A C 1 ATOM 1722 O O . SER A 1 218 ? 26.048 -59.924 34.187 1.00 27.43 ? 300 SER A O 1 ATOM 1723 C CB . SER A 1 218 ? 27.711 -62.358 34.531 1.00 25.09 ? 300 SER A CB 1 ATOM 1724 O OG . SER A 1 218 ? 28.310 -63.517 33.977 1.00 24.10 ? 300 SER A OG 1 ATOM 1725 N N . ASN A 1 219 ? 28.000 -58.881 34.595 1.00 24.18 ? 301 ASN A N 1 ATOM 1726 C CA . ASN A 1 219 ? 27.380 -57.566 34.731 1.00 25.23 ? 301 ASN A CA 1 ATOM 1727 C C . ASN A 1 219 ? 27.439 -56.903 33.359 1.00 23.81 ? 301 ASN A C 1 ATOM 1728 O O . ASN A 1 219 ? 28.210 -57.343 32.500 1.00 23.11 ? 301 ASN A O 1 ATOM 1729 C CB . ASN A 1 219 ? 28.089 -56.709 35.788 1.00 18.00 ? 301 ASN A CB 1 ATOM 1730 C CG . ASN A 1 219 ? 29.609 -56.705 35.630 1.00 23.59 ? 301 ASN A CG 1 ATOM 1731 O OD1 . ASN A 1 219 ? 30.181 -57.554 34.942 1.00 23.74 ? 301 ASN A OD1 1 ATOM 1732 N ND2 . ASN A 1 219 ? 30.269 -55.757 36.288 1.00 20.48 ? 301 ASN A ND2 1 ATOM 1733 N N . ARG A 1 220 ? 26.636 -55.867 33.129 1.00 23.68 ? 302 ARG A N 1 ATOM 1734 C CA . ARG A 1 220 ? 26.628 -55.242 31.806 1.00 19.21 ? 302 ARG A CA 1 ATOM 1735 C C . ARG A 1 220 ? 27.434 -53.961 31.745 1.00 17.32 ? 302 ARG A C 1 ATOM 1736 O O . ARG A 1 220 ? 27.334 -53.110 32.637 1.00 18.88 ? 302 ARG A O 1 ATOM 1737 C CB . ARG A 1 220 ? 25.201 -54.978 31.313 1.00 16.11 ? 302 ARG A CB 1 ATOM 1738 C CG . ARG A 1 220 ? 24.401 -56.252 31.055 1.00 23.52 ? 302 ARG A CG 1 ATOM 1739 C CD . ARG A 1 220 ? 23.102 -55.973 30.299 1.00 17.09 ? 302 ARG A CD 1 ATOM 1740 N NE . ARG A 1 220 ? 22.407 -57.221 29.975 1.00 19.83 ? 302 ARG A NE 1 ATOM 1741 C CZ . ARG A 1 220 ? 22.675 -57.969 28.906 1.00 19.83 ? 302 ARG A CZ 1 ATOM 1742 N NH1 . ARG A 1 220 ? 23.619 -57.593 28.045 1.00 14.79 ? 302 ARG A NH1 1 ATOM 1743 N NH2 . ARG A 1 220 ? 22.002 -59.093 28.694 1.00 15.21 ? 302 ARG A NH2 1 ATOM 1744 N N . PRO A 1 221 ? 28.231 -53.816 30.675 1.00 19.60 ? 303 PRO A N 1 ATOM 1745 C CA . PRO A 1 221 ? 28.938 -52.561 30.412 1.00 22.03 ? 303 PRO A CA 1 ATOM 1746 C C . PRO A 1 221 ? 27.972 -51.490 29.943 1.00 25.63 ? 303 PRO A C 1 ATOM 1747 O O . PRO A 1 221 ? 26.961 -51.788 29.286 1.00 22.84 ? 303 PRO A O 1 ATOM 1748 C CB . PRO A 1 221 ? 29.921 -52.934 29.295 1.00 24.57 ? 303 PRO A CB 1 ATOM 1749 C CG . PRO A 1 221 ? 29.311 -54.100 28.620 1.00 23.53 ? 303 PRO A CG 1 ATOM 1750 C CD . PRO A 1 221 ? 28.555 -54.856 29.681 1.00 21.50 ? 303 PRO A CD 1 ATOM 1751 N N . VAL A 1 222 ? 28.270 -50.251 30.316 1.00 19.47 ? 304 VAL A N 1 ATOM 1752 C CA . VAL A 1 222 ? 27.452 -49.110 29.953 1.00 16.63 ? 304 VAL A CA 1 ATOM 1753 C C . VAL A 1 222 ? 28.332 -48.093 29.247 1.00 28.12 ? 304 VAL A C 1 ATOM 1754 O O . VAL A 1 222 ? 29.469 -47.842 29.666 1.00 24.12 ? 304 VAL A O 1 ATOM 1755 C CB . VAL A 1 222 ? 26.810 -48.462 31.195 1.00 20.52 ? 304 VAL A CB 1 ATOM 1756 C CG1 . VAL A 1 222 ? 26.115 -47.147 30.837 1.00 16.47 ? 304 VAL A CG1 1 ATOM 1757 C CG2 . VAL A 1 222 ? 25.828 -49.411 31.830 1.00 20.13 ? 304 VAL A CG2 1 ATOM 1758 N N . ILE A 1 223 ? 27.816 -47.532 28.159 1.00 24.22 ? 305 ILE A N 1 ATOM 1759 C CA . ILE A 1 223 ? 28.488 -46.443 27.470 1.00 17.99 ? 305 ILE A CA 1 ATOM 1760 C C . ILE A 1 223 ? 27.560 -45.246 27.484 1.00 21.68 ? 305 ILE A C 1 ATOM 1761 O O . ILE A 1 223 ? 26.410 -45.348 27.047 1.00 19.72 ? 305 ILE A O 1 ATOM 1762 C CB . ILE A 1 223 ? 28.809 -46.822 26.019 1.00 21.34 ? 305 ILE A CB 1 ATOM 1763 C CG1 . ILE A 1 223 ? 29.877 -47.924 25.989 1.00 17.89 ? 305 ILE A CG1 1 ATOM 1764 C CG2 . ILE A 1 223 ? 29.252 -45.592 25.222 1.00 17.84 ? 305 ILE A CG2 1 ATOM 1765 C CD1 . ILE A 1 223 ? 30.149 -48.468 24.587 1.00 22.76 ? 305 ILE A CD1 1 ATOM 1766 N N . GLN A 1 224 ? 28.046 -44.122 28.003 1.00 23.11 ? 306 GLN A N 1 ATOM 1767 C CA . GLN A 1 224 ? 27.249 -42.904 28.063 1.00 20.77 ? 306 GLN A CA 1 ATOM 1768 C C . GLN A 1 224 ? 27.813 -41.915 27.057 1.00 25.72 ? 306 GLN A C 1 ATOM 1769 O O . GLN A 1 224 ? 28.988 -41.571 27.120 1.00 21.78 ? 306 GLN A O 1 ATOM 1770 C CB . GLN A 1 224 ? 27.258 -42.322 29.485 1.00 25.43 ? 306 GLN A CB 1 ATOM 1771 C CG . GLN A 1 224 ? 26.424 -43.147 30.474 1.00 40.59 ? 306 GLN A CG 1 ATOM 1772 C CD . GLN A 1 224 ? 26.616 -42.733 31.923 1.00 42.31 ? 306 GLN A CD 1 ATOM 1773 O OE1 . GLN A 1 224 ? 27.697 -42.902 32.494 1.00 42.47 ? 306 GLN A OE1 1 ATOM 1774 N NE2 . GLN A 1 224 ? 25.562 -42.196 32.529 1.00 48.60 ? 306 GLN A NE2 1 ATOM 1775 N N . ILE A 1 225 ? 26.978 -41.469 26.124 1.00 25.15 ? 307 ILE A N 1 ATOM 1776 C CA . ILE A 1 225 ? 27.456 -40.672 24.998 1.00 24.10 ? 307 ILE A CA 1 ATOM 1777 C C . ILE A 1 225 ? 26.908 -39.251 25.044 1.00 21.27 ? 307 ILE A C 1 ATOM 1778 O O . ILE A 1 225 ? 25.692 -39.057 25.154 1.00 24.77 ? 307 ILE A O 1 ATOM 1779 C CB . ILE A 1 225 ? 27.035 -41.320 23.646 1.00 20.91 ? 307 ILE A CB 1 ATOM 1780 C CG1 . ILE A 1 225 ? 27.601 -42.738 23.528 1.00 19.02 ? 307 ILE A CG1 1 ATOM 1781 C CG2 . ILE A 1 225 ? 27.482 -40.467 22.466 1.00 18.66 ? 307 ILE A CG2 1 ATOM 1782 C CD1 . ILE A 1 225 ? 26.976 -43.568 22.399 1.00 16.40 ? 307 ILE A CD1 1 ATOM 1783 N N . ASP A 1 226 ? 27.800 -38.265 24.964 1.00 24.44 ? 308 ASP A N 1 ATOM 1784 C CA . ASP A 1 226 ? 27.394 -36.879 24.751 1.00 25.79 ? 308 ASP A CA 1 ATOM 1785 C C . ASP A 1 226 ? 27.339 -36.646 23.243 1.00 26.80 ? 308 ASP A C 1 ATOM 1786 O O . ASP A 1 226 ? 28.374 -36.655 22.583 1.00 26.89 ? 308 ASP A O 1 ATOM 1787 C CB . ASP A 1 226 ? 28.415 -35.930 25.384 1.00 27.16 ? 308 ASP A CB 1 ATOM 1788 C CG . ASP A 1 226 ? 27.984 -34.462 25.329 1.00 29.47 ? 308 ASP A CG 1 ATOM 1789 O OD1 . ASP A 1 226 ? 27.134 -34.090 24.483 1.00 25.96 ? 308 ASP A OD1 1 ATOM 1790 O OD2 . ASP A 1 226 ? 28.512 -33.673 26.148 1.00 33.23 ? 308 ASP A OD2 1 ATOM 1791 N N . PRO A 1 227 ? 26.131 -36.444 22.688 1.00 26.81 ? 309 PRO A N 1 ATOM 1792 C CA . PRO A 1 227 ? 26.000 -36.300 21.231 1.00 31.74 ? 309 PRO A CA 1 ATOM 1793 C C . PRO A 1 227 ? 26.318 -34.888 20.728 1.00 21.97 ? 309 PRO A C 1 ATOM 1794 O O . PRO A 1 227 ? 26.430 -34.699 19.510 1.00 28.35 ? 309 PRO A O 1 ATOM 1795 C CB . PRO A 1 227 ? 24.523 -36.629 20.982 1.00 22.13 ? 309 PRO A CB 1 ATOM 1796 C CG . PRO A 1 227 ? 23.835 -36.178 22.240 1.00 28.83 ? 309 PRO A CG 1 ATOM 1797 C CD . PRO A 1 227 ? 24.820 -36.471 23.362 1.00 28.34 ? 309 PRO A CD 1 ATOM 1798 N N . VAL A 1 228 ? 26.447 -33.917 21.631 1.00 29.52 ? 310 VAL A N 1 ATOM 1799 C CA . VAL A 1 228 ? 26.835 -32.563 21.223 1.00 28.94 ? 310 VAL A CA 1 ATOM 1800 C C . VAL A 1 228 ? 28.356 -32.452 21.135 1.00 29.09 ? 310 VAL A C 1 ATOM 1801 O O . VAL A 1 228 ? 28.902 -32.025 20.112 1.00 34.28 ? 310 VAL A O 1 ATOM 1802 C CB . VAL A 1 228 ? 26.293 -31.478 22.179 1.00 34.33 ? 310 VAL A CB 1 ATOM 1803 C CG1 . VAL A 1 228 ? 26.826 -30.097 21.776 1.00 30.45 ? 310 VAL A CG1 1 ATOM 1804 C CG2 . VAL A 1 228 ? 24.775 -31.478 22.183 1.00 27.54 ? 310 VAL A CG2 1 ATOM 1805 N N . ALA A 1 229 ? 29.030 -32.844 22.213 1.00 27.81 ? 311 ALA A N 1 ATOM 1806 C CA . ALA A 1 229 ? 30.490 -32.841 22.265 1.00 26.30 ? 311 ALA A CA 1 ATOM 1807 C C . ALA A 1 229 ? 31.062 -33.998 21.453 1.00 28.14 ? 311 ALA A C 1 ATOM 1808 O O . ALA A 1 229 ? 32.239 -33.975 21.062 1.00 28.25 ? 311 ALA A O 1 ATOM 1809 C CB . ALA A 1 229 ? 30.968 -32.933 23.714 1.00 23.98 ? 311 ALA A CB 1 ATOM 1810 N N . MET A 1 230 ? 30.221 -35.008 21.220 1.00 18.80 ? 312 MET A N 1 ATOM 1811 C CA . MET A 1 230 ? 30.623 -36.220 20.511 1.00 22.05 ? 312 MET A CA 1 ATOM 1812 C C . MET A 1 230 ? 31.733 -36.948 21.255 1.00 22.89 ? 312 MET A C 1 ATOM 1813 O O . MET A 1 230 ? 32.775 -37.281 20.687 1.00 20.48 ? 312 MET A O 1 ATOM 1814 C CB . MET A 1 230 ? 31.010 -35.919 19.063 1.00 18.44 ? 312 MET A CB 1 ATOM 1815 C CG . MET A 1 230 ? 29.858 -35.317 18.271 1.00 21.28 ? 312 MET A CG 1 ATOM 1816 S SD . MET A 1 230 ? 30.150 -35.277 16.494 1.00 26.09 ? 312 MET A SD 1 ATOM 1817 C CE . MET A 1 230 ? 31.507 -34.101 16.428 1.00 22.65 ? 312 MET A CE 1 ATOM 1818 N N . THR A 1 231 ? 31.494 -37.180 22.543 1.00 27.23 ? 313 THR A N 1 ATOM 1819 C CA . THR A 1 231 ? 32.415 -37.934 23.389 1.00 25.94 ? 313 THR A CA 1 ATOM 1820 C C . THR A 1 231 ? 31.603 -38.886 24.246 1.00 21.05 ? 313 THR A C 1 ATOM 1821 O O . THR A 1 231 ? 30.366 -38.834 24.248 1.00 24.74 ? 313 THR A O 1 ATOM 1822 C CB . THR A 1 231 ? 33.256 -37.019 24.301 1.00 30.97 ? 313 THR A CB 1 ATOM 1823 O OG1 . THR A 1 231 ? 32.389 -36.167 25.067 1.00 25.86 ? 313 THR A OG1 1 ATOM 1824 C CG2 . THR A 1 231 ? 34.216 -36.168 23.470 1.00 29.99 ? 313 THR A CG2 1 ATOM 1825 N N . HIS A 1 232 ? 32.291 -39.758 24.970 1.00 25.13 ? 314 HIS A N 1 ATOM 1826 C CA . HIS A 1 232 ? 31.611 -40.797 25.723 1.00 25.45 ? 314 HIS A CA 1 ATOM 1827 C C . HIS A 1 232 ? 32.476 -41.240 26.901 1.00 29.77 ? 314 HIS A C 1 ATOM 1828 O O . HIS A 1 232 ? 33.664 -40.913 26.966 1.00 22.21 ? 314 HIS A O 1 ATOM 1829 C CB . HIS A 1 232 ? 31.334 -42.001 24.815 1.00 22.61 ? 314 HIS A CB 1 ATOM 1830 C CG . HIS A 1 232 ? 32.557 -42.806 24.507 1.00 23.95 ? 314 HIS A CG 1 ATOM 1831 N ND1 . HIS A 1 232 ? 33.452 -42.454 23.516 1.00 23.48 ? 314 HIS A ND1 1 ATOM 1832 C CD2 . HIS A 1 232 ? 33.058 -43.927 25.081 1.00 24.43 ? 314 HIS A CD2 1 ATOM 1833 C CE1 . HIS A 1 232 ? 34.438 -43.331 23.484 1.00 27.53 ? 314 HIS A CE1 1 ATOM 1834 N NE2 . HIS A 1 232 ? 34.227 -44.233 24.430 1.00 24.00 ? 314 HIS A NE2 1 ATOM 1835 N N . THR A 1 233 ? 31.874 -41.978 27.828 1.00 25.78 ? 315 THR A N 1 ATOM 1836 C CA . THR A 1 233 ? 32.613 -42.664 28.884 1.00 23.95 ? 315 THR A CA 1 ATOM 1837 C C . THR A 1 233 ? 32.051 -44.077 28.957 1.00 22.35 ? 315 THR A C 1 ATOM 1838 O O . THR A 1 233 ? 30.994 -44.357 28.376 1.00 20.94 ? 315 THR A O 1 ATOM 1839 C CB . THR A 1 233 ? 32.433 -41.977 30.252 1.00 31.18 ? 315 THR A CB 1 ATOM 1840 O OG1 . THR A 1 233 ? 31.034 -41.783 30.513 1.00 30.50 ? 315 THR A OG1 1 ATOM 1841 C CG2 . THR A 1 233 ? 33.136 -40.626 30.275 1.00 33.90 ? 315 THR A CG2 1 ATOM 1842 N N . SER A 1 234 ? 32.743 -44.971 29.656 1.00 24.27 ? 316 SER A N 1 ATOM 1843 C CA . SER A 1 234 ? 32.201 -46.305 29.867 1.00 21.16 ? 316 SER A CA 1 ATOM 1844 C C . SER A 1 234 ? 32.501 -46.831 31.267 1.00 26.61 ? 316 SER A C 1 ATOM 1845 O O . SER A 1 234 ? 33.481 -46.426 31.913 1.00 25.12 ? 316 SER A O 1 ATOM 1846 C CB . SER A 1 234 ? 32.683 -47.290 28.789 1.00 20.75 ? 316 SER A CB 1 ATOM 1847 O OG . SER A 1 234 ? 33.987 -47.796 29.060 1.00 22.24 ? 316 SER A OG 1 ATOM 1848 N N . GLN A 1 235 ? 31.623 -47.712 31.735 1.00 23.27 ? 317 GLN A N 1 ATOM 1849 C CA . GLN A 1 235 ? 31.824 -48.455 32.975 1.00 21.73 ? 317 GLN A CA 1 ATOM 1850 C C . GLN A 1 235 ? 30.883 -49.660 32.942 1.00 21.38 ? 317 GLN A C 1 ATOM 1851 O O . GLN A 1 235 ? 30.422 -50.058 31.870 1.00 23.34 ? 317 GLN A O 1 ATOM 1852 C CB . GLN A 1 235 ? 31.552 -47.574 34.203 1.00 21.07 ? 317 GLN A CB 1 ATOM 1853 C CG . GLN A 1 235 ? 30.094 -47.105 34.351 1.00 22.23 ? 317 GLN A CG 1 ATOM 1854 C CD . GLN A 1 235 ? 29.840 -46.390 35.676 1.00 35.19 ? 317 GLN A CD 1 ATOM 1855 O OE1 . GLN A 1 235 ? 30.122 -45.197 35.811 1.00 27.75 ? 317 GLN A OE1 1 ATOM 1856 N NE2 . GLN A 1 235 ? 29.306 -47.120 36.662 1.00 21.02 ? 317 GLN A NE2 1 ATOM 1857 N N . TYR A 1 236 ? 30.603 -50.243 34.104 1.00 21.04 ? 318 TYR A N 1 ATOM 1858 C CA . TYR A 1 236 ? 29.634 -51.323 34.201 1.00 18.99 ? 318 TYR A CA 1 ATOM 1859 C C . TYR A 1 236 ? 28.481 -50.857 35.076 1.00 25.37 ? 318 TYR A C 1 ATOM 1860 O O . TYR A 1 236 ? 28.595 -49.848 35.770 1.00 20.24 ? 318 TYR A O 1 ATOM 1861 C CB . TYR A 1 236 ? 30.276 -52.573 34.813 1.00 20.88 ? 318 TYR A CB 1 ATOM 1862 C CG . TYR A 1 236 ? 31.201 -53.324 33.879 1.00 18.36 ? 318 TYR A CG 1 ATOM 1863 C CD1 . TYR A 1 236 ? 32.522 -52.929 33.715 1.00 21.03 ? 318 TYR A CD1 1 ATOM 1864 C CD2 . TYR A 1 236 ? 30.754 -54.442 33.175 1.00 23.95 ? 318 TYR A CD2 1 ATOM 1865 C CE1 . TYR A 1 236 ? 33.375 -53.615 32.863 1.00 22.27 ? 318 TYR A CE1 1 ATOM 1866 C CE2 . TYR A 1 236 ? 31.600 -55.136 32.319 1.00 20.11 ? 318 TYR A CE2 1 ATOM 1867 C CZ . TYR A 1 236 ? 32.912 -54.711 32.169 1.00 23.68 ? 318 TYR A CZ 1 ATOM 1868 O OH . TYR A 1 236 ? 33.782 -55.379 31.328 1.00 24.32 ? 318 TYR A OH 1 ATOM 1869 N N . ILE A 1 237 ? 27.361 -51.573 35.028 1.00 21.29 ? 319 ILE A N 1 ATOM 1870 C CA . ILE A 1 237 ? 26.313 -51.359 36.018 1.00 20.75 ? 319 ILE A CA 1 ATOM 1871 C C . ILE A 1 237 ? 26.877 -51.862 37.350 1.00 18.54 ? 319 ILE A C 1 ATOM 1872 O O . ILE A 1 237 ? 27.252 -53.036 37.461 1.00 20.76 ? 319 ILE A O 1 ATOM 1873 C CB . ILE A 1 237 ? 25.020 -52.120 35.645 1.00 21.78 ? 319 ILE A CB 1 ATOM 1874 C CG1 . ILE A 1 237 ? 24.486 -51.626 34.291 1.00 21.93 ? 319 ILE A CG1 1 ATOM 1875 C CG2 . ILE A 1 237 ? 23.953 -51.958 36.735 1.00 17.69 ? 319 ILE A CG2 1 ATOM 1876 C CD1 . ILE A 1 237 ? 23.295 -52.421 33.752 1.00 20.37 ? 319 ILE A CD1 1 ATOM 1877 N N . CYS A 1 238 ? 26.966 -50.978 38.344 1.00 17.87 ? 320 CYS A N 1 ATOM 1878 C CA . CYS A 1 238 ? 27.577 -51.332 39.635 1.00 21.63 ? 320 CYS A CA 1 ATOM 1879 C C . CYS A 1 238 ? 26.774 -52.400 40.374 1.00 19.97 ? 320 CYS A C 1 ATOM 1880 O O . CYS A 1 238 ? 27.327 -53.188 41.140 1.00 23.77 ? 320 CYS A O 1 ATOM 1881 C CB . CYS A 1 238 ? 27.694 -50.102 40.548 1.00 16.69 ? 320 CYS A CB 1 ATOM 1882 S SG . CYS A 1 238 ? 28.849 -48.794 40.028 1.00 28.60 ? 320 CYS A SG 1 ATOM 1883 N N . SER A 1 239 ? 25.464 -52.408 40.153 1.00 24.60 ? 321 SER A N 1 ATOM 1884 C CA . SER A 1 239 ? 24.554 -53.262 40.918 1.00 18.89 ? 321 SER A CA 1 ATOM 1885 C C . SER A 1 239 ? 24.934 -54.742 40.920 1.00 20.14 ? 321 SER A C 1 ATOM 1886 O O . SER A 1 239 ? 25.409 -55.275 39.911 1.00 24.81 ? 321 SER A O 1 ATOM 1887 C CB . SER A 1 239 ? 23.116 -53.094 40.412 1.00 22.12 ? 321 SER A CB 1 ATOM 1888 O OG . SER A 1 239 ? 22.216 -53.904 41.159 1.00 20.45 ? 321 SER A OG 1 ATOM 1889 N N . PRO A 1 240 ? 24.737 -55.408 42.070 1.00 21.70 ? 322 PRO A N 1 ATOM 1890 C CA . PRO A 1 240 ? 24.923 -56.861 42.156 1.00 18.43 ? 322 PRO A CA 1 ATOM 1891 C C . PRO A 1 240 ? 23.759 -57.634 41.541 1.00 21.88 ? 322 PRO A C 1 ATOM 1892 O O . PRO A 1 240 ? 23.807 -58.870 41.487 1.00 19.75 ? 322 PRO A O 1 ATOM 1893 C CB . PRO A 1 240 ? 24.991 -57.115 43.670 1.00 22.41 ? 322 PRO A CB 1 ATOM 1894 C CG . PRO A 1 240 ? 24.224 -55.982 44.280 1.00 24.03 ? 322 PRO A CG 1 ATOM 1895 C CD . PRO A 1 240 ? 24.535 -54.797 43.398 1.00 20.58 ? 322 PRO A CD 1 ATOM 1896 N N . VAL A 1 241 ? 22.722 -56.924 41.101 1.00 20.44 ? 323 VAL A N 1 ATOM 1897 C CA . VAL A 1 241 ? 21.671 -57.549 40.304 1.00 23.29 ? 323 VAL A CA 1 ATOM 1898 C C . VAL A 1 241 ? 22.221 -57.733 38.883 1.00 21.92 ? 323 VAL A C 1 ATOM 1899 O O . VAL A 1 241 ? 22.190 -56.803 38.067 1.00 21.18 ? 323 VAL A O 1 ATOM 1900 C CB . VAL A 1 241 ? 20.374 -56.706 40.310 1.00 24.60 ? 323 VAL A CB 1 ATOM 1901 C CG1 . VAL A 1 241 ? 19.307 -57.340 39.428 1.00 24.75 ? 323 VAL A CG1 1 ATOM 1902 C CG2 . VAL A 1 241 ? 19.850 -56.560 41.739 1.00 20.67 ? 323 VAL A CG2 1 ATOM 1903 N N . LEU A 1 242 ? 22.757 -58.922 38.607 1.00 18.40 ? 324 LEU A N 1 ATOM 1904 C CA . LEU A 1 242 ? 23.476 -59.175 37.357 1.00 20.33 ? 324 LEU A CA 1 ATOM 1905 C C . LEU A 1 242 ? 22.496 -59.481 36.231 1.00 22.08 ? 324 LEU A C 1 ATOM 1906 O O . LEU A 1 242 ? 21.496 -60.180 36.443 1.00 18.98 ? 324 LEU A O 1 ATOM 1907 C CB . LEU A 1 242 ? 24.452 -60.336 37.527 1.00 21.97 ? 324 LEU A CB 1 ATOM 1908 C CG . LEU A 1 242 ? 25.430 -60.207 38.693 1.00 24.69 ? 324 LEU A CG 1 ATOM 1909 C CD1 . LEU A 1 242 ? 26.355 -61.413 38.740 1.00 22.59 ? 324 LEU A CD1 1 ATOM 1910 C CD2 . LEU A 1 242 ? 26.226 -58.926 38.564 1.00 25.29 ? 324 LEU A CD2 1 ATOM 1911 N N . THR A 1 243 ? 22.773 -58.964 35.035 1.00 22.34 ? 325 THR A N 1 ATOM 1912 C CA . THR A 1 243 ? 21.766 -58.996 33.974 1.00 19.23 ? 325 THR A CA 1 ATOM 1913 C C . THR A 1 243 ? 22.175 -59.598 32.627 1.00 19.75 ? 325 THR A C 1 ATOM 1914 O O . THR A 1 243 ? 21.411 -59.518 31.655 1.00 18.31 ? 325 THR A O 1 ATOM 1915 C CB . THR A 1 243 ? 21.126 -57.609 33.767 1.00 19.14 ? 325 THR A CB 1 ATOM 1916 O OG1 . THR A 1 243 ? 22.133 -56.656 33.405 1.00 15.52 ? 325 THR A OG1 1 ATOM 1917 C CG2 . THR A 1 243 ? 20.428 -57.157 35.051 1.00 16.49 ? 325 THR A CG2 1 ATOM 1918 N N . ASP A 1 244 ? 23.335 -60.242 32.569 1.00 22.87 ? 326 ASP A N 1 ATOM 1919 C CA . ASP A 1 244 ? 23.728 -60.900 31.338 1.00 21.72 ? 326 ASP A CA 1 ATOM 1920 C C . ASP A 1 244 ? 23.137 -62.386 31.519 1.00 22.78 ? 326 ASP A C 1 ATOM 1921 O O . ASP A 1 244 ? 22.533 -62.720 32.539 1.00 22.33 ? 326 ASP A O 1 ATOM 1922 C CB . ASP A 1 244 ? 25.230 -60.880 31.108 1.00 21.52 ? 326 ASP A CB 1 ATOM 1923 C CG . ASP A 1 244 ? 25.605 -61.199 29.675 1.00 26.99 ? 326 ASP A CG 1 ATOM 1924 O OD1 . ASP A 1 244 ? 24.786 -61.785 28.932 1.00 29.21 ? 326 ASP A OD1 1 ATOM 1925 O OD2 . ASP A 1 244 ? 26.747 -60.874 29.301 1.00 30.14 ? 326 ASP A OD2 1 ATOM 1926 N N . ASN A 1 245 ? 23.357 -63.200 30.496 1.00 18.71 ? 327 ASN A N 1 ATOM 1927 C CA . ASN A 1 245 ? 22.963 -64.600 30.520 1.00 24.08 ? 327 ASN A CA 1 ATOM 1928 C C . ASN A 1 245 ? 23.876 -65.380 29.593 1.00 21.18 ? 327 ASN A C 1 ATOM 1929 O O . ASN A 1 245 ? 24.079 -64.972 28.446 1.00 19.49 ? 327 ASN A O 1 ATOM 1930 C CB . ASN A 1 245 ? 21.508 -64.777 30.084 1.00 17.41 ? 327 ASN A CB 1 ATOM 1931 C CG . ASN A 1 245 ? 21.104 -66.238 30.014 1.00 19.54 ? 327 ASN A CG 1 ATOM 1932 O OD1 . ASN A 1 245 ? 21.212 -66.873 28.963 1.00 21.85 ? 327 ASN A OD1 1 ATOM 1933 N ND2 . ASN A 1 245 ? 20.656 -66.790 31.145 1.00 21.57 ? 327 ASN A ND2 1 ATOM 1934 N N . PRO A 1 246 ? 24.447 -66.498 30.077 1.00 19.50 ? 328 PRO A N 1 ATOM 1935 C CA . PRO A 1 246 ? 24.343 -67.036 31.440 1.00 22.73 ? 328 PRO A CA 1 ATOM 1936 C C . PRO A 1 246 ? 25.078 -66.143 32.441 1.00 28.03 ? 328 PRO A C 1 ATOM 1937 O O . PRO A 1 246 ? 25.806 -65.239 32.019 1.00 23.05 ? 328 PRO A O 1 ATOM 1938 C CB . PRO A 1 246 ? 25.038 -68.398 31.330 1.00 26.77 ? 328 PRO A CB 1 ATOM 1939 C CG . PRO A 1 246 ? 25.997 -68.241 30.182 1.00 24.19 ? 328 PRO A CG 1 ATOM 1940 C CD . PRO A 1 246 ? 25.269 -67.358 29.205 1.00 26.36 ? 328 PRO A CD 1 ATOM 1941 N N . ARG A 1 247 ? 24.878 -66.378 33.735 1.00 23.27 ? 329 ARG A N 1 ATOM 1942 C CA . ARG A 1 247 ? 25.439 -65.507 34.763 1.00 20.05 ? 329 ARG A CA 1 ATOM 1943 C C . ARG A 1 247 ? 25.482 -66.223 36.115 1.00 26.51 ? 329 ARG A C 1 ATOM 1944 O O . ARG A 1 247 ? 24.710 -67.154 36.348 1.00 21.13 ? 329 ARG A O 1 ATOM 1945 C CB . ARG A 1 247 ? 24.581 -64.240 34.887 1.00 18.79 ? 329 ARG A CB 1 ATOM 1946 C CG . ARG A 1 247 ? 23.124 -64.524 35.315 1.00 21.36 ? 329 ARG A CG 1 ATOM 1947 C CD . ARG A 1 247 ? 22.360 -63.252 35.686 1.00 23.46 ? 329 ARG A CD 1 ATOM 1948 N NE . ARG A 1 247 ? 21.029 -63.556 36.222 1.00 19.09 ? 329 ARG A NE 1 ATOM 1949 C CZ . ARG A 1 247 ? 19.925 -63.646 35.481 1.00 18.95 ? 329 ARG A CZ 1 ATOM 1950 N NH1 . ARG A 1 247 ? 19.981 -63.441 34.165 1.00 16.07 ? 329 ARG A NH1 1 ATOM 1951 N NH2 . ARG A 1 247 ? 18.763 -63.935 36.056 1.00 20.48 ? 329 ARG A NH2 1 ATOM 1952 N N . PRO A 1 248 ? 26.385 -65.788 37.018 1.00 23.55 ? 330 PRO A N 1 ATOM 1953 C CA . PRO A 1 248 ? 26.378 -66.313 38.388 1.00 24.91 ? 330 PRO A CA 1 ATOM 1954 C C . PRO A 1 248 ? 25.157 -65.819 39.145 1.00 24.69 ? 330 PRO A C 1 ATOM 1955 O O . PRO A 1 248 ? 24.421 -64.962 38.641 1.00 24.12 ? 330 PRO A O 1 ATOM 1956 C CB . PRO A 1 248 ? 27.621 -65.671 39.021 1.00 27.49 ? 330 PRO A CB 1 ATOM 1957 C CG . PRO A 1 248 ? 28.461 -65.203 37.877 1.00 26.68 ? 330 PRO A CG 1 ATOM 1958 C CD . PRO A 1 248 ? 27.482 -64.830 36.808 1.00 23.02 ? 330 PRO A CD 1 ATOM 1959 N N . ASN A 1 249 ? 24.947 -66.339 40.348 1.00 26.80 ? 331 ASN A N 1 ATOM 1960 C CA . ASN A 1 249 ? 23.875 -65.832 41.188 1.00 27.05 ? 331 ASN A CA 1 ATOM 1961 C C . ASN A 1 249 ? 24.189 -64.417 41.663 1.00 21.66 ? 331 ASN A C 1 ATOM 1962 O O . ASN A 1 249 ? 25.357 -64.019 41.677 1.00 19.80 ? 331 ASN A O 1 ATOM 1963 C CB . ASN A 1 249 ? 23.605 -66.782 42.362 1.00 28.09 ? 331 ASN A CB 1 ATOM 1964 C CG . ASN A 1 249 ? 22.944 -68.076 41.916 1.00 32.14 ? 331 ASN A CG 1 ATOM 1965 O OD1 . ASN A 1 249 ? 22.020 -68.063 41.103 1.00 33.09 ? 331 ASN A OD1 1 ATOM 1966 N ND2 . ASN A 1 249 ? 23.432 -69.201 42.427 1.00 29.07 ? 331 ASN A ND2 1 ATOM 1967 N N . ASP A 1 250 ? 23.158 -63.653 42.019 1.00 21.50 ? 332 ASP A N 1 ATOM 1968 C CA . ASP A 1 250 ? 23.370 -62.281 42.476 1.00 25.75 ? 332 ASP A CA 1 ATOM 1969 C C . ASP A 1 250 ? 24.092 -62.263 43.820 1.00 27.84 ? 332 ASP A C 1 ATOM 1970 O O . ASP A 1 250 ? 23.574 -62.780 44.814 1.00 27.16 ? 332 ASP A O 1 ATOM 1971 C CB . ASP A 1 250 ? 22.045 -61.526 42.616 1.00 24.42 ? 332 ASP A CB 1 ATOM 1972 C CG . ASP A 1 250 ? 21.360 -61.276 41.281 1.00 29.11 ? 332 ASP A CG 1 ATOM 1973 O OD1 . ASP A 1 250 ? 22.029 -61.385 40.224 1.00 21.35 ? 332 ASP A OD1 1 ATOM 1974 O OD2 . ASP A 1 250 ? 20.145 -60.958 41.299 1.00 23.74 ? 332 ASP A OD2 1 ATOM 1975 N N . PRO A 1 251 ? 25.288 -61.658 43.855 1.00 21.88 ? 333 PRO A N 1 ATOM 1976 C CA . PRO A 1 251 ? 26.015 -61.451 45.112 1.00 18.72 ? 333 PRO A CA 1 ATOM 1977 C C . PRO A 1 251 ? 25.448 -60.222 45.818 1.00 20.80 ? 333 PRO A C 1 ATOM 1978 O O . PRO A 1 251 ? 24.375 -59.748 45.429 1.00 21.69 ? 333 PRO A O 1 ATOM 1979 C CB . PRO A 1 251 ? 27.437 -61.167 44.630 1.00 17.83 ? 333 PRO A CB 1 ATOM 1980 C CG . PRO A 1 251 ? 27.225 -60.425 43.331 1.00 23.48 ? 333 PRO A CG 1 ATOM 1981 C CD . PRO A 1 251 ? 26.007 -61.081 42.700 1.00 18.07 ? 333 PRO A CD 1 ATOM 1982 N N . ASN A 1 252 ? 26.149 -59.708 46.826 1.00 23.72 ? 334 ASN A N 1 ATOM 1983 C CA . ASN A 1 252 ? 25.696 -58.507 47.528 1.00 22.08 ? 334 ASN A CA 1 ATOM 1984 C C . ASN A 1 252 ? 26.555 -57.287 47.213 1.00 25.28 ? 334 ASN A C 1 ATOM 1985 O O . ASN A 1 252 ? 26.224 -56.166 47.610 1.00 27.21 ? 334 ASN A O 1 ATOM 1986 C CB . ASN A 1 252 ? 25.654 -58.728 49.044 1.00 26.06 ? 334 ASN A CB 1 ATOM 1987 C CG . ASN A 1 252 ? 24.571 -59.706 49.470 1.00 31.89 ? 334 ASN A CG 1 ATOM 1988 O OD1 . ASN A 1 252 ? 23.599 -59.942 48.747 1.00 27.10 ? 334 ASN A OD1 1 ATOM 1989 N ND2 . ASN A 1 252 ? 24.734 -60.275 50.661 1.00 27.28 ? 334 ASN A ND2 1 ATOM 1990 N N . ILE A 1 253 ? 27.666 -57.509 46.516 1.00 27.42 ? 335 ILE A N 1 ATOM 1991 C CA . ILE A 1 253 ? 28.487 -56.404 46.026 1.00 23.61 ? 335 ILE A CA 1 ATOM 1992 C C . ILE A 1 253 ? 28.750 -56.613 44.539 1.00 26.26 ? 335 ILE A C 1 ATOM 1993 O O . ILE A 1 253 ? 29.283 -57.658 44.136 1.00 25.87 ? 335 ILE A O 1 ATOM 1994 C CB . ILE A 1 253 ? 29.836 -56.305 46.772 1.00 26.49 ? 335 ILE A CB 1 ATOM 1995 C CG1 . ILE A 1 253 ? 29.618 -56.203 48.286 1.00 28.69 ? 335 ILE A CG1 1 ATOM 1996 C CG2 . ILE A 1 253 ? 30.661 -55.122 46.254 1.00 23.29 ? 335 ILE A CG2 1 ATOM 1997 C CD1 . ILE A 1 253 ? 30.915 -56.162 49.080 1.00 31.55 ? 335 ILE A CD1 1 ATOM 1998 N N . GLY A 1 254 ? 28.359 -55.635 43.724 1.00 22.80 ? 336 GLY A N 1 ATOM 1999 C CA . GLY A 1 254 ? 28.570 -55.728 42.290 1.00 21.53 ? 336 GLY A CA 1 ATOM 2000 C C . GLY A 1 254 ? 29.916 -55.136 41.927 1.00 27.28 ? 336 GLY A C 1 ATOM 2001 O O . GLY A 1 254 ? 30.744 -54.921 42.812 1.00 23.86 ? 336 GLY A O 1 ATOM 2002 N N . LYS A 1 255 ? 30.138 -54.871 40.639 1.00 26.86 ? 337 LYS A N 1 ATOM 2003 C CA . LYS A 1 255 ? 31.404 -54.286 40.188 1.00 24.95 ? 337 LYS A CA 1 ATOM 2004 C C . LYS A 1 255 ? 31.156 -53.150 39.197 1.00 26.64 ? 337 LYS A C 1 ATOM 2005 O O . LYS A 1 255 ? 30.467 -53.335 38.185 1.00 23.37 ? 337 LYS A O 1 ATOM 2006 C CB . LYS A 1 255 ? 32.314 -55.356 39.567 1.00 27.37 ? 337 LYS A CB 1 ATOM 2007 C CG . LYS A 1 255 ? 32.937 -56.324 40.572 1.00 26.19 ? 337 LYS A CG 1 ATOM 2008 C CD . LYS A 1 255 ? 34.186 -55.747 41.230 1.00 35.29 ? 337 LYS A CD 1 ATOM 2009 C CE . LYS A 1 255 ? 35.456 -56.206 40.524 1.00 36.02 ? 337 LYS A CE 1 ATOM 2010 N NZ . LYS A 1 255 ? 36.666 -55.472 41.009 1.00 37.48 ? 337 LYS A NZ 1 ATOM 2011 N N . CYS A 1 256 ? 31.715 -51.979 39.499 1.00 22.00 ? 338 CYS A N 1 ATOM 2012 C CA . CYS A 1 256 ? 31.515 -50.779 38.689 1.00 25.32 ? 338 CYS A CA 1 ATOM 2013 C C . CYS A 1 256 ? 32.480 -50.666 37.504 1.00 23.61 ? 338 CYS A C 1 ATOM 2014 O O . CYS A 1 256 ? 32.126 -50.105 36.458 1.00 26.46 ? 338 CYS A O 1 ATOM 2015 C CB . CYS A 1 256 ? 31.675 -49.520 39.551 1.00 20.17 ? 338 CYS A CB 1 ATOM 2016 S SG . CYS A 1 256 ? 30.553 -49.379 40.966 1.00 35.06 ? 338 CYS A SG 1 ATOM 2017 N N . ASN A 1 257 ? 33.698 -51.182 37.665 1.00 24.51 ? 339 ASN A N 1 ATOM 2018 C CA . ASN A 1 257 ? 34.772 -50.883 36.712 1.00 23.88 ? 339 ASN A CA 1 ATOM 2019 C C . ASN A 1 257 ? 35.516 -52.103 36.190 1.00 20.67 ? 339 ASN A C 1 ATOM 2020 O O . ASN A 1 257 ? 36.590 -51.981 35.592 1.00 24.05 ? 339 ASN A O 1 ATOM 2021 C CB . ASN A 1 257 ? 35.757 -49.885 37.331 1.00 22.77 ? 339 ASN A CB 1 ATOM 2022 C CG . ASN A 1 257 ? 35.132 -48.533 37.571 1.00 29.28 ? 339 ASN A CG 1 ATOM 2023 O OD1 . ASN A 1 257 ? 34.630 -47.890 36.640 1.00 36.91 ? 339 ASN A OD1 1 ATOM 2024 N ND2 . ASN A 1 257 ? 35.130 -48.098 38.828 1.00 28.69 ? 339 ASN A ND2 1 ATOM 2025 N N . ASP A 1 258 ? 34.946 -53.278 36.421 1.00 25.85 ? 340 ASP A N 1 ATOM 2026 C CA . ASP A 1 258 ? 35.493 -54.517 35.884 1.00 24.88 ? 340 ASP A CA 1 ATOM 2027 C C . ASP A 1 258 ? 34.369 -55.543 35.743 1.00 25.25 ? 340 ASP A C 1 ATOM 2028 O O . ASP A 1 258 ? 33.302 -55.386 36.336 1.00 25.97 ? 340 ASP A O 1 ATOM 2029 C CB . ASP A 1 258 ? 36.634 -55.043 36.770 1.00 26.52 ? 340 ASP A CB 1 ATOM 2030 C CG . ASP A 1 258 ? 38.004 -54.583 36.295 1.00 31.62 ? 340 ASP A CG 1 ATOM 2031 O OD1 . ASP A 1 258 ? 38.252 -54.601 35.065 1.00 25.94 ? 340 ASP A OD1 1 ATOM 2032 O OD2 . ASP A 1 258 ? 38.830 -54.200 37.152 1.00 33.82 ? 340 ASP A OD2 1 ATOM 2033 N N . PRO A 1 259 ? 34.592 -56.578 34.923 1.00 25.88 ? 341 PRO A N 1 ATOM 2034 C CA . PRO A 1 259 ? 33.599 -57.639 34.752 1.00 26.37 ? 341 PRO A CA 1 ATOM 2035 C C . PRO A 1 259 ? 33.360 -58.424 36.041 1.00 28.02 ? 341 PRO A C 1 ATOM 2036 O O . PRO A 1 259 ? 34.332 -58.763 36.727 1.00 27.01 ? 341 PRO A O 1 ATOM 2037 C CB . PRO A 1 259 ? 34.259 -58.554 33.709 1.00 22.56 ? 341 PRO A CB 1 ATOM 2038 C CG . PRO A 1 259 ? 35.717 -58.223 33.748 1.00 24.26 ? 341 PRO A CG 1 ATOM 2039 C CD . PRO A 1 259 ? 35.737 -56.754 34.010 1.00 20.66 ? 341 PRO A CD 1 ATOM 2040 N N . TYR A 1 260 ? 32.102 -58.706 36.377 1.00 26.10 ? 342 TYR A N 1 ATOM 2041 C CA . TYR A 1 260 ? 31.832 -59.662 37.448 1.00 22.58 ? 342 TYR A CA 1 ATOM 2042 C C . TYR A 1 260 ? 32.046 -61.069 36.893 1.00 24.07 ? 342 TYR A C 1 ATOM 2043 O O . TYR A 1 260 ? 31.466 -61.428 35.870 1.00 21.53 ? 342 TYR A O 1 ATOM 2044 C CB . TYR A 1 260 ? 30.421 -59.507 38.035 1.00 26.80 ? 342 TYR A CB 1 ATOM 2045 C CG . TYR A 1 260 ? 30.282 -60.268 39.338 1.00 27.52 ? 342 TYR A CG 1 ATOM 2046 C CD1 . TYR A 1 260 ? 29.838 -61.585 39.353 1.00 24.32 ? 342 TYR A CD1 1 ATOM 2047 C CD2 . TYR A 1 260 ? 30.648 -59.683 40.548 1.00 29.54 ? 342 TYR A CD2 1 ATOM 2048 C CE1 . TYR A 1 260 ? 29.738 -62.293 40.535 1.00 30.09 ? 342 TYR A CE1 1 ATOM 2049 C CE2 . TYR A 1 260 ? 30.552 -60.381 41.738 1.00 30.12 ? 342 TYR A CE2 1 ATOM 2050 C CZ . TYR A 1 260 ? 30.094 -61.684 41.725 1.00 32.35 ? 342 TYR A CZ 1 ATOM 2051 O OH . TYR A 1 260 ? 29.993 -62.383 42.907 1.00 39.85 ? 342 TYR A OH 1 ATOM 2052 N N . PRO A 1 261 ? 32.901 -61.863 37.559 1.00 24.66 ? 343 PRO A N 1 ATOM 2053 C CA . PRO A 1 261 ? 33.369 -63.153 37.032 1.00 25.00 ? 343 PRO A CA 1 ATOM 2054 C C . PRO A 1 261 ? 32.429 -64.332 37.304 1.00 24.96 ? 343 PRO A C 1 ATOM 2055 O O . PRO A 1 261 ? 31.571 -64.266 38.192 1.00 23.87 ? 343 PRO A O 1 ATOM 2056 C CB . PRO A 1 261 ? 34.689 -63.359 37.781 1.00 25.99 ? 343 PRO A CB 1 ATOM 2057 C CG . PRO A 1 261 ? 34.449 -62.713 39.114 1.00 29.71 ? 343 PRO A CG 1 ATOM 2058 C CD . PRO A 1 261 ? 33.535 -61.528 38.848 1.00 21.37 ? 343 PRO A CD 1 ATOM 2059 N N . GLY A 1 262 ? 32.602 -65.409 36.543 1.00 26.69 ? 344 GLY A N 1 ATOM 2060 C CA . GLY A 1 262 ? 31.828 -66.620 36.744 1.00 25.92 ? 344 GLY A CA 1 ATOM 2061 C C . GLY A 1 262 ? 31.478 -67.319 35.441 1.00 29.23 ? 344 GLY A C 1 ATOM 2062 O O . GLY A 1 262 ? 31.485 -68.553 35.357 1.00 29.06 ? 344 GLY A O 1 ATOM 2063 N N . ASN A 1 263 ? 31.154 -66.523 34.425 1.00 24.53 ? 345 ASN A N 1 ATOM 2064 C CA . ASN A 1 263 ? 30.832 -67.047 33.103 1.00 28.72 ? 345 ASN A CA 1 ATOM 2065 C C . ASN A 1 263 ? 31.667 -66.326 32.049 1.00 23.66 ? 345 ASN A C 1 ATOM 2066 O O . ASN A 1 263 ? 31.623 -65.095 31.936 1.00 29.25 ? 345 ASN A O 1 ATOM 2067 C CB . ASN A 1 263 ? 29.333 -66.901 32.800 1.00 23.25 ? 345 ASN A CB 1 ATOM 2068 C CG . ASN A 1 263 ? 28.459 -67.676 33.777 1.00 28.54 ? 345 ASN A CG 1 ATOM 2069 O OD1 . ASN A 1 263 ? 28.201 -67.218 34.888 1.00 32.03 ? 345 ASN A OD1 1 ATOM 2070 N ND2 . ASN A 1 263 ? 27.994 -68.851 33.361 1.00 27.30 ? 345 ASN A ND2 1 ATOM 2071 N N . ASN A 1 264 ? 32.445 -67.098 31.300 1.00 26.03 ? 346 ASN A N 1 ATOM 2072 C CA . ASN A 1 264 ? 33.320 -66.543 30.277 1.00 33.96 ? 346 ASN A CA 1 ATOM 2073 C C . ASN A 1 264 ? 32.814 -66.864 28.873 1.00 32.66 ? 346 ASN A C 1 ATOM 2074 O O . ASN A 1 264 ? 32.118 -67.864 28.671 1.00 29.29 ? 346 ASN A O 1 ATOM 2075 C CB . ASN A 1 264 ? 34.742 -67.089 30.449 1.00 36.77 ? 346 ASN A CB 1 ATOM 2076 C CG . ASN A 1 264 ? 35.360 -66.713 31.791 1.00 46.28 ? 346 ASN A CG 1 ATOM 2077 O OD1 . ASN A 1 264 ? 35.259 -65.570 32.236 1.00 40.67 ? 346 ASN A OD1 1 ATOM 2078 N ND2 . ASN A 1 264 ? 36.001 -67.679 32.439 1.00 52.91 ? 346 ASN A ND2 1 ATOM 2079 N N . ASN A 1 265 ? 33.158 -66.014 27.908 1.00 28.70 ? 347 ASN A N 1 ATOM 2080 C CA . ASN A 1 265 ? 32.919 -66.319 26.497 1.00 21.98 ? 347 ASN A CA 1 ATOM 2081 C C . ASN A 1 265 ? 31.464 -66.658 26.146 1.00 23.97 ? 347 ASN A C 1 ATOM 2082 O O . ASN A 1 265 ? 31.205 -67.597 25.394 1.00 21.62 ? 347 ASN A O 1 ATOM 2083 C CB . ASN A 1 265 ? 33.835 -67.462 26.036 1.00 25.59 ? 347 ASN A CB 1 ATOM 2084 C CG . ASN A 1 265 ? 35.311 -67.161 26.259 1.00 36.42 ? 347 ASN A CG 1 ATOM 2085 O OD1 . ASN A 1 265 ? 35.720 -66.002 26.337 1.00 32.35 ? 347 ASN A OD1 1 ATOM 2086 N ND2 . ASN A 1 265 ? 36.117 -68.213 26.354 1.00 37.79 ? 347 ASN A ND2 1 ATOM 2087 N N . ASN A 1 266 ? 30.520 -65.911 26.707 1.00 21.32 ? 348 ASN A N 1 ATOM 2088 C CA . ASN A 1 266 ? 29.108 -66.061 26.347 1.00 33.05 ? 348 ASN A CA 1 ATOM 2089 C C . ASN A 1 266 ? 28.351 -64.831 26.805 1.00 35.07 ? 348 ASN A C 1 ATOM 2090 O O . ASN A 1 266 ? 28.939 -63.949 27.415 1.00 25.93 ? 348 ASN A O 1 ATOM 2091 C CB . ASN A 1 266 ? 28.485 -67.351 26.914 1.00 27.52 ? 348 ASN A CB 1 ATOM 2092 C CG . ASN A 1 266 ? 28.927 -67.650 28.336 1.00 42.54 ? 348 ASN A CG 1 ATOM 2093 O OD1 . ASN A 1 266 ? 29.132 -66.740 29.145 1.00 43.86 ? 348 ASN A OD1 1 ATOM 2094 N ND2 . ASN A 1 266 ? 29.076 -68.936 28.649 1.00 47.59 ? 348 ASN A ND2 1 ATOM 2095 N N . GLY A 1 267 ? 27.065 -64.751 26.494 1.00 25.44 ? 349 GLY A N 1 ATOM 2096 C CA . GLY A 1 267 ? 26.286 -63.587 26.880 1.00 24.27 ? 349 GLY A CA 1 ATOM 2097 C C . GLY A 1 267 ? 25.085 -63.410 25.975 1.00 23.91 ? 349 GLY A C 1 ATOM 2098 O O . GLY A 1 267 ? 24.958 -64.111 24.965 1.00 20.44 ? 349 GLY A O 1 ATOM 2099 N N . VAL A 1 268 ? 24.200 -62.482 26.334 1.00 16.04 ? 350 VAL A N 1 ATOM 2100 C CA . VAL A 1 268 ? 23.060 -62.159 25.485 1.00 18.90 ? 350 VAL A CA 1 ATOM 2101 C C . VAL A 1 268 ? 22.922 -60.643 25.367 1.00 18.86 ? 350 VAL A C 1 ATOM 2102 O O . VAL A 1 268 ? 23.262 -59.909 26.305 1.00 20.95 ? 350 VAL A O 1 ATOM 2103 C CB . VAL A 1 268 ? 21.737 -62.818 26.004 1.00 16.97 ? 350 VAL A CB 1 ATOM 2104 C CG1 . VAL A 1 268 ? 21.139 -62.026 27.157 1.00 16.36 ? 350 VAL A CG1 1 ATOM 2105 C CG2 . VAL A 1 268 ? 20.719 -62.932 24.880 1.00 14.34 ? 350 VAL A CG2 1 ATOM 2106 N N . LYS A 1 269 ? 22.465 -60.165 24.209 1.00 20.63 ? 351 LYS A N 1 ATOM 2107 C CA . LYS A 1 269 ? 22.138 -58.750 24.070 1.00 21.86 ? 351 LYS A CA 1 ATOM 2108 C C . LYS A 1 269 ? 20.986 -58.414 25.013 1.00 21.52 ? 351 LYS A C 1 ATOM 2109 O O . LYS A 1 269 ? 19.991 -59.155 25.076 1.00 16.63 ? 351 LYS A O 1 ATOM 2110 C CB . LYS A 1 269 ? 21.752 -58.394 22.629 1.00 18.10 ? 351 LYS A CB 1 ATOM 2111 C CG . LYS A 1 269 ? 21.266 -56.943 22.464 1.00 18.01 ? 351 LYS A CG 1 ATOM 2112 C CD . LYS A 1 269 ? 20.836 -56.636 21.030 1.00 15.92 ? 351 LYS A CD 1 ATOM 2113 C CE . LYS A 1 269 ? 20.131 -55.288 20.947 1.00 17.16 ? 351 LYS A CE 1 ATOM 2114 N NZ . LYS A 1 269 ? 21.063 -54.127 21.174 1.00 20.14 ? 351 LYS A NZ 1 ATOM 2115 N N . GLY A 1 270 ? 21.138 -57.314 25.753 1.00 15.63 ? 352 GLY A N 1 ATOM 2116 C CA . GLY A 1 270 ? 20.123 -56.852 26.688 1.00 14.62 ? 352 GLY A CA 1 ATOM 2117 C C . GLY A 1 270 ? 20.099 -55.337 26.809 1.00 20.43 ? 352 GLY A C 1 ATOM 2118 O O . GLY A 1 270 ? 20.728 -54.635 26.010 1.00 16.92 ? 352 GLY A O 1 ATOM 2119 N N . PHE A 1 271 ? 19.390 -54.824 27.816 1.00 17.45 ? 353 PHE A N 1 ATOM 2120 C CA . PHE A 1 271 ? 19.201 -53.382 27.938 1.00 17.82 ? 353 PHE A CA 1 ATOM 2121 C C . PHE A 1 271 ? 18.919 -52.982 29.383 1.00 18.18 ? 353 PHE A C 1 ATOM 2122 O O . PHE A 1 271 ? 18.662 -53.832 30.237 1.00 21.71 ? 353 PHE A O 1 ATOM 2123 C CB . PHE A 1 271 ? 18.013 -52.932 27.077 1.00 16.04 ? 353 PHE A CB 1 ATOM 2124 C CG . PHE A 1 271 ? 16.683 -53.167 27.730 1.00 19.52 ? 353 PHE A CG 1 ATOM 2125 C CD1 . PHE A 1 271 ? 16.088 -54.421 27.689 1.00 21.74 ? 353 PHE A CD1 1 ATOM 2126 C CD2 . PHE A 1 271 ? 16.032 -52.139 28.402 1.00 20.61 ? 353 PHE A CD2 1 ATOM 2127 C CE1 . PHE A 1 271 ? 14.867 -54.641 28.297 1.00 20.06 ? 353 PHE A CE1 1 ATOM 2128 C CE2 . PHE A 1 271 ? 14.817 -52.352 29.019 1.00 17.31 ? 353 PHE A CE2 1 ATOM 2129 C CZ . PHE A 1 271 ? 14.235 -53.605 28.972 1.00 21.75 ? 353 PHE A CZ 1 ATOM 2130 N N . SER A 1 272 ? 18.944 -51.678 29.648 1.00 18.46 ? 354 SER A N 1 ATOM 2131 C CA . SER A 1 272 ? 18.453 -51.159 30.916 1.00 20.43 ? 354 SER A CA 1 ATOM 2132 C C . SER A 1 272 ? 18.036 -49.715 30.723 1.00 23.86 ? 354 SER A C 1 ATOM 2133 O O . SER A 1 272 ? 18.413 -49.082 29.728 1.00 22.27 ? 354 SER A O 1 ATOM 2134 C CB . SER A 1 272 ? 19.534 -51.246 31.994 1.00 18.21 ? 354 SER A CB 1 ATOM 2135 O OG . SER A 1 272 ? 20.565 -50.305 31.759 1.00 21.80 ? 354 SER A OG 1 ATOM 2136 N N . TYR A 1 273 ? 17.242 -49.202 31.660 1.00 22.12 ? 355 TYR A N 1 ATOM 2137 C CA . TYR A 1 273 ? 16.974 -47.772 31.735 1.00 19.87 ? 355 TYR A CA 1 ATOM 2138 C C . TYR A 1 273 ? 17.551 -47.261 33.047 1.00 27.07 ? 355 TYR A C 1 ATOM 2139 O O . TYR A 1 273 ? 17.063 -47.602 34.132 1.00 23.74 ? 355 TYR A O 1 ATOM 2140 C CB . TYR A 1 273 ? 15.476 -47.472 31.616 1.00 22.76 ? 355 TYR A CB 1 ATOM 2141 C CG . TYR A 1 273 ? 14.985 -47.484 30.182 1.00 18.05 ? 355 TYR A CG 1 ATOM 2142 C CD1 . TYR A 1 273 ? 15.055 -46.337 29.398 1.00 18.32 ? 355 TYR A CD1 1 ATOM 2143 C CD2 . TYR A 1 273 ? 14.473 -48.643 29.611 1.00 15.67 ? 355 TYR A CD2 1 ATOM 2144 C CE1 . TYR A 1 273 ? 14.618 -46.337 28.084 1.00 13.13 ? 355 TYR A CE1 1 ATOM 2145 C CE2 . TYR A 1 273 ? 14.031 -48.659 28.295 1.00 18.63 ? 355 TYR A CE2 1 ATOM 2146 C CZ . TYR A 1 273 ? 14.106 -47.501 27.540 1.00 15.24 ? 355 TYR A CZ 1 ATOM 2147 O OH . TYR A 1 273 ? 13.671 -47.500 26.234 1.00 18.40 ? 355 TYR A OH 1 ATOM 2148 N N . LEU A 1 274 ? 18.620 -46.477 32.938 1.00 20.82 ? 356 LEU A N 1 ATOM 2149 C CA . LEU A 1 274 ? 19.381 -46.024 34.100 1.00 24.34 ? 356 LEU A CA 1 ATOM 2150 C C . LEU A 1 274 ? 19.035 -44.569 34.407 1.00 25.47 ? 356 LEU A C 1 ATOM 2151 O O . LEU A 1 274 ? 19.474 -43.658 33.700 1.00 23.76 ? 356 LEU A O 1 ATOM 2152 C CB . LEU A 1 274 ? 20.881 -46.176 33.826 1.00 21.50 ? 356 LEU A CB 1 ATOM 2153 C CG . LEU A 1 274 ? 21.290 -47.582 33.383 1.00 23.71 ? 356 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 274 ? 22.729 -47.638 32.877 1.00 23.75 ? 356 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 274 ? 21.075 -48.597 34.516 1.00 17.31 ? 356 LEU A CD2 1 ATOM 2156 N N . ASP A 1 275 ? 18.252 -44.355 35.463 1.00 25.55 ? 357 ASP A N 1 ATOM 2157 C CA . ASP A 1 275 ? 17.654 -43.047 35.707 1.00 28.25 ? 357 ASP A CA 1 ATOM 2158 C C . ASP A 1 275 ? 17.412 -42.792 37.202 1.00 27.07 ? 357 ASP A C 1 ATOM 2159 O O . ASP A 1 275 ? 16.267 -42.586 37.624 1.00 24.44 ? 357 ASP A O 1 ATOM 2160 C CB . ASP A 1 275 ? 16.328 -42.951 34.939 1.00 28.81 ? 357 ASP A CB 1 ATOM 2161 C CG . ASP A 1 275 ? 15.755 -41.545 34.929 1.00 25.60 ? 357 ASP A CG 1 ATOM 2162 O OD1 . ASP A 1 275 ? 16.552 -40.582 34.942 1.00 32.21 ? 357 ASP A OD1 1 ATOM 2163 O OD2 . ASP A 1 275 ? 14.507 -41.408 34.899 1.00 29.44 ? 357 ASP A OD2 1 ATOM 2164 N N . GLY A 1 276 ? 18.484 -42.792 37.996 1.00 28.90 ? 358 GLY A N 1 ATOM 2165 C CA . GLY A 1 276 ? 18.372 -42.589 39.437 1.00 20.75 ? 358 GLY A CA 1 ATOM 2166 C C . GLY A 1 276 ? 17.383 -43.540 40.094 1.00 22.82 ? 358 GLY A C 1 ATOM 2167 O O . GLY A 1 276 ? 17.470 -44.757 39.917 1.00 23.79 ? 358 GLY A O 1 ATOM 2168 N N . ALA A 1 277 ? 16.426 -42.988 40.838 1.00 20.70 ? 359 ALA A N 1 ATOM 2169 C CA . ALA A 1 277 ? 15.407 -43.805 41.493 1.00 26.75 ? 359 ALA A CA 1 ATOM 2170 C C . ALA A 1 277 ? 14.409 -44.391 40.491 1.00 27.07 ? 359 ALA A C 1 ATOM 2171 O O . ALA A 1 277 ? 13.589 -45.244 40.852 1.00 26.59 ? 359 ALA A O 1 ATOM 2172 C CB . ALA A 1 277 ? 14.678 -43.000 42.564 1.00 22.49 ? 359 ALA A CB 1 ATOM 2173 N N . ASN A 1 278 ? 14.470 -43.932 39.242 1.00 25.46 ? 360 ASN A N 1 ATOM 2174 C CA . ASN A 1 278 ? 13.582 -44.445 38.198 1.00 26.39 ? 360 ASN A CA 1 ATOM 2175 C C . ASN A 1 278 ? 14.278 -45.510 37.343 1.00 26.43 ? 360 ASN A C 1 ATOM 2176 O O . ASN A 1 278 ? 13.910 -45.736 36.186 1.00 25.82 ? 360 ASN A O 1 ATOM 2177 C CB . ASN A 1 278 ? 13.070 -43.295 37.323 1.00 23.26 ? 360 ASN A CB 1 ATOM 2178 C CG . ASN A 1 278 ? 11.851 -43.679 36.493 1.00 26.97 ? 360 ASN A CG 1 ATOM 2179 O OD1 . ASN A 1 278 ? 10.950 -44.385 36.969 1.00 23.75 ? 360 ASN A OD1 1 ATOM 2180 N ND2 . ASN A 1 278 ? 11.819 -43.219 35.244 1.00 24.12 ? 360 ASN A ND2 1 ATOM 2181 N N . THR A 1 279 ? 15.277 -46.173 37.922 1.00 19.76 ? 361 THR A N 1 ATOM 2182 C CA . THR A 1 279 ? 16.044 -47.190 37.203 1.00 20.32 ? 361 THR A CA 1 ATOM 2183 C C . THR A 1 279 ? 15.334 -48.546 37.129 1.00 20.66 ? 361 THR A C 1 ATOM 2184 O O . THR A 1 279 ? 14.882 -49.070 38.151 1.00 18.92 ? 361 THR A O 1 ATOM 2185 C CB . THR A 1 279 ? 17.439 -47.376 37.828 1.00 17.08 ? 361 THR A CB 1 ATOM 2186 O OG1 . THR A 1 279 ? 18.216 -46.188 37.622 1.00 19.58 ? 361 THR A OG1 1 ATOM 2187 C CG2 . THR A 1 279 ? 18.167 -48.570 37.196 1.00 19.15 ? 361 THR A CG2 1 ATOM 2188 N N . TRP A 1 280 ? 15.245 -49.105 35.919 1.00 22.19 ? 362 TRP A N 1 ATOM 2189 C CA . TRP A 1 280 ? 14.742 -50.467 35.718 1.00 23.45 ? 362 TRP A CA 1 ATOM 2190 C C . TRP A 1 280 ? 15.707 -51.291 34.864 1.00 23.88 ? 362 TRP A C 1 ATOM 2191 O O . TRP A 1 280 ? 16.225 -50.807 33.848 1.00 20.69 ? 362 TRP A O 1 ATOM 2192 C CB . TRP A 1 280 ? 13.365 -50.450 35.047 1.00 24.65 ? 362 TRP A CB 1 ATOM 2193 C CG . TRP A 1 280 ? 12.244 -50.022 35.949 1.00 26.71 ? 362 TRP A CG 1 ATOM 2194 C CD1 . TRP A 1 280 ? 11.987 -48.756 36.393 1.00 21.43 ? 362 TRP A CD1 1 ATOM 2195 C CD2 . TRP A 1 280 ? 11.212 -50.858 36.498 1.00 19.15 ? 362 TRP A CD2 1 ATOM 2196 N NE1 . TRP A 1 280 ? 10.864 -48.755 37.192 1.00 16.02 ? 362 TRP A NE1 1 ATOM 2197 C CE2 . TRP A 1 280 ? 10.373 -50.032 37.275 1.00 21.68 ? 362 TRP A CE2 1 ATOM 2198 C CE3 . TRP A 1 280 ? 10.925 -52.225 36.416 1.00 22.84 ? 362 TRP A CE3 1 ATOM 2199 C CZ2 . TRP A 1 280 ? 9.258 -50.530 37.958 1.00 23.31 ? 362 TRP A CZ2 1 ATOM 2200 C CZ3 . TRP A 1 280 ? 9.817 -52.719 37.101 1.00 26.26 ? 362 TRP A CZ3 1 ATOM 2201 C CH2 . TRP A 1 280 ? 8.998 -51.874 37.858 1.00 22.18 ? 362 TRP A CH2 1 ATOM 2202 N N . LEU A 1 281 ? 15.932 -52.540 35.267 1.00 21.07 ? 363 LEU A N 1 ATOM 2203 C CA . LEU A 1 281 ? 16.829 -53.430 34.534 1.00 17.98 ? 363 LEU A CA 1 ATOM 2204 C C . LEU A 1 281 ? 16.051 -54.620 33.983 1.00 21.33 ? 363 LEU A C 1 ATOM 2205 O O . LEU A 1 281 ? 15.157 -55.158 34.660 1.00 18.89 ? 363 LEU A O 1 ATOM 2206 C CB . LEU A 1 281 ? 17.947 -53.954 35.446 1.00 18.12 ? 363 LEU A CB 1 ATOM 2207 C CG . LEU A 1 281 ? 18.643 -52.994 36.411 1.00 23.84 ? 363 LEU A CG 1 ATOM 2208 C CD1 . LEU A 1 281 ? 19.693 -53.746 37.211 1.00 16.10 ? 363 LEU A CD1 1 ATOM 2209 C CD2 . LEU A 1 281 ? 19.272 -51.816 35.659 1.00 17.30 ? 363 LEU A CD2 1 ATOM 2210 N N . GLY A 1 282 ? 16.395 -55.041 32.767 1.00 19.23 ? 364 GLY A N 1 ATOM 2211 C CA . GLY A 1 282 ? 15.808 -56.243 32.199 1.00 16.02 ? 364 GLY A CA 1 ATOM 2212 C C . GLY A 1 282 ? 16.795 -57.394 32.277 1.00 17.78 ? 364 GLY A C 1 ATOM 2213 O O . GLY A 1 282 ? 18.006 -57.181 32.173 1.00 15.35 ? 364 GLY A O 1 ATOM 2214 N N . ARG A 1 283 ? 16.286 -58.609 32.480 1.00 15.96 ? 365 ARG A N 1 ATOM 2215 C CA . ARG A 1 283 ? 17.121 -59.798 32.415 1.00 15.01 ? 365 ARG A CA 1 ATOM 2216 C C . ARG A 1 283 ? 16.284 -61.042 32.181 1.00 17.21 ? 365 ARG A C 1 ATOM 2217 O O . ARG A 1 283 ? 15.079 -61.042 32.430 1.00 18.29 ? 365 ARG A O 1 ATOM 2218 C CB . ARG A 1 283 ? 17.954 -59.960 33.691 1.00 16.56 ? 365 ARG A CB 1 ATOM 2219 C CG . ARG A 1 283 ? 17.166 -60.227 34.967 1.00 15.94 ? 365 ARG A CG 1 ATOM 2220 C CD . ARG A 1 283 ? 18.151 -60.409 36.113 1.00 23.40 ? 365 ARG A CD 1 ATOM 2221 N NE . ARG A 1 283 ? 17.527 -60.742 37.391 1.00 22.93 ? 365 ARG A NE 1 ATOM 2222 C CZ . ARG A 1 283 ? 18.218 -60.969 38.505 1.00 21.35 ? 365 ARG A CZ 1 ATOM 2223 N NH1 . ARG A 1 283 ? 19.545 -60.907 38.489 1.00 18.92 ? 365 ARG A NH1 1 ATOM 2224 N NH2 . ARG A 1 283 ? 17.589 -61.256 39.630 1.00 18.58 ? 365 ARG A NH2 1 ATOM 2225 N N . THR A 1 284 ? 16.930 -62.093 31.687 1.00 15.04 ? 366 THR A N 1 ATOM 2226 C CA . THR A 1 284 ? 16.304 -63.401 31.594 1.00 17.15 ? 366 THR A CA 1 ATOM 2227 C C . THR A 1 284 ? 16.048 -63.876 33.017 1.00 19.55 ? 366 THR A C 1 ATOM 2228 O O . THR A 1 284 ? 16.748 -63.471 33.946 1.00 19.46 ? 366 THR A O 1 ATOM 2229 C CB . THR A 1 284 ? 17.217 -64.415 30.871 1.00 18.43 ? 366 THR A CB 1 ATOM 2230 O OG1 . THR A 1 284 ? 18.464 -64.532 31.573 1.00 19.35 ? 366 THR A OG1 1 ATOM 2231 C CG2 . THR A 1 284 ? 17.487 -63.962 29.447 1.00 13.07 ? 366 THR A CG2 1 ATOM 2232 N N . ILE A 1 285 ? 15.030 -64.703 33.210 1.00 21.24 ? 367 ILE A N 1 ATOM 2233 C CA . ILE A 1 285 ? 14.812 -65.276 34.536 1.00 21.69 ? 367 ILE A CA 1 ATOM 2234 C C . ILE A 1 285 ? 15.900 -66.309 34.844 1.00 21.20 ? 367 ILE A C 1 ATOM 2235 O O . ILE A 1 285 ? 16.571 -66.217 35.874 1.00 27.11 ? 367 ILE A O 1 ATOM 2236 C CB . ILE A 1 285 ? 13.392 -65.864 34.694 1.00 24.07 ? 367 ILE A CB 1 ATOM 2237 C CG1 . ILE A 1 285 ? 12.368 -64.725 34.721 1.00 23.16 ? 367 ILE A CG1 1 ATOM 2238 C CG2 . ILE A 1 285 ? 13.284 -66.723 35.969 1.00 20.47 ? 367 ILE A CG2 1 ATOM 2239 C CD1 . ILE A 1 285 ? 10.911 -65.182 34.577 1.00 20.89 ? 367 ILE A CD1 1 ATOM 2240 N N . SER A 1 286 ? 16.092 -67.270 33.944 1.00 27.56 ? 368 SER A N 1 ATOM 2241 C CA . SER A 1 286 ? 17.149 -68.270 34.112 1.00 30.01 ? 368 SER A CA 1 ATOM 2242 C C . SER A 1 286 ? 18.542 -67.645 34.149 1.00 28.22 ? 368 SER A C 1 ATOM 2243 O O . SER A 1 286 ? 18.797 -66.637 33.482 1.00 21.26 ? 368 SER A O 1 ATOM 2244 C CB . SER A 1 286 ? 17.087 -69.302 32.984 1.00 24.67 ? 368 SER A CB 1 ATOM 2245 O OG . SER A 1 286 ? 18.227 -70.148 32.993 1.00 33.55 ? 368 SER A OG 1 ATOM 2246 N N . THR A 1 287 ? 19.439 -68.251 34.929 1.00 21.65 ? 369 THR A N 1 ATOM 2247 C CA . THR A 1 287 ? 20.841 -67.842 34.955 1.00 23.60 ? 369 THR A CA 1 ATOM 2248 C C . THR A 1 287 ? 21.654 -68.712 34.011 1.00 21.76 ? 369 THR A C 1 ATOM 2249 O O . THR A 1 287 ? 22.830 -68.451 33.790 1.00 23.56 ? 369 THR A O 1 ATOM 2250 C CB . THR A 1 287 ? 21.469 -67.991 36.360 1.00 23.16 ? 369 THR A CB 1 ATOM 2251 O OG1 . THR A 1 287 ? 21.358 -69.357 36.792 1.00 16.43 ? 369 THR A OG1 1 ATOM 2252 C CG2 . THR A 1 287 ? 20.789 -67.075 37.364 1.00 23.33 ? 369 THR A CG2 1 ATOM 2253 N N . ALA A 1 288 ? 21.029 -69.755 33.469 1.00 23.90 ? 370 ALA A N 1 ATOM 2254 C CA . ALA A 1 288 ? 21.744 -70.718 32.629 1.00 24.84 ? 370 ALA A CA 1 ATOM 2255 C C . ALA A 1 288 ? 21.441 -70.541 31.141 1.00 22.78 ? 370 ALA A C 1 ATOM 2256 O O . ALA A 1 288 ? 22.315 -70.757 30.285 1.00 23.76 ? 370 ALA A O 1 ATOM 2257 C CB . ALA A 1 288 ? 21.436 -72.154 33.069 1.00 23.94 ? 370 ALA A CB 1 ATOM 2258 N N . SER A 1 289 ? 20.206 -70.167 30.826 1.00 23.49 ? 371 SER A N 1 ATOM 2259 C CA . SER A 1 289 ? 19.810 -70.067 29.423 1.00 19.68 ? 371 SER A CA 1 ATOM 2260 C C . SER A 1 289 ? 18.864 -68.908 29.117 1.00 23.74 ? 371 SER A C 1 ATOM 2261 O O . SER A 1 289 ? 18.346 -68.229 30.021 1.00 16.31 ? 371 SER A O 1 ATOM 2262 C CB . SER A 1 289 ? 19.196 -71.386 28.942 1.00 24.97 ? 371 SER A CB 1 ATOM 2263 O OG . SER A 1 289 ? 17.946 -71.615 29.564 1.00 34.54 ? 371 SER A OG 1 ATOM 2264 N N . ARG A 1 290 ? 18.649 -68.695 27.824 1.00 20.60 ? 372 ARG A N 1 ATOM 2265 C CA . ARG A 1 290 ? 17.811 -67.611 27.341 1.00 22.50 ? 372 ARG A CA 1 ATOM 2266 C C . ARG A 1 290 ? 16.334 -67.971 27.488 1.00 20.84 ? 372 ARG A C 1 ATOM 2267 O O . ARG A 1 290 ? 15.616 -68.181 26.501 1.00 23.33 ? 372 ARG A O 1 ATOM 2268 C CB . ARG A 1 290 ? 18.175 -67.288 25.891 1.00 17.20 ? 372 ARG A CB 1 ATOM 2269 C CG . ARG A 1 290 ? 19.652 -66.901 25.729 1.00 16.57 ? 372 ARG A CG 1 ATOM 2270 C CD . ARG A 1 290 ? 20.043 -66.727 24.266 1.00 19.45 ? 372 ARG A CD 1 ATOM 2271 N NE . ARG A 1 290 ? 21.360 -66.104 24.129 1.00 17.43 ? 372 ARG A NE 1 ATOM 2272 C CZ . ARG A 1 290 ? 21.922 -65.787 22.966 1.00 21.86 ? 372 ARG A CZ 1 ATOM 2273 N NH1 . ARG A 1 290 ? 21.289 -66.042 21.828 1.00 19.32 ? 372 ARG A NH1 1 ATOM 2274 N NH2 . ARG A 1 290 ? 23.117 -65.216 22.939 1.00 16.25 ? 372 ARG A NH2 1 ATOM 2275 N N . SER A 1 291 ? 15.886 -68.047 28.736 1.00 22.57 ? 373 SER A N 1 ATOM 2276 C CA . SER A 1 291 ? 14.493 -68.351 29.012 1.00 24.00 ? 373 SER A CA 1 ATOM 2277 C C . SER A 1 291 ? 13.937 -67.378 30.039 1.00 19.36 ? 373 SER A C 1 ATOM 2278 O O . SER A 1 291 ? 14.636 -66.964 30.980 1.00 19.00 ? 373 SER A O 1 ATOM 2279 C CB . SER A 1 291 ? 14.323 -69.801 29.478 1.00 27.55 ? 373 SER A CB 1 ATOM 2280 O OG . SER A 1 291 ? 15.014 -70.055 30.685 1.00 36.18 ? 373 SER A OG 1 ATOM 2281 N N . GLY A 1 292 ? 12.684 -66.990 29.834 1.00 18.08 ? 374 GLY A N 1 ATOM 2282 C CA . GLY A 1 292 ? 12.029 -66.046 30.717 1.00 16.02 ? 374 GLY A CA 1 ATOM 2283 C C . GLY A 1 292 ? 12.564 -64.645 30.520 1.00 14.70 ? 374 GLY A C 1 ATOM 2284 O O . GLY A 1 292 ? 13.630 -64.441 29.923 1.00 16.98 ? 374 GLY A O 1 ATOM 2285 N N . TYR A 1 293 ? 11.818 -63.668 31.013 1.00 18.56 ? 375 TYR A N 1 ATOM 2286 C CA . TYR A 1 293 ? 12.312 -62.304 31.040 1.00 18.55 ? 375 TYR A CA 1 ATOM 2287 C C . TYR A 1 293 ? 11.572 -61.543 32.124 1.00 19.48 ? 375 TYR A C 1 ATOM 2288 O O . TYR A 1 293 ? 10.361 -61.713 32.288 1.00 20.00 ? 375 TYR A O 1 ATOM 2289 C CB . TYR A 1 293 ? 12.135 -61.627 29.680 1.00 18.92 ? 375 TYR A CB 1 ATOM 2290 C CG . TYR A 1 293 ? 13.126 -60.510 29.482 1.00 16.43 ? 375 TYR A CG 1 ATOM 2291 C CD1 . TYR A 1 293 ? 14.394 -60.768 28.975 1.00 16.12 ? 375 TYR A CD1 1 ATOM 2292 C CD2 . TYR A 1 293 ? 12.812 -59.204 29.839 1.00 16.13 ? 375 TYR A CD2 1 ATOM 2293 C CE1 . TYR A 1 293 ? 15.318 -59.749 28.810 1.00 21.04 ? 375 TYR A CE1 1 ATOM 2294 C CE2 . TYR A 1 293 ? 13.726 -58.178 29.677 1.00 16.50 ? 375 TYR A CE2 1 ATOM 2295 C CZ . TYR A 1 293 ? 14.976 -58.455 29.160 1.00 18.88 ? 375 TYR A CZ 1 ATOM 2296 O OH . TYR A 1 293 ? 15.894 -57.437 28.998 1.00 19.88 ? 375 TYR A OH 1 ATOM 2297 N N . GLU A 1 294 ? 12.299 -60.724 32.879 1.00 19.84 ? 376 GLU A N 1 ATOM 2298 C CA . GLU A 1 294 ? 11.683 -59.919 33.932 1.00 18.78 ? 376 GLU A CA 1 ATOM 2299 C C . GLU A 1 294 ? 12.299 -58.524 33.966 1.00 18.99 ? 376 GLU A C 1 ATOM 2300 O O . GLU A 1 294 ? 13.457 -58.342 33.579 1.00 19.84 ? 376 GLU A O 1 ATOM 2301 C CB . GLU A 1 294 ? 11.853 -60.592 35.305 1.00 18.60 ? 376 GLU A CB 1 ATOM 2302 C CG . GLU A 1 294 ? 13.314 -60.712 35.748 1.00 18.02 ? 376 GLU A CG 1 ATOM 2303 C CD . GLU A 1 294 ? 13.490 -61.466 37.061 1.00 24.87 ? 376 GLU A CD 1 ATOM 2304 O OE1 . GLU A 1 294 ? 12.484 -61.743 37.758 1.00 24.00 ? 376 GLU A OE1 1 ATOM 2305 O OE2 . GLU A 1 294 ? 14.651 -61.776 37.395 1.00 26.63 ? 376 GLU A OE2 1 ATOM 2306 N N . MET A 1 295 ? 11.517 -57.547 34.419 1.00 17.02 ? 377 MET A N 1 ATOM 2307 C CA . MET A 1 295 ? 12.027 -56.206 34.689 1.00 20.86 ? 377 MET A CA 1 ATOM 2308 C C . MET A 1 295 ? 12.150 -56.025 36.201 1.00 24.60 ? 377 MET A C 1 ATOM 2309 O O . MET A 1 295 ? 11.267 -56.450 36.955 1.00 21.14 ? 377 MET A O 1 ATOM 2310 C CB . MET A 1 295 ? 11.078 -55.143 34.135 1.00 18.77 ? 377 MET A CB 1 ATOM 2311 C CG . MET A 1 295 ? 10.928 -55.164 32.629 1.00 19.86 ? 377 MET A CG 1 ATOM 2312 S SD . MET A 1 295 ? 12.511 -55.003 31.778 1.00 22.52 ? 377 MET A SD 1 ATOM 2313 C CE . MET A 1 295 ? 12.947 -53.335 32.307 1.00 17.45 ? 377 MET A CE 1 ATOM 2314 N N . LEU A 1 296 ? 13.230 -55.390 36.644 1.00 25.23 ? 378 LEU A N 1 ATOM 2315 C CA . LEU A 1 296 ? 13.444 -55.163 38.072 1.00 22.06 ? 378 LEU A CA 1 ATOM 2316 C C . LEU A 1 296 ? 13.745 -53.695 38.356 1.00 21.47 ? 378 LEU A C 1 ATOM 2317 O O . LEU A 1 296 ? 14.624 -53.100 37.725 1.00 19.36 ? 378 LEU A O 1 ATOM 2318 C CB . LEU A 1 296 ? 14.582 -56.050 38.592 1.00 20.69 ? 378 LEU A CB 1 ATOM 2319 C CG . LEU A 1 296 ? 14.331 -57.562 38.537 1.00 21.04 ? 378 LEU A CG 1 ATOM 2320 C CD1 . LEU A 1 296 ? 15.568 -58.370 38.951 1.00 16.29 ? 378 LEU A CD1 1 ATOM 2321 C CD2 . LEU A 1 296 ? 13.146 -57.920 39.419 1.00 18.98 ? 378 LEU A CD2 1 ATOM 2322 N N . LYS A 1 297 ? 13.012 -53.107 39.299 1.00 17.63 ? 379 LYS A N 1 ATOM 2323 C CA . LYS A 1 297 ? 13.266 -51.725 39.680 1.00 22.68 ? 379 LYS A CA 1 ATOM 2324 C C . LYS A 1 297 ? 14.417 -51.693 40.688 1.00 21.61 ? 379 LYS A C 1 ATOM 2325 O O . LYS A 1 297 ? 14.265 -52.146 41.821 1.00 24.20 ? 379 LYS A O 1 ATOM 2326 C CB . LYS A 1 297 ? 12.013 -51.085 40.279 1.00 22.92 ? 379 LYS A CB 1 ATOM 2327 C CG . LYS A 1 297 ? 12.171 -49.591 40.547 1.00 26.14 ? 379 LYS A CG 1 ATOM 2328 C CD . LYS A 1 297 ? 10.935 -49.007 41.213 1.00 25.80 ? 379 LYS A CD 1 ATOM 2329 C CE . LYS A 1 297 ? 11.107 -47.515 41.483 1.00 24.02 ? 379 LYS A CE 1 ATOM 2330 N NZ . LYS A 1 297 ? 9.910 -46.965 42.180 1.00 22.82 ? 379 LYS A NZ 1 ATOM 2331 N N . VAL A 1 298 ? 15.567 -51.175 40.267 1.00 19.73 ? 380 VAL A N 1 ATOM 2332 C CA . VAL A 1 298 ? 16.766 -51.179 41.107 1.00 19.50 ? 380 VAL A CA 1 ATOM 2333 C C . VAL A 1 298 ? 17.333 -49.767 41.204 1.00 25.11 ? 380 VAL A C 1 ATOM 2334 O O . VAL A 1 298 ? 18.104 -49.345 40.340 1.00 21.11 ? 380 VAL A O 1 ATOM 2335 C CB . VAL A 1 298 ? 17.846 -52.128 40.555 1.00 18.28 ? 380 VAL A CB 1 ATOM 2336 C CG1 . VAL A 1 298 ? 19.033 -52.205 41.517 1.00 20.42 ? 380 VAL A CG1 1 ATOM 2337 C CG2 . VAL A 1 298 ? 17.268 -53.520 40.312 1.00 22.71 ? 380 VAL A CG2 1 ATOM 2338 N N . PRO A 1 299 ? 16.949 -49.032 42.263 1.00 24.01 ? 381 PRO A N 1 ATOM 2339 C CA . PRO A 1 299 ? 17.325 -47.618 42.395 1.00 26.40 ? 381 PRO A CA 1 ATOM 2340 C C . PRO A 1 299 ? 18.836 -47.424 42.291 1.00 21.99 ? 381 PRO A C 1 ATOM 2341 O O . PRO A 1 299 ? 19.579 -48.113 42.996 1.00 23.32 ? 381 PRO A O 1 ATOM 2342 C CB . PRO A 1 299 ? 16.843 -47.255 43.808 1.00 20.92 ? 381 PRO A CB 1 ATOM 2343 C CG . PRO A 1 299 ? 15.734 -48.239 44.095 1.00 23.72 ? 381 PRO A CG 1 ATOM 2344 C CD . PRO A 1 299 ? 16.167 -49.515 43.419 1.00 22.88 ? 381 PRO A CD 1 ATOM 2345 N N . ASN A 1 300 ? 19.267 -46.523 41.407 1.00 22.29 ? 382 ASN A N 1 ATOM 2346 C CA . ASN A 1 300 ? 20.678 -46.160 41.261 1.00 19.61 ? 382 ASN A CA 1 ATOM 2347 C C . ASN A 1 300 ? 21.587 -47.337 40.919 1.00 21.52 ? 382 ASN A C 1 ATOM 2348 O O . ASN A 1 300 ? 22.755 -47.360 41.326 1.00 23.02 ? 382 ASN A O 1 ATOM 2349 C CB . ASN A 1 300 ? 21.197 -45.465 42.529 1.00 23.26 ? 382 ASN A CB 1 ATOM 2350 C CG . ASN A 1 300 ? 20.374 -44.241 42.913 1.00 27.34 ? 382 ASN A CG 1 ATOM 2351 O OD1 . ASN A 1 300 ? 20.160 -43.336 42.103 1.00 31.67 ? 382 ASN A OD1 1 ATOM 2352 N ND2 . ASN A 1 300 ? 19.909 -44.213 44.155 1.00 34.36 ? 382 ASN A ND2 1 ATOM 2353 N N . ALA A 1 301 ? 21.053 -48.307 40.177 1.00 21.13 ? 383 ALA A N 1 ATOM 2354 C CA . ALA A 1 301 ? 21.799 -49.512 39.797 1.00 20.61 ? 383 ALA A CA 1 ATOM 2355 C C . ALA A 1 301 ? 23.153 -49.182 39.173 1.00 22.71 ? 383 ALA A C 1 ATOM 2356 O O . ALA A 1 301 ? 24.154 -49.859 39.427 1.00 22.84 ? 383 ALA A O 1 ATOM 2357 C CB . ALA A 1 301 ? 20.968 -50.370 38.839 1.00 18.96 ? 383 ALA A CB 1 ATOM 2358 N N . LEU A 1 302 ? 23.171 -48.140 38.349 1.00 25.81 ? 384 LEU A N 1 ATOM 2359 C CA . LEU A 1 302 ? 24.386 -47.723 37.653 1.00 21.03 ? 384 LEU A CA 1 ATOM 2360 C C . LEU A 1 302 ? 25.546 -47.395 38.599 1.00 25.90 ? 384 LEU A C 1 ATOM 2361 O O . LEU A 1 302 ? 26.686 -47.777 38.335 1.00 25.12 ? 384 LEU A O 1 ATOM 2362 C CB . LEU A 1 302 ? 24.085 -46.517 36.753 1.00 16.55 ? 384 LEU A CB 1 ATOM 2363 C CG . LEU A 1 302 ? 25.310 -45.903 36.067 1.00 25.77 ? 384 LEU A CG 1 ATOM 2364 C CD1 . LEU A 1 302 ? 26.039 -46.933 35.192 1.00 20.98 ? 384 LEU A CD1 1 ATOM 2365 C CD2 . LEU A 1 302 ? 24.937 -44.670 35.263 1.00 23.07 ? 384 LEU A CD2 1 ATOM 2366 N N . THR A 1 303 ? 25.250 -46.706 39.700 1.00 19.59 ? 385 THR A N 1 ATOM 2367 C CA . THR A 1 303 ? 26.292 -46.183 40.588 1.00 23.50 ? 385 THR A CA 1 ATOM 2368 C C . THR A 1 303 ? 26.420 -46.885 41.952 1.00 22.31 ? 385 THR A C 1 ATOM 2369 O O . THR A 1 303 ? 27.454 -46.767 42.627 1.00 23.61 ? 385 THR A O 1 ATOM 2370 C CB . THR A 1 303 ? 26.093 -44.670 40.822 1.00 29.26 ? 385 THR A CB 1 ATOM 2371 O OG1 . THR A 1 303 ? 24.790 -44.441 41.373 1.00 23.63 ? 385 THR A OG1 1 ATOM 2372 C CG2 . THR A 1 303 ? 26.220 -43.905 39.504 1.00 21.16 ? 385 THR A CG2 1 ATOM 2373 N N . ASP A 1 304 ? 25.383 -47.613 42.355 1.00 21.95 ? 386 ASP A N 1 ATOM 2374 C CA . ASP A 1 304 ? 25.347 -48.222 43.691 1.00 25.61 ? 386 ASP A CA 1 ATOM 2375 C C . ASP A 1 304 ? 25.666 -49.718 43.631 1.00 25.30 ? 386 ASP A C 1 ATOM 2376 O O . ASP A 1 304 ? 24.833 -50.502 43.177 1.00 25.82 ? 386 ASP A O 1 ATOM 2377 C CB . ASP A 1 304 ? 23.958 -48.002 44.318 1.00 25.84 ? 386 ASP A CB 1 ATOM 2378 C CG . ASP A 1 304 ? 23.843 -48.550 45.739 1.00 32.24 ? 386 ASP A CG 1 ATOM 2379 O OD1 . ASP A 1 304 ? 24.769 -49.250 46.215 1.00 26.14 ? 386 ASP A OD1 1 ATOM 2380 O OD2 . ASP A 1 304 ? 22.806 -48.278 46.383 1.00 32.99 ? 386 ASP A OD2 1 ATOM 2381 N N . ASP A 1 305 ? 26.843 -50.116 44.121 1.00 25.57 ? 387 ASP A N 1 ATOM 2382 C CA . ASP A 1 305 ? 27.247 -51.526 44.067 1.00 24.29 ? 387 ASP A CA 1 ATOM 2383 C C . ASP A 1 305 ? 26.602 -52.433 45.125 1.00 25.47 ? 387 ASP A C 1 ATOM 2384 O O . ASP A 1 305 ? 26.978 -53.604 45.252 1.00 27.18 ? 387 ASP A O 1 ATOM 2385 C CB . ASP A 1 305 ? 28.778 -51.679 44.078 1.00 22.80 ? 387 ASP A CB 1 ATOM 2386 C CG . ASP A 1 305 ? 29.421 -51.256 45.399 1.00 29.41 ? 387 ASP A CG 1 ATOM 2387 O OD1 . ASP A 1 305 ? 28.704 -50.994 46.396 1.00 27.14 ? 387 ASP A OD1 1 ATOM 2388 O OD2 . ASP A 1 305 ? 30.675 -51.205 45.434 1.00 28.84 ? 387 ASP A OD2 1 ATOM 2389 N N . ARG A 1 306 ? 25.641 -51.895 45.875 1.00 25.84 ? 388 ARG A N 1 ATOM 2390 C CA . ARG A 1 306 ? 24.903 -52.683 46.866 1.00 24.89 ? 388 ARG A CA 1 ATOM 2391 C C . ARG A 1 306 ? 23.426 -52.794 46.485 1.00 26.86 ? 388 ARG A C 1 ATOM 2392 O O . ARG A 1 306 ? 22.654 -53.482 47.161 1.00 24.97 ? 388 ARG A O 1 ATOM 2393 C CB . ARG A 1 306 ? 24.994 -52.042 48.262 1.00 27.78 ? 388 ARG A CB 1 ATOM 2394 C CG . ARG A 1 306 ? 26.396 -51.702 48.732 1.00 26.80 ? 388 ARG A CG 1 ATOM 2395 C CD . ARG A 1 306 ? 27.277 -52.943 48.798 1.00 25.19 ? 388 ARG A CD 1 ATOM 2396 N NE . ARG A 1 306 ? 28.675 -52.577 49.016 1.00 31.32 ? 388 ARG A NE 1 ATOM 2397 C CZ . ARG A 1 306 ? 29.274 -52.560 50.204 1.00 33.87 ? 388 ARG A CZ 1 ATOM 2398 N NH1 . ARG A 1 306 ? 28.601 -52.906 51.301 1.00 30.53 ? 388 ARG A NH1 1 ATOM 2399 N NH2 . ARG A 1 306 ? 30.552 -52.209 50.291 1.00 32.22 ? 388 ARG A NH2 1 ATOM 2400 N N . SER A 1 307 ? 23.034 -52.119 45.407 1.00 17.54 ? 389 SER A N 1 ATOM 2401 C CA . SER A 1 307 ? 21.611 -51.936 45.098 1.00 21.42 ? 389 SER A CA 1 ATOM 2402 C C . SER A 1 307 ? 20.870 -53.227 44.738 1.00 25.06 ? 389 SER A C 1 ATOM 2403 O O . SER A 1 307 ? 21.390 -54.090 44.018 1.00 22.48 ? 389 SER A O 1 ATOM 2404 C CB . SER A 1 307 ? 21.430 -50.886 43.997 1.00 23.66 ? 389 SER A CB 1 ATOM 2405 O OG . SER A 1 307 ? 22.232 -51.193 42.872 1.00 23.95 ? 389 SER A OG 1 ATOM 2406 N N . LYS A 1 308 ? 19.650 -53.340 45.255 1.00 20.52 ? 390 LYS A N 1 ATOM 2407 C CA . LYS A 1 308 ? 18.814 -54.528 45.092 1.00 26.93 ? 390 LYS A CA 1 ATOM 2408 C C . LYS A 1 308 ? 17.426 -54.099 44.599 1.00 23.37 ? 390 LYS A C 1 ATOM 2409 O O . LYS A 1 308 ? 17.116 -52.906 44.601 1.00 26.05 ? 390 LYS A O 1 ATOM 2410 C CB . LYS A 1 308 ? 18.711 -55.279 46.430 1.00 23.60 ? 390 LYS A CB 1 ATOM 2411 C CG . LYS A 1 308 ? 19.990 -55.995 46.850 1.00 24.17 ? 390 LYS A CG 1 ATOM 2412 C CD . LYS A 1 308 ? 20.420 -57.004 45.793 1.00 23.09 ? 390 LYS A CD 1 ATOM 2413 C CE . LYS A 1 308 ? 21.627 -57.819 46.256 1.00 35.87 ? 390 LYS A CE 1 ATOM 2414 N NZ . LYS A 1 308 ? 21.387 -58.496 47.572 1.00 34.25 ? 390 LYS A NZ 1 ATOM 2415 N N . PRO A 1 309 ? 16.591 -55.061 44.161 1.00 28.76 ? 391 PRO A N 1 ATOM 2416 C CA . PRO A 1 309 ? 15.264 -54.686 43.644 1.00 21.59 ? 391 PRO A CA 1 ATOM 2417 C C . PRO A 1 309 ? 14.265 -54.277 44.732 1.00 24.77 ? 391 PRO A C 1 ATOM 2418 O O . PRO A 1 309 ? 14.293 -54.834 45.835 1.00 27.61 ? 391 PRO A O 1 ATOM 2419 C CB . PRO A 1 309 ? 14.776 -55.973 42.960 1.00 19.91 ? 391 PRO A CB 1 ATOM 2420 C CG . PRO A 1 309 ? 16.018 -56.812 42.752 1.00 26.68 ? 391 PRO A CG 1 ATOM 2421 C CD . PRO A 1 309 ? 16.888 -56.486 43.920 1.00 23.28 ? 391 PRO A CD 1 ATOM 2422 N N . ILE A 1 310 ? 13.395 -53.314 44.416 1.00 18.86 ? 392 ILE A N 1 ATOM 2423 C CA . ILE A 1 310 ? 12.304 -52.929 45.312 1.00 24.63 ? 392 ILE A CA 1 ATOM 2424 C C . ILE A 1 310 ? 10.940 -53.134 44.642 1.00 26.18 ? 392 ILE A C 1 ATOM 2425 O O . ILE A 1 310 ? 9.893 -53.008 45.283 1.00 26.36 ? 392 ILE A O 1 ATOM 2426 C CB . ILE A 1 310 ? 12.427 -51.465 45.787 1.00 27.99 ? 392 ILE A CB 1 ATOM 2427 C CG1 . ILE A 1 310 ? 12.234 -50.493 44.619 1.00 23.82 ? 392 ILE A CG1 1 ATOM 2428 C CG2 . ILE A 1 310 ? 13.768 -51.232 46.492 1.00 23.83 ? 392 ILE A CG2 1 ATOM 2429 C CD1 . ILE A 1 310 ? 12.204 -49.032 45.057 1.00 20.84 ? 392 ILE A CD1 1 ATOM 2430 N N . GLN A 1 311 ? 10.965 -53.448 43.350 1.00 24.77 ? 393 GLN A N 1 ATOM 2431 C CA . GLN A 1 311 ? 9.746 -53.701 42.585 1.00 25.23 ? 393 GLN A CA 1 ATOM 2432 C C . GLN A 1 311 ? 10.127 -54.460 41.317 1.00 25.91 ? 393 GLN A C 1 ATOM 2433 O O . GLN A 1 311 ? 11.294 -54.446 40.904 1.00 24.71 ? 393 GLN A O 1 ATOM 2434 C CB . GLN A 1 311 ? 9.032 -52.387 42.241 1.00 27.06 ? 393 GLN A CB 1 ATOM 2435 C CG . GLN A 1 311 ? 7.570 -52.559 41.812 1.00 19.54 ? 393 GLN A CG 1 ATOM 2436 C CD . GLN A 1 311 ? 6.956 -51.290 41.230 1.00 30.21 ? 393 GLN A CD 1 ATOM 2437 O OE1 . GLN A 1 311 ? 7.313 -50.166 41.615 1.00 22.82 ? 393 GLN A OE1 1 ATOM 2438 N NE2 . GLN A 1 311 ? 6.026 -51.466 40.292 1.00 20.46 ? 393 GLN A NE2 1 ATOM 2439 N N . GLY A 1 312 ? 9.161 -55.136 40.703 1.00 25.68 ? 394 GLY A N 1 ATOM 2440 C CA . GLY A 1 312 ? 9.454 -55.924 39.519 1.00 21.22 ? 394 GLY A CA 1 ATOM 2441 C C . GLY A 1 312 ? 8.248 -56.266 38.669 1.00 28.17 ? 394 GLY A C 1 ATOM 2442 O O . GLY A 1 312 ? 7.097 -56.011 39.047 1.00 23.13 ? 394 GLY A O 1 ATOM 2443 N N . GLN A 1 313 ? 8.514 -56.841 37.501 1.00 23.42 ? 395 GLN A N 1 ATOM 2444 C CA . GLN A 1 313 ? 7.445 -57.309 36.638 1.00 21.65 ? 395 GLN A CA 1 ATOM 2445 C C . GLN A 1 313 ? 7.945 -58.429 35.741 1.00 25.74 ? 395 GLN A C 1 ATOM 2446 O O . GLN A 1 313 ? 8.959 -58.280 35.042 1.00 21.18 ? 395 GLN A O 1 ATOM 2447 C CB . GLN A 1 313 ? 6.867 -56.166 35.805 1.00 21.46 ? 395 GLN A CB 1 ATOM 2448 C CG . GLN A 1 313 ? 5.665 -56.596 34.975 1.00 18.02 ? 395 GLN A CG 1 ATOM 2449 C CD . GLN A 1 313 ? 4.908 -55.423 34.387 1.00 21.71 ? 395 GLN A CD 1 ATOM 2450 O OE1 . GLN A 1 313 ? 4.953 -54.307 34.920 1.00 19.02 ? 395 GLN A OE1 1 ATOM 2451 N NE2 . GLN A 1 313 ? 4.205 -55.666 33.279 1.00 18.54 ? 395 GLN A NE2 1 ATOM 2452 N N . THR A 1 314 ? 7.247 -59.560 35.788 1.00 23.10 ? 396 THR A N 1 ATOM 2453 C CA . THR A 1 314 ? 7.548 -60.674 34.897 1.00 19.41 ? 396 THR A CA 1 ATOM 2454 C C . THR A 1 314 ? 6.983 -60.384 33.506 1.00 28.12 ? 396 THR A C 1 ATOM 2455 O O . THR A 1 314 ? 5.838 -59.938 33.373 1.00 26.32 ? 396 THR A O 1 ATOM 2456 C CB . THR A 1 314 ? 6.992 -62.002 35.451 1.00 26.84 ? 396 THR A CB 1 ATOM 2457 O OG1 . THR A 1 314 ? 7.776 -62.400 36.585 1.00 24.65 ? 396 THR A OG1 1 ATOM 2458 C CG2 . THR A 1 314 ? 7.069 -63.100 34.400 1.00 25.64 ? 396 THR A CG2 1 ATOM 2459 N N . ILE A 1 315 ? 7.794 -60.619 32.478 1.00 20.80 ? 397 ILE A N 1 ATOM 2460 C CA . ILE A 1 315 ? 7.393 -60.334 31.107 1.00 21.55 ? 397 ILE A CA 1 ATOM 2461 C C . ILE A 1 315 ? 7.139 -61.643 30.359 1.00 21.16 ? 397 ILE A C 1 ATOM 2462 O O . ILE A 1 315 ? 6.122 -61.803 29.674 1.00 19.54 ? 397 ILE A O 1 ATOM 2463 C CB . ILE A 1 315 ? 8.474 -59.508 30.376 1.00 19.19 ? 397 ILE A CB 1 ATOM 2464 C CG1 . ILE A 1 315 ? 8.852 -58.263 31.187 1.00 20.23 ? 397 ILE A CG1 1 ATOM 2465 C CG2 . ILE A 1 315 ? 8.000 -59.125 28.980 1.00 18.24 ? 397 ILE A CG2 1 ATOM 2466 C CD1 . ILE A 1 315 ? 7.681 -57.287 31.442 1.00 20.16 ? 397 ILE A CD1 1 ATOM 2467 N N . VAL A 1 316 ? 8.079 -62.574 30.494 1.00 13.70 ? 398 VAL A N 1 ATOM 2468 C CA . VAL A 1 316 ? 7.963 -63.903 29.908 1.00 20.29 ? 398 VAL A CA 1 ATOM 2469 C C . VAL A 1 316 ? 8.290 -64.914 31.008 1.00 25.97 ? 398 VAL A C 1 ATOM 2470 O O . VAL A 1 316 ? 9.254 -64.716 31.751 1.00 19.32 ? 398 VAL A O 1 ATOM 2471 C CB . VAL A 1 316 ? 8.962 -64.086 28.742 1.00 18.80 ? 398 VAL A CB 1 ATOM 2472 C CG1 . VAL A 1 316 ? 8.846 -65.485 28.143 1.00 17.65 ? 398 VAL A CG1 1 ATOM 2473 C CG2 . VAL A 1 316 ? 8.741 -63.027 27.665 1.00 19.09 ? 398 VAL A CG2 1 ATOM 2474 N N . LEU A 1 317 ? 7.497 -65.980 31.124 1.00 17.22 ? 399 LEU A N 1 ATOM 2475 C CA . LEU A 1 317 ? 7.736 -67.003 32.148 1.00 21.78 ? 399 LEU A CA 1 ATOM 2476 C C . LEU A 1 317 ? 9.027 -67.760 31.861 1.00 27.03 ? 399 LEU A C 1 ATOM 2477 O O . LEU A 1 317 ? 9.430 -67.890 30.702 1.00 20.97 ? 399 LEU A O 1 ATOM 2478 C CB . LEU A 1 317 ? 6.574 -68.002 32.220 1.00 23.08 ? 399 LEU A CB 1 ATOM 2479 C CG . LEU A 1 317 ? 5.189 -67.485 32.617 1.00 23.96 ? 399 LEU A CG 1 ATOM 2480 C CD1 . LEU A 1 317 ? 4.145 -68.585 32.478 1.00 27.67 ? 399 LEU A CD1 1 ATOM 2481 C CD2 . LEU A 1 317 ? 5.195 -66.946 34.038 1.00 24.00 ? 399 LEU A CD2 1 ATOM 2482 N N . ASN A 1 318 ? 9.660 -68.278 32.911 1.00 21.05 ? 400 ASN A N 1 ATOM 2483 C CA . ASN A 1 318 ? 10.901 -69.034 32.761 1.00 18.34 ? 400 ASN A CA 1 ATOM 2484 C C . ASN A 1 318 ? 10.719 -70.294 31.912 1.00 21.97 ? 400 ASN A C 1 ATOM 2485 O O . ASN A 1 318 ? 11.665 -70.781 31.302 1.00 27.64 ? 400 ASN A O 1 ATOM 2486 C CB . ASN A 1 318 ? 11.485 -69.385 34.135 1.00 23.35 ? 400 ASN A CB 1 ATOM 2487 C CG . ASN A 1 318 ? 12.860 -70.019 34.040 1.00 34.35 ? 400 ASN A CG 1 ATOM 2488 O OD1 . ASN A 1 318 ? 13.783 -69.436 33.466 1.00 31.95 ? 400 ASN A OD1 1 ATOM 2489 N ND2 . ASN A 1 318 ? 13.006 -71.215 34.604 1.00 38.34 ? 400 ASN A ND2 1 ATOM 2490 N N . ALA A 1 319 ? 9.495 -70.813 31.867 1.00 25.50 ? 401 ALA A N 1 ATOM 2491 C CA . ALA A 1 319 ? 9.177 -71.986 31.049 1.00 28.14 ? 401 ALA A CA 1 ATOM 2492 C C . ALA A 1 319 ? 9.228 -71.679 29.550 1.00 29.29 ? 401 ALA A C 1 ATOM 2493 O O . ALA A 1 319 ? 9.254 -72.599 28.716 1.00 31.16 ? 401 ALA A O 1 ATOM 2494 C CB . ALA A 1 319 ? 7.811 -72.512 31.414 1.00 28.40 ? 401 ALA A CB 1 ATOM 2495 N N . ASP A 1 320 ? 9.217 -70.390 29.214 1.00 22.02 ? 402 ASP A N 1 ATOM 2496 C CA . ASP A 1 320 ? 9.179 -69.947 27.818 1.00 22.34 ? 402 ASP A CA 1 ATOM 2497 C C . ASP A 1 320 ? 10.508 -69.343 27.352 1.00 26.17 ? 402 ASP A C 1 ATOM 2498 O O . ASP A 1 320 ? 11.179 -68.626 28.108 1.00 23.72 ? 402 ASP A O 1 ATOM 2499 C CB . ASP A 1 320 ? 8.042 -68.941 27.616 1.00 25.01 ? 402 ASP A CB 1 ATOM 2500 C CG . ASP A 1 320 ? 6.668 -69.577 27.746 1.00 28.09 ? 402 ASP A CG 1 ATOM 2501 O OD1 . ASP A 1 320 ? 6.431 -70.619 27.090 1.00 30.89 ? 402 ASP A OD1 1 ATOM 2502 O OD2 . ASP A 1 320 ? 5.825 -69.036 28.501 1.00 22.65 ? 402 ASP A OD2 1 ATOM 2503 N N . TRP A 1 321 ? 10.881 -69.634 26.106 1.00 21.75 ? 403 TRP A N 1 ATOM 2504 C CA . TRP A 1 321 ? 12.133 -69.132 25.541 1.00 18.80 ? 403 TRP A CA 1 ATOM 2505 C C . TRP A 1 321 ? 12.082 -67.627 25.300 1.00 20.31 ? 403 TRP A C 1 ATOM 2506 O O . TRP A 1 321 ? 11.071 -67.087 24.826 1.00 18.57 ? 403 TRP A O 1 ATOM 2507 C CB . TRP A 1 321 ? 12.481 -69.856 24.233 1.00 20.52 ? 403 TRP A CB 1 ATOM 2508 C CG . TRP A 1 321 ? 12.595 -71.348 24.391 1.00 24.95 ? 403 TRP A CG 1 ATOM 2509 C CD1 . TRP A 1 321 ? 11.808 -72.303 23.809 1.00 24.05 ? 403 TRP A CD1 1 ATOM 2510 C CD2 . TRP A 1 321 ? 13.546 -72.051 25.200 1.00 25.74 ? 403 TRP A CD2 1 ATOM 2511 N NE1 . TRP A 1 321 ? 12.218 -73.560 24.204 1.00 25.89 ? 403 TRP A NE1 1 ATOM 2512 C CE2 . TRP A 1 321 ? 13.281 -73.432 25.058 1.00 31.20 ? 403 TRP A CE2 1 ATOM 2513 C CE3 . TRP A 1 321 ? 14.600 -71.648 26.028 1.00 27.06 ? 403 TRP A CE3 1 ATOM 2514 C CZ2 . TRP A 1 321 ? 14.035 -74.411 25.717 1.00 22.16 ? 403 TRP A CZ2 1 ATOM 2515 C CZ3 . TRP A 1 321 ? 15.344 -72.617 26.682 1.00 26.09 ? 403 TRP A CZ3 1 ATOM 2516 C CH2 . TRP A 1 321 ? 15.057 -73.983 26.524 1.00 30.88 ? 403 TRP A CH2 1 ATOM 2517 N N . SER A 1 322 ? 13.170 -66.944 25.637 1.00 18.97 ? 404 SER A N 1 ATOM 2518 C CA . SER A 1 322 ? 13.295 -65.538 25.302 1.00 17.86 ? 404 SER A CA 1 ATOM 2519 C C . SER A 1 322 ? 14.463 -65.365 24.329 1.00 16.87 ? 404 SER A C 1 ATOM 2520 O O . SER A 1 322 ? 14.586 -66.123 23.359 1.00 18.88 ? 404 SER A O 1 ATOM 2521 C CB . SER A 1 322 ? 13.457 -64.684 26.563 1.00 18.72 ? 404 SER A CB 1 ATOM 2522 O OG . SER A 1 322 ? 14.549 -65.119 27.352 1.00 18.41 ? 404 SER A OG 1 ATOM 2523 N N . GLY A 1 323 ? 15.310 -64.370 24.567 1.00 16.11 ? 405 GLY A N 1 ATOM 2524 C CA . GLY A 1 323 ? 16.400 -64.082 23.649 1.00 13.01 ? 405 GLY A CA 1 ATOM 2525 C C . GLY A 1 323 ? 16.901 -62.659 23.812 1.00 19.68 ? 405 GLY A C 1 ATOM 2526 O O . GLY A 1 323 ? 16.912 -62.115 24.929 1.00 21.15 ? 405 GLY A O 1 ATOM 2527 N N . TYR A 1 324 ? 17.328 -62.052 22.706 1.00 17.10 ? 406 TYR A N 1 ATOM 2528 C CA . TYR A 1 324 ? 17.777 -60.662 22.733 1.00 16.45 ? 406 TYR A CA 1 ATOM 2529 C C . TYR A 1 324 ? 16.688 -59.734 23.276 1.00 18.10 ? 406 TYR A C 1 ATOM 2530 O O . TYR A 1 324 ? 15.481 -60.002 23.152 1.00 16.46 ? 406 TYR A O 1 ATOM 2531 C CB . TYR A 1 324 ? 18.197 -60.195 21.333 1.00 16.31 ? 406 TYR A CB 1 ATOM 2532 C CG . TYR A 1 324 ? 19.586 -60.633 20.904 1.00 18.57 ? 406 TYR A CG 1 ATOM 2533 C CD1 . TYR A 1 324 ? 20.259 -61.652 21.571 1.00 21.94 ? 406 TYR A CD1 1 ATOM 2534 C CD2 . TYR A 1 324 ? 20.231 -60.006 19.837 1.00 17.99 ? 406 TYR A CD2 1 ATOM 2535 C CE1 . TYR A 1 324 ? 21.533 -62.043 21.181 1.00 24.14 ? 406 TYR A CE1 1 ATOM 2536 C CE2 . TYR A 1 324 ? 21.502 -60.390 19.439 1.00 14.65 ? 406 TYR A CE2 1 ATOM 2537 C CZ . TYR A 1 324 ? 22.148 -61.404 20.118 1.00 19.76 ? 406 TYR A CZ 1 ATOM 2538 O OH . TYR A 1 324 ? 23.411 -61.787 19.729 1.00 19.25 ? 406 TYR A OH 1 ATOM 2539 N N . SER A 1 325 ? 17.117 -58.643 23.893 1.00 17.83 ? 407 SER A N 1 ATOM 2540 C CA . SER A 1 325 ? 16.182 -57.619 24.329 1.00 20.93 ? 407 SER A CA 1 ATOM 2541 C C . SER A 1 325 ? 16.876 -56.286 24.141 1.00 21.55 ? 407 SER A C 1 ATOM 2542 O O . SER A 1 325 ? 18.109 -56.207 24.235 1.00 20.24 ? 407 SER A O 1 ATOM 2543 C CB . SER A 1 325 ? 15.775 -57.830 25.787 1.00 15.40 ? 407 SER A CB 1 ATOM 2544 O OG . SER A 1 325 ? 16.907 -57.853 26.642 1.00 19.48 ? 407 SER A OG 1 ATOM 2545 N N . GLY A 1 326 ? 16.106 -55.242 23.849 1.00 16.75 ? 408 GLY A N 1 ATOM 2546 C CA . GLY A 1 326 ? 16.712 -53.946 23.604 1.00 15.07 ? 408 GLY A CA 1 ATOM 2547 C C . GLY A 1 326 ? 15.760 -52.790 23.810 1.00 17.67 ? 408 GLY A C 1 ATOM 2548 O O . GLY A 1 326 ? 14.548 -52.987 23.946 1.00 15.73 ? 408 GLY A O 1 ATOM 2549 N N . SER A 1 327 ? 16.305 -51.578 23.828 1.00 16.98 ? 409 SER A N 1 ATOM 2550 C CA . SER A 1 327 ? 15.497 -50.395 24.097 1.00 20.92 ? 409 SER A CA 1 ATOM 2551 C C . SER A 1 327 ? 15.117 -49.608 22.841 1.00 18.06 ? 409 SER A C 1 ATOM 2552 O O . SER A 1 327 ? 15.804 -49.663 21.815 1.00 17.44 ? 409 SER A O 1 ATOM 2553 C CB . SER A 1 327 ? 16.217 -49.476 25.095 1.00 20.19 ? 409 SER A CB 1 ATOM 2554 O OG . SER A 1 327 ? 17.573 -49.263 24.717 1.00 15.03 ? 409 SER A OG 1 ATOM 2555 N N . PHE A 1 328 ? 14.002 -48.890 22.938 1.00 13.18 ? 410 PHE A N 1 ATOM 2556 C CA . PHE A 1 328 ? 13.606 -47.904 21.939 1.00 17.96 ? 410 PHE A CA 1 ATOM 2557 C C . PHE A 1 328 ? 12.586 -46.999 22.605 1.00 17.95 ? 410 PHE A C 1 ATOM 2558 O O . PHE A 1 328 ? 11.991 -47.374 23.616 1.00 18.13 ? 410 PHE A O 1 ATOM 2559 C CB . PHE A 1 328 ? 12.986 -48.560 20.698 1.00 19.47 ? 410 PHE A CB 1 ATOM 2560 C CG . PHE A 1 328 ? 11.631 -49.173 20.945 1.00 16.72 ? 410 PHE A CG 1 ATOM 2561 C CD1 . PHE A 1 328 ? 11.523 -50.437 21.511 1.00 14.84 ? 410 PHE A CD1 1 ATOM 2562 C CD2 . PHE A 1 328 ? 10.474 -48.492 20.601 1.00 16.86 ? 410 PHE A CD2 1 ATOM 2563 C CE1 . PHE A 1 328 ? 10.279 -51.010 21.736 1.00 20.06 ? 410 PHE A CE1 1 ATOM 2564 C CE2 . PHE A 1 328 ? 9.225 -49.053 20.828 1.00 20.13 ? 410 PHE A CE2 1 ATOM 2565 C CZ . PHE A 1 328 ? 9.127 -50.316 21.391 1.00 20.66 ? 410 PHE A CZ 1 ATOM 2566 N N . MET A 1 329 ? 12.387 -45.806 22.057 1.00 22.27 ? 411 MET A N 1 ATOM 2567 C CA . MET A 1 329 ? 11.315 -44.931 22.530 1.00 21.19 ? 411 MET A CA 1 ATOM 2568 C C . MET A 1 329 ? 10.695 -44.201 21.345 1.00 24.09 ? 411 MET A C 1 ATOM 2569 O O . MET A 1 329 ? 11.365 -43.980 20.333 1.00 20.59 ? 411 MET A O 1 ATOM 2570 C CB . MET A 1 329 ? 11.838 -43.923 23.563 1.00 19.41 ? 411 MET A CB 1 ATOM 2571 C CG . MET A 1 329 ? 12.416 -44.554 24.823 1.00 23.01 ? 411 MET A CG 1 ATOM 2572 S SD . MET A 1 329 ? 12.533 -43.409 26.213 1.00 22.15 ? 411 MET A SD 1 ATOM 2573 C CE . MET A 1 329 ? 13.912 -42.398 25.672 1.00 14.50 ? 411 MET A CE 1 ATOM 2574 N N . ASP A 1 330 ? 9.415 -43.846 21.457 1.00 22.07 ? 412 ASP A N 1 ATOM 2575 C CA . ASP A 1 330 ? 8.787 -42.977 20.465 1.00 19.23 ? 412 ASP A CA 1 ATOM 2576 C C . ASP A 1 330 ? 9.155 -41.527 20.786 1.00 23.24 ? 412 ASP A C 1 ATOM 2577 O O . ASP A 1 330 ? 8.459 -40.850 21.556 1.00 19.74 ? 412 ASP A O 1 ATOM 2578 C CB . ASP A 1 330 ? 7.262 -43.154 20.470 1.00 18.16 ? 412 ASP A CB 1 ATOM 2579 C CG . ASP A 1 330 ? 6.580 -42.429 19.321 1.00 21.58 ? 412 ASP A CG 1 ATOM 2580 O OD1 . ASP A 1 330 ? 7.256 -41.665 18.589 1.00 17.97 ? 412 ASP A OD1 1 ATOM 2581 O OD2 . ASP A 1 330 ? 5.355 -42.623 19.150 1.00 26.07 ? 412 ASP A OD2 1 ATOM 2582 N N . TYR A 1 331 ? 10.242 -41.047 20.191 1.00 22.45 ? 413 TYR A N 1 ATOM 2583 C CA . TYR A 1 331 ? 10.716 -39.692 20.463 1.00 25.98 ? 413 TYR A CA 1 ATOM 2584 C C . TYR A 1 331 ? 9.774 -38.599 19.947 1.00 29.70 ? 413 TYR A C 1 ATOM 2585 O O . TYR A 1 331 ? 9.948 -37.425 20.279 1.00 26.12 ? 413 TYR A O 1 ATOM 2586 C CB . TYR A 1 331 ? 12.152 -39.508 19.942 1.00 23.21 ? 413 TYR A CB 1 ATOM 2587 C CG . TYR A 1 331 ? 13.127 -40.422 20.646 1.00 20.92 ? 413 TYR A CG 1 ATOM 2588 C CD1 . TYR A 1 331 ? 13.670 -40.075 21.881 1.00 18.30 ? 413 TYR A CD1 1 ATOM 2589 C CD2 . TYR A 1 331 ? 13.476 -41.649 20.096 1.00 20.45 ? 413 TYR A CD2 1 ATOM 2590 C CE1 . TYR A 1 331 ? 14.545 -40.925 22.543 1.00 16.10 ? 413 TYR A CE1 1 ATOM 2591 C CE2 . TYR A 1 331 ? 14.347 -42.498 20.744 1.00 19.12 ? 413 TYR A CE2 1 ATOM 2592 C CZ . TYR A 1 331 ? 14.881 -42.131 21.966 1.00 20.76 ? 413 TYR A CZ 1 ATOM 2593 O OH . TYR A 1 331 ? 15.744 -42.991 22.610 1.00 21.14 ? 413 TYR A OH 1 ATOM 2594 N N . TRP A 1 332 ? 8.761 -38.985 19.170 1.00 22.85 ? 414 TRP A N 1 ATOM 2595 C CA . TRP A 1 332 ? 7.836 -38.007 18.590 1.00 25.80 ? 414 TRP A CA 1 ATOM 2596 C C . TRP A 1 332 ? 6.419 -38.052 19.190 1.00 27.43 ? 414 TRP A C 1 ATOM 2597 O O . TRP A 1 332 ? 5.475 -37.482 18.636 1.00 25.76 ? 414 TRP A O 1 ATOM 2598 C CB . TRP A 1 332 ? 7.815 -38.158 17.064 1.00 21.16 ? 414 TRP A CB 1 ATOM 2599 C CG . TRP A 1 332 ? 9.186 -37.924 16.486 1.00 22.68 ? 414 TRP A CG 1 ATOM 2600 C CD1 . TRP A 1 332 ? 9.683 -36.741 16.011 1.00 23.64 ? 414 TRP A CD1 1 ATOM 2601 C CD2 . TRP A 1 332 ? 10.253 -38.882 16.371 1.00 16.36 ? 414 TRP A CD2 1 ATOM 2602 N NE1 . TRP A 1 332 ? 10.987 -36.909 15.594 1.00 21.15 ? 414 TRP A NE1 1 ATOM 2603 C CE2 . TRP A 1 332 ? 11.359 -38.213 15.805 1.00 21.00 ? 414 TRP A CE2 1 ATOM 2604 C CE3 . TRP A 1 332 ? 10.378 -40.242 16.688 1.00 19.28 ? 414 TRP A CE3 1 ATOM 2605 C CZ2 . TRP A 1 332 ? 12.576 -38.857 15.547 1.00 17.94 ? 414 TRP A CZ2 1 ATOM 2606 C CZ3 . TRP A 1 332 ? 11.589 -40.884 16.430 1.00 17.23 ? 414 TRP A CZ3 1 ATOM 2607 C CH2 . TRP A 1 332 ? 12.673 -40.187 15.866 1.00 16.40 ? 414 TRP A CH2 1 ATOM 2608 N N . ALA A 1 333 ? 6.285 -38.712 20.336 1.00 19.24 ? 415 ALA A N 1 ATOM 2609 C CA . ALA A 1 333 ? 5.005 -38.755 21.052 1.00 20.80 ? 415 ALA A CA 1 ATOM 2610 C C . ALA A 1 333 ? 4.684 -37.430 21.754 1.00 19.70 ? 415 ALA A C 1 ATOM 2611 O O . ALA A 1 333 ? 5.580 -36.627 22.023 1.00 25.75 ? 415 ALA A O 1 ATOM 2612 C CB . ALA A 1 333 ? 5.004 -39.890 22.057 1.00 17.93 ? 415 ALA A CB 1 ATOM 2613 N N . GLU A 1 334 ? 3.406 -37.222 22.068 1.00 31.79 ? 416 GLU A N 1 ATOM 2614 C CA . GLU A 1 334 ? 2.964 -36.046 22.822 1.00 40.33 ? 416 GLU A CA 1 ATOM 2615 C C . GLU A 1 334 ? 3.371 -36.136 24.294 1.00 34.92 ? 416 GLU A C 1 ATOM 2616 O O . GLU A 1 334 ? 3.664 -37.223 24.795 1.00 30.31 ? 416 GLU A O 1 ATOM 2617 C CB . GLU A 1 334 ? 1.440 -35.897 22.725 1.00 42.82 ? 416 GLU A CB 1 ATOM 2618 C CG . GLU A 1 334 ? 0.931 -35.447 21.358 1.00 55.32 ? 416 GLU A CG 1 ATOM 2619 C CD . GLU A 1 334 ? 1.368 -34.034 21.008 1.00 63.82 ? 416 GLU A CD 1 ATOM 2620 O OE1 . GLU A 1 334 ? 1.204 -33.128 21.855 1.00 62.22 ? 416 GLU A OE1 1 ATOM 2621 O OE2 . GLU A 1 334 ? 1.881 -33.832 19.887 1.00 64.74 ? 416 GLU A OE2 1 ATOM 2622 N N . GLY A 1 335 ? 3.396 -35.000 24.988 1.00 33.40 ? 417 GLY A N 1 ATOM 2623 C CA . GLY A 1 335 ? 3.666 -35.009 26.418 1.00 27.52 ? 417 GLY A CA 1 ATOM 2624 C C . GLY A 1 335 ? 4.995 -34.407 26.845 1.00 33.83 ? 417 GLY A C 1 ATOM 2625 O O . GLY A 1 335 ? 5.761 -33.899 26.020 1.00 29.35 ? 417 GLY A O 1 ATOM 2626 N N . ASP A 1 336 ? 5.275 -34.475 28.145 1.00 30.07 ? 418 ASP A N 1 ATOM 2627 C CA . ASP A 1 336 ? 6.446 -33.804 28.703 1.00 26.91 ? 418 ASP A CA 1 ATOM 2628 C C . ASP A 1 336 ? 7.599 -34.759 28.990 1.00 27.18 ? 418 ASP A C 1 ATOM 2629 O O . ASP A 1 336 ? 8.650 -34.339 29.485 1.00 21.75 ? 418 ASP A O 1 ATOM 2630 C CB . ASP A 1 336 ? 6.073 -33.010 29.968 1.00 36.54 ? 418 ASP A CB 1 ATOM 2631 C CG . ASP A 1 336 ? 5.537 -33.892 31.099 1.00 50.32 ? 418 ASP A CG 1 ATOM 2632 O OD1 . ASP A 1 336 ? 6.093 -34.988 31.361 1.00 49.26 ? 418 ASP A OD1 1 ATOM 2633 O OD2 . ASP A 1 336 ? 4.555 -33.468 31.749 1.00 62.76 ? 418 ASP A OD2 1 ATOM 2634 N N . CYS A 1 337 ? 7.401 -36.042 28.700 1.00 25.13 ? 419 CYS A N 1 ATOM 2635 C CA . CYS A 1 337 ? 8.420 -37.032 29.009 1.00 21.82 ? 419 CYS A CA 1 ATOM 2636 C C . CYS A 1 337 ? 8.489 -38.127 27.954 1.00 26.39 ? 419 CYS A C 1 ATOM 2637 O O . CYS A 1 337 ? 7.528 -38.353 27.205 1.00 24.99 ? 419 CYS A O 1 ATOM 2638 C CB . CYS A 1 337 ? 8.180 -37.637 30.400 1.00 24.30 ? 419 CYS A CB 1 ATOM 2639 S SG . CYS A 1 337 ? 6.563 -38.444 30.637 1.00 26.52 ? 419 CYS A SG 1 ATOM 2640 N N . TYR A 1 338 ? 9.637 -38.796 27.900 1.00 20.01 ? 420 TYR A N 1 ATOM 2641 C CA . TYR A 1 338 ? 9.845 -39.908 26.982 1.00 23.26 ? 420 TYR A CA 1 ATOM 2642 C C . TYR A 1 338 ? 9.442 -41.191 27.687 1.00 23.83 ? 420 TYR A C 1 ATOM 2643 O O . TYR A 1 338 ? 9.902 -41.465 28.806 1.00 19.79 ? 420 TYR A O 1 ATOM 2644 C CB . TYR A 1 338 ? 11.319 -40.005 26.571 1.00 22.14 ? 420 TYR A CB 1 ATOM 2645 C CG . TYR A 1 338 ? 11.811 -38.897 25.662 1.00 25.54 ? 420 TYR A CG 1 ATOM 2646 C CD1 . TYR A 1 338 ? 11.039 -38.442 24.601 1.00 19.13 ? 420 TYR A CD1 1 ATOM 2647 C CD2 . TYR A 1 338 ? 13.059 -38.316 25.863 1.00 18.05 ? 420 TYR A CD2 1 ATOM 2648 C CE1 . TYR A 1 338 ? 11.495 -37.436 23.767 1.00 21.20 ? 420 TYR A CE1 1 ATOM 2649 C CE2 . TYR A 1 338 ? 13.520 -37.315 25.041 1.00 25.74 ? 420 TYR A CE2 1 ATOM 2650 C CZ . TYR A 1 338 ? 12.736 -36.877 23.996 1.00 20.11 ? 420 TYR A CZ 1 ATOM 2651 O OH . TYR A 1 338 ? 13.200 -35.874 23.176 1.00 24.87 ? 420 TYR A OH 1 ATOM 2652 N N . ARG A 1 339 ? 8.590 -41.975 27.032 1.00 18.35 ? 421 ARG A N 1 ATOM 2653 C CA . ARG A 1 339 ? 8.094 -43.220 27.606 1.00 17.43 ? 421 ARG A CA 1 ATOM 2654 C C . ARG A 1 339 ? 9.044 -44.358 27.249 1.00 21.03 ? 421 ARG A C 1 ATOM 2655 O O . ARG A 1 339 ? 9.163 -44.740 26.078 1.00 22.94 ? 421 ARG A O 1 ATOM 2656 C CB . ARG A 1 339 ? 6.681 -43.506 27.086 1.00 22.49 ? 421 ARG A CB 1 ATOM 2657 C CG . ARG A 1 339 ? 5.987 -44.693 27.727 1.00 21.99 ? 421 ARG A CG 1 ATOM 2658 C CD . ARG A 1 339 ? 4.642 -44.975 27.042 1.00 25.02 ? 421 ARG A CD 1 ATOM 2659 N NE . ARG A 1 339 ? 3.646 -43.945 27.328 1.00 21.98 ? 421 ARG A NE 1 ATOM 2660 C CZ . ARG A 1 339 ? 2.412 -44.198 27.755 1.00 25.16 ? 421 ARG A CZ 1 ATOM 2661 N NH1 . ARG A 1 339 ? 2.014 -45.452 27.932 1.00 23.21 ? 421 ARG A NH1 1 ATOM 2662 N NH2 . ARG A 1 339 ? 1.568 -43.201 27.999 1.00 27.68 ? 421 ARG A NH2 1 ATOM 2663 N N . ALA A 1 340 ? 9.735 -44.882 28.255 1.00 14.99 ? 422 ALA A N 1 ATOM 2664 C CA . ALA A 1 340 ? 10.647 -46.009 28.064 1.00 20.00 ? 422 ALA A CA 1 ATOM 2665 C C . ALA A 1 340 ? 9.924 -47.212 27.451 1.00 20.56 ? 422 ALA A C 1 ATOM 2666 O O . ALA A 1 340 ? 8.844 -47.593 27.916 1.00 18.98 ? 422 ALA A O 1 ATOM 2667 C CB . ALA A 1 340 ? 11.263 -46.401 29.399 1.00 21.65 ? 422 ALA A CB 1 ATOM 2668 N N . CYS A 1 341 ? 10.524 -47.804 26.416 1.00 15.11 ? 423 CYS A N 1 ATOM 2669 C CA . CYS A 1 341 ? 9.999 -49.028 25.809 1.00 22.51 ? 423 CYS A CA 1 ATOM 2670 C C . CYS A 1 341 ? 11.107 -50.055 25.616 1.00 21.87 ? 423 CYS A C 1 ATOM 2671 O O . CYS A 1 341 ? 12.290 -49.718 25.634 1.00 18.31 ? 423 CYS A O 1 ATOM 2672 C CB . CYS A 1 341 ? 9.353 -48.742 24.447 1.00 17.10 ? 423 CYS A CB 1 ATOM 2673 S SG . CYS A 1 341 ? 7.977 -47.564 24.450 1.00 20.70 ? 423 CYS A SG 1 ATOM 2674 N N . PHE A 1 342 ? 10.722 -51.311 25.423 1.00 18.04 ? 424 PHE A N 1 ATOM 2675 C CA . PHE A 1 342 ? 11.689 -52.339 25.085 1.00 17.86 ? 424 PHE A CA 1 ATOM 2676 C C . PHE A 1 342 ? 11.007 -53.459 24.320 1.00 16.24 ? 424 PHE A C 1 ATOM 2677 O O . PHE A 1 342 ? 9.781 -53.562 24.319 1.00 17.74 ? 424 PHE A O 1 ATOM 2678 C CB . PHE A 1 342 ? 12.379 -52.876 26.340 1.00 14.19 ? 424 PHE A CB 1 ATOM 2679 C CG . PHE A 1 342 ? 11.460 -53.620 27.275 1.00 18.67 ? 424 PHE A CG 1 ATOM 2680 C CD1 . PHE A 1 342 ? 10.695 -52.937 28.209 1.00 19.29 ? 424 PHE A CD1 1 ATOM 2681 C CD2 . PHE A 1 342 ? 11.375 -55.007 27.227 1.00 20.97 ? 424 PHE A CD2 1 ATOM 2682 C CE1 . PHE A 1 342 ? 9.847 -53.621 29.074 1.00 17.00 ? 424 PHE A CE1 1 ATOM 2683 C CE2 . PHE A 1 342 ? 10.534 -55.701 28.086 1.00 17.48 ? 424 PHE A CE2 1 ATOM 2684 C CZ . PHE A 1 342 ? 9.769 -55.003 29.014 1.00 23.67 ? 424 PHE A CZ 1 ATOM 2685 N N . TYR A 1 343 ? 11.802 -54.282 23.649 1.00 16.74 ? 425 TYR A N 1 ATOM 2686 C CA . TYR A 1 343 ? 11.273 -55.474 23.002 1.00 16.36 ? 425 TYR A CA 1 ATOM 2687 C C . TYR A 1 343 ? 12.015 -56.660 23.591 1.00 22.49 ? 425 TYR A C 1 ATOM 2688 O O . TYR A 1 343 ? 13.148 -56.525 24.082 1.00 15.87 ? 425 TYR A O 1 ATOM 2689 C CB . TYR A 1 343 ? 11.507 -55.427 21.489 1.00 12.80 ? 425 TYR A CB 1 ATOM 2690 C CG . TYR A 1 343 ? 12.970 -55.453 21.154 1.00 16.15 ? 425 TYR A CG 1 ATOM 2691 C CD1 . TYR A 1 343 ? 13.680 -54.269 20.994 1.00 16.05 ? 425 TYR A CD1 1 ATOM 2692 C CD2 . TYR A 1 343 ? 13.658 -56.661 21.024 1.00 10.46 ? 425 TYR A CD2 1 ATOM 2693 C CE1 . TYR A 1 343 ? 15.037 -54.284 20.707 1.00 18.19 ? 425 TYR A CE1 1 ATOM 2694 C CE2 . TYR A 1 343 ? 15.011 -56.683 20.743 1.00 15.97 ? 425 TYR A CE2 1 ATOM 2695 C CZ . TYR A 1 343 ? 15.694 -55.491 20.586 1.00 13.87 ? 425 TYR A CZ 1 ATOM 2696 O OH . TYR A 1 343 ? 17.045 -55.511 20.299 1.00 18.10 ? 425 TYR A OH 1 ATOM 2697 N N . VAL A 1 344 ? 11.395 -57.828 23.536 1.00 19.95 ? 426 VAL A N 1 ATOM 2698 C CA . VAL A 1 344 ? 12.119 -59.048 23.851 1.00 15.55 ? 426 VAL A CA 1 ATOM 2699 C C . VAL A 1 344 ? 11.984 -59.961 22.634 1.00 22.65 ? 426 VAL A C 1 ATOM 2700 O O . VAL A 1 344 ? 10.883 -60.119 22.086 1.00 15.08 ? 426 VAL A O 1 ATOM 2701 C CB . VAL A 1 344 ? 11.563 -59.738 25.110 1.00 23.79 ? 426 VAL A CB 1 ATOM 2702 C CG1 . VAL A 1 344 ? 12.385 -60.970 25.438 1.00 18.95 ? 426 VAL A CG1 1 ATOM 2703 C CG2 . VAL A 1 344 ? 11.549 -58.774 26.308 1.00 16.72 ? 426 VAL A CG2 1 ATOM 2704 N N . GLU A 1 345 ? 13.105 -60.525 22.190 1.00 19.25 ? 427 GLU A N 1 ATOM 2705 C CA . GLU A 1 345 ? 13.105 -61.499 21.105 1.00 16.75 ? 427 GLU A CA 1 ATOM 2706 C C . GLU A 1 345 ? 12.763 -62.869 21.685 1.00 18.64 ? 427 GLU A C 1 ATOM 2707 O O . GLU A 1 345 ? 13.411 -63.325 22.628 1.00 19.17 ? 427 GLU A O 1 ATOM 2708 C CB . GLU A 1 345 ? 14.484 -61.540 20.432 1.00 12.74 ? 427 GLU A CB 1 ATOM 2709 C CG . GLU A 1 345 ? 14.692 -62.695 19.444 1.00 15.91 ? 427 GLU A CG 1 ATOM 2710 C CD . GLU A 1 345 ? 16.149 -62.837 19.020 1.00 22.74 ? 427 GLU A CD 1 ATOM 2711 O OE1 . GLU A 1 345 ? 17.036 -62.761 19.902 1.00 19.24 ? 427 GLU A OE1 1 ATOM 2712 O OE2 . GLU A 1 345 ? 16.408 -63.022 17.807 1.00 18.15 ? 427 GLU A OE2 1 ATOM 2713 N N . LEU A 1 346 ? 11.733 -63.511 21.141 1.00 15.13 ? 428 LEU A N 1 ATOM 2714 C CA . LEU A 1 346 ? 11.329 -64.835 21.601 1.00 14.17 ? 428 LEU A CA 1 ATOM 2715 C C . LEU A 1 346 ? 11.828 -65.856 20.590 1.00 19.64 ? 428 LEU A C 1 ATOM 2716 O O . LEU A 1 346 ? 11.177 -66.109 19.574 1.00 18.23 ? 428 LEU A O 1 ATOM 2717 C CB . LEU A 1 346 ? 9.810 -64.904 21.748 1.00 16.82 ? 428 LEU A CB 1 ATOM 2718 C CG . LEU A 1 346 ? 9.237 -63.715 22.524 1.00 17.69 ? 428 LEU A CG 1 ATOM 2719 C CD1 . LEU A 1 346 ? 7.706 -63.745 22.584 1.00 14.84 ? 428 LEU A CD1 1 ATOM 2720 C CD2 . LEU A 1 346 ? 9.833 -63.685 23.933 1.00 19.24 ? 428 LEU A CD2 1 ATOM 2721 N N . ILE A 1 347 ? 13.000 -66.423 20.860 1.00 15.29 ? 429 ILE A N 1 ATOM 2722 C CA . ILE A 1 347 ? 13.643 -67.337 19.918 1.00 14.95 ? 429 ILE A CA 1 ATOM 2723 C C . ILE A 1 347 ? 12.978 -68.713 19.910 1.00 17.75 ? 429 ILE A C 1 ATOM 2724 O O . ILE A 1 347 ? 12.798 -69.331 20.963 1.00 19.14 ? 429 ILE A O 1 ATOM 2725 C CB . ILE A 1 347 ? 15.148 -67.507 20.239 1.00 19.16 ? 429 ILE A CB 1 ATOM 2726 C CG1 . ILE A 1 347 ? 15.866 -66.153 20.168 1.00 14.98 ? 429 ILE A CG1 1 ATOM 2727 C CG2 . ILE A 1 347 ? 15.787 -68.520 19.288 1.00 10.52 ? 429 ILE A CG2 1 ATOM 2728 C CD1 . ILE A 1 347 ? 17.365 -66.197 20.554 1.00 13.97 ? 429 ILE A CD1 1 ATOM 2729 N N . ARG A 1 348 ? 12.608 -69.192 18.725 1.00 16.33 ? 430 ARG A N 1 ATOM 2730 C CA . ARG A 1 348 ? 12.070 -70.545 18.602 1.00 18.03 ? 430 ARG A CA 1 ATOM 2731 C C . ARG A 1 348 ? 12.956 -71.346 17.665 1.00 20.63 ? 430 ARG A C 1 ATOM 2732 O O . ARG A 1 348 ? 13.604 -70.780 16.775 1.00 18.20 ? 430 ARG A O 1 ATOM 2733 C CB . ARG A 1 348 ? 10.632 -70.536 18.074 1.00 20.81 ? 430 ARG A CB 1 ATOM 2734 C CG . ARG A 1 348 ? 9.645 -69.722 18.903 1.00 18.94 ? 430 ARG A CG 1 ATOM 2735 C CD . ARG A 1 348 ? 9.621 -70.159 20.362 1.00 20.62 ? 430 ARG A CD 1 ATOM 2736 N NE . ARG A 1 348 ? 9.328 -71.584 20.520 1.00 18.39 ? 430 ARG A NE 1 ATOM 2737 C CZ . ARG A 1 348 ? 8.104 -72.100 20.636 1.00 24.45 ? 430 ARG A CZ 1 ATOM 2738 N NH1 . ARG A 1 348 ? 7.031 -71.314 20.616 1.00 14.87 ? 430 ARG A NH1 1 ATOM 2739 N NH2 . ARG A 1 348 ? 7.950 -73.411 20.782 1.00 21.92 ? 430 ARG A NH2 1 ATOM 2740 N N . GLY A 1 349 ? 12.992 -72.661 17.864 1.00 24.47 ? 431 GLY A N 1 ATOM 2741 C CA . GLY A 1 349 ? 13.826 -73.513 17.040 1.00 19.96 ? 431 GLY A CA 1 ATOM 2742 C C . GLY A 1 349 ? 15.179 -73.783 17.669 1.00 19.61 ? 431 GLY A C 1 ATOM 2743 O O . GLY A 1 349 ? 15.298 -73.894 18.895 1.00 21.72 ? 431 GLY A O 1 ATOM 2744 N N . ARG A 1 350 ? 16.207 -73.888 16.830 1.00 16.16 ? 432 ARG A N 1 ATOM 2745 C CA . ARG A 1 350 ? 17.524 -74.303 17.301 1.00 21.00 ? 432 ARG A CA 1 ATOM 2746 C C . ARG A 1 350 ? 18.271 -73.183 18.024 1.00 20.22 ? 432 ARG A C 1 ATOM 2747 O O . ARG A 1 350 ? 18.037 -72.003 17.749 1.00 17.53 ? 432 ARG A O 1 ATOM 2748 C CB . ARG A 1 350 ? 18.339 -74.881 16.138 1.00 17.28 ? 432 ARG A CB 1 ATOM 2749 C CG . ARG A 1 350 ? 17.822 -76.249 15.729 1.00 18.32 ? 432 ARG A CG 1 ATOM 2750 C CD . ARG A 1 350 ? 18.658 -76.936 14.663 1.00 23.38 ? 432 ARG A CD 1 ATOM 2751 N NE . ARG A 1 350 ? 18.127 -78.277 14.431 1.00 26.95 ? 432 ARG A NE 1 ATOM 2752 C CZ . ARG A 1 350 ? 18.807 -79.285 13.896 1.00 29.17 ? 432 ARG A CZ 1 ATOM 2753 N NH1 . ARG A 1 350 ? 20.068 -79.120 13.517 1.00 30.41 ? 432 ARG A NH1 1 ATOM 2754 N NH2 . ARG A 1 350 ? 18.219 -80.463 13.748 1.00 26.05 ? 432 ARG A NH2 1 ATOM 2755 N N . PRO A 1 351 ? 19.185 -73.546 18.948 1.00 23.15 ? 433 PRO A N 1 ATOM 2756 C CA . PRO A 1 351 ? 19.598 -74.917 19.287 1.00 18.84 ? 433 PRO A CA 1 ATOM 2757 C C . PRO A 1 351 ? 18.715 -75.604 20.327 1.00 25.49 ? 433 PRO A C 1 ATOM 2758 O O . PRO A 1 351 ? 18.804 -76.827 20.475 1.00 20.72 ? 433 PRO A O 1 ATOM 2759 C CB . PRO A 1 351 ? 21.008 -74.720 19.853 1.00 23.52 ? 433 PRO A CB 1 ATOM 2760 C CG . PRO A 1 351 ? 20.948 -73.358 20.504 1.00 22.61 ? 433 PRO A CG 1 ATOM 2761 C CD . PRO A 1 351 ? 19.983 -72.533 19.666 1.00 17.91 ? 433 PRO A CD 1 ATOM 2762 N N . LYS A 1 352 ? 17.879 -74.842 21.026 1.00 21.42 ? 434 LYS A N 1 ATOM 2763 C CA . LYS A 1 352 ? 17.068 -75.383 22.121 1.00 22.61 ? 434 LYS A CA 1 ATOM 2764 C C . LYS A 1 352 ? 15.952 -76.337 21.670 1.00 22.75 ? 434 LYS A C 1 ATOM 2765 O O . LYS A 1 352 ? 15.586 -77.271 22.393 1.00 21.71 ? 434 LYS A O 1 ATOM 2766 C CB . LYS A 1 352 ? 16.488 -74.237 22.960 1.00 18.13 ? 434 LYS A CB 1 ATOM 2767 C CG . LYS A 1 352 ? 17.534 -73.515 23.824 1.00 22.68 ? 434 LYS A CG 1 ATOM 2768 C CD . LYS A 1 352 ? 18.105 -74.478 24.868 1.00 28.27 ? 434 LYS A CD 1 ATOM 2769 C CE . LYS A 1 352 ? 19.136 -73.822 25.778 1.00 30.82 ? 434 LYS A CE 1 ATOM 2770 N NZ . LYS A 1 352 ? 20.413 -73.547 25.056 1.00 35.47 ? 434 LYS A NZ 1 ATOM 2771 N N . GLU A 1 353 ? 15.412 -76.106 20.478 1.00 23.32 ? 435 GLU A N 1 ATOM 2772 C CA . GLU A 1 353 ? 14.326 -76.936 19.969 1.00 22.40 ? 435 GLU A CA 1 ATOM 2773 C C . GLU A 1 353 ? 14.741 -77.530 18.629 1.00 28.07 ? 435 GLU A C 1 ATOM 2774 O O . GLU A 1 353 ? 14.385 -77.006 17.574 1.00 28.34 ? 435 GLU A O 1 ATOM 2775 C CB . GLU A 1 353 ? 13.047 -76.100 19.837 1.00 30.25 ? 435 GLU A CB 1 ATOM 2776 C CG . GLU A 1 353 ? 12.613 -75.429 21.149 1.00 26.66 ? 435 GLU A CG 1 ATOM 2777 C CD . GLU A 1 353 ? 11.463 -74.444 20.978 1.00 29.30 ? 435 GLU A CD 1 ATOM 2778 O OE1 . GLU A 1 353 ? 11.634 -73.429 20.262 1.00 27.07 ? 435 GLU A OE1 1 ATOM 2779 O OE2 . GLU A 1 353 ? 10.388 -74.683 21.568 1.00 28.52 ? 435 GLU A OE2 1 ATOM 2780 N N . ASP A 1 354 ? 15.498 -78.624 18.673 1.00 24.71 ? 436 ASP A N 1 ATOM 2781 C CA . ASP A 1 354 ? 16.175 -79.132 17.478 1.00 24.54 ? 436 ASP A CA 1 ATOM 2782 C C . ASP A 1 354 ? 15.383 -80.175 16.688 1.00 27.08 ? 436 ASP A C 1 ATOM 2783 O O . ASP A 1 354 ? 15.919 -80.805 15.773 1.00 26.76 ? 436 ASP A O 1 ATOM 2784 C CB . ASP A 1 354 ? 17.567 -79.675 17.833 1.00 30.29 ? 436 ASP A CB 1 ATOM 2785 C CG . ASP A 1 354 ? 17.510 -80.900 18.732 1.00 39.89 ? 436 ASP A CG 1 ATOM 2786 O OD1 . ASP A 1 354 ? 16.410 -81.249 19.215 1.00 36.02 ? 436 ASP A OD1 1 ATOM 2787 O OD2 . ASP A 1 354 ? 18.577 -81.507 18.968 1.00 49.49 ? 436 ASP A OD2 1 ATOM 2788 N N . LYS A 1 355 ? 14.116 -80.359 17.038 1.00 27.34 ? 437 LYS A N 1 ATOM 2789 C CA . LYS A 1 355 ? 13.251 -81.218 16.241 1.00 25.78 ? 437 LYS A CA 1 ATOM 2790 C C . LYS A 1 355 ? 12.948 -80.560 14.896 1.00 31.88 ? 437 LYS A C 1 ATOM 2791 O O . LYS A 1 355 ? 12.705 -81.250 13.900 1.00 23.69 ? 437 LYS A O 1 ATOM 2792 C CB . LYS A 1 355 ? 11.968 -81.570 17.000 1.00 29.11 ? 437 LYS A CB 1 ATOM 2793 C CG . LYS A 1 355 ? 12.181 -82.679 18.038 1.00 31.60 ? 437 LYS A CG 1 ATOM 2794 C CD . LYS A 1 355 ? 10.880 -83.081 18.724 1.00 52.87 ? 437 LYS A CD 1 ATOM 2795 C CE . LYS A 1 355 ? 11.111 -84.227 19.709 1.00 57.81 ? 437 LYS A CE 1 ATOM 2796 N NZ . LYS A 1 355 ? 12.069 -83.858 20.793 1.00 51.96 ? 437 LYS A NZ 1 ATOM 2797 N N . VAL A 1 356 ? 12.967 -79.225 14.879 1.00 22.89 ? 438 VAL A N 1 ATOM 2798 C CA . VAL A 1 356 ? 12.927 -78.465 13.630 1.00 18.78 ? 438 VAL A CA 1 ATOM 2799 C C . VAL A 1 356 ? 14.356 -78.110 13.233 1.00 27.29 ? 438 VAL A C 1 ATOM 2800 O O . VAL A 1 356 ? 15.265 -78.164 14.069 1.00 24.34 ? 438 VAL A O 1 ATOM 2801 C CB . VAL A 1 356 ? 12.117 -77.165 13.764 1.00 20.65 ? 438 VAL A CB 1 ATOM 2802 C CG1 . VAL A 1 356 ? 10.653 -77.463 14.079 1.00 24.24 ? 438 VAL A CG1 1 ATOM 2803 C CG2 . VAL A 1 356 ? 12.735 -76.258 14.826 1.00 18.65 ? 438 VAL A CG2 1 ATOM 2804 N N . TRP A 1 357 ? 14.550 -77.731 11.971 1.00 20.81 ? 439 TRP A N 1 ATOM 2805 C CA . TRP A 1 357 ? 15.889 -77.499 11.435 1.00 18.05 ? 439 TRP A CA 1 ATOM 2806 C C . TRP A 1 357 ? 16.186 -76.019 11.280 1.00 19.88 ? 439 TRP A C 1 ATOM 2807 O O . TRP A 1 357 ? 17.303 -75.632 10.917 1.00 20.94 ? 439 TRP A O 1 ATOM 2808 C CB . TRP A 1 357 ? 16.046 -78.209 10.095 1.00 23.28 ? 439 TRP A CB 1 ATOM 2809 C CG . TRP A 1 357 ? 16.111 -79.689 10.253 1.00 32.78 ? 439 TRP A CG 1 ATOM 2810 C CD1 . TRP A 1 357 ? 15.061 -80.558 10.304 1.00 33.29 ? 439 TRP A CD1 1 ATOM 2811 C CD2 . TRP A 1 357 ? 17.297 -80.477 10.406 1.00 33.40 ? 439 TRP A CD2 1 ATOM 2812 N NE1 . TRP A 1 357 ? 15.523 -81.844 10.474 1.00 43.27 ? 439 TRP A NE1 1 ATOM 2813 C CE2 . TRP A 1 357 ? 16.892 -81.821 10.536 1.00 39.17 ? 439 TRP A CE2 1 ATOM 2814 C CE3 . TRP A 1 357 ? 18.662 -80.176 10.438 1.00 34.07 ? 439 TRP A CE3 1 ATOM 2815 C CZ2 . TRP A 1 357 ? 17.806 -82.864 10.699 1.00 46.04 ? 439 TRP A CZ2 1 ATOM 2816 C CZ3 . TRP A 1 357 ? 19.567 -81.212 10.601 1.00 40.45 ? 439 TRP A CZ3 1 ATOM 2817 C CH2 . TRP A 1 357 ? 19.136 -82.538 10.727 1.00 41.17 ? 439 TRP A CH2 1 ATOM 2818 N N . TRP A 1 358 ? 15.176 -75.201 11.568 1.00 17.14 ? 440 TRP A N 1 ATOM 2819 C CA . TRP A 1 358 ? 15.293 -73.753 11.465 1.00 19.37 ? 440 TRP A CA 1 ATOM 2820 C C . TRP A 1 358 ? 15.516 -73.071 12.812 1.00 19.54 ? 440 TRP A C 1 ATOM 2821 O O . TRP A 1 358 ? 15.446 -73.708 13.875 1.00 19.22 ? 440 TRP A O 1 ATOM 2822 C CB . TRP A 1 358 ? 14.060 -73.147 10.779 1.00 16.07 ? 440 TRP A CB 1 ATOM 2823 C CG . TRP A 1 358 ? 12.708 -73.617 11.305 1.00 20.13 ? 440 TRP A CG 1 ATOM 2824 C CD1 . TRP A 1 358 ? 11.899 -74.570 10.745 1.00 22.09 ? 440 TRP A CD1 1 ATOM 2825 C CD2 . TRP A 1 358 ? 11.997 -73.119 12.453 1.00 19.14 ? 440 TRP A CD2 1 ATOM 2826 N NE1 . TRP A 1 358 ? 10.741 -74.706 11.481 1.00 14.67 ? 440 TRP A NE1 1 ATOM 2827 C CE2 . TRP A 1 358 ? 10.776 -73.829 12.533 1.00 21.75 ? 440 TRP A CE2 1 ATOM 2828 C CE3 . TRP A 1 358 ? 12.278 -72.151 13.424 1.00 17.81 ? 440 TRP A CE3 1 ATOM 2829 C CZ2 . TRP A 1 358 ? 9.840 -73.602 13.550 1.00 21.90 ? 440 TRP A CZ2 1 ATOM 2830 C CZ3 . TRP A 1 358 ? 11.348 -71.926 14.435 1.00 18.12 ? 440 TRP A CZ3 1 ATOM 2831 C CH2 . TRP A 1 358 ? 10.144 -72.646 14.488 1.00 21.90 ? 440 TRP A CH2 1 ATOM 2832 N N . THR A 1 359 ? 15.805 -71.774 12.743 1.00 19.13 ? 441 THR A N 1 ATOM 2833 C CA . THR A 1 359 ? 15.848 -70.904 13.914 1.00 18.51 ? 441 THR A CA 1 ATOM 2834 C C . THR A 1 359 ? 15.174 -69.593 13.541 1.00 18.03 ? 441 THR A C 1 ATOM 2835 O O . THR A 1 359 ? 15.528 -68.969 12.537 1.00 18.95 ? 441 THR A O 1 ATOM 2836 C CB . THR A 1 359 ? 17.295 -70.606 14.365 1.00 25.57 ? 441 THR A CB 1 ATOM 2837 O OG1 . THR A 1 359 ? 17.907 -71.804 14.857 1.00 19.45 ? 441 THR A OG1 1 ATOM 2838 C CG2 . THR A 1 359 ? 17.312 -69.554 15.472 1.00 18.38 ? 441 THR A CG2 1 ATOM 2839 N N . SER A 1 360 ? 14.189 -69.180 14.330 1.00 17.79 ? 442 SER A N 1 ATOM 2840 C CA . SER A 1 360 ? 13.519 -67.912 14.074 1.00 14.18 ? 442 SER A CA 1 ATOM 2841 C C . SER A 1 360 ? 13.081 -67.290 15.393 1.00 23.17 ? 442 SER A C 1 ATOM 2842 O O . SER A 1 360 ? 13.606 -67.641 16.459 1.00 23.26 ? 442 SER A O 1 ATOM 2843 C CB . SER A 1 360 ? 12.319 -68.101 13.139 1.00 16.71 ? 442 SER A CB 1 ATOM 2844 O OG . SER A 1 360 ? 11.902 -66.850 12.622 1.00 16.31 ? 442 SER A OG 1 ATOM 2845 N N . ASN A 1 361 ? 12.115 -66.378 15.332 1.00 19.47 ? 443 ASN A N 1 ATOM 2846 C CA . ASN A 1 361 ? 11.659 -65.711 16.543 1.00 15.51 ? 443 ASN A CA 1 ATOM 2847 C C . ASN A 1 361 ? 10.354 -64.974 16.310 1.00 17.81 ? 443 ASN A C 1 ATOM 2848 O O . ASN A 1 361 ? 9.948 -64.762 15.162 1.00 17.54 ? 443 ASN A O 1 ATOM 2849 C CB . ASN A 1 361 ? 12.711 -64.698 17.000 1.00 13.06 ? 443 ASN A CB 1 ATOM 2850 C CG . ASN A 1 361 ? 12.814 -63.517 16.056 1.00 17.92 ? 443 ASN A CG 1 ATOM 2851 O OD1 . ASN A 1 361 ? 13.433 -63.612 14.989 1.00 14.79 ? 443 ASN A OD1 1 ATOM 2852 N ND2 . ASN A 1 361 ? 12.184 -62.403 16.427 1.00 14.84 ? 443 ASN A ND2 1 ATOM 2853 N N . SER A 1 362 ? 9.694 -64.585 17.400 1.00 14.14 ? 444 SER A N 1 ATOM 2854 C CA . SER A 1 362 ? 8.647 -63.578 17.309 1.00 15.07 ? 444 SER A CA 1 ATOM 2855 C C . SER A 1 362 ? 9.069 -62.437 18.215 1.00 19.41 ? 444 SER A C 1 ATOM 2856 O O . SER A 1 362 ? 10.138 -62.495 18.833 1.00 15.58 ? 444 SER A O 1 ATOM 2857 C CB . SER A 1 362 ? 7.277 -64.132 17.713 1.00 14.92 ? 444 SER A CB 1 ATOM 2858 O OG . SER A 1 362 ? 7.216 -64.455 19.091 1.00 21.79 ? 444 SER A OG 1 ATOM 2859 N N . ILE A 1 363 ? 8.241 -61.401 18.281 1.00 16.75 ? 445 ILE A N 1 ATOM 2860 C CA . ILE A 1 363 ? 8.548 -60.218 19.063 1.00 19.53 ? 445 ILE A CA 1 ATOM 2861 C C . ILE A 1 363 ? 7.434 -59.951 20.073 1.00 19.81 ? 445 ILE A C 1 ATOM 2862 O O . ILE A 1 363 ? 6.247 -60.103 19.758 1.00 17.78 ? 445 ILE A O 1 ATOM 2863 C CB . ILE A 1 363 ? 8.693 -58.978 18.142 1.00 20.12 ? 445 ILE A CB 1 ATOM 2864 C CG1 . ILE A 1 363 ? 9.845 -59.163 17.152 1.00 14.30 ? 445 ILE A CG1 1 ATOM 2865 C CG2 . ILE A 1 363 ? 8.907 -57.707 18.956 1.00 16.96 ? 445 ILE A CG2 1 ATOM 2866 C CD1 . ILE A 1 363 ? 9.857 -58.114 16.011 1.00 13.51 ? 445 ILE A CD1 1 ATOM 2867 N N . VAL A 1 364 ? 7.815 -59.580 21.294 1.00 16.47 ? 446 VAL A N 1 ATOM 2868 C CA . VAL A 1 364 ? 6.871 -58.934 22.201 1.00 18.19 ? 446 VAL A CA 1 ATOM 2869 C C . VAL A 1 364 ? 7.506 -57.611 22.623 1.00 22.17 ? 446 VAL A C 1 ATOM 2870 O O . VAL A 1 364 ? 8.727 -57.514 22.740 1.00 17.71 ? 446 VAL A O 1 ATOM 2871 C CB . VAL A 1 364 ? 6.491 -59.816 23.423 1.00 18.04 ? 446 VAL A CB 1 ATOM 2872 C CG1 . VAL A 1 364 ? 7.687 -60.057 24.325 1.00 9.89 ? 446 VAL A CG1 1 ATOM 2873 C CG2 . VAL A 1 364 ? 5.355 -59.167 24.218 1.00 12.37 ? 446 VAL A CG2 1 ATOM 2874 N N . SER A 1 365 ? 6.687 -56.585 22.821 1.00 17.42 ? 447 SER A N 1 ATOM 2875 C CA . SER A 1 365 ? 7.209 -55.262 23.143 1.00 19.19 ? 447 SER A CA 1 ATOM 2876 C C . SER A 1 365 ? 6.354 -54.628 24.239 1.00 17.32 ? 447 SER A C 1 ATOM 2877 O O . SER A 1 365 ? 5.136 -54.838 24.260 1.00 20.11 ? 447 SER A O 1 ATOM 2878 C CB . SER A 1 365 ? 7.194 -54.388 21.880 1.00 15.43 ? 447 SER A CB 1 ATOM 2879 O OG . SER A 1 365 ? 7.922 -53.196 22.092 1.00 23.85 ? 447 SER A OG 1 ATOM 2880 N N . MET A 1 366 ? 6.979 -53.866 25.143 1.00 20.84 ? 448 MET A N 1 ATOM 2881 C CA . MET A 1 366 ? 6.258 -53.153 26.204 1.00 14.47 ? 448 MET A CA 1 ATOM 2882 C C . MET A 1 366 ? 6.733 -51.710 26.324 1.00 24.11 ? 448 MET A C 1 ATOM 2883 O O . MET A 1 366 ? 7.867 -51.395 25.954 1.00 18.92 ? 448 MET A O 1 ATOM 2884 C CB . MET A 1 366 ? 6.474 -53.814 27.575 1.00 14.23 ? 448 MET A CB 1 ATOM 2885 C CG . MET A 1 366 ? 6.571 -55.333 27.563 1.00 21.42 ? 448 MET A CG 1 ATOM 2886 S SD . MET A 1 366 ? 4.973 -56.130 27.773 1.00 27.41 ? 448 MET A SD 1 ATOM 2887 C CE . MET A 1 366 ? 4.532 -55.553 29.413 1.00 20.97 ? 448 MET A CE 1 ATOM 2888 N N . CYS A 1 367 ? 5.867 -50.847 26.864 1.00 18.85 ? 449 CYS A N 1 ATOM 2889 C CA . CYS A 1 367 ? 6.240 -49.485 27.248 1.00 18.86 ? 449 CYS A CA 1 ATOM 2890 C C . CYS A 1 367 ? 5.848 -49.224 28.709 1.00 23.56 ? 449 CYS A C 1 ATOM 2891 O O . CYS A 1 367 ? 5.003 -49.936 29.273 1.00 19.48 ? 449 CYS A O 1 ATOM 2892 C CB . CYS A 1 367 ? 5.582 -48.454 26.328 1.00 20.93 ? 449 CYS A CB 1 ATOM 2893 S SG . CYS A 1 367 ? 6.183 -48.514 24.606 1.00 25.32 ? 449 CYS A SG 1 ATOM 2894 N N . SER A 1 368 ? 6.460 -48.213 29.321 1.00 21.82 ? 450 SER A N 1 ATOM 2895 C CA . SER A 1 368 ? 6.209 -47.930 30.733 1.00 24.68 ? 450 SER A CA 1 ATOM 2896 C C . SER A 1 368 ? 4.872 -47.227 30.942 1.00 21.03 ? 450 SER A C 1 ATOM 2897 O O . SER A 1 368 ? 4.376 -46.529 30.052 1.00 18.40 ? 450 SER A O 1 ATOM 2898 C CB . SER A 1 368 ? 7.345 -47.099 31.344 1.00 19.65 ? 450 SER A CB 1 ATOM 2899 O OG . SER A 1 368 ? 7.354 -45.768 30.841 1.00 20.87 ? 450 SER A OG 1 ATOM 2900 N N . SER A 1 369 ? 4.287 -47.433 32.119 1.00 26.53 ? 451 SER A N 1 ATOM 2901 C CA . SER A 1 369 ? 3.067 -46.735 32.516 1.00 25.63 ? 451 SER A CA 1 ATOM 2902 C C . SER A 1 369 ? 3.311 -46.055 33.861 1.00 25.62 ? 451 SER A C 1 ATOM 2903 O O . SER A 1 369 ? 4.078 -46.566 34.682 1.00 23.84 ? 451 SER A O 1 ATOM 2904 C CB . SER A 1 369 ? 1.904 -47.727 32.633 1.00 23.52 ? 451 SER A CB 1 ATOM 2905 O OG . SER A 1 369 ? 0.756 -47.131 33.219 1.00 24.83 ? 451 SER A OG 1 ATOM 2906 N N . THR A 1 370 ? 2.682 -44.905 34.094 1.00 21.14 ? 452 THR A N 1 ATOM 2907 C CA . THR A 1 370 ? 2.774 -44.276 35.412 1.00 23.09 ? 452 THR A CA 1 ATOM 2908 C C . THR A 1 370 ? 1.771 -44.901 36.369 1.00 27.71 ? 452 THR A C 1 ATOM 2909 O O . THR A 1 370 ? 1.793 -44.612 37.562 1.00 23.91 ? 452 THR A O 1 ATOM 2910 C CB . THR A 1 370 ? 2.548 -42.756 35.379 1.00 22.92 ? 452 THR A CB 1 ATOM 2911 O OG1 . THR A 1 370 ? 1.298 -42.474 34.741 1.00 25.81 ? 452 THR A OG1 1 ATOM 2912 C CG2 . THR A 1 370 ? 3.686 -42.058 34.630 1.00 20.92 ? 452 THR A CG2 1 ATOM 2913 N N . GLU A 1 371 ? 0.887 -45.749 35.843 1.00 20.87 ? 453 GLU A N 1 ATOM 2914 C CA . GLU A 1 371 ? 0.015 -46.555 36.693 1.00 23.37 ? 453 GLU A CA 1 ATOM 2915 C C . GLU A 1 371 ? 0.778 -47.778 37.209 1.00 22.88 ? 453 GLU A C 1 ATOM 2916 O O . GLU A 1 371 ? 1.882 -48.064 36.746 1.00 24.45 ? 453 GLU A O 1 ATOM 2917 C CB . GLU A 1 371 ? -1.227 -47.003 35.917 1.00 23.45 ? 453 GLU A CB 1 ATOM 2918 C CG . GLU A 1 371 ? -2.020 -45.859 35.292 1.00 26.58 ? 453 GLU A CG 1 ATOM 2919 C CD . GLU A 1 371 ? -2.579 -44.890 36.328 1.00 28.66 ? 453 GLU A CD 1 ATOM 2920 O OE1 . GLU A 1 371 ? -3.091 -45.356 37.370 1.00 35.33 ? 453 GLU A OE1 1 ATOM 2921 O OE2 . GLU A 1 371 ? -2.512 -43.662 36.096 1.00 37.00 ? 453 GLU A OE2 1 ATOM 2922 N N . PHE A 1 372 ? 0.204 -48.476 38.186 1.00 21.91 ? 454 PHE A N 1 ATOM 2923 C CA . PHE A 1 372 ? 0.750 -49.752 38.653 1.00 19.77 ? 454 PHE A CA 1 ATOM 2924 C C . PHE A 1 372 ? -0.146 -50.865 38.131 1.00 22.35 ? 454 PHE A C 1 ATOM 2925 O O . PHE A 1 372 ? -1.039 -51.343 38.838 1.00 25.85 ? 454 PHE A O 1 ATOM 2926 C CB . PHE A 1 372 ? 0.818 -49.797 40.184 1.00 23.56 ? 454 PHE A CB 1 ATOM 2927 C CG . PHE A 1 372 ? 1.863 -48.885 40.774 1.00 27.83 ? 454 PHE A CG 1 ATOM 2928 C CD1 . PHE A 1 372 ? 1.622 -47.520 40.902 1.00 25.04 ? 454 PHE A CD1 1 ATOM 2929 C CD2 . PHE A 1 372 ? 3.083 -49.392 41.202 1.00 29.13 ? 454 PHE A CD2 1 ATOM 2930 C CE1 . PHE A 1 372 ? 2.579 -46.675 41.446 1.00 27.49 ? 454 PHE A CE1 1 ATOM 2931 C CE2 . PHE A 1 372 ? 4.051 -48.557 41.744 1.00 27.35 ? 454 PHE A CE2 1 ATOM 2932 C CZ . PHE A 1 372 ? 3.797 -47.192 41.866 1.00 20.25 ? 454 PHE A CZ 1 ATOM 2933 N N . LEU A 1 373 ? 0.092 -51.254 36.880 1.00 20.64 ? 455 LEU A N 1 ATOM 2934 C CA . LEU A 1 373 ? -0.789 -52.165 36.156 1.00 23.97 ? 455 LEU A CA 1 ATOM 2935 C C . LEU A 1 373 ? -0.530 -53.621 36.508 1.00 21.49 ? 455 LEU A C 1 ATOM 2936 O O . LEU A 1 373 ? 0.612 -54.012 36.762 1.00 21.04 ? 455 LEU A O 1 ATOM 2937 C CB . LEU A 1 373 ? -0.596 -51.992 34.650 1.00 19.73 ? 455 LEU A CB 1 ATOM 2938 C CG . LEU A 1 373 ? -0.808 -50.600 34.060 1.00 22.43 ? 455 LEU A CG 1 ATOM 2939 C CD1 . LEU A 1 373 ? -0.582 -50.627 32.551 1.00 21.13 ? 455 LEU A CD1 1 ATOM 2940 C CD2 . LEU A 1 373 ? -2.209 -50.092 34.386 1.00 21.82 ? 455 LEU A CD2 1 ATOM 2941 N N . GLY A 1 374 ? -1.592 -54.421 36.507 1.00 22.29 ? 456 GLY A N 1 ATOM 2942 C CA . GLY A 1 374 ? -1.460 -55.859 36.645 1.00 21.26 ? 456 GLY A CA 1 ATOM 2943 C C . GLY A 1 374 ? -0.530 -56.419 35.581 1.00 26.74 ? 456 GLY A C 1 ATOM 2944 O O . GLY A 1 374 ? -0.393 -55.843 34.496 1.00 22.43 ? 456 GLY A O 1 ATOM 2945 N N . GLN A 1 375 ? 0.119 -57.537 35.882 1.00 20.55 ? 457 GLN A N 1 ATOM 2946 C CA . GLN A 1 375 ? 1.063 -58.117 34.935 1.00 24.64 ? 457 GLN A CA 1 ATOM 2947 C C . GLN A 1 375 ? 0.545 -59.426 34.326 1.00 21.19 ? 457 GLN A C 1 ATOM 2948 O O . GLN A 1 375 ? -0.213 -60.177 34.961 1.00 23.44 ? 457 GLN A O 1 ATOM 2949 C CB . GLN A 1 375 ? 2.432 -58.337 35.603 1.00 16.93 ? 457 GLN A CB 1 ATOM 2950 C CG . GLN A 1 375 ? 2.441 -59.417 36.698 1.00 24.75 ? 457 GLN A CG 1 ATOM 2951 C CD . GLN A 1 375 ? 3.812 -59.587 37.336 1.00 30.01 ? 457 GLN A CD 1 ATOM 2952 O OE1 . GLN A 1 375 ? 4.609 -58.653 37.375 1.00 32.90 ? 457 GLN A OE1 1 ATOM 2953 N NE2 . GLN A 1 375 ? 4.086 -60.781 37.845 1.00 39.02 ? 457 GLN A NE2 1 ATOM 2954 N N . TRP A 1 376 ? 0.943 -59.683 33.084 1.00 18.85 ? 458 TRP A N 1 ATOM 2955 C CA . TRP A 1 376 ? 0.701 -60.976 32.454 1.00 18.77 ? 458 TRP A CA 1 ATOM 2956 C C . TRP A 1 376 ? 2.051 -61.535 32.028 1.00 23.40 ? 458 TRP A C 1 ATOM 2957 O O . TRP A 1 376 ? 3.088 -60.932 32.309 1.00 23.81 ? 458 TRP A O 1 ATOM 2958 C CB . TRP A 1 376 ? -0.200 -60.812 31.232 1.00 21.39 ? 458 TRP A CB 1 ATOM 2959 C CG . TRP A 1 376 ? -1.105 -61.994 30.975 1.00 19.78 ? 458 TRP A CG 1 ATOM 2960 C CD1 . TRP A 1 376 ? -1.230 -63.123 31.742 1.00 20.87 ? 458 TRP A CD1 1 ATOM 2961 C CD2 . TRP A 1 376 ? -2.009 -62.157 29.873 1.00 21.97 ? 458 TRP A CD2 1 ATOM 2962 N NE1 . TRP A 1 376 ? -2.158 -63.972 31.180 1.00 20.42 ? 458 TRP A NE1 1 ATOM 2963 C CE2 . TRP A 1 376 ? -2.654 -63.398 30.036 1.00 23.30 ? 458 TRP A CE2 1 ATOM 2964 C CE3 . TRP A 1 376 ? -2.339 -61.367 28.765 1.00 19.91 ? 458 TRP A CE3 1 ATOM 2965 C CZ2 . TRP A 1 376 ? -3.609 -63.868 29.129 1.00 23.44 ? 458 TRP A CZ2 1 ATOM 2966 C CZ3 . TRP A 1 376 ? -3.290 -61.833 27.872 1.00 21.86 ? 458 TRP A CZ3 1 ATOM 2967 C CH2 . TRP A 1 376 ? -3.911 -63.069 28.057 1.00 21.31 ? 458 TRP A CH2 1 ATOM 2968 N N . ASN A 1 377 ? 2.049 -62.685 31.366 1.00 21.41 ? 459 ASN A N 1 ATOM 2969 C CA . ASN A 1 377 ? 3.265 -63.185 30.736 1.00 21.73 ? 459 ASN A CA 1 ATOM 2970 C C . ASN A 1 377 ? 2.983 -63.370 29.257 1.00 22.21 ? 459 ASN A C 1 ATOM 2971 O O . ASN A 1 377 ? 1.844 -63.665 28.881 1.00 23.18 ? 459 ASN A O 1 ATOM 2972 C CB . ASN A 1 377 ? 3.706 -64.506 31.355 1.00 18.27 ? 459 ASN A CB 1 ATOM 2973 C CG . ASN A 1 377 ? 2.726 -65.620 31.085 1.00 21.52 ? 459 ASN A CG 1 ATOM 2974 O OD1 . ASN A 1 377 ? 2.837 -66.332 30.082 1.00 20.42 ? 459 ASN A OD1 1 ATOM 2975 N ND2 . ASN A 1 377 ? 1.747 -65.775 31.974 1.00 22.37 ? 459 ASN A ND2 1 ATOM 2976 N N . TRP A 1 378 ? 4.012 -63.217 28.426 1.00 17.52 ? 460 TRP A N 1 ATOM 2977 C CA . TRP A 1 378 ? 3.818 -63.171 26.978 1.00 20.36 ? 460 TRP A CA 1 ATOM 2978 C C . TRP A 1 378 ? 4.693 -64.165 26.213 1.00 17.21 ? 460 TRP A C 1 ATOM 2979 O O . TRP A 1 378 ? 5.825 -63.846 25.826 1.00 20.56 ? 460 TRP A O 1 ATOM 2980 C CB . TRP A 1 378 ? 4.072 -61.749 26.484 1.00 13.21 ? 460 TRP A CB 1 ATOM 2981 C CG . TRP A 1 378 ? 3.141 -60.739 27.103 1.00 18.10 ? 460 TRP A CG 1 ATOM 2982 C CD1 . TRP A 1 378 ? 3.345 -60.008 28.245 1.00 20.23 ? 460 TRP A CD1 1 ATOM 2983 C CD2 . TRP A 1 378 ? 1.850 -60.356 26.607 1.00 18.61 ? 460 TRP A CD2 1 ATOM 2984 N NE1 . TRP A 1 378 ? 2.254 -59.192 28.486 1.00 15.58 ? 460 TRP A NE1 1 ATOM 2985 C CE2 . TRP A 1 378 ? 1.324 -59.393 27.496 1.00 16.05 ? 460 TRP A CE2 1 ATOM 2986 C CE3 . TRP A 1 378 ? 1.089 -60.736 25.494 1.00 16.76 ? 460 TRP A CE3 1 ATOM 2987 C CZ2 . TRP A 1 378 ? 0.078 -58.798 27.296 1.00 14.59 ? 460 TRP A CZ2 1 ATOM 2988 C CZ3 . TRP A 1 378 ? -0.145 -60.152 25.300 1.00 18.83 ? 460 TRP A CZ3 1 ATOM 2989 C CH2 . TRP A 1 378 ? -0.642 -59.189 26.198 1.00 15.92 ? 460 TRP A CH2 1 ATOM 2990 N N . PRO A 1 379 ? 4.171 -65.379 25.993 1.00 23.76 ? 461 PRO A N 1 ATOM 2991 C CA . PRO A 1 379 ? 4.962 -66.400 25.292 1.00 22.26 ? 461 PRO A CA 1 ATOM 2992 C C . PRO A 1 379 ? 4.917 -66.182 23.785 1.00 20.50 ? 461 PRO A C 1 ATOM 2993 O O . PRO A 1 379 ? 4.045 -65.455 23.288 1.00 19.17 ? 461 PRO A O 1 ATOM 2994 C CB . PRO A 1 379 ? 4.237 -67.711 25.630 1.00 19.34 ? 461 PRO A CB 1 ATOM 2995 C CG . PRO A 1 379 ? 3.151 -67.352 26.635 1.00 28.40 ? 461 PRO A CG 1 ATOM 2996 C CD . PRO A 1 379 ? 2.869 -65.896 26.443 1.00 19.99 ? 461 PRO A CD 1 ATOM 2997 N N . ASP A 1 380 ? 5.850 -66.797 23.067 1.00 19.84 ? 462 ASP A N 1 ATOM 2998 C CA . ASP A 1 380 ? 5.790 -66.799 21.618 1.00 19.41 ? 462 ASP A CA 1 ATOM 2999 C C . ASP A 1 380 ? 4.465 -67.402 21.175 1.00 20.93 ? 462 ASP A C 1 ATOM 3000 O O . ASP A 1 380 ? 3.762 -66.840 20.323 1.00 17.44 ? 462 ASP A O 1 ATOM 3001 C CB . ASP A 1 380 ? 6.935 -67.612 21.025 1.00 19.94 ? 462 ASP A CB 1 ATOM 3002 C CG . ASP A 1 380 ? 6.693 -67.959 19.576 1.00 21.03 ? 462 ASP A CG 1 ATOM 3003 O OD1 . ASP A 1 380 ? 6.737 -67.030 18.738 1.00 20.55 ? 462 ASP A OD1 1 ATOM 3004 O OD2 . ASP A 1 380 ? 6.446 -69.150 19.276 1.00 20.02 ? 462 ASP A OD2 1 ATOM 3005 N N . GLY A 1 381 ? 4.135 -68.555 21.750 1.00 17.30 ? 463 GLY A N 1 ATOM 3006 C CA . GLY A 1 381 ? 2.824 -69.150 21.547 1.00 19.42 ? 463 GLY A CA 1 ATOM 3007 C C . GLY A 1 381 ? 2.704 -70.220 20.478 1.00 20.62 ? 463 GLY A C 1 ATOM 3008 O O . GLY A 1 381 ? 1.620 -70.790 20.289 1.00 18.48 ? 463 GLY A O 1 ATOM 3009 N N . ALA A 1 382 ? 3.793 -70.497 19.767 1.00 15.51 ? 464 ALA A N 1 ATOM 3010 C CA . ALA A 1 382 ? 3.759 -71.537 18.735 1.00 17.93 ? 464 ALA A CA 1 ATOM 3011 C C . ALA A 1 382 ? 4.012 -72.916 19.341 1.00 18.58 ? 464 ALA A C 1 ATOM 3012 O O . ALA A 1 382 ? 4.756 -73.044 20.314 1.00 19.25 ? 464 ALA A O 1 ATOM 3013 C CB . ALA A 1 382 ? 4.775 -71.257 17.657 1.00 14.18 ? 464 ALA A CB 1 ATOM 3014 N N . LYS A 1 383 ? 3.406 -73.945 18.759 1.00 22.56 ? 465 LYS A N 1 ATOM 3015 C CA . LYS A 1 383 ? 3.675 -75.317 19.174 1.00 21.77 ? 465 LYS A CA 1 ATOM 3016 C C . LYS A 1 383 ? 4.611 -75.973 18.161 1.00 24.94 ? 465 LYS A C 1 ATOM 3017 O O . LYS A 1 383 ? 4.226 -76.191 17.006 1.00 21.03 ? 465 LYS A O 1 ATOM 3018 C CB . LYS A 1 383 ? 2.365 -76.108 19.288 1.00 24.72 ? 465 LYS A CB 1 ATOM 3019 C CG . LYS A 1 383 ? 1.312 -75.433 20.166 1.00 30.13 ? 465 LYS A CG 1 ATOM 3020 C CD . LYS A 1 383 ? -0.056 -76.095 20.027 1.00 40.85 ? 465 LYS A CD 1 ATOM 3021 C CE . LYS A 1 383 ? -0.184 -77.371 20.848 1.00 46.04 ? 465 LYS A CE 1 ATOM 3022 N NZ . LYS A 1 383 ? -0.673 -77.062 22.227 1.00 57.99 ? 465 LYS A NZ 1 ATOM 3023 N N . ILE A 1 384 ? 5.835 -76.274 18.596 1.00 24.51 ? 466 ILE A N 1 ATOM 3024 C CA . ILE A 1 384 ? 6.855 -76.883 17.741 1.00 25.34 ? 466 ILE A CA 1 ATOM 3025 C C . ILE A 1 384 ? 6.342 -78.116 16.997 1.00 24.27 ? 466 ILE A C 1 ATOM 3026 O O . ILE A 1 384 ? 6.691 -78.335 15.835 1.00 23.31 ? 466 ILE A O 1 ATOM 3027 C CB . ILE A 1 384 ? 8.106 -77.289 18.555 1.00 31.03 ? 466 ILE A CB 1 ATOM 3028 C CG1 . ILE A 1 384 ? 8.712 -76.073 19.246 1.00 32.69 ? 466 ILE A CG1 1 ATOM 3029 C CG2 . ILE A 1 384 ? 9.159 -77.928 17.650 1.00 38.77 ? 466 ILE A CG2 1 ATOM 3030 C CD1 . ILE A 1 384 ? 9.340 -75.081 18.266 1.00 41.88 ? 466 ILE A CD1 1 ATOM 3031 N N . GLU A 1 385 ? 5.504 -78.909 17.666 1.00 20.77 ? 467 GLU A N 1 ATOM 3032 C CA . GLU A 1 385 ? 5.016 -80.168 17.100 1.00 29.96 ? 467 GLU A CA 1 ATOM 3033 C C . GLU A 1 385 ? 4.284 -79.963 15.773 1.00 24.32 ? 467 GLU A C 1 ATOM 3034 O O . GLU A 1 385 ? 4.265 -80.858 14.917 1.00 24.17 ? 467 GLU A O 1 ATOM 3035 C CB . GLU A 1 385 ? 4.119 -80.914 18.102 1.00 28.58 ? 467 GLU A CB 1 ATOM 3036 C CG . GLU A 1 385 ? 2.955 -80.094 18.651 1.00 40.40 ? 467 GLU A CG 1 ATOM 3037 C CD . GLU A 1 385 ? 3.141 -79.708 20.117 1.00 55.27 ? 467 GLU A CD 1 ATOM 3038 O OE1 . GLU A 1 385 ? 2.224 -79.994 20.920 1.00 54.63 ? 467 GLU A OE1 1 ATOM 3039 O OE2 . GLU A 1 385 ? 4.194 -79.115 20.465 1.00 42.98 ? 467 GLU A OE2 1 ATOM 3040 N N . TYR A 1 386 ? 3.703 -78.780 15.594 1.00 21.40 ? 468 TYR A N 1 ATOM 3041 C CA . TYR A 1 386 ? 2.964 -78.469 14.368 1.00 25.73 ? 468 TYR A CA 1 ATOM 3042 C C . TYR A 1 386 ? 3.864 -78.387 13.136 1.00 27.84 ? 468 TYR A C 1 ATOM 3043 O O . TYR A 1 386 ? 3.401 -78.585 12.001 1.00 20.81 ? 468 TYR A O 1 ATOM 3044 C CB . TYR A 1 386 ? 2.203 -77.155 14.524 1.00 17.64 ? 468 TYR A CB 1 ATOM 3045 C CG . TYR A 1 386 ? 0.988 -77.227 15.428 1.00 26.71 ? 468 TYR A CG 1 ATOM 3046 C CD1 . TYR A 1 386 ? 0.422 -78.448 15.786 1.00 28.12 ? 468 TYR A CD1 1 ATOM 3047 C CD2 . TYR A 1 386 ? 0.406 -76.066 15.923 1.00 21.84 ? 468 TYR A CD2 1 ATOM 3048 C CE1 . TYR A 1 386 ? -0.690 -78.504 16.616 1.00 25.37 ? 468 TYR A CE1 1 ATOM 3049 C CE2 . TYR A 1 386 ? -0.705 -76.111 16.740 1.00 22.68 ? 468 TYR A CE2 1 ATOM 3050 C CZ . TYR A 1 386 ? -1.246 -77.327 17.088 1.00 26.12 ? 468 TYR A CZ 1 ATOM 3051 O OH . TYR A 1 386 ? -2.350 -77.349 17.913 1.00 25.64 ? 468 TYR A OH 1 ATOM 3052 N N . PHE A 1 387 ? 5.142 -78.082 13.360 1.00 19.10 ? 469 PHE A N 1 ATOM 3053 C CA . PHE A 1 387 ? 6.098 -77.890 12.267 1.00 23.53 ? 469 PHE A CA 1 ATOM 3054 C C . PHE A 1 387 ? 6.777 -79.201 11.884 1.00 28.04 ? 469 PHE A C 1 ATOM 3055 O O . PHE A 1 387 ? 7.640 -79.225 11.000 1.00 29.96 ? 469 PHE A O 1 ATOM 3056 C CB . PHE A 1 387 ? 7.172 -76.868 12.665 1.00 19.60 ? 469 PHE A CB 1 ATOM 3057 C CG . PHE A 1 387 ? 6.670 -75.450 12.745 1.00 23.29 ? 469 PHE A CG 1 ATOM 3058 C CD1 . PHE A 1 387 ? 6.092 -74.969 13.913 1.00 20.07 ? 469 PHE A CD1 1 ATOM 3059 C CD2 . PHE A 1 387 ? 6.789 -74.592 11.654 1.00 20.63 ? 469 PHE A CD2 1 ATOM 3060 C CE1 . PHE A 1 387 ? 5.634 -73.664 13.991 1.00 20.31 ? 469 PHE A CE1 1 ATOM 3061 C CE2 . PHE A 1 387 ? 6.336 -73.279 11.724 1.00 23.96 ? 469 PHE A CE2 1 ATOM 3062 C CZ . PHE A 1 387 ? 5.758 -72.813 12.889 1.00 19.46 ? 469 PHE A CZ 1 ATOM 3063 N N . LEU A 1 388 ? 6.391 -80.284 12.555 1.00 28.22 ? 470 LEU A N 1 ATOM 3064 C CA . LEU A 1 388 ? 7.050 -81.578 12.370 1.00 32.80 ? 470 LEU A CA 1 ATOM 3065 C C . LEU A 1 388 ? 6.451 -82.383 11.223 1.00 37.56 ? 470 LEU A C 1 ATOM 3066 O O . LEU A 1 388 ? 5.362 -82.075 10.736 1.00 39.26 ? 470 LEU A O 1 ATOM 3067 C CB . LEU A 1 388 ? 7.014 -82.394 13.663 1.00 35.64 ? 470 LEU A CB 1 ATOM 3068 C CG . LEU A 1 388 ? 7.762 -81.775 14.846 1.00 38.09 ? 470 LEU A CG 1 ATOM 3069 C CD1 . LEU A 1 388 ? 7.908 -82.777 15.995 1.00 34.46 ? 470 LEU A CD1 1 ATOM 3070 C CD2 . LEU A 1 388 ? 9.118 -81.262 14.395 1.00 33.21 ? 470 LEU A CD2 1 ATOM 3071 O OXT . LEU A 1 388 ? 7.050 -83.355 10.753 1.00 46.31 ? 470 LEU A OXT 1 HETATM 3072 C C1 . NAG B 2 . ? 16.844 -28.749 17.695 1.00 52.04 ? 501 NAG A C1 1 HETATM 3073 C C2 . NAG B 2 . ? 15.620 -28.158 16.978 1.00 55.44 ? 501 NAG A C2 1 HETATM 3074 C C3 . NAG B 2 . ? 16.030 -27.301 15.782 1.00 61.31 ? 501 NAG A C3 1 HETATM 3075 C C4 . NAG B 2 . ? 17.054 -26.260 16.225 1.00 63.74 ? 501 NAG A C4 1 HETATM 3076 C C5 . NAG B 2 . ? 18.245 -26.995 16.841 1.00 64.22 ? 501 NAG A C5 1 HETATM 3077 C C6 . NAG B 2 . ? 19.410 -26.056 17.186 1.00 54.98 ? 501 NAG A C6 1 HETATM 3078 C C7 . NAG B 2 . ? 13.386 -29.118 16.906 1.00 60.24 ? 501 NAG A C7 1 HETATM 3079 C C8 . NAG B 2 . ? 12.490 -30.258 16.505 1.00 52.29 ? 501 NAG A C8 1 HETATM 3080 N N2 . NAG B 2 . ? 14.678 -29.193 16.574 1.00 53.78 ? 501 NAG A N2 1 HETATM 3081 O O3 . NAG B 2 . ? 14.893 -26.686 15.213 1.00 60.71 ? 501 NAG A O3 1 HETATM 3082 O O4 . NAG B 2 . ? 17.479 -25.486 15.124 1.00 65.06 ? 501 NAG A O4 1 HETATM 3083 O O5 . NAG B 2 . ? 17.820 -27.747 17.972 1.00 50.75 ? 501 NAG A O5 1 HETATM 3084 O O6 . NAG B 2 . ? 19.191 -25.378 18.405 1.00 63.73 ? 501 NAG A O6 1 HETATM 3085 O O7 . NAG B 2 . ? 12.916 -28.160 17.520 1.00 61.16 ? 501 NAG A O7 1 HETATM 3086 C C1 . NAG C 2 . ? 17.994 -80.317 6.776 1.00 44.50 ? 502 NAG A C1 1 HETATM 3087 C C2 . NAG C 2 . ? 17.063 -81.506 6.539 1.00 49.34 ? 502 NAG A C2 1 HETATM 3088 C C3 . NAG C 2 . ? 17.727 -82.810 6.954 1.00 54.98 ? 502 NAG A C3 1 HETATM 3089 C C4 . NAG C 2 . ? 19.026 -82.970 6.180 1.00 52.70 ? 502 NAG A C4 1 HETATM 3090 C C5 . NAG C 2 . ? 19.919 -81.747 6.382 1.00 54.96 ? 502 NAG A C5 1 HETATM 3091 C C6 . NAG C 2 . ? 21.136 -81.840 5.465 1.00 59.49 ? 502 NAG A C6 1 HETATM 3092 C C7 . NAG C 2 . ? 14.659 -81.380 6.516 1.00 49.86 ? 502 NAG A C7 1 HETATM 3093 C C8 . NAG C 2 . ? 13.402 -80.915 7.195 1.00 42.52 ? 502 NAG A C8 1 HETATM 3094 N N2 . NAG C 2 . ? 15.790 -81.330 7.216 1.00 47.96 ? 502 NAG A N2 1 HETATM 3095 O O3 . NAG C 2 . ? 16.856 -83.883 6.681 1.00 56.35 ? 502 NAG A O3 1 HETATM 3096 O O4 . NAG C 2 . ? 19.708 -84.126 6.619 1.00 69.60 ? 502 NAG A O4 1 HETATM 3097 O O5 . NAG C 2 . ? 19.236 -80.528 6.120 1.00 49.13 ? 502 NAG A O5 1 HETATM 3098 O O6 . NAG C 2 . ? 22.146 -80.957 5.901 1.00 60.90 ? 502 NAG A O6 1 HETATM 3099 O O7 . NAG C 2 . ? 14.627 -81.793 5.357 1.00 44.12 ? 502 NAG A O7 1 HETATM 3100 C C1 . NAG D 2 . ? 39.817 -58.210 1.259 1.00 31.87 ? 503 NAG A C1 1 HETATM 3101 C C2 . NAG D 2 . ? 40.744 -59.299 0.707 1.00 33.04 ? 503 NAG A C2 1 HETATM 3102 C C3 . NAG D 2 . ? 41.705 -58.753 -0.351 1.00 30.27 ? 503 NAG A C3 1 HETATM 3103 C C4 . NAG D 2 . ? 40.985 -57.884 -1.374 1.00 29.76 ? 503 NAG A C4 1 HETATM 3104 C C5 . NAG D 2 . ? 40.099 -56.856 -0.666 1.00 25.27 ? 503 NAG A C5 1 HETATM 3105 C C6 . NAG D 2 . ? 39.328 -55.969 -1.639 1.00 24.76 ? 503 NAG A C6 1 HETATM 3106 C C7 . NAG D 2 . ? 41.437 -61.207 2.086 1.00 42.33 ? 503 NAG A C7 1 HETATM 3107 C C8 . NAG D 2 . ? 42.208 -61.656 3.300 1.00 32.58 ? 503 NAG A C8 1 HETATM 3108 N N2 . NAG D 2 . ? 41.490 -59.904 1.799 1.00 28.45 ? 503 NAG A N2 1 HETATM 3109 O O3 . NAG D 2 . ? 42.339 -59.817 -1.021 1.00 30.26 ? 503 NAG A O3 1 HETATM 3110 O O4 . NAG D 2 . ? 41.962 -57.248 -2.177 1.00 33.37 ? 503 NAG A O4 1 HETATM 3111 O O5 . NAG D 2 . ? 39.188 -57.516 0.193 1.00 28.06 ? 503 NAG A O5 1 HETATM 3112 O O6 . NAG D 2 . ? 38.653 -56.771 -2.583 1.00 24.19 ? 503 NAG A O6 1 HETATM 3113 O O7 . NAG D 2 . ? 40.805 -62.029 1.413 1.00 36.25 ? 503 NAG A O7 1 HETATM 3114 C C1 . NAG E 2 . ? 41.795 -57.566 -3.575 1.00 27.86 ? 504 NAG A C1 1 HETATM 3115 C C2 . NAG E 2 . ? 42.373 -56.461 -4.462 1.00 23.29 ? 504 NAG A C2 1 HETATM 3116 C C3 . NAG E 2 . ? 41.999 -56.753 -5.909 1.00 25.11 ? 504 NAG A C3 1 HETATM 3117 C C4 . NAG E 2 . ? 42.468 -58.151 -6.299 1.00 29.71 ? 504 NAG A C4 1 HETATM 3118 C C5 . NAG E 2 . ? 41.976 -59.176 -5.272 1.00 29.65 ? 504 NAG A C5 1 HETATM 3119 C C6 . NAG E 2 . ? 42.507 -60.576 -5.559 1.00 24.39 ? 504 NAG A C6 1 HETATM 3120 C C7 . NAG E 2 . ? 42.581 -54.371 -3.242 1.00 29.49 ? 504 NAG A C7 1 HETATM 3121 C C8 . NAG E 2 . ? 41.965 -53.053 -2.864 1.00 22.25 ? 504 NAG A C8 1 HETATM 3122 N N2 . NAG E 2 . ? 41.885 -55.153 -4.064 1.00 21.76 ? 504 NAG A N2 1 HETATM 3123 O O3 . NAG E 2 . ? 42.518 -55.768 -6.774 1.00 24.80 ? 504 NAG A O3 1 HETATM 3124 O O4 . NAG E 2 . ? 41.937 -58.459 -7.569 1.00 25.42 ? 504 NAG A O4 1 HETATM 3125 O O5 . NAG E 2 . ? 42.354 -58.801 -3.956 1.00 24.59 ? 504 NAG A O5 1 HETATM 3126 O O6 . NAG E 2 . ? 43.906 -60.500 -5.727 1.00 42.59 ? 504 NAG A O6 1 HETATM 3127 O O7 . NAG E 2 . ? 43.680 -54.697 -2.797 1.00 28.28 ? 504 NAG A O7 1 HETATM 3128 C C1 . BMA F 3 . ? 42.944 -58.712 -8.562 1.00 30.76 ? 505 BMA A C1 1 HETATM 3129 C C2 . BMA F 3 . ? 42.256 -59.420 -9.727 1.00 27.53 ? 505 BMA A C2 1 HETATM 3130 C C3 . BMA F 3 . ? 43.188 -59.642 -10.910 1.00 30.04 ? 505 BMA A C3 1 HETATM 3131 C C4 . BMA F 3 . ? 43.980 -58.379 -11.237 1.00 29.12 ? 505 BMA A C4 1 HETATM 3132 C C5 . BMA F 3 . ? 44.592 -57.772 -9.979 1.00 32.94 ? 505 BMA A C5 1 HETATM 3133 C C6 . BMA F 3 . ? 45.271 -56.456 -10.315 1.00 27.30 ? 505 BMA A C6 1 HETATM 3134 O O2 . BMA F 3 . ? 41.168 -58.596 -10.176 1.00 23.16 ? 505 BMA A O2 1 HETATM 3135 O O3 . BMA F 3 . ? 42.368 -60.023 -12.031 1.00 29.65 ? 505 BMA A O3 1 HETATM 3136 O O4 . BMA F 3 . ? 45.031 -58.678 -12.164 1.00 34.18 ? 505 BMA A O4 1 HETATM 3137 O O5 . BMA F 3 . ? 43.556 -57.513 -9.029 1.00 27.90 ? 505 BMA A O5 1 HETATM 3138 O O6 . BMA F 3 . ? 46.112 -55.995 -9.243 1.00 36.36 ? 505 BMA A O6 1 HETATM 3139 C C1 . MAN G 4 . ? 42.968 -61.133 -12.723 1.00 31.92 ? 506 MAN A C1 1 HETATM 3140 C C2 . MAN G 4 . ? 42.228 -61.447 -14.019 1.00 29.38 ? 506 MAN A C2 1 HETATM 3141 C C3 . MAN G 4 . ? 40.808 -61.904 -13.670 1.00 29.73 ? 506 MAN A C3 1 HETATM 3142 C C4 . MAN G 4 . ? 40.913 -63.161 -12.814 1.00 29.10 ? 506 MAN A C4 1 HETATM 3143 C C5 . MAN G 4 . ? 41.753 -62.846 -11.580 1.00 29.79 ? 506 MAN A C5 1 HETATM 3144 C C6 . MAN G 4 . ? 41.969 -64.087 -10.724 1.00 34.24 ? 506 MAN A C6 1 HETATM 3145 O O2 . MAN G 4 . ? 43.017 -62.472 -14.588 1.00 37.64 ? 506 MAN A O2 1 HETATM 3146 O O3 . MAN G 4 . ? 39.967 -62.111 -14.801 1.00 16.98 ? 506 MAN A O3 1 HETATM 3147 O O4 . MAN G 4 . ? 39.624 -63.583 -12.421 1.00 34.38 ? 506 MAN A O4 1 HETATM 3148 O O5 . MAN G 4 . ? 43.020 -62.321 -11.947 1.00 25.29 ? 506 MAN A O5 1 HETATM 3149 O O6 . MAN G 4 . ? 42.183 -63.669 -9.393 1.00 44.29 ? 506 MAN A O6 1 HETATM 3150 C C1 . MAN H 4 . ? 42.705 -62.781 -15.961 1.00 35.97 ? 507 MAN A C1 1 HETATM 3151 C C2 . MAN H 4 . ? 43.649 -63.886 -16.429 1.00 32.27 ? 507 MAN A C2 1 HETATM 3152 C C3 . MAN H 4 . ? 45.076 -63.352 -16.530 1.00 36.06 ? 507 MAN A C3 1 HETATM 3153 C C4 . MAN H 4 . ? 45.066 -62.163 -17.482 1.00 35.97 ? 507 MAN A C4 1 HETATM 3154 C C5 . MAN H 4 . ? 44.073 -61.118 -16.984 1.00 40.76 ? 507 MAN A C5 1 HETATM 3155 C C6 . MAN H 4 . ? 44.035 -59.906 -17.914 1.00 32.02 ? 507 MAN A C6 1 HETATM 3156 O O2 . MAN H 4 . ? 43.187 -64.354 -17.679 1.00 35.38 ? 507 MAN A O2 1 HETATM 3157 O O3 . MAN H 4 . ? 45.961 -64.354 -16.996 1.00 32.10 ? 507 MAN A O3 1 HETATM 3158 O O4 . MAN H 4 . ? 46.350 -61.581 -17.561 1.00 37.00 ? 507 MAN A O4 1 HETATM 3159 O O5 . MAN H 4 . ? 42.775 -61.682 -16.860 1.00 34.60 ? 507 MAN A O5 1 HETATM 3160 O O6 . MAN H 4 . ? 43.690 -60.311 -19.226 1.00 33.38 ? 507 MAN A O6 1 HETATM 3161 C C1 . MAN I 4 . ? 42.591 -65.658 -17.540 1.00 31.78 ? 508 MAN A C1 1 HETATM 3162 C C2 . MAN I 4 . ? 42.361 -66.150 -18.963 1.00 34.42 ? 508 MAN A C2 1 HETATM 3163 C C3 . MAN I 4 . ? 41.341 -65.217 -19.610 1.00 32.29 ? 508 MAN A C3 1 HETATM 3164 C C4 . MAN I 4 . ? 40.042 -65.240 -18.815 1.00 33.62 ? 508 MAN A C4 1 HETATM 3165 C C5 . MAN I 4 . ? 40.324 -64.861 -17.364 1.00 29.48 ? 508 MAN A C5 1 HETATM 3166 C C6 . MAN I 4 . ? 39.055 -64.963 -16.515 1.00 34.15 ? 508 MAN A C6 1 HETATM 3167 O O2 . MAN I 4 . ? 41.932 -67.499 -18.976 1.00 30.97 ? 508 MAN A O2 1 HETATM 3168 O O3 . MAN I 4 . ? 41.086 -65.616 -20.931 1.00 30.38 ? 508 MAN A O3 1 HETATM 3169 O O4 . MAN I 4 . ? 39.112 -64.328 -19.364 1.00 26.49 ? 508 MAN A O4 1 HETATM 3170 O O5 . MAN I 4 . ? 41.364 -65.667 -16.815 1.00 36.70 ? 508 MAN A O5 1 HETATM 3171 O O6 . MAN I 4 . ? 38.553 -66.286 -16.516 1.00 32.10 ? 508 MAN A O6 1 HETATM 3172 C C1 . MAN J 4 . ? 47.396 -56.644 -9.315 1.00 37.96 ? 509 MAN A C1 1 HETATM 3173 C C2 . MAN J 4 . ? 48.208 -56.304 -8.066 1.00 34.76 ? 509 MAN A C2 1 HETATM 3174 C C3 . MAN J 4 . ? 48.501 -54.807 -8.004 1.00 36.55 ? 509 MAN A C3 1 HETATM 3175 C C4 . MAN J 4 . ? 49.140 -54.357 -9.314 1.00 35.60 ? 509 MAN A C4 1 HETATM 3176 C C5 . MAN J 4 . ? 48.268 -54.808 -10.483 1.00 35.94 ? 509 MAN A C5 1 HETATM 3177 C C6 . MAN J 4 . ? 48.817 -54.386 -11.839 1.00 41.12 ? 509 MAN A C6 1 HETATM 3178 O O2 . MAN J 4 . ? 49.424 -57.018 -8.097 1.00 32.73 ? 509 MAN A O2 1 HETATM 3179 O O3 . MAN J 4 . ? 49.330 -54.510 -6.893 1.00 40.23 ? 509 MAN A O3 1 HETATM 3180 O O4 . MAN J 4 . ? 49.245 -52.949 -9.317 1.00 37.59 ? 509 MAN A O4 1 HETATM 3181 O O5 . MAN J 4 . ? 48.126 -56.218 -10.454 1.00 35.31 ? 509 MAN A O5 1 HETATM 3182 O O6 . MAN J 4 . ? 50.150 -54.842 -11.918 1.00 49.98 ? 509 MAN A O6 1 HETATM 3183 C C1 . MAN K 4 . ? 50.754 -54.523 -13.187 1.00 52.28 ? 510 MAN A C1 1 HETATM 3184 C C2 . MAN K 4 . ? 52.074 -55.282 -13.266 1.00 61.56 ? 510 MAN A C2 1 HETATM 3185 C C3 . MAN K 4 . ? 52.920 -54.875 -12.063 1.00 65.79 ? 510 MAN A C3 1 HETATM 3186 C C4 . MAN K 4 . ? 53.128 -53.361 -12.077 1.00 57.27 ? 510 MAN A C4 1 HETATM 3187 C C5 . MAN K 4 . ? 51.777 -52.650 -12.187 1.00 59.58 ? 510 MAN A C5 1 HETATM 3188 C C6 . MAN K 4 . ? 51.917 -51.135 -12.303 1.00 63.62 ? 510 MAN A C6 1 HETATM 3189 O O2 . MAN K 4 . ? 52.767 -54.971 -14.457 1.00 56.20 ? 510 MAN A O2 1 HETATM 3190 O O3 . MAN K 4 . ? 54.154 -55.562 -12.075 1.00 65.58 ? 510 MAN A O3 1 HETATM 3191 O O4 . MAN K 4 . ? 53.773 -52.961 -10.890 1.00 60.18 ? 510 MAN A O4 1 HETATM 3192 O O5 . MAN K 4 . ? 51.048 -53.143 -13.301 1.00 54.36 ? 510 MAN A O5 1 HETATM 3193 O O6 . MAN K 4 . ? 50.656 -50.554 -12.573 1.00 68.80 ? 510 MAN A O6 1 HETATM 3194 C C1 . MAN L 4 . ? 48.657 -53.623 -5.967 1.00 46.04 ? 511 MAN A C1 1 HETATM 3195 C C2 . MAN L 4 . ? 49.646 -53.083 -4.925 1.00 54.27 ? 511 MAN A C2 1 HETATM 3196 C C3 . MAN L 4 . ? 50.124 -54.215 -4.016 1.00 55.76 ? 511 MAN A C3 1 HETATM 3197 C C4 . MAN L 4 . ? 48.935 -54.977 -3.433 1.00 56.61 ? 511 MAN A C4 1 HETATM 3198 C C5 . MAN L 4 . ? 47.982 -55.396 -4.552 1.00 43.37 ? 511 MAN A C5 1 HETATM 3199 C C6 . MAN L 4 . ? 46.739 -56.109 -4.023 1.00 42.97 ? 511 MAN A C6 1 HETATM 3200 O O2 . MAN L 4 . ? 49.063 -52.040 -4.160 1.00 46.11 ? 511 MAN A O2 1 HETATM 3201 O O3 . MAN L 4 . ? 50.929 -53.698 -2.979 1.00 49.40 ? 511 MAN A O3 1 HETATM 3202 O O4 . MAN L 4 . ? 49.409 -56.114 -2.744 1.00 46.64 ? 511 MAN A O4 1 HETATM 3203 O O5 . MAN L 4 . ? 47.587 -54.250 -5.286 1.00 46.11 ? 511 MAN A O5 1 HETATM 3204 O O6 . MAN L 4 . ? 46.003 -56.678 -5.088 1.00 40.52 ? 511 MAN A O6 1 HETATM 3205 CA CA . CA M 5 . ? 28.860 -62.288 29.665 1.00 42.06 ? 512 CA A CA 1 HETATM 3206 C C2 . BCZ N 6 . ? 24.679 -63.097 16.320 1.00 20.07 ? 513 BCZ A C2 1 HETATM 3207 N N25 . BCZ N 6 . ? 24.352 -61.812 15.774 1.00 14.26 ? 513 BCZ A N25 1 HETATM 3208 C C26 . BCZ N 6 . ? 23.956 -61.648 14.354 1.00 18.16 ? 513 BCZ A C26 1 HETATM 3209 N N30 . BCZ N 6 . ? 23.858 -62.712 13.562 1.00 19.20 ? 513 BCZ A N30 1 HETATM 3210 N N27 . BCZ N 6 . ? 23.680 -60.458 13.849 1.00 19.04 ? 513 BCZ A N27 1 HETATM 3211 C C3 . BCZ N 6 . ? 25.748 -62.969 17.320 1.00 19.72 ? 513 BCZ A C3 1 HETATM 3212 C C10 . BCZ N 6 . ? 27.119 -62.685 16.613 1.00 20.01 ? 513 BCZ A C10 1 HETATM 3213 C C24 . BCZ N 6 . ? 28.447 -62.674 17.556 1.00 23.97 ? 513 BCZ A C24 1 HETATM 3214 C C37 . BCZ N 6 . ? 28.221 -61.763 18.776 1.00 25.07 ? 513 BCZ A C37 1 HETATM 3215 C C38 . BCZ N 6 . ? 28.038 -60.296 18.490 1.00 24.03 ? 513 BCZ A C38 1 HETATM 3216 C C36 . BCZ N 6 . ? 29.716 -62.360 16.799 1.00 20.38 ? 513 BCZ A C36 1 HETATM 3217 C C39 . BCZ N 6 . ? 31.049 -62.482 17.508 1.00 22.83 ? 513 BCZ A C39 1 HETATM 3218 N N11 . BCZ N 6 . ? 27.135 -61.458 15.642 1.00 19.76 ? 513 BCZ A N11 1 HETATM 3219 C C13 . BCZ N 6 . ? 27.312 -61.628 14.226 1.00 21.55 ? 513 BCZ A C13 1 HETATM 3220 C C15 . BCZ N 6 . ? 27.312 -60.411 13.364 1.00 18.86 ? 513 BCZ A C15 1 HETATM 3221 O O14 . BCZ N 6 . ? 27.453 -62.740 13.743 1.00 21.34 ? 513 BCZ A O14 1 HETATM 3222 C C4 . BCZ N 6 . ? 25.684 -64.235 18.076 1.00 23.84 ? 513 BCZ A C4 1 HETATM 3223 O O9 . BCZ N 6 . ? 26.521 -65.198 17.507 1.00 20.84 ? 513 BCZ A O9 1 HETATM 3224 C C5 . BCZ N 6 . ? 24.296 -64.697 18.003 1.00 21.50 ? 513 BCZ A C5 1 HETATM 3225 C C6 . BCZ N 6 . ? 23.686 -64.707 19.391 1.00 19.86 ? 513 BCZ A C6 1 HETATM 3226 O O8 . BCZ N 6 . ? 22.367 -65.126 19.522 1.00 21.37 ? 513 BCZ A O8 1 HETATM 3227 O O7 . BCZ N 6 . ? 24.514 -64.888 20.499 1.00 23.23 ? 513 BCZ A O7 1 HETATM 3228 C C1 . BCZ N 6 . ? 23.573 -63.743 17.122 1.00 20.55 ? 513 BCZ A C1 1 HETATM 3229 O O . HOH O 7 . ? 25.269 -59.238 16.710 1.00 17.34 ? 601 HOH A O 1 HETATM 3230 O O . HOH O 7 . ? 10.338 -47.004 11.702 1.00 15.06 ? 602 HOH A O 1 HETATM 3231 O O . HOH O 7 . ? 11.525 -60.664 14.103 1.00 14.18 ? 603 HOH A O 1 HETATM 3232 O O . HOH O 7 . ? 5.104 -62.661 19.542 1.00 15.21 ? 604 HOH A O 1 HETATM 3233 O O . HOH O 7 . ? 0.721 -53.110 18.656 1.00 13.86 ? 605 HOH A O 1 HETATM 3234 O O . HOH O 7 . ? -3.253 -70.343 6.022 1.00 18.91 ? 606 HOH A O 1 HETATM 3235 O O . HOH O 7 . ? 28.309 -54.398 3.091 1.00 18.24 ? 607 HOH A O 1 HETATM 3236 O O . HOH O 7 . ? 4.519 -66.552 17.479 1.00 14.98 ? 608 HOH A O 1 HETATM 3237 O O . HOH O 7 . ? 0.813 -60.404 13.806 1.00 15.41 ? 609 HOH A O 1 HETATM 3238 O O . HOH O 7 . ? 15.876 -43.582 17.889 1.00 20.01 ? 610 HOH A O 1 HETATM 3239 O O . HOH O 7 . ? 16.092 -45.409 21.912 1.00 16.41 ? 611 HOH A O 1 HETATM 3240 O O . HOH O 7 . ? 17.166 -67.082 12.254 1.00 13.22 ? 612 HOH A O 1 HETATM 3241 O O . HOH O 7 . ? 15.433 -50.820 19.302 1.00 13.36 ? 613 HOH A O 1 HETATM 3242 O O . HOH O 7 . ? 21.177 -65.279 13.796 1.00 14.65 ? 614 HOH A O 1 HETATM 3243 O O . HOH O 7 . ? 27.834 -64.198 30.949 1.00 26.88 ? 615 HOH A O 1 HETATM 3244 O O . HOH O 7 . ? 5.509 -66.548 29.148 1.00 17.26 ? 616 HOH A O 1 HETATM 3245 O O . HOH O 7 . ? 5.620 -44.492 32.316 1.00 18.16 ? 617 HOH A O 1 HETATM 3246 O O . HOH O 7 . ? 20.617 -68.176 16.159 1.00 15.97 ? 618 HOH A O 1 HETATM 3247 O O . HOH O 7 . ? 7.675 -47.385 40.647 1.00 28.24 ? 619 HOH A O 1 HETATM 3248 O O . HOH O 7 . ? 19.476 -67.644 13.530 1.00 19.33 ? 620 HOH A O 1 HETATM 3249 O O . HOH O 7 . ? 19.277 -71.112 4.495 1.00 23.47 ? 621 HOH A O 1 HETATM 3250 O O . HOH O 7 . ? 23.151 -39.945 10.035 1.00 16.49 ? 622 HOH A O 1 HETATM 3251 O O . HOH O 7 . ? -1.202 -69.559 10.697 1.00 21.64 ? 623 HOH A O 1 HETATM 3252 O O . HOH O 7 . ? 35.503 -58.057 9.216 1.00 16.07 ? 624 HOH A O 1 HETATM 3253 O O . HOH O 7 . ? 24.824 -62.050 22.110 1.00 20.10 ? 625 HOH A O 1 HETATM 3254 O O . HOH O 7 . ? 19.090 -59.808 29.101 1.00 13.82 ? 626 HOH A O 1 HETATM 3255 O O . HOH O 7 . ? 3.472 -54.438 37.264 1.00 19.04 ? 627 HOH A O 1 HETATM 3256 O O . HOH O 7 . ? 19.785 -55.090 32.459 1.00 20.46 ? 628 HOH A O 1 HETATM 3257 O O . HOH O 7 . ? 28.023 -55.206 38.806 1.00 21.85 ? 629 HOH A O 1 HETATM 3258 O O . HOH O 7 . ? 25.792 -53.424 3.682 1.00 11.79 ? 630 HOH A O 1 HETATM 3259 O O . HOH O 7 . ? 21.171 -32.396 25.808 1.00 39.61 ? 631 HOH A O 1 HETATM 3260 O O . HOH O 7 . ? 11.835 -47.938 8.039 1.00 18.91 ? 632 HOH A O 1 HETATM 3261 O O . HOH O 7 . ? 6.128 -41.644 16.198 1.00 20.18 ? 633 HOH A O 1 HETATM 3262 O O . HOH O 7 . ? 19.893 -68.458 20.985 1.00 15.35 ? 634 HOH A O 1 HETATM 3263 O O . HOH O 7 . ? 32.680 -56.402 2.688 1.00 20.82 ? 635 HOH A O 1 HETATM 3264 O O . HOH O 7 . ? 1.659 -68.776 29.689 1.00 24.97 ? 636 HOH A O 1 HETATM 3265 O O . HOH O 7 . ? 26.890 -69.551 12.738 1.00 29.10 ? 637 HOH A O 1 HETATM 3266 O O . HOH O 7 . ? 27.532 -58.467 29.991 1.00 18.59 ? 638 HOH A O 1 HETATM 3267 O O . HOH O 7 . ? 31.891 -43.626 -1.447 1.00 19.82 ? 639 HOH A O 1 HETATM 3268 O O . HOH O 7 . ? 23.011 -66.648 26.502 1.00 24.69 ? 640 HOH A O 1 HETATM 3269 O O . HOH O 7 . ? 9.029 -61.484 14.711 1.00 16.73 ? 641 HOH A O 1 HETATM 3270 O O . HOH O 7 . ? 18.132 -57.501 18.747 1.00 14.63 ? 642 HOH A O 1 HETATM 3271 O O . HOH O 7 . ? 18.061 -60.264 26.485 1.00 17.01 ? 643 HOH A O 1 HETATM 3272 O O . HOH O 7 . ? 30.889 -63.642 34.440 1.00 22.52 ? 644 HOH A O 1 HETATM 3273 O O . HOH O 7 . ? -0.888 -72.039 12.535 1.00 20.17 ? 645 HOH A O 1 HETATM 3274 O O . HOH O 7 . ? 19.757 -61.701 31.203 1.00 17.18 ? 646 HOH A O 1 HETATM 3275 O O . HOH O 7 . ? 1.252 -57.671 31.011 1.00 21.40 ? 647 HOH A O 1 HETATM 3276 O O . HOH O 7 . ? 22.008 -63.448 39.041 1.00 24.81 ? 648 HOH A O 1 HETATM 3277 O O . HOH O 7 . ? 19.708 -56.421 13.554 1.00 15.31 ? 649 HOH A O 1 HETATM 3278 O O . HOH O 7 . ? 0.865 -55.178 31.980 1.00 15.17 ? 650 HOH A O 1 HETATM 3279 O O . HOH O 7 . ? 12.566 -44.725 17.704 1.00 15.42 ? 651 HOH A O 1 HETATM 3280 O O . HOH O 7 . ? 19.893 -49.785 27.499 1.00 23.01 ? 652 HOH A O 1 HETATM 3281 O O . HOH O 7 . ? 24.159 -33.282 18.502 1.00 19.46 ? 653 HOH A O 1 HETATM 3282 O O . HOH O 7 . ? 20.211 -70.308 26.068 1.00 22.73 ? 654 HOH A O 1 HETATM 3283 O O . HOH O 7 . ? 23.469 -55.523 25.179 1.00 18.99 ? 655 HOH A O 1 HETATM 3284 O O . HOH O 7 . ? 16.865 -61.240 2.835 1.00 23.93 ? 656 HOH A O 1 HETATM 3285 O O . HOH O 7 . ? 8.733 -67.730 35.726 1.00 19.99 ? 657 HOH A O 1 HETATM 3286 O O . HOH O 7 . ? 31.018 -63.350 7.737 1.00 18.25 ? 658 HOH A O 1 HETATM 3287 O O . HOH O 7 . ? 29.891 -65.787 6.922 1.00 22.09 ? 659 HOH A O 1 HETATM 3288 O O . HOH O 7 . ? 40.522 -58.603 18.923 1.00 21.97 ? 660 HOH A O 1 HETATM 3289 O O . HOH O 7 . ? 14.117 -61.777 2.990 1.00 20.92 ? 661 HOH A O 1 HETATM 3290 O O . HOH O 7 . ? 20.992 -46.316 37.565 1.00 18.53 ? 662 HOH A O 1 HETATM 3291 O O . HOH O 7 . ? 34.455 -64.380 34.039 1.00 34.11 ? 663 HOH A O 1 HETATM 3292 O O . HOH O 7 . ? 6.382 -69.840 6.782 1.00 18.80 ? 664 HOH A O 1 HETATM 3293 O O . HOH O 7 . ? 18.823 -57.171 29.711 1.00 20.74 ? 665 HOH A O 1 HETATM 3294 O O . HOH O 7 . ? 27.186 -57.326 16.893 1.00 18.19 ? 666 HOH A O 1 HETATM 3295 O O . HOH O 7 . ? 9.450 -43.849 31.001 1.00 19.50 ? 667 HOH A O 1 HETATM 3296 O O . HOH O 7 . ? 14.176 -72.072 21.172 1.00 21.59 ? 668 HOH A O 1 HETATM 3297 O O . HOH O 7 . ? 9.732 -63.468 12.782 1.00 24.17 ? 669 HOH A O 1 HETATM 3298 O O . HOH O 7 . ? 32.191 -52.812 43.907 1.00 22.52 ? 670 HOH A O 1 HETATM 3299 O O . HOH O 7 . ? 16.511 -40.883 17.143 1.00 19.02 ? 671 HOH A O 1 HETATM 3300 O O . HOH O 7 . ? 3.559 -49.452 11.618 1.00 22.19 ? 672 HOH A O 1 HETATM 3301 O O . HOH O 7 . ? 37.457 -61.150 0.694 1.00 19.76 ? 673 HOH A O 1 HETATM 3302 O O . HOH O 7 . ? 28.527 -56.240 18.840 1.00 19.17 ? 674 HOH A O 1 HETATM 3303 O O . HOH O 7 . ? 16.847 -71.907 20.650 1.00 20.37 ? 675 HOH A O 1 HETATM 3304 O O . HOH O 7 . ? 7.260 -41.359 24.409 1.00 22.21 ? 676 HOH A O 1 HETATM 3305 O O . HOH O 7 . ? 36.930 -47.534 5.680 1.00 22.34 ? 677 HOH A O 1 HETATM 3306 O O . HOH O 7 . ? -1.690 -51.953 24.456 1.00 17.29 ? 678 HOH A O 1 HETATM 3307 O O . HOH O 7 . ? 5.103 -54.139 39.351 1.00 21.52 ? 679 HOH A O 1 HETATM 3308 O O . HOH O 7 . ? 27.058 -52.341 19.574 1.00 19.08 ? 680 HOH A O 1 HETATM 3309 O O . HOH O 7 . ? 35.095 -52.536 39.641 1.00 24.68 ? 681 HOH A O 1 HETATM 3310 O O . HOH O 7 . ? -0.528 -54.433 29.441 1.00 21.27 ? 682 HOH A O 1 HETATM 3311 O O . HOH O 7 . ? 11.768 -35.319 21.201 1.00 28.84 ? 683 HOH A O 1 HETATM 3312 O O . HOH O 7 . ? 5.989 -39.194 34.365 1.00 26.11 ? 684 HOH A O 1 HETATM 3313 O O . HOH O 7 . ? 17.805 -69.848 22.317 1.00 23.70 ? 685 HOH A O 1 HETATM 3314 O O . HOH O 7 . ? 44.714 -55.090 -6.980 1.00 28.37 ? 686 HOH A O 1 HETATM 3315 O O . HOH O 7 . ? 37.471 -38.920 13.916 1.00 31.40 ? 687 HOH A O 1 HETATM 3316 O O . HOH O 7 . ? 7.326 -44.079 41.619 1.00 24.26 ? 688 HOH A O 1 HETATM 3317 O O . HOH O 7 . ? 10.644 -34.698 31.008 1.00 27.98 ? 689 HOH A O 1 HETATM 3318 O O . HOH O 7 . ? 28.873 -48.821 48.241 1.00 36.77 ? 690 HOH A O 1 HETATM 3319 O O . HOH O 7 . ? 23.713 -62.501 47.547 1.00 27.62 ? 691 HOH A O 1 HETATM 3320 O O . HOH O 7 . ? 20.720 -60.963 1.236 1.00 17.40 ? 692 HOH A O 1 HETATM 3321 O O . HOH O 7 . ? 30.572 -57.658 1.577 1.00 17.67 ? 693 HOH A O 1 HETATM 3322 O O . HOH O 7 . ? 35.107 -54.823 22.724 1.00 22.52 ? 694 HOH A O 1 HETATM 3323 O O . HOH O 7 . ? 22.321 -69.835 22.195 1.00 28.16 ? 695 HOH A O 1 HETATM 3324 O O . HOH O 7 . ? 6.212 -75.802 21.407 1.00 24.44 ? 696 HOH A O 1 HETATM 3325 O O . HOH O 7 . ? 39.899 -48.485 16.711 1.00 30.55 ? 697 HOH A O 1 HETATM 3326 O O . HOH O 7 . ? 30.865 -60.039 45.452 0.50 25.56 ? 698 HOH A O 1 HETATM 3327 O O . HOH O 7 . ? 6.147 -52.393 4.847 1.00 33.85 ? 699 HOH A O 1 HETATM 3328 O O . HOH O 7 . ? 37.705 -54.909 24.420 1.00 25.14 ? 700 HOH A O 1 HETATM 3329 O O . HOH O 7 . ? 28.962 -48.171 44.944 1.00 39.38 ? 701 HOH A O 1 HETATM 3330 O O . HOH O 7 . ? 39.826 -50.749 35.275 1.00 33.14 ? 702 HOH A O 1 HETATM 3331 O O . HOH O 7 . ? 9.665 -65.752 11.698 1.00 21.38 ? 703 HOH A O 1 HETATM 3332 O O . HOH O 7 . ? 15.120 -78.528 4.035 1.00 25.55 ? 704 HOH A O 1 HETATM 3333 O O . HOH O 7 . ? 3.039 -70.796 0.924 1.00 32.82 ? 705 HOH A O 1 HETATM 3334 O O . HOH O 7 . ? 18.351 -35.507 15.580 1.00 25.56 ? 706 HOH A O 1 HETATM 3335 O O . HOH O 7 . ? 20.227 -67.139 5.317 1.00 19.04 ? 707 HOH A O 1 HETATM 3336 O O . HOH O 7 . ? 31.195 -63.396 29.916 1.00 21.82 ? 708 HOH A O 1 HETATM 3337 O O . HOH O 7 . ? 15.920 -68.563 23.506 1.00 20.65 ? 709 HOH A O 1 HETATM 3338 O O . HOH O 7 . ? 35.157 -62.525 16.480 1.00 27.17 ? 710 HOH A O 1 HETATM 3339 O O . HOH O 7 . ? 33.318 -51.406 41.733 1.00 30.70 ? 711 HOH A O 1 HETATM 3340 O O . HOH O 7 . ? 4.135 -39.475 27.076 1.00 39.74 ? 712 HOH A O 1 HETATM 3341 O O . HOH O 7 . ? 7.906 -44.021 23.766 1.00 23.96 ? 713 HOH A O 1 HETATM 3342 O O . HOH O 7 . ? 8.243 -70.688 24.644 1.00 30.77 ? 714 HOH A O 1 HETATM 3343 O O . HOH O 7 . ? 21.571 -37.691 10.955 1.00 28.68 ? 715 HOH A O 1 HETATM 3344 O O . HOH O 7 . ? 12.481 -39.485 35.257 1.00 27.77 ? 716 HOH A O 1 HETATM 3345 O O . HOH O 7 . ? 14.889 -41.997 -1.381 1.00 30.54 ? 717 HOH A O 1 HETATM 3346 O O . HOH O 7 . ? 11.531 -45.272 7.636 1.00 27.14 ? 718 HOH A O 1 HETATM 3347 O O . HOH O 7 . ? 45.007 -56.485 -1.136 1.00 33.75 ? 719 HOH A O 1 HETATM 3348 O O . HOH O 7 . ? 37.603 -63.428 2.646 1.00 28.02 ? 720 HOH A O 1 HETATM 3349 O O . HOH O 7 . ? 15.722 -43.384 -3.963 1.00 24.49 ? 721 HOH A O 1 HETATM 3350 O O . HOH O 7 . ? 14.156 -38.525 -2.134 1.00 37.77 ? 722 HOH A O 1 HETATM 3351 O O . HOH O 7 . ? 18.079 -34.482 6.186 1.00 25.80 ? 723 HOH A O 1 HETATM 3352 O O . HOH O 7 . ? 21.340 -43.471 37.339 1.00 27.33 ? 724 HOH A O 1 HETATM 3353 O O . HOH O 7 . ? 19.345 -69.592 18.327 1.00 19.12 ? 725 HOH A O 1 HETATM 3354 O O . HOH O 7 . ? 4.119 -58.356 31.900 1.00 19.93 ? 726 HOH A O 1 HETATM 3355 O O . HOH O 7 . ? 26.558 -37.722 27.965 1.00 40.27 ? 727 HOH A O 1 HETATM 3356 O O . HOH O 7 . ? 14.244 -43.496 15.548 1.00 21.77 ? 728 HOH A O 1 HETATM 3357 O O . HOH O 7 . ? 40.417 -56.179 34.201 1.00 23.96 ? 729 HOH A O 1 HETATM 3358 O O . HOH O 7 . ? 24.328 -55.181 37.291 1.00 21.84 ? 730 HOH A O 1 HETATM 3359 O O . HOH O 7 . ? 11.828 -34.062 14.922 1.00 26.50 ? 731 HOH A O 1 HETATM 3360 O O . HOH O 7 . ? 10.075 -58.410 1.094 1.00 21.38 ? 732 HOH A O 1 HETATM 3361 O O . HOH O 7 . ? 14.677 -47.467 40.503 1.00 34.35 ? 733 HOH A O 1 HETATM 3362 O O . HOH O 7 . ? 39.170 -48.413 27.499 1.00 33.35 ? 734 HOH A O 1 HETATM 3363 O O . HOH O 7 . ? 12.356 -79.545 19.726 1.00 34.52 ? 735 HOH A O 1 HETATM 3364 O O . HOH O 7 . ? 23.869 -60.607 3.830 1.00 22.22 ? 736 HOH A O 1 HETATM 3365 O O . HOH O 7 . ? 18.256 -70.463 36.574 1.00 32.89 ? 737 HOH A O 1 HETATM 3366 O O . HOH O 7 . ? 17.257 -50.919 0.720 1.00 25.43 ? 738 HOH A O 1 HETATM 3367 O O . HOH O 7 . ? 5.219 -70.575 23.503 1.00 28.42 ? 739 HOH A O 1 HETATM 3368 O O . HOH O 7 . ? 34.374 -44.855 34.249 1.00 37.84 ? 740 HOH A O 1 HETATM 3369 O O . HOH O 7 . ? 18.599 -49.584 20.925 1.00 22.33 ? 741 HOH A O 1 HETATM 3370 O O . HOH O 7 . ? 4.370 -41.180 25.291 1.00 29.38 ? 742 HOH A O 1 HETATM 3371 O O . HOH O 7 . ? 39.005 -49.490 19.462 1.00 33.82 ? 743 HOH A O 1 HETATM 3372 O O . HOH O 7 . ? 41.559 -55.986 29.714 1.00 30.10 ? 744 HOH A O 1 HETATM 3373 O O . HOH O 7 . ? 1.406 -55.555 7.143 1.00 31.41 ? 745 HOH A O 1 HETATM 3374 O O . HOH O 7 . ? 37.979 -51.203 22.206 1.00 25.50 ? 746 HOH A O 1 HETATM 3375 O O . HOH O 7 . ? 20.636 -34.283 25.634 1.00 52.53 ? 747 HOH A O 1 HETATM 3376 O O . HOH O 7 . ? 39.969 -54.986 2.779 1.00 22.17 ? 748 HOH A O 1 HETATM 3377 O O . HOH O 7 . ? 21.245 -69.821 5.714 1.00 37.05 ? 749 HOH A O 1 HETATM 3378 O O . HOH O 7 . ? 36.338 -44.873 9.355 1.00 35.16 ? 750 HOH A O 1 HETATM 3379 O O . HOH O 7 . ? 38.483 -52.670 24.720 1.00 36.84 ? 751 HOH A O 1 HETATM 3380 O O . HOH O 7 . ? 12.084 -77.999 10.274 1.00 23.24 ? 752 HOH A O 1 HETATM 3381 O O . HOH O 7 . ? 22.335 -61.762 51.543 1.00 43.02 ? 753 HOH A O 1 HETATM 3382 O O . HOH O 7 . ? 33.763 -48.585 42.426 1.00 44.27 ? 754 HOH A O 1 HETATM 3383 O O . HOH O 7 . ? 7.637 -70.828 34.236 1.00 35.97 ? 755 HOH A O 1 HETATM 3384 O O . HOH O 7 . ? 2.899 -46.821 14.248 1.00 34.85 ? 756 HOH A O 1 HETATM 3385 O O . HOH O 7 . ? 13.660 -76.661 7.863 1.00 31.14 ? 757 HOH A O 1 HETATM 3386 O O . HOH O 7 . ? 32.090 -43.418 2.206 1.00 30.41 ? 758 HOH A O 1 HETATM 3387 O O . HOH O 7 . ? 13.822 -41.903 5.608 1.00 28.61 ? 759 HOH A O 1 HETATM 3388 O O . HOH O 7 . ? 34.508 -45.281 36.748 1.00 34.92 ? 760 HOH A O 1 HETATM 3389 O O . HOH O 7 . ? 31.900 -51.937 47.828 1.00 31.04 ? 761 HOH A O 1 HETATM 3390 O O . HOH O 7 . ? 24.218 -56.096 34.809 1.00 19.51 ? 762 HOH A O 1 HETATM 3391 O O . HOH O 7 . ? 23.556 -55.770 48.531 1.00 32.43 ? 763 HOH A O 1 HETATM 3392 O O . HOH O 7 . ? 22.889 -45.709 19.303 1.00 29.08 ? 764 HOH A O 1 HETATM 3393 O O . HOH O 7 . ? 3.132 -81.793 12.723 1.00 37.12 ? 765 HOH A O 1 HETATM 3394 O O . HOH O 7 . ? 26.849 -64.763 21.694 1.00 38.45 ? 766 HOH A O 1 HETATM 3395 O O . HOH O 7 . ? 35.241 -39.501 24.515 1.00 31.93 ? 767 HOH A O 1 HETATM 3396 O O . HOH O 7 . ? 43.221 -51.024 11.037 1.00 41.27 ? 768 HOH A O 1 HETATM 3397 O O . HOH O 7 . ? 8.263 -48.833 43.806 1.00 33.00 ? 769 HOH A O 1 HETATM 3398 O O . HOH O 7 . ? 39.948 -68.407 -17.184 1.00 42.96 ? 770 HOH A O 1 HETATM 3399 O O . HOH O 7 . ? 26.844 -68.433 41.463 1.00 29.96 ? 771 HOH A O 1 HETATM 3400 O O . HOH O 7 . ? 8.506 -73.296 24.494 1.00 43.34 ? 772 HOH A O 1 HETATM 3401 O O . HOH O 7 . ? 16.933 -72.531 33.335 1.00 42.76 ? 773 HOH A O 1 HETATM 3402 O O . HOH O 7 . ? 9.955 -45.816 39.074 1.00 24.20 ? 774 HOH A O 1 HETATM 3403 O O . HOH O 7 . ? 12.003 -60.505 1.471 1.00 22.67 ? 775 HOH A O 1 HETATM 3404 O O . HOH O 7 . ? -0.000 -71.236 0.000 0.25 46.18 ? 776 HOH A O 1 HETATM 3405 O O . HOH O 7 . ? 29.927 -68.090 8.653 1.00 32.90 ? 777 HOH A O 1 HETATM 3406 O O . HOH O 7 . ? 12.496 -38.875 4.644 1.00 31.80 ? 778 HOH A O 1 HETATM 3407 O O . HOH O 7 . ? 29.720 -64.572 20.614 1.00 29.89 ? 779 HOH A O 1 HETATM 3408 O O . HOH O 7 . ? 38.580 -50.493 27.171 1.00 40.38 ? 780 HOH A O 1 HETATM 3409 O O . HOH O 7 . ? 9.814 -34.437 12.641 1.00 30.58 ? 781 HOH A O 1 HETATM 3410 O O . HOH O 7 . ? -3.383 -75.012 18.693 1.00 28.77 ? 782 HOH A O 1 HETATM 3411 O O . HOH O 7 . ? 34.000 -65.638 6.747 1.00 28.68 ? 783 HOH A O 1 HETATM 3412 O O . HOH O 7 . ? 29.248 -38.886 28.406 1.00 34.90 ? 784 HOH A O 1 HETATM 3413 O O . HOH O 7 . ? 2.396 -48.997 7.450 1.00 31.06 ? 785 HOH A O 1 HETATM 3414 O O . HOH O 7 . ? 31.091 -37.350 27.439 1.00 31.79 ? 786 HOH A O 1 HETATM 3415 O O . HOH O 7 . ? 5.410 -45.567 23.048 1.00 26.63 ? 787 HOH A O 1 HETATM 3416 O O . HOH O 7 . ? 9.189 -72.953 35.065 1.00 41.45 ? 788 HOH A O 1 HETATM 3417 O O . HOH O 7 . ? 20.706 -41.198 28.672 1.00 33.21 ? 789 HOH A O 1 HETATM 3418 O O . HOH O 7 . ? 27.947 -67.470 10.593 1.00 37.98 ? 790 HOH A O 1 HETATM 3419 O O . HOH O 7 . ? 44.889 -59.150 -2.419 1.00 45.57 ? 791 HOH A O 1 HETATM 3420 O O . HOH O 7 . ? 13.760 -51.422 -0.318 1.00 31.50 ? 792 HOH A O 1 HETATM 3421 O O . HOH O 7 . ? 4.113 -43.803 21.328 1.00 26.96 ? 793 HOH A O 1 HETATM 3422 O O . HOH O 7 . ? 28.766 -67.012 14.370 1.00 38.92 ? 794 HOH A O 1 HETATM 3423 O O . HOH O 7 . ? 12.251 -71.905 28.192 1.00 53.73 ? 795 HOH A O 1 HETATM 3424 O O . HOH O 7 . ? 40.932 -60.305 15.909 1.00 32.12 ? 796 HOH A O 1 HETATM 3425 O O . HOH O 7 . ? 15.140 -38.973 32.865 1.00 24.83 ? 797 HOH A O 1 HETATM 3426 O O . HOH O 7 . ? -3.329 -66.271 32.450 1.00 39.76 ? 798 HOH A O 1 HETATM 3427 O O . HOH O 7 . ? 38.572 -62.866 10.864 1.00 37.03 ? 799 HOH A O 1 HETATM 3428 O O . HOH O 7 . ? 33.321 -33.844 26.281 1.00 32.82 ? 800 HOH A O 1 HETATM 3429 O O . HOH O 7 . ? 39.682 -55.007 27.623 1.00 25.76 ? 801 HOH A O 1 HETATM 3430 O O . HOH O 7 . ? 11.720 -53.990 0.022 1.00 29.33 ? 802 HOH A O 1 HETATM 3431 O O . HOH O 7 . ? 6.564 -36.860 25.139 1.00 42.11 ? 803 HOH A O 1 HETATM 3432 O O . HOH O 7 . ? 22.081 -84.761 8.950 1.00 41.59 ? 804 HOH A O 1 HETATM 3433 O O . HOH O 7 . ? 15.961 -38.323 18.117 1.00 33.48 ? 805 HOH A O 1 HETATM 3434 O O . HOH O 7 . ? 31.804 -48.386 44.427 1.00 32.92 ? 806 HOH A O 1 HETATM 3435 O O . HOH O 7 . ? 9.404 -77.123 22.442 1.00 33.79 ? 807 HOH A O 1 HETATM 3436 O O . HOH O 7 . ? 40.395 -57.592 31.794 1.00 38.59 ? 808 HOH A O 1 HETATM 3437 O O . HOH O 7 . ? -0.781 -53.717 40.384 1.00 27.28 ? 809 HOH A O 1 HETATM 3438 O O . HOH O 7 . ? 10.848 -36.621 32.929 1.00 37.73 ? 810 HOH A O 1 HETATM 3439 O O . HOH O 7 . ? 38.124 -48.695 7.976 1.00 33.61 ? 811 HOH A O 1 HETATM 3440 O O . HOH O 7 . ? 4.323 -79.976 9.316 1.00 35.81 ? 812 HOH A O 1 HETATM 3441 O O . HOH O 7 . ? 34.124 -65.151 17.192 1.00 32.85 ? 813 HOH A O 1 HETATM 3442 O O . HOH O 7 . ? 38.957 -56.147 39.214 1.00 35.58 ? 814 HOH A O 1 HETATM 3443 O O . HOH O 7 . ? 12.601 -78.005 5.636 1.00 31.63 ? 815 HOH A O 1 HETATM 3444 O O . HOH O 7 . ? 24.372 -30.519 18.368 1.00 42.65 ? 816 HOH A O 1 HETATM 3445 O O . HOH O 7 . ? 1.640 -62.027 39.117 1.00 43.09 ? 817 HOH A O 1 HETATM 3446 O O . HOH O 7 . ? 29.063 -65.754 18.900 1.00 35.69 ? 818 HOH A O 1 HETATM 3447 O O . HOH O 7 . ? 2.068 -69.144 -0.599 1.00 42.11 ? 819 HOH A O 1 HETATM 3448 O O . HOH O 7 . ? 42.282 -60.002 21.579 1.00 38.43 ? 820 HOH A O 1 HETATM 3449 O O . HOH O 7 . ? -0.837 -76.142 8.312 1.00 35.21 ? 821 HOH A O 1 HETATM 3450 O O . HOH O 7 . ? 19.076 -42.219 31.408 1.00 40.04 ? 822 HOH A O 1 HETATM 3451 O O . HOH O 7 . ? 19.351 -28.221 19.352 1.00 38.36 ? 823 HOH A O 1 HETATM 3452 O O . HOH O 7 . ? 16.336 -48.230 0.413 1.00 37.29 ? 824 HOH A O 1 HETATM 3453 O O . HOH O 7 . ? 36.523 -64.447 19.273 1.00 32.71 ? 825 HOH A O 1 HETATM 3454 O O . HOH O 7 . ? 13.721 -48.473 -0.886 1.00 38.34 ? 826 HOH A O 1 HETATM 3455 O O . HOH O 7 . ? 1.257 -63.802 34.639 1.00 39.19 ? 827 HOH A O 1 HETATM 3456 O O . HOH O 7 . ? 28.089 -64.517 42.527 1.00 43.11 ? 828 HOH A O 1 HETATM 3457 O O . HOH O 7 . ? 24.477 -39.886 28.546 1.00 34.67 ? 829 HOH A O 1 HETATM 3458 O O . HOH O 7 . ? 38.755 -46.533 9.773 1.00 38.65 ? 830 HOH A O 1 HETATM 3459 O O . HOH O 7 . ? 21.920 -64.340 44.904 1.00 42.43 ? 831 HOH A O 1 HETATM 3460 O O . HOH O 7 . ? 37.534 -45.169 37.059 1.00 48.16 ? 832 HOH A O 1 HETATM 3461 O O . HOH O 7 . ? 10.930 -40.139 37.460 1.00 38.16 ? 833 HOH A O 1 HETATM 3462 O O . HOH O 7 . ? 23.195 -42.275 -2.856 1.00 33.44 ? 834 HOH A O 1 HETATM 3463 O O . HOH O 7 . ? 20.052 -48.085 45.642 1.00 40.25 ? 835 HOH A O 1 HETATM 3464 O O . HOH O 7 . ? 15.883 -38.287 36.427 1.00 37.30 ? 836 HOH A O 1 HETATM 3465 O O . HOH O 7 . ? 10.935 -40.416 6.849 1.00 37.35 ? 837 HOH A O 1 HETATM 3466 O O . HOH O 7 . ? 22.538 -43.255 39.982 1.00 39.47 ? 838 HOH A O 1 HETATM 3467 O O . HOH O 7 . ? 24.618 -72.040 31.070 1.00 35.99 ? 839 HOH A O 1 HETATM 3468 O O . HOH O 7 . ? 8.198 -42.110 7.840 1.00 30.92 ? 840 HOH A O 1 HETATM 3469 O O . HOH O 7 . ? 29.308 -69.921 31.210 1.00 44.41 ? 841 HOH A O 1 HETATM 3470 O O . HOH O 7 . ? 19.399 -86.092 9.839 1.00 41.77 ? 842 HOH A O 1 HETATM 3471 O O . HOH O 7 . ? 24.341 -33.052 25.607 1.00 44.67 ? 843 HOH A O 1 HETATM 3472 O O . HOH O 7 . ? 4.004 -45.624 19.331 1.00 36.31 ? 844 HOH A O 1 HETATM 3473 O O . HOH O 7 . ? 16.421 -47.216 5.709 1.00 32.52 ? 845 HOH A O 1 HETATM 3474 O O . HOH O 7 . ? 38.192 -64.251 17.552 1.00 36.72 ? 846 HOH A O 1 HETATM 3475 O O . HOH O 7 . ? 25.800 -53.288 51.837 1.00 38.54 ? 847 HOH A O 1 HETATM 3476 O O . HOH O 7 . ? 22.097 -52.955 1.042 1.00 33.22 ? 848 HOH A O 1 HETATM 3477 O O . HOH O 7 . ? 9.486 -75.719 8.175 1.00 40.59 ? 849 HOH A O 1 HETATM 3478 O O . HOH O 7 . ? 39.586 -66.378 -12.759 1.00 42.19 ? 850 HOH A O 1 HETATM 3479 O O . HOH O 7 . ? 31.093 -66.821 22.118 1.00 41.44 ? 851 HOH A O 1 HETATM 3480 O O . HOH O 7 . ? 29.397 -44.967 41.716 1.00 34.60 ? 852 HOH A O 1 HETATM 3481 O O . HOH O 7 . ? 3.565 -62.109 34.725 1.00 34.16 ? 853 HOH A O 1 HETATM 3482 O O . HOH O 7 . ? 10.767 -32.863 33.262 1.00 43.24 ? 854 HOH A O 1 HETATM 3483 O O . HOH O 7 . ? 21.736 -42.733 32.337 1.00 40.09 ? 855 HOH A O 1 HETATM 3484 O O . HOH O 7 . ? 32.193 -57.848 43.929 1.00 38.98 ? 856 HOH A O 1 HETATM 3485 O O . HOH O 7 . ? 19.287 -28.357 13.534 1.00 40.34 ? 857 HOH A O 1 HETATM 3486 O O . HOH O 7 . ? 35.324 -45.064 6.389 1.00 35.66 ? 858 HOH A O 1 HETATM 3487 O O . HOH O 7 . ? 8.603 -35.944 21.856 1.00 36.83 ? 859 HOH A O 1 HETATM 3488 O O . HOH O 7 . ? 45.064 -52.752 -1.401 1.00 37.14 ? 860 HOH A O 1 HETATM 3489 O O . HOH O 7 . ? 20.045 -70.845 23.559 1.00 34.65 ? 861 HOH A O 1 HETATM 3490 O O . HOH O 7 . ? 9.916 -43.975 40.915 1.00 37.09 ? 862 HOH A O 1 HETATM 3491 O O . HOH O 7 . ? -2.204 -72.748 20.182 1.00 35.71 ? 863 HOH A O 1 HETATM 3492 O O . HOH O 7 . ? 32.407 -70.139 31.905 1.00 45.16 ? 864 HOH A O 1 HETATM 3493 O O . HOH O 7 . ? -0.437 -59.891 16.623 1.00 31.26 ? 865 HOH A O 1 HETATM 3494 O O . HOH O 7 . ? 29.387 -53.336 19.066 1.00 28.46 ? 866 HOH A O 1 HETATM 3495 O O . HOH O 7 . ? 40.857 -64.767 2.955 1.00 45.69 ? 867 HOH A O 1 HETATM 3496 O O . HOH O 7 . ? 18.618 -37.994 0.121 1.00 43.93 ? 868 HOH A O 1 HETATM 3497 O O . HOH O 7 . ? 9.884 -83.982 11.130 1.00 42.21 ? 869 HOH A O 1 HETATM 3498 O O . HOH O 7 . ? 10.777 -33.343 17.438 1.00 38.47 ? 870 HOH A O 1 HETATM 3499 O O . HOH O 7 . ? 3.670 -70.547 28.789 1.00 34.06 ? 871 HOH A O 1 HETATM 3500 O O . HOH O 7 . ? 42.679 -49.383 9.452 1.00 46.87 ? 872 HOH A O 1 HETATM 3501 O O . HOH O 7 . ? 41.358 -53.139 36.507 1.00 37.39 ? 873 HOH A O 1 HETATM 3502 O O . HOH O 7 . ? 8.171 -77.005 6.885 1.00 43.46 ? 874 HOH A O 1 HETATM 3503 O O . HOH O 7 . ? 24.750 -44.438 44.175 1.00 42.80 ? 875 HOH A O 1 HETATM 3504 O O . HOH O 7 . ? -2.096 -47.336 39.460 1.00 40.92 ? 876 HOH A O 1 HETATM 3505 O O . HOH O 7 . ? 4.383 -50.162 5.232 1.00 39.46 ? 877 HOH A O 1 HETATM 3506 O O . HOH O 7 . ? 16.684 -28.878 12.288 1.00 38.68 ? 878 HOH A O 1 HETATM 3507 O O . HOH O 7 . ? 0.014 -72.590 21.868 1.00 36.91 ? 879 HOH A O 1 HETATM 3508 O O . HOH O 7 . ? 36.899 -57.075 43.317 1.00 32.51 ? 880 HOH A O 1 HETATM 3509 O O . HOH O 7 . ? 43.294 -57.908 2.711 1.00 47.11 ? 881 HOH A O 1 HETATM 3510 O O . HOH O 7 . ? 39.056 -65.936 26.860 1.00 46.38 ? 882 HOH A O 1 HETATM 3511 O O . HOH O 7 . ? 9.356 -82.531 -1.169 1.00 42.06 ? 883 HOH A O 1 HETATM 3512 O O . HOH O 7 . ? 19.795 -74.379 11.564 1.00 17.04 ? 884 HOH A O 1 HETATM 3513 O O . HOH O 7 . ? 16.573 -45.538 -2.953 1.00 31.65 ? 885 HOH A O 1 HETATM 3514 O O . HOH O 7 . ? 35.709 -58.952 29.944 1.00 30.53 ? 886 HOH A O 1 HETATM 3515 O O . HOH O 7 . ? 21.186 -76.546 12.065 1.00 25.90 ? 887 HOH A O 1 HETATM 3516 O O . HOH O 7 . ? 8.398 -68.112 24.119 1.00 30.04 ? 888 HOH A O 1 HETATM 3517 O O . HOH O 7 . ? 17.446 -47.878 3.288 1.00 30.92 ? 889 HOH A O 1 HETATM 3518 O O . HOH O 7 . ? 39.168 -59.406 -7.488 1.00 33.48 ? 890 HOH A O 1 HETATM 3519 O O . HOH O 7 . ? -1.480 -74.637 6.186 1.00 29.94 ? 891 HOH A O 1 HETATM 3520 O O . HOH O 7 . ? 0.169 -81.606 13.742 1.00 32.10 ? 892 HOH A O 1 HETATM 3521 O O . HOH O 7 . ? 31.408 -39.725 5.382 1.00 32.18 ? 893 HOH A O 1 HETATM 3522 O O . HOH O 7 . ? 30.568 -43.270 -3.729 1.00 36.56 ? 894 HOH A O 1 HETATM 3523 O O . HOH O 7 . ? 22.390 -39.669 -1.309 1.00 30.91 ? 895 HOH A O 1 HETATM 3524 O O . HOH O 7 . ? 9.292 -77.179 10.014 1.00 39.16 ? 896 HOH A O 1 HETATM 3525 O O . HOH O 7 . ? 33.696 -41.133 4.903 1.00 36.61 ? 897 HOH A O 1 HETATM 3526 O O . HOH O 7 . ? 22.869 -66.761 8.054 1.00 31.53 ? 898 HOH A O 1 HETATM 3527 O O . HOH O 7 . ? 22.662 -34.892 25.293 1.00 50.08 ? 899 HOH A O 1 HETATM 3528 O O . HOH O 7 . ? 40.009 -67.530 -14.631 1.00 42.97 ? 900 HOH A O 1 HETATM 3529 O O . HOH O 7 . ? 43.869 -56.973 28.345 1.00 38.89 ? 901 HOH A O 1 HETATM 3530 O O . HOH O 7 . ? 25.127 -38.383 -0.398 1.00 41.29 ? 902 HOH A O 1 HETATM 3531 O O . HOH O 7 . ? 16.248 -24.886 13.863 1.00 47.36 ? 903 HOH A O 1 HETATM 3532 O O . HOH O 7 . ? 51.371 -54.593 -16.506 1.00 40.06 ? 904 HOH A O 1 HETATM 3533 O O . HOH O 7 . ? -0.012 -53.971 8.958 1.00 47.30 ? 905 HOH A O 1 HETATM 3534 O O . HOH O 7 . ? 32.068 -41.034 -0.737 1.00 42.74 ? 906 HOH A O 1 HETATM 3535 O O . HOH O 7 . ? 20.884 -39.628 1.022 1.00 39.27 ? 907 HOH A O 1 HETATM 3536 O O . HOH O 7 . ? 23.237 -67.988 16.052 1.00 33.01 ? 908 HOH A O 1 HETATM 3537 O O . HOH O 7 . ? 21.668 -63.015 53.967 1.00 35.24 ? 909 HOH A O 1 HETATM 3538 O O . HOH O 7 . ? 20.791 -60.951 46.002 1.00 48.29 ? 910 HOH A O 1 HETATM 3539 O O . HOH O 7 . ? 40.105 -44.954 29.764 1.00 41.86 ? 911 HOH A O 1 HETATM 3540 O O . HOH O 7 . ? 12.905 -44.324 5.255 1.00 43.90 ? 912 HOH A O 1 HETATM 3541 O O . HOH O 7 . ? 11.217 -49.688 -0.565 1.00 50.36 ? 913 HOH A O 1 HETATM 3542 O O . HOH O 7 . ? 37.951 -68.997 28.674 1.00 42.76 ? 914 HOH A O 1 HETATM 3543 O O . HOH O 7 . ? 5.068 -71.963 33.409 1.00 50.57 ? 915 HOH A O 1 HETATM 3544 O O . HOH O 7 . ? 12.330 -74.677 28.876 1.00 49.16 ? 916 HOH A O 1 HETATM 3545 O O . HOH O 7 . ? 21.175 -70.174 39.744 1.00 48.53 ? 917 HOH A O 1 HETATM 3546 O O . HOH O 7 . ? 31.716 -43.848 33.802 1.00 39.01 ? 918 HOH A O 1 HETATM 3547 O O . HOH O 7 . ? 35.851 -65.555 1.852 1.00 44.88 ? 919 HOH A O 1 HETATM 3548 O O . HOH O 7 . ? 0.434 -50.353 8.091 1.00 43.16 ? 920 HOH A O 1 HETATM 3549 O O . HOH O 7 . ? 36.558 -53.094 42.508 1.00 38.20 ? 921 HOH A O 1 HETATM 3550 O O . HOH O 7 . ? 12.888 -31.727 19.771 1.00 38.86 ? 922 HOH A O 1 HETATM 3551 O O . HOH O 7 . ? 29.985 -44.210 31.848 1.00 40.46 ? 923 HOH A O 1 HETATM 3552 O O . HOH O 7 . ? 10.138 -63.253 37.562 1.00 35.98 ? 924 HOH A O 1 HETATM 3553 O O . HOH O 7 . ? 34.212 -57.009 44.718 1.00 56.62 ? 925 HOH A O 1 HETATM 3554 O O . HOH O 7 . ? 36.513 -41.912 9.169 1.00 41.35 ? 926 HOH A O 1 HETATM 3555 O O . HOH O 7 . ? 36.339 -49.791 40.925 1.00 44.18 ? 927 HOH A O 1 HETATM 3556 O O . HOH O 7 . ? 14.592 -81.360 20.752 1.00 47.54 ? 928 HOH A O 1 HETATM 3557 O O . HOH O 7 . ? 36.354 -64.748 12.685 1.00 37.73 ? 929 HOH A O 1 HETATM 3558 O O . HOH O 7 . ? 25.359 -70.689 0.281 1.00 43.85 ? 930 HOH A O 1 HETATM 3559 O O . HOH O 7 . ? 46.914 -60.365 -11.260 1.00 41.90 ? 931 HOH A O 1 HETATM 3560 O O . HOH O 7 . ? 41.686 -56.737 17.382 1.00 45.57 ? 932 HOH A O 1 HETATM 3561 O O . HOH O 7 . ? 25.350 -35.250 27.007 1.00 49.35 ? 933 HOH A O 1 HETATM 3562 O O . HOH O 7 . ? 21.947 -49.435 48.537 1.00 36.25 ? 934 HOH A O 1 HETATM 3563 O O . HOH O 7 . ? 24.195 -56.144 51.093 1.00 44.32 ? 935 HOH A O 1 HETATM 3564 O O . HOH O 7 . ? 41.971 -61.492 11.281 1.00 44.89 ? 936 HOH A O 1 HETATM 3565 O O . HOH O 7 . ? 38.635 -38.830 17.367 1.00 44.04 ? 937 HOH A O 1 HETATM 3566 O O . HOH O 7 . ? 21.037 -78.377 19.339 1.00 43.19 ? 938 HOH A O 1 HETATM 3567 O O . HOH O 7 . ? 44.421 -62.798 -8.405 1.00 41.20 ? 939 HOH A O 1 HETATM 3568 O O . HOH O 7 . ? 32.443 -68.408 10.488 1.00 38.65 ? 940 HOH A O 1 HETATM 3569 O O . HOH O 7 . ? 22.203 -42.008 34.824 1.00 44.43 ? 941 HOH A O 1 HETATM 3570 O O . HOH O 7 . ? 41.593 -62.351 22.066 1.00 53.30 ? 942 HOH A O 1 HETATM 3571 O O . HOH O 7 . ? 14.775 -24.293 12.075 1.00 51.10 ? 943 HOH A O 1 HETATM 3572 O O . HOH O 7 . ? 41.570 -47.439 10.850 1.00 46.83 ? 944 HOH A O 1 HETATM 3573 O O . HOH O 7 . ? 38.663 -58.261 37.934 1.00 51.65 ? 945 HOH A O 1 HETATM 3574 O O . HOH O 7 . ? 24.068 -68.636 22.935 1.00 47.29 ? 946 HOH A O 1 HETATM 3575 O O . HOH O 7 . ? 40.831 -51.501 27.847 1.00 43.05 ? 947 HOH A O 1 HETATM 3576 O O . HOH O 7 . ? 42.540 -58.403 14.610 1.00 42.40 ? 948 HOH A O 1 HETATM 3577 O O . HOH O 7 . ? 47.113 -60.692 -14.713 1.00 53.38 ? 949 HOH A O 1 HETATM 3578 O O . HOH O 7 . ? 1.417 -50.888 5.440 1.00 46.11 ? 950 HOH A O 1 HETATM 3579 O O . HOH O 7 . ? 44.195 -58.905 28.202 1.00 52.27 ? 951 HOH A O 1 HETATM 3580 O O . HOH O 7 . ? 32.834 -68.072 13.235 1.00 42.89 ? 952 HOH A O 1 HETATM 3581 O O . HOH O 7 . ? 42.191 -49.272 15.475 1.00 48.75 ? 953 HOH A O 1 HETATM 3582 O O . HOH O 7 . ? 5.605 -36.373 14.799 1.00 48.16 ? 954 HOH A O 1 HETATM 3583 O O . HOH O 7 . ? 6.409 -32.339 22.611 1.00 45.78 ? 955 HOH A O 1 HETATM 3584 O O . HOH O 7 . ? 27.911 -39.741 -0.181 1.00 43.78 ? 956 HOH A O 1 HETATM 3585 O O . HOH O 7 . ? 39.177 -42.492 22.531 1.00 44.97 ? 957 HOH A O 1 HETATM 3586 O O . HOH O 7 . ? 4.036 -84.219 9.174 1.00 46.50 ? 958 HOH A O 1 HETATM 3587 O O . HOH O 7 . ? 32.160 -70.065 37.733 1.00 45.04 ? 959 HOH A O 1 HETATM 3588 O O . HOH O 7 . ? 3.970 -83.407 15.576 1.00 49.14 ? 960 HOH A O 1 HETATM 3589 O O . HOH O 7 . ? 4.431 -86.365 9.639 1.00 53.85 ? 961 HOH A O 1 HETATM 3590 O O . HOH O 7 . ? 1.665 -53.807 4.936 1.00 47.28 ? 962 HOH A O 1 HETATM 3591 O O . HOH O 7 . ? 28.342 -30.972 25.701 1.00 43.60 ? 963 HOH A O 1 HETATM 3592 O O . HOH O 7 . ? -0.400 -67.600 31.697 1.00 53.39 ? 964 HOH A O 1 HETATM 3593 O O . HOH O 7 . ? 10.784 -30.665 25.272 1.00 47.42 ? 965 HOH A O 1 HETATM 3594 O O . HOH O 7 . ? 30.156 -61.618 21.694 1.00 26.10 ? 966 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 ? 0.7650 0.7018 0.7177 0.0075 0.0096 0.0049 83 ARG A N 2 C CA . ARG A 1 ? 0.6871 0.6280 0.6413 0.0052 0.0088 0.0029 83 ARG A CA 3 C C . ARG A 1 ? 0.6447 0.5821 0.5966 0.0013 0.0092 0.0013 83 ARG A C 4 O O . ARG A 1 ? 0.5579 0.4928 0.5084 -0.0007 0.0093 0.0019 83 ARG A O 5 C CB . ARG A 1 ? 0.6538 0.6025 0.6115 0.0047 0.0071 0.0035 83 ARG A CB 6 C CG . ARG A 1 ? 0.7522 0.7065 0.7129 0.0068 0.0065 0.0032 83 ARG A CG 7 C CD . ARG A 1 ? 0.8155 0.7767 0.7792 0.0057 0.0048 0.0034 83 ARG A CD 8 N NE . ARG A 1 ? 0.7956 0.7621 0.7622 0.0075 0.0042 0.0034 83 ARG A NE 9 C CZ . ARG A 1 ? 0.8196 0.7920 0.7889 0.0070 0.0029 0.0034 83 ARG A CZ 10 N NH1 . ARG A 1 ? 0.8100 0.7840 0.7795 0.0048 0.0020 0.0036 83 ARG A NH1 11 N NH2 . ARG A 1 ? 0.7089 0.6857 0.6807 0.0085 0.0024 0.0034 83 ARG A NH2 12 N N . ASN A 2 ? 0.6096 0.5469 0.5611 0.0003 0.0094 -0.0008 84 ASN A N 13 C CA . ASN A 2 ? 0.5589 0.4937 0.5085 -0.0034 0.0096 -0.0025 84 ASN A CA 14 C C . ASN A 2 ? 0.4994 0.4406 0.4513 -0.0055 0.0082 -0.0037 84 ASN A C 15 O O . ASN A 2 ? 0.4321 0.3782 0.3865 -0.0039 0.0075 -0.0037 84 ASN A O 16 C CB . ASN A 2 ? 0.6028 0.5313 0.5492 -0.0032 0.0111 -0.0041 84 ASN A CB 17 C CG . ASN A 2 ? 0.7322 0.6537 0.6761 -0.0009 0.0126 -0.0030 84 ASN A CG 18 O OD1 . ASN A 2 ? 0.7207 0.6374 0.6624 -0.0024 0.0132 -0.0024 84 ASN A OD1 19 N ND2 . ASN A 2 ? 0.6301 0.5511 0.5743 0.0029 0.0134 -0.0027 84 ASN A ND2 20 N N . PHE A 3 ? 0.3834 0.3244 0.3344 -0.0091 0.0077 -0.0046 85 PHE A N 21 C CA . PHE A 3 ? 0.3372 0.2836 0.2900 -0.0112 0.0066 -0.0058 85 PHE A CA 22 C C . PHE A 3 ? 0.3677 0.3135 0.3197 -0.0104 0.0070 -0.0074 85 PHE A C 23 O O . PHE A 3 ? 0.3895 0.3295 0.3385 -0.0102 0.0083 -0.0084 85 PHE A O 24 C CB . PHE A 3 ? 0.3245 0.2699 0.2760 -0.0152 0.0063 -0.0066 85 PHE A CB 25 C CG . PHE A 3 ? 0.4149 0.3625 0.3677 -0.0164 0.0057 -0.0052 85 PHE A CG 26 C CD1 . PHE A 3 ? 0.3469 0.3006 0.3029 -0.0153 0.0045 -0.0040 85 PHE A CD1 27 C CD2 . PHE A 3 ? 0.3930 0.3362 0.3435 -0.0188 0.0064 -0.0050 85 PHE A CD2 28 C CE1 . PHE A 3 ? 0.3326 0.2883 0.2896 -0.0164 0.0041 -0.0028 85 PHE A CE1 29 C CE2 . PHE A 3 ? 0.4320 0.3773 0.3835 -0.0200 0.0059 -0.0036 85 PHE A CE2 30 C CZ . PHE A 3 ? 0.3374 0.2890 0.2922 -0.0187 0.0048 -0.0025 85 PHE A CZ 31 N N . ASN A 4 ? 0.3602 0.3117 0.3147 -0.0100 0.0060 -0.0078 86 ASN A N 32 C CA . ASN A 4 ? 0.3481 0.2997 0.3018 -0.0096 0.0064 -0.0093 86 ASN A CA 33 C C . ASN A 4 ? 0.3512 0.3014 0.3027 -0.0129 0.0063 -0.0112 86 ASN A C 34 O O . ASN A 4 ? 0.2980 0.2510 0.2503 -0.0156 0.0052 -0.0113 86 ASN A O 35 C CB . ASN A 4 ? 0.3094 0.2674 0.2663 -0.0082 0.0055 -0.0090 86 ASN A CB 36 C CG . ASN A 4 ? 0.3682 0.3264 0.3242 -0.0079 0.0059 -0.0105 86 ASN A CG 37 O OD1 . ASN A 4 ? 0.4070 0.3689 0.3638 -0.0094 0.0050 -0.0112 86 ASN A OD1 38 N ND2 . ASN A 4 ? 0.2844 0.2387 0.2387 -0.0057 0.0073 -0.0109 86 ASN A ND2 39 N N . ASN A 5 ? 0.3025 0.2484 0.2511 -0.0128 0.0074 -0.0128 87 ASN A N 40 C CA . ASN A 5 ? 0.2925 0.2374 0.2389 -0.0159 0.0073 -0.0148 87 ASN A CA 41 C C . ASN A 5 ? 0.2988 0.2469 0.2454 -0.0153 0.0070 -0.0159 87 ASN A C 42 O O . ASN A 5 ? 0.3492 0.2969 0.2960 -0.0124 0.0079 -0.0158 87 ASN A O 43 C CB . ASN A 5 ? 0.4058 0.3427 0.3479 -0.0169 0.0088 -0.0161 87 ASN A CB 44 C CG . ASN A 5 ? 0.4662 0.3994 0.4077 -0.0178 0.0091 -0.0149 87 ASN A CG 45 O OD1 . ASN A 5 ? 0.4405 0.3769 0.3837 -0.0197 0.0080 -0.0140 87 ASN A OD1 46 N ND2 . ASN A 5 ? 0.5094 0.4355 0.4482 -0.0164 0.0108 -0.0149 87 ASN A ND2 47 N N . LEU A 6 ? 0.3216 0.2731 0.2683 -0.0179 0.0059 -0.0168 88 LEU A N 48 C CA . LEU A 6 ? 0.3429 0.2974 0.2894 -0.0176 0.0056 -0.0178 88 LEU A CA 49 C C . LEU A 6 ? 0.3479 0.2971 0.2903 -0.0181 0.0070 -0.0199 88 LEU A C 50 O O . LEU A 6 ? 0.3774 0.3257 0.3174 -0.0211 0.0066 -0.0215 88 LEU A O 51 C CB . LEU A 6 ? 0.2879 0.2479 0.2358 -0.0202 0.0039 -0.0180 88 LEU A CB 52 C CG . LEU A 6 ? 0.3728 0.3377 0.3246 -0.0199 0.0026 -0.0161 88 LEU A CG 53 C CD1 . LEU A 6 ? 0.2177 0.1877 0.1707 -0.0224 0.0010 -0.0163 88 LEU A CD1 54 C CD2 . LEU A 6 ? 0.2970 0.2649 0.2515 -0.0167 0.0027 -0.0148 88 LEU A CD2 55 N N . THR A 7 ? 0.3615 0.3075 0.3030 -0.0152 0.0085 -0.0200 89 THR A N 56 C CA . THR A 7 ? 0.4298 0.3699 0.3671 -0.0153 0.0101 -0.0220 89 THR A CA 57 C C . THR A 7 ? 0.4498 0.3916 0.3863 -0.0139 0.0106 -0.0230 89 THR A C 58 O O . THR A 7 ? 0.4022 0.3395 0.3351 -0.0140 0.0120 -0.0249 89 THR A O 59 C CB . THR A 7 ? 0.4300 0.3638 0.3660 -0.0129 0.0118 -0.0216 89 THR A CB 60 O OG1 . THR A 7 ? 0.4403 0.3769 0.3793 -0.0092 0.0121 -0.0199 89 THR A OG1 61 C CG2 . THR A 7 ? 0.3796 0.3105 0.3155 -0.0145 0.0115 -0.0207 89 THR A CG2 62 N N . LYS A 8 ? 0.3004 0.2487 0.2402 -0.0126 0.0097 -0.0218 90 LYS A N 63 C CA . LYS A 8 ? 0.3065 0.2568 0.2459 -0.0111 0.0104 -0.0225 90 LYS A CA 64 C C . LYS A 8 ? 0.3399 0.2952 0.2795 -0.0133 0.0089 -0.0229 90 LYS A C 65 O O . LYS A 8 ? 0.3751 0.3339 0.3165 -0.0152 0.0072 -0.0222 90 LYS A O 66 C CB . LYS A 8 ? 0.3679 0.3212 0.3107 -0.0076 0.0108 -0.0207 90 LYS A CB 67 C CG . LYS A 8 ? 0.3148 0.2637 0.2577 -0.0050 0.0121 -0.0200 90 LYS A CG 68 C CD . LYS A 8 ? 0.4031 0.3563 0.3500 -0.0019 0.0121 -0.0180 90 LYS A CD 69 C CE . LYS A 8 ? 0.4482 0.3973 0.3951 0.0009 0.0134 -0.0172 90 LYS A CE 70 N NZ . LYS A 8 ? 0.3932 0.3468 0.3441 0.0037 0.0131 -0.0152 90 LYS A NZ 71 N N . GLY A 9 ? 0.3357 0.2916 0.2734 -0.0128 0.0096 -0.0241 91 GLY A N 72 C CA . GLY A 9 ? 0.3669 0.3281 0.3051 -0.0142 0.0084 -0.0241 91 GLY A CA 73 C C . GLY A 9 ? 0.3540 0.3203 0.2960 -0.0119 0.0081 -0.0223 91 GLY A C 74 O O . GLY A 9 ? 0.3576 0.3232 0.3014 -0.0092 0.0091 -0.0213 91 GLY A O 75 N N . LEU A 10 ? 0.2805 0.2519 0.2236 -0.0128 0.0069 -0.0217 92 LEU A N 76 C CA . LEU A 10 ? 0.3308 0.3068 0.2771 -0.0108 0.0068 -0.0201 92 LEU A CA 77 C C . LEU A 10 ? 0.3565 0.3317 0.3015 -0.0087 0.0086 -0.0207 92 LEU A C 78 O O . LEU A 10 ? 0.3346 0.3071 0.2758 -0.0093 0.0095 -0.0224 92 LEU A O 79 C CB . LEU A 10 ? 0.3111 0.2922 0.2585 -0.0124 0.0051 -0.0194 92 LEU A CB 80 C CG . LEU A 10 ? 0.3078 0.2908 0.2567 -0.0144 0.0032 -0.0187 92 LEU A CG 81 C CD1 . LEU A 10 ? 0.3308 0.3186 0.2803 -0.0156 0.0018 -0.0181 92 LEU A CD1 82 C CD2 . LEU A 10 ? 0.2905 0.2744 0.2432 -0.0131 0.0029 -0.0170 92 LEU A CD2 83 N N . CYS A 11 ? 0.2662 0.2438 0.2143 -0.0063 0.0091 -0.0192 93 CYS A N 84 C CA . CYS A 11 ? 0.2599 0.2381 0.2073 -0.0044 0.0107 -0.0195 93 CYS A CA 85 C C . CYS A 11 ? 0.3204 0.3020 0.2667 -0.0057 0.0102 -0.0197 93 CYS A C 86 O O . CYS A 11 ? 0.2467 0.2314 0.1943 -0.0074 0.0084 -0.0188 93 CYS A O 87 C CB . CYS A 11 ? 0.3767 0.3577 0.3282 -0.0018 0.0112 -0.0178 93 CYS A CB 88 S SG . CYS A 11 ? 0.3598 0.3374 0.3128 0.0002 0.0117 -0.0173 93 CYS A SG 89 N N . THR A 12 ? 0.3330 0.3140 0.2769 -0.0049 0.0117 -0.0207 94 THR A N 90 C CA . THR A 12 ? 0.3029 0.2872 0.2455 -0.0059 0.0114 -0.0207 94 THR A CA 91 C C . THR A 12 ? 0.3104 0.2998 0.2571 -0.0050 0.0108 -0.0184 94 THR A C 92 O O . THR A 12 ? 0.2760 0.2664 0.2255 -0.0029 0.0118 -0.0175 94 THR A O 93 C CB . THR A 12 ? 0.3594 0.3420 0.2986 -0.0049 0.0135 -0.0222 94 THR A CB 94 O OG1 . THR A 12 ? 0.3670 0.3445 0.3019 -0.0060 0.0140 -0.0245 94 THR A OG1 95 C CG2 . THR A 12 ? 0.3073 0.2937 0.2453 -0.0057 0.0132 -0.0219 94 THR A CG2 96 N N . ILE A 13 ? 0.3320 0.3246 0.2793 -0.0067 0.0092 -0.0175 95 ILE A N 97 C CA . ILE A 13 ? 0.2571 0.2541 0.2081 -0.0062 0.0085 -0.0154 95 ILE A CA 98 C C . ILE A 13 ? 0.2398 0.2395 0.1896 -0.0060 0.0092 -0.0151 95 ILE A C 99 O O . ILE A 13 ? 0.2923 0.2931 0.2399 -0.0076 0.0084 -0.0152 95 ILE A O 100 C CB . ILE A 13 ? 0.2819 0.2809 0.2345 -0.0079 0.0063 -0.0144 95 ILE A CB 101 C CG1 . ILE A 13 ? 0.2402 0.2367 0.1938 -0.0083 0.0055 -0.0148 95 ILE A CG1 102 C CG2 . ILE A 13 ? 0.2886 0.2915 0.2448 -0.0074 0.0056 -0.0123 95 ILE A CG2 103 C CD1 . ILE A 13 ? 0.2508 0.2484 0.2044 -0.0104 0.0036 -0.0146 95 ILE A CD1 104 N N . ASN A 14 ? 0.2768 0.2776 0.2281 -0.0042 0.0108 -0.0146 96 ASN A N 105 C CA . ASN A 14 ? 0.3261 0.3296 0.2765 -0.0040 0.0117 -0.0140 96 ASN A CA 106 C C . ASN A 14 ? 0.3370 0.3446 0.2913 -0.0038 0.0111 -0.0118 96 ASN A C 107 O O . ASN A 14 ? 0.3072 0.3172 0.2608 -0.0042 0.0114 -0.0109 96 ASN A O 108 C CB . ASN A 14 ? 0.2845 0.2868 0.2334 -0.0022 0.0141 -0.0152 96 ASN A CB 109 C CG . ASN A 14 ? 0.3306 0.3288 0.2746 -0.0027 0.0149 -0.0175 96 ASN A CG 110 O OD1 . ASN A 14 ? 0.3223 0.3199 0.2633 -0.0047 0.0138 -0.0183 96 ASN A OD1 111 N ND2 . ASN A 14 ? 0.2848 0.2802 0.2281 -0.0009 0.0167 -0.0188 96 ASN A ND2 112 N N . SER A 15 ? 0.3556 0.3636 0.3136 -0.0033 0.0104 -0.0109 97 SER A N 113 C CA . SER A 15 ? 0.3090 0.3204 0.2707 -0.0034 0.0096 -0.0089 97 SER A CA 114 C C . SER A 15 ? 0.2840 0.2950 0.2489 -0.0031 0.0085 -0.0084 97 SER A C 115 O O . SER A 15 ? 0.2656 0.2739 0.2298 -0.0029 0.0083 -0.0094 97 SER A O 116 C CB . SER A 15 ? 0.2573 0.2712 0.2206 -0.0022 0.0112 -0.0081 97 SER A CB 117 O OG . SER A 15 ? 0.2998 0.3129 0.2642 -0.0003 0.0126 -0.0088 97 SER A OG 118 N N . TRP A 16 ? 0.2358 0.2494 0.2041 -0.0032 0.0077 -0.0068 98 TRP A N 119 C CA . TRP A 16 ? 0.2222 0.2358 0.1936 -0.0029 0.0067 -0.0063 98 TRP A CA 120 C C . TRP A 16 ? 0.3043 0.3203 0.2792 -0.0018 0.0074 -0.0054 98 TRP A C 121 O O . TRP A 16 ? 0.2645 0.2830 0.2404 -0.0020 0.0078 -0.0044 98 TRP A O 122 C CB . TRP A 16 ? 0.2294 0.2436 0.2015 -0.0043 0.0048 -0.0055 98 TRP A CB 123 C CG . TRP A 16 ? 0.3091 0.3215 0.2779 -0.0056 0.0040 -0.0064 98 TRP A CG 124 C CD1 . TRP A 16 ? 0.2641 0.2770 0.2303 -0.0065 0.0039 -0.0064 98 TRP A CD1 125 C CD2 . TRP A 16 ? 0.2377 0.2478 0.2056 -0.0061 0.0033 -0.0074 98 TRP A CD2 126 N NE1 . TRP A 16 ? 0.2699 0.2813 0.2338 -0.0076 0.0030 -0.0074 98 TRP A NE1 127 C CE2 . TRP A 16 ? 0.2940 0.3036 0.2590 -0.0075 0.0026 -0.0080 98 TRP A CE2 128 C CE3 . TRP A 16 ? 0.2658 0.2743 0.2351 -0.0056 0.0030 -0.0077 98 TRP A CE3 129 C CZ2 . TRP A 16 ? 0.2418 0.2494 0.2052 -0.0085 0.0018 -0.0091 98 TRP A CZ2 130 C CZ3 . TRP A 16 ? 0.2683 0.2746 0.2360 -0.0065 0.0023 -0.0087 98 TRP A CZ3 131 C CH2 . TRP A 16 ? 0.1974 0.2033 0.1623 -0.0081 0.0017 -0.0094 98 TRP A CH2 132 N N . HIS A 17 ? 0.2095 0.2249 0.1861 -0.0006 0.0075 -0.0056 99 HIS A N 133 C CA . HIS A 17 ? 0.2269 0.2450 0.2071 0.0004 0.0079 -0.0048 99 HIS A CA 134 C C . HIS A 17 ? 0.2087 0.2275 0.1916 -0.0001 0.0063 -0.0040 99 HIS A C 135 O O . HIS A 17 ? 0.2146 0.2314 0.1967 -0.0006 0.0052 -0.0044 99 HIS A O 136 C CB . HIS A 17 ? 0.1986 0.2161 0.1789 0.0024 0.0093 -0.0054 99 HIS A CB 137 C CG . HIS A 17 ? 0.2530 0.2677 0.2330 0.0032 0.0087 -0.0060 99 HIS A CG 138 N ND1 . HIS A 17 ? 0.2659 0.2817 0.2488 0.0036 0.0078 -0.0053 99 HIS A ND1 139 C CD2 . HIS A 17 ? 0.2889 0.2997 0.2660 0.0034 0.0091 -0.0072 99 HIS A CD2 140 C CE1 . HIS A 17 ? 0.2674 0.2801 0.2492 0.0042 0.0076 -0.0059 99 HIS A CE1 141 N NE2 . HIS A 17 ? 0.3265 0.3360 0.3048 0.0041 0.0084 -0.0070 99 HIS A NE2 142 N N . ILE A 18 ? 0.2268 0.2486 0.2128 0.0000 0.0063 -0.0030 100 ILE A N 143 C CA . ILE A 18 ? 0.2616 0.2842 0.2502 -0.0004 0.0049 -0.0025 100 ILE A CA 144 C C . ILE A 18 ? 0.2511 0.2724 0.2401 0.0008 0.0047 -0.0030 100 ILE A C 145 O O . ILE A 18 ? 0.2393 0.2606 0.2283 0.0024 0.0058 -0.0033 100 ILE A O 146 C CB . ILE A 18 ? 0.2457 0.2718 0.2374 -0.0007 0.0050 -0.0015 100 ILE A CB 147 C CG1 . ILE A 18 ? 0.2039 0.2305 0.1978 -0.0013 0.0035 -0.0011 100 ILE A CG1 148 C CG2 . ILE A 18 ? 0.1907 0.2191 0.1841 0.0008 0.0063 -0.0015 100 ILE A CG2 149 C CD1 . ILE A 18 ? 0.1790 0.2039 0.1718 -0.0027 0.0023 -0.0009 100 ILE A CD1 150 N N . TYR A 19 ? 0.2303 0.2503 0.2194 0.0002 0.0033 -0.0030 101 TYR A N 151 C CA . TYR A 19 ? 0.1794 0.1980 0.1686 0.0012 0.0030 -0.0033 101 TYR A CA 152 C C . TYR A 19 ? 0.2327 0.2531 0.2247 0.0011 0.0019 -0.0026 101 TYR A C 153 O O . TYR A 19 ? 0.2145 0.2359 0.2079 0.0024 0.0020 -0.0024 101 TYR A O 154 C CB . TYR A 19 ? 0.1763 0.1914 0.1628 0.0005 0.0025 -0.0040 101 TYR A CB 155 C CG . TYR A 19 ? 0.1769 0.1900 0.1632 0.0012 0.0022 -0.0042 101 TYR A CG 156 C CD1 . TYR A 19 ? 0.2916 0.3030 0.2771 0.0028 0.0032 -0.0045 101 TYR A CD1 157 C CD2 . TYR A 19 ? 0.2394 0.2523 0.2263 0.0003 0.0009 -0.0039 101 TYR A CD2 158 C CE1 . TYR A 19 ? 0.2732 0.2825 0.2583 0.0035 0.0030 -0.0045 101 TYR A CE1 159 C CE2 . TYR A 19 ? 0.2099 0.2209 0.1964 0.0009 0.0006 -0.0040 101 TYR A CE2 160 C CZ . TYR A 19 ? 0.2353 0.2445 0.2209 0.0024 0.0017 -0.0042 101 TYR A CZ 161 O OH . TYR A 19 ? 0.2641 0.2712 0.2492 0.0030 0.0015 -0.0041 101 TYR A OH 162 N N . GLY A 20 ? 0.2008 0.2218 0.1934 -0.0003 0.0009 -0.0023 102 GLY A N 163 C CA . GLY A 20 ? 0.2010 0.2235 0.1959 -0.0006 -0.0002 -0.0018 102 GLY A CA 164 C C . GLY A 20 ? 0.2762 0.2998 0.2721 -0.0021 -0.0009 -0.0014 102 GLY A C 165 O O . GLY A 20 ? 0.2596 0.2820 0.2539 -0.0029 -0.0010 -0.0015 102 GLY A O 166 N N . LYS A 21 ? 0.2626 0.2883 0.2608 -0.0023 -0.0014 -0.0011 103 LYS A N 167 C CA . LYS A 21 ? 0.2085 0.2348 0.2077 -0.0037 -0.0020 -0.0007 103 LYS A CA 168 C C . LYS A 21 ? 0.2535 0.2814 0.2548 -0.0038 -0.0028 -0.0007 103 LYS A C 169 O O . LYS A 21 ? 0.2569 0.2870 0.2599 -0.0032 -0.0025 -0.0006 103 LYS A O 170 C CB . LYS A 21 ? 0.1785 0.2062 0.1782 -0.0042 -0.0011 -0.0002 103 LYS A CB 171 C CG . LYS A 21 ? 0.1894 0.2169 0.1896 -0.0056 -0.0016 0.0003 103 LYS A CG 172 C CD . LYS A 21 ? 0.2469 0.2759 0.2477 -0.0062 -0.0006 0.0009 103 LYS A CD 173 C CE . LYS A 21 ? 0.2735 0.3013 0.2739 -0.0074 -0.0009 0.0016 103 LYS A CE 174 N NZ . LYS A 21 ? 0.2107 0.2379 0.2123 -0.0081 -0.0019 0.0015 103 LYS A NZ 175 N N . ASP A 22 ? 0.2261 0.2531 0.2275 -0.0046 -0.0037 -0.0008 104 ASP A N 176 C CA . ASP A 22 ? 0.1963 0.2248 0.1995 -0.0047 -0.0045 -0.0010 104 ASP A CA 177 C C . ASP A 22 ? 0.1973 0.2270 0.2022 -0.0060 -0.0047 -0.0008 104 ASP A C 178 O O . ASP A 22 ? 0.1866 0.2180 0.1930 -0.0062 -0.0052 -0.0010 104 ASP A O 179 C CB . ASP A 22 ? 0.2293 0.2564 0.2317 -0.0045 -0.0053 -0.0013 104 ASP A CB 180 C CG . ASP A 22 ? 0.2140 0.2391 0.2152 -0.0052 -0.0057 -0.0014 104 ASP A CG 181 O OD1 . ASP A 22 ? 0.2266 0.2513 0.2277 -0.0059 -0.0054 -0.0011 104 ASP A OD1 182 O OD2 . ASP A 22 ? 0.2327 0.2568 0.2332 -0.0051 -0.0063 -0.0017 104 ASP A OD2 183 N N . ASN A 23 ? 0.1636 0.1923 0.1680 -0.0068 -0.0044 -0.0005 105 ASN A N 184 C CA . ASN A 23 ? 0.2282 0.2573 0.2339 -0.0081 -0.0045 -0.0003 105 ASN A CA 185 C C . ASN A 23 ? 0.2052 0.2337 0.2114 -0.0086 -0.0055 -0.0009 105 ASN A C 186 O O . ASN A 23 ? 0.1978 0.2273 0.2055 -0.0096 -0.0057 -0.0011 105 ASN A O 187 C CB . ASN A 23 ? 0.1699 0.2020 0.1776 -0.0085 -0.0039 -0.0001 105 ASN A CB 188 C CG . ASN A 23 ? 0.2525 0.2853 0.2597 -0.0081 -0.0027 0.0004 105 ASN A CG 189 O OD1 . ASN A 23 ? 0.2145 0.2462 0.2208 -0.0087 -0.0022 0.0010 105 ASN A OD1 190 N ND2 . ASN A 23 ? 0.2005 0.2351 0.2082 -0.0069 -0.0023 0.0003 105 ASN A ND2 191 N N . ALA A 24 ? 0.2174 0.2442 0.2223 -0.0080 -0.0060 -0.0012 106 ALA A N 192 C CA . ALA A 24 ? 0.2242 0.2507 0.2294 -0.0082 -0.0068 -0.0018 106 ALA A CA 193 C C . ALA A 24 ? 0.2486 0.2741 0.2544 -0.0093 -0.0071 -0.0020 106 ALA A C 194 O O . ALA A 24 ? 0.2195 0.2456 0.2261 -0.0098 -0.0076 -0.0026 106 ALA A O 195 C CB . ALA A 24 ? 0.2202 0.2451 0.2238 -0.0074 -0.0072 -0.0020 106 ALA A CB 196 N N . VAL A 25 ? 0.1880 0.2118 0.1932 -0.0096 -0.0066 -0.0014 107 VAL A N 197 C CA . VAL A 25 ? 0.2616 0.2837 0.2671 -0.0105 -0.0067 -0.0015 107 VAL A CA 198 C C . VAL A 25 ? 0.2388 0.2621 0.2458 -0.0119 -0.0065 -0.0015 107 VAL A C 199 O O . VAL A 25 ? 0.2735 0.2960 0.2811 -0.0128 -0.0068 -0.0022 107 VAL A O 200 C CB . VAL A 25 ? 0.2493 0.2692 0.2536 -0.0103 -0.0064 -0.0006 107 VAL A CB 201 C CG1 . VAL A 25 ? 0.2155 0.2331 0.2199 -0.0109 -0.0065 -0.0007 107 VAL A CG1 202 C CG2 . VAL A 25 ? 0.2073 0.2268 0.2103 -0.0091 -0.0067 -0.0006 107 VAL A CG2 203 N N . ARG A 26 ? 0.2387 0.2637 0.2463 -0.0121 -0.0058 -0.0010 108 ARG A N 204 C CA . ARG A 26 ? 0.2281 0.2550 0.2375 -0.0135 -0.0055 -0.0010 108 ARG A CA 205 C C . ARG A 26 ? 0.2624 0.2914 0.2730 -0.0138 -0.0063 -0.0020 108 ARG A C 206 O O . ARG A 26 ? 0.2552 0.2844 0.2668 -0.0152 -0.0065 -0.0025 108 ARG A O 207 C CB . ARG A 26 ? 0.2168 0.2460 0.2267 -0.0133 -0.0047 -0.0002 108 ARG A CB 208 C CG . ARG A 26 ? 0.2334 0.2611 0.2422 -0.0134 -0.0037 0.0008 108 ARG A CG 209 C CD . ARG A 26 ? 0.2135 0.2437 0.2225 -0.0129 -0.0028 0.0013 108 ARG A CD 210 N NE . ARG A 26 ? 0.1763 0.2099 0.1877 -0.0137 -0.0026 0.0012 108 ARG A NE 211 C CZ . ARG A 26 ? 0.2324 0.2668 0.2449 -0.0154 -0.0019 0.0017 108 ARG A CZ 212 N NH1 . ARG A 26 ? 0.2385 0.2703 0.2500 -0.0162 -0.0014 0.0024 108 ARG A NH1 213 N NH2 . ARG A 26 ? 0.2394 0.2775 0.2543 -0.0162 -0.0018 0.0015 108 ARG A NH2 214 N N . ILE A 27 ? 0.2093 0.2399 0.2197 -0.0124 -0.0066 -0.0022 109 ILE A N 215 C CA . ILE A 27 ? 0.2213 0.2544 0.2328 -0.0125 -0.0074 -0.0029 109 ILE A CA 216 C C . ILE A 27 ? 0.2868 0.3181 0.2976 -0.0128 -0.0082 -0.0038 109 ILE A C 217 O O . ILE A 27 ? 0.2557 0.2884 0.2674 -0.0138 -0.0088 -0.0046 109 ILE A O 218 C CB . ILE A 27 ? 0.2299 0.2647 0.2412 -0.0107 -0.0075 -0.0027 109 ILE A CB 219 C CG1 . ILE A 27 ? 0.2348 0.2715 0.2469 -0.0104 -0.0066 -0.0019 109 ILE A CG1 220 C CG2 . ILE A 27 ? 0.2362 0.2733 0.2482 -0.0105 -0.0084 -0.0032 109 ILE A CG2 221 C CD1 . ILE A 27 ? 0.1680 0.2054 0.1795 -0.0085 -0.0063 -0.0016 109 ILE A CD1 222 N N . GLY A 28 ? 0.2031 0.2315 0.2123 -0.0121 -0.0082 -0.0038 110 GLY A N 223 C CA . GLY A 28 ? 0.2171 0.2437 0.2255 -0.0122 -0.0088 -0.0047 110 GLY A CA 224 C C . GLY A 28 ? 0.2867 0.3114 0.2953 -0.0137 -0.0087 -0.0052 110 GLY A C 225 O O . GLY A 28 ? 0.2275 0.2508 0.2355 -0.0138 -0.0091 -0.0061 110 GLY A O 226 N N . GLU A 29 ? 0.2035 0.2281 0.2129 -0.0148 -0.0081 -0.0047 111 GLU A N 227 C CA . GLU A 29 ? 0.2283 0.2510 0.2380 -0.0165 -0.0080 -0.0052 111 GLU A CA 228 C C . GLU A 29 ? 0.2473 0.2720 0.2580 -0.0177 -0.0087 -0.0065 111 GLU A C 229 O O . GLU A 29 ? 0.2142 0.2370 0.2246 -0.0189 -0.0089 -0.0075 111 GLU A O 230 C CB . GLU A 29 ? 0.2338 0.2563 0.2443 -0.0176 -0.0072 -0.0042 111 GLU A CB 231 C CG . GLU A 29 ? 0.2390 0.2586 0.2495 -0.0194 -0.0069 -0.0046 111 GLU A CG 232 C CD . GLU A 29 ? 0.2501 0.2718 0.2621 -0.0215 -0.0072 -0.0056 111 GLU A CD 233 O OE1 . GLU A 29 ? 0.2751 0.3010 0.2886 -0.0217 -0.0074 -0.0054 111 GLU A OE1 234 O OE2 . GLU A 29 ? 0.2254 0.2447 0.2371 -0.0229 -0.0073 -0.0065 111 GLU A OE2 235 N N . SER A 30 ? 0.2022 0.2307 0.2138 -0.0172 -0.0092 -0.0064 112 SER A N 236 C CA . SER A 30 ? 0.2697 0.3011 0.2823 -0.0183 -0.0100 -0.0075 112 SER A CA 237 C C . SER A 30 ? 0.2844 0.3190 0.2971 -0.0168 -0.0106 -0.0073 112 SER A C 238 O O . SER A 30 ? 0.3429 0.3813 0.3572 -0.0170 -0.0108 -0.0071 112 SER A O 239 C CB . SER A 30 ? 0.2854 0.3190 0.2999 -0.0202 -0.0097 -0.0073 112 SER A CB 240 O OG . SER A 30 ? 0.4518 0.4880 0.4673 -0.0217 -0.0106 -0.0085 112 SER A OG 241 N N A SER A 31 ? 0.2857 0.3188 0.2969 -0.0153 -0.0108 -0.0074 113 SER A N 242 N N B SER A 31 ? 0.2865 0.3195 0.2976 -0.0153 -0.0108 -0.0074 113 SER A N 243 C CA A SER A 31 ? 0.2647 0.2999 0.2755 -0.0138 -0.0114 -0.0072 113 SER A CA 244 C CA B SER A 31 ? 0.2646 0.2999 0.2755 -0.0138 -0.0113 -0.0072 113 SER A CA 245 C C A SER A 31 ? 0.2511 0.2837 0.2600 -0.0128 -0.0114 -0.0075 113 SER A C 246 C C B SER A 31 ? 0.2512 0.2838 0.2601 -0.0127 -0.0114 -0.0075 113 SER A C 247 O O A SER A 31 ? 0.2384 0.2680 0.2465 -0.0128 -0.0110 -0.0076 113 SER A O 248 O O B SER A 31 ? 0.2378 0.2674 0.2459 -0.0127 -0.0110 -0.0075 113 SER A O 249 C CB A SER A 31 ? 0.2434 0.2803 0.2548 -0.0126 -0.0109 -0.0060 113 SER A CB 250 C CB B SER A 31 ? 0.2427 0.2795 0.2542 -0.0126 -0.0108 -0.0060 113 SER A CB 251 O OG A SER A 31 ? 0.3074 0.3476 0.3208 -0.0134 -0.0108 -0.0057 113 SER A OG 252 O OG B SER A 31 ? 0.3129 0.3534 0.3263 -0.0132 -0.0109 -0.0057 113 SER A OG 253 N N . ASP A 32 ? 0.1658 0.2000 0.1741 -0.0118 -0.0120 -0.0076 114 ASP A N 254 C CA . ASP A 32 ? 0.2140 0.2461 0.2205 -0.0108 -0.0121 -0.0078 114 ASP A CA 255 C C . ASP A 32 ? 0.1850 0.2160 0.1909 -0.0095 -0.0115 -0.0068 114 ASP A C 256 O O . ASP A 32 ? 0.1881 0.2199 0.1933 -0.0084 -0.0116 -0.0063 114 ASP A O 257 C CB . ASP A 32 ? 0.1647 0.1988 0.1706 -0.0106 -0.0129 -0.0084 114 ASP A CB 258 C CG . ASP A 32 ? 0.2488 0.2838 0.2550 -0.0121 -0.0135 -0.0096 114 ASP A CG 259 O OD1 . ASP A 32 ? 0.2226 0.2554 0.2289 -0.0132 -0.0132 -0.0104 114 ASP A OD1 260 O OD2 . ASP A 32 ? 0.2811 0.3189 0.2873 -0.0122 -0.0143 -0.0099 114 ASP A OD2 261 N N . VAL A 33 ? 0.2282 0.2572 0.2341 -0.0096 -0.0108 -0.0064 115 VAL A N 262 C CA . VAL A 33 ? 0.2431 0.2710 0.2484 -0.0086 -0.0103 -0.0055 115 VAL A CA 263 C C . VAL A 33 ? 0.2232 0.2488 0.2272 -0.0082 -0.0102 -0.0057 115 VAL A C 264 O O . VAL A 33 ? 0.2261 0.2501 0.2301 -0.0088 -0.0101 -0.0061 115 VAL A O 265 C CB . VAL A 33 ? 0.2745 0.3021 0.2805 -0.0090 -0.0097 -0.0048 115 VAL A CB 266 C CG1 . VAL A 33 ? 0.2230 0.2489 0.2279 -0.0082 -0.0092 -0.0041 115 VAL A CG1 267 C CG2 . VAL A 33 ? 0.1538 0.1841 0.1611 -0.0091 -0.0096 -0.0045 115 VAL A CG2 268 N N . LEU A 34 ? 0.1548 0.1802 0.1578 -0.0073 -0.0102 -0.0054 116 LEU A N 269 C CA . LEU A 34 ? 0.1951 0.2192 0.1972 -0.0070 -0.0101 -0.0055 116 LEU A CA 270 C C . LEU A 34 ? 0.1904 0.2129 0.1924 -0.0069 -0.0097 -0.0050 116 LEU A C 271 O O . LEU A 34 ? 0.2374 0.2599 0.2395 -0.0069 -0.0094 -0.0044 116 LEU A O 272 C CB . LEU A 34 ? 0.2326 0.2571 0.2337 -0.0063 -0.0102 -0.0052 116 LEU A CB 273 C CG . LEU A 34 ? 0.2155 0.2412 0.2162 -0.0061 -0.0106 -0.0056 116 LEU A CG 274 C CD1 . LEU A 34 ? 0.1600 0.1859 0.1597 -0.0054 -0.0105 -0.0050 116 LEU A CD1 275 C CD2 . LEU A 34 ? 0.1712 0.1966 0.1715 -0.0063 -0.0108 -0.0065 116 LEU A CD2 276 N N . VAL A 35 ? 0.1774 0.1987 0.1793 -0.0069 -0.0097 -0.0053 117 VAL A N 277 C CA . VAL A 35 ? 0.1569 0.1770 0.1586 -0.0066 -0.0094 -0.0047 117 VAL A CA 278 C C . VAL A 35 ? 0.1435 0.1641 0.1443 -0.0060 -0.0094 -0.0042 117 VAL A C 279 O O . VAL A 35 ? 0.2337 0.2550 0.2341 -0.0058 -0.0095 -0.0046 117 VAL A O 280 C CB . VAL A 35 ? 0.2226 0.2413 0.2243 -0.0063 -0.0093 -0.0051 117 VAL A CB 281 C CG1 . VAL A 35 ? 0.1922 0.2102 0.1937 -0.0057 -0.0092 -0.0043 117 VAL A CG1 282 C CG2 . VAL A 35 ? 0.2023 0.2197 0.2045 -0.0070 -0.0093 -0.0056 117 VAL A CG2 283 N N . THR A 36 ? 0.1806 0.2009 0.1811 -0.0060 -0.0092 -0.0035 118 THR A N 284 C CA . THR A 36 ? 0.1950 0.2157 0.1947 -0.0058 -0.0092 -0.0032 118 THR A CA 285 C C . THR A 36 ? 0.2003 0.2206 0.1997 -0.0057 -0.0091 -0.0026 118 THR A C 286 O O . THR A 36 ? 0.2241 0.2437 0.2239 -0.0057 -0.0090 -0.0022 118 THR A O 287 C CB . THR A 36 ? 0.2314 0.2524 0.2306 -0.0059 -0.0090 -0.0030 118 THR A CB 288 O OG1 . THR A 36 ? 0.1870 0.2079 0.1865 -0.0061 -0.0086 -0.0026 118 THR A OG1 289 C CG2 . THR A 36 ? 0.1815 0.2032 0.1810 -0.0058 -0.0091 -0.0034 118 THR A CG2 290 N N . ARG A 37 ? 0.1760 0.1968 0.1746 -0.0057 -0.0092 -0.0024 119 ARG A N 291 C CA . ARG A 37 ? 0.1686 0.1893 0.1665 -0.0058 -0.0092 -0.0018 119 ARG A CA 292 C C . ARG A 37 ? 0.2025 0.2237 0.1993 -0.0061 -0.0092 -0.0019 119 ARG A C 293 O O . ARG A 37 ? 0.1391 0.1603 0.1356 -0.0062 -0.0092 -0.0023 119 ARG A O 294 C CB . ARG A 37 ? 0.1624 0.1833 0.1607 -0.0053 -0.0094 -0.0014 119 ARG A CB 295 C CG . ARG A 37 ? 0.1769 0.1968 0.1753 -0.0052 -0.0093 -0.0007 119 ARG A CG 296 C CD . ARG A 37 ? 0.2515 0.2718 0.2497 -0.0047 -0.0095 0.0002 119 ARG A CD 297 N NE . ARG A 37 ? 0.2431 0.2643 0.2401 -0.0051 -0.0097 0.0004 119 ARG A NE 298 C CZ . ARG A 37 ? 0.2464 0.2690 0.2430 -0.0049 -0.0101 0.0009 119 ARG A CZ 299 N NH1 . ARG A 37 ? 0.1749 0.1981 0.1723 -0.0041 -0.0104 0.0012 119 ARG A NH1 300 N NH2 . ARG A 37 ? 0.2200 0.2433 0.2153 -0.0055 -0.0103 0.0009 119 ARG A NH2 301 N N . GLU A 38 ? 0.1613 0.1827 0.1572 -0.0064 -0.0093 -0.0015 120 GLU A N 302 C CA . GLU A 38 ? 0.1741 0.1956 0.1687 -0.0069 -0.0093 -0.0018 120 GLU A CA 303 C C . GLU A 38 ? 0.2134 0.2337 0.2073 -0.0071 -0.0088 -0.0022 120 GLU A C 304 O O . GLU A 38 ? 0.2031 0.2232 0.1966 -0.0074 -0.0088 -0.0026 120 GLU A O 305 C CB . GLU A 38 ? 0.1805 0.2031 0.1754 -0.0072 -0.0097 -0.0020 120 GLU A CB 306 C CG . GLU A 38 ? 0.1986 0.2227 0.1942 -0.0068 -0.0102 -0.0015 120 GLU A CG 307 C CD . GLU A 38 ? 0.1790 0.2032 0.1761 -0.0059 -0.0102 -0.0014 120 GLU A CD 308 O OE1 . GLU A 38 ? 0.1759 0.1996 0.1734 -0.0058 -0.0100 -0.0019 120 GLU A OE1 309 O OE2 . GLU A 38 ? 0.1908 0.2152 0.1883 -0.0053 -0.0104 -0.0008 120 GLU A OE2 310 N N . PRO A 39 ? 0.2056 0.2253 0.1994 -0.0069 -0.0084 -0.0021 121 PRO A N 311 C CA . PRO A 39 ? 0.1981 0.2170 0.1915 -0.0067 -0.0079 -0.0024 121 PRO A CA 312 C C . PRO A 39 ? 0.2261 0.2438 0.2176 -0.0071 -0.0076 -0.0027 121 PRO A C 313 O O . PRO A 39 ? 0.2229 0.2408 0.2135 -0.0076 -0.0077 -0.0026 121 PRO A O 314 C CB . PRO A 39 ? 0.2423 0.2613 0.2364 -0.0063 -0.0075 -0.0021 121 PRO A CB 315 C CG . PRO A 39 ? 0.2126 0.2319 0.2065 -0.0065 -0.0076 -0.0017 121 PRO A CG 316 C CD . PRO A 39 ? 0.2065 0.2263 0.2006 -0.0067 -0.0083 -0.0016 121 PRO A CD 317 N N . TYR A 40 ? 0.1659 0.1825 0.1568 -0.0068 -0.0071 -0.0029 122 TYR A N 318 C CA . TYR A 40 ? 0.1737 0.1886 0.1626 -0.0069 -0.0065 -0.0033 122 TYR A CA 319 C C . TYR A 40 ? 0.2136 0.2275 0.2025 -0.0060 -0.0058 -0.0034 122 TYR A C 320 O O . TYR A 40 ? 0.2246 0.2395 0.2150 -0.0053 -0.0059 -0.0030 122 TYR A O 321 C CB . TYR A 40 ? 0.1883 0.2023 0.1757 -0.0079 -0.0067 -0.0037 122 TYR A CB 322 C CG . TYR A 40 ? 0.2112 0.2251 0.1990 -0.0082 -0.0070 -0.0037 122 TYR A CG 323 C CD1 . TYR A 40 ? 0.2121 0.2279 0.2014 -0.0083 -0.0076 -0.0034 122 TYR A CD1 324 C CD2 . TYR A 40 ? 0.2013 0.2132 0.1879 -0.0084 -0.0065 -0.0040 122 TYR A CD2 325 C CE1 . TYR A 40 ? 0.2032 0.2191 0.1927 -0.0086 -0.0078 -0.0035 122 TYR A CE1 326 C CE2 . TYR A 40 ? 0.2026 0.2145 0.1893 -0.0087 -0.0067 -0.0039 122 TYR A CE2 327 C CZ . TYR A 40 ? 0.2068 0.2208 0.1950 -0.0089 -0.0074 -0.0036 122 TYR A CZ 328 O OH . TYR A 40 ? 0.2208 0.2350 0.2091 -0.0093 -0.0075 -0.0035 122 TYR A OH 329 N N . VAL A 41 ? 0.2329 0.2449 0.2199 -0.0060 -0.0051 -0.0038 123 VAL A N 330 C CA . VAL A 41 ? 0.1729 0.1836 0.1597 -0.0048 -0.0044 -0.0038 123 VAL A CA 331 C C . VAL A 41 ? 0.2572 0.2651 0.2419 -0.0052 -0.0041 -0.0042 123 VAL A C 332 O O . VAL A 41 ? 0.2351 0.2420 0.2182 -0.0064 -0.0041 -0.0048 123 VAL A O 333 C CB . VAL A 41 ? 0.2955 0.3063 0.2819 -0.0041 -0.0035 -0.0039 123 VAL A CB 334 C CG1 . VAL A 41 ? 0.2540 0.2643 0.2408 -0.0026 -0.0028 -0.0037 123 VAL A CG1 335 C CG2 . VAL A 41 ? 0.2300 0.2433 0.2181 -0.0043 -0.0038 -0.0035 123 VAL A CG2 336 N N . SER A 42 ? 0.2480 0.2547 0.2326 -0.0043 -0.0037 -0.0040 124 SER A N 337 C CA . SER A 42 ? 0.2704 0.2738 0.2529 -0.0047 -0.0033 -0.0043 124 SER A CA 338 C C . SER A 42 ? 0.2856 0.2876 0.2680 -0.0029 -0.0025 -0.0039 124 SER A C 339 O O . SER A 42 ? 0.2518 0.2557 0.2360 -0.0018 -0.0028 -0.0032 124 SER A O 340 C CB . SER A 42 ? 0.2748 0.2784 0.2574 -0.0059 -0.0039 -0.0041 124 SER A CB 341 O OG . SER A 42 ? 0.2337 0.2340 0.2142 -0.0064 -0.0034 -0.0044 124 SER A OG 342 N N . CYS A 43 ? 0.1764 0.1748 0.1565 -0.0027 -0.0016 -0.0043 125 CYS A N 343 C CA . CYS A 43 ? 0.2713 0.2678 0.2510 -0.0008 -0.0008 -0.0039 125 CYS A CA 344 C C . CYS A 43 ? 0.2626 0.2562 0.2410 -0.0008 -0.0006 -0.0035 125 CYS A C 345 O O . CYS A 43 ? 0.2694 0.2607 0.2461 -0.0025 -0.0006 -0.0040 125 CYS A O 346 C CB . CYS A 43 ? 0.2199 0.2142 0.1980 0.0000 0.0004 -0.0046 125 CYS A CB 347 S SG . CYS A 43 ? 0.2862 0.2839 0.2658 0.0004 0.0006 -0.0049 125 CYS A SG 348 N N . ASP A 44 ? 0.2575 0.2512 0.2366 0.0010 -0.0005 -0.0025 126 ASP A N 349 C CA . ASP A 44 ? 0.2684 0.2586 0.2459 0.0017 0.0000 -0.0019 126 ASP A CA 350 C C . ASP A 44 ? 0.2925 0.2796 0.2686 0.0034 0.0014 -0.0021 126 ASP A C 351 O O . ASP A 44 ? 0.3566 0.3448 0.3332 0.0041 0.0018 -0.0027 126 ASP A O 352 C CB . ASP A 44 ? 0.3102 0.3028 0.2894 0.0028 -0.0006 -0.0006 126 ASP A CB 353 C CG . ASP A 44 ? 0.3625 0.3577 0.3427 0.0012 -0.0018 -0.0005 126 ASP A CG 354 O OD1 . ASP A 44 ? 0.2991 0.2950 0.2793 -0.0007 -0.0021 -0.0013 126 ASP A OD1 355 O OD2 . ASP A 44 ? 0.3291 0.3258 0.3101 0.0018 -0.0023 0.0005 126 ASP A OD2 356 N N . PRO A 45 ? 0.3345 0.3173 0.3086 0.0043 0.0021 -0.0016 127 PRO A N 357 C CA . PRO A 45 ? 0.2959 0.2753 0.2685 0.0062 0.0035 -0.0019 127 PRO A CA 358 C C . PRO A 45 ? 0.3712 0.3538 0.3461 0.0091 0.0037 -0.0010 127 PRO A C 359 O O . PRO A 45 ? 0.2992 0.2803 0.2734 0.0108 0.0049 -0.0014 127 PRO A O 360 C CB . PRO A 45 ? 0.3397 0.3139 0.3098 0.0065 0.0042 -0.0013 127 PRO A CB 361 C CG . PRO A 45 ? 0.3112 0.2851 0.2807 0.0036 0.0034 -0.0015 127 PRO A CG 362 C CD . PRO A 45 ? 0.2752 0.2552 0.2477 0.0031 0.0020 -0.0011 127 PRO A CD 363 N N . ASP A 46 ? 0.3275 0.3145 0.3049 0.0096 0.0026 0.0000 128 ASP A N 364 C CA . ASP A 46 ? 0.3827 0.3731 0.3624 0.0121 0.0026 0.0009 128 ASP A CA 365 C C . ASP A 46 ? 0.4229 0.4192 0.4057 0.0114 0.0016 0.0007 128 ASP A C 366 O O . ASP A 46 ? 0.4002 0.4002 0.3853 0.0131 0.0015 0.0014 128 ASP A O 367 C CB . ASP A 46 ? 0.3991 0.3895 0.3790 0.0137 0.0022 0.0025 128 ASP A CB 368 C CG . ASP A 46 ? 0.5671 0.5588 0.5472 0.0119 0.0010 0.0030 128 ASP A CG 369 O OD1 . ASP A 46 ? 0.4948 0.4879 0.4754 0.0095 0.0003 0.0021 128 ASP A OD1 370 O OD2 . ASP A 46 ? 0.6758 0.6670 0.6555 0.0129 0.0007 0.0043 128 ASP A OD2 371 N N . GLU A 47 ? 0.2977 0.2948 0.2805 0.0089 0.0010 -0.0001 129 GLU A N 372 C CA . GLU A 47 ? 0.3939 0.3960 0.3793 0.0081 0.0000 -0.0002 129 GLU A CA 373 C C . GLU A 47 ? 0.3609 0.3629 0.3458 0.0057 -0.0004 -0.0012 129 GLU A C 374 O O . GLU A 47 ? 0.3282 0.3274 0.3112 0.0042 -0.0005 -0.0016 129 GLU A O 375 C CB . GLU A 47 ? 0.3303 0.3351 0.3173 0.0081 -0.0012 0.0007 129 GLU A CB 376 C CG . GLU A 47 ? 0.4820 0.4916 0.4716 0.0073 -0.0022 0.0006 129 GLU A CG 377 C CD . GLU A 47 ? 0.4879 0.4998 0.4786 0.0069 -0.0034 0.0012 129 GLU A CD 378 O OE1 . GLU A 47 ? 0.4537 0.4634 0.4429 0.0071 -0.0035 0.0018 129 GLU A OE1 379 O OE2 . GLU A 47 ? 0.4765 0.4920 0.4692 0.0063 -0.0042 0.0011 129 GLU A OE2 380 N N . CYS A 48 ? 0.2833 0.2884 0.2698 0.0053 -0.0005 -0.0015 130 CYS A N 381 C CA . CYS A 48 ? 0.2900 0.2957 0.2764 0.0032 -0.0011 -0.0022 130 CYS A CA 382 C C . CYS A 48 ? 0.3220 0.3315 0.3109 0.0025 -0.0022 -0.0018 130 CYS A C 383 O O . CYS A 48 ? 0.2348 0.2472 0.2257 0.0035 -0.0024 -0.0014 130 CYS A O 384 C CB . CYS A 48 ? 0.2663 0.2719 0.2521 0.0031 -0.0003 -0.0029 130 CYS A CB 385 S SG . CYS A 48 ? 0.3206 0.3211 0.3029 0.0034 0.0011 -0.0038 130 CYS A SG 386 N N . ARG A 49 ? 0.2235 0.2331 0.2122 0.0009 -0.0030 -0.0021 131 ARG A N 387 C CA . ARG A 49 ? 0.2272 0.2397 0.2178 0.0003 -0.0040 -0.0019 131 ARG A CA 388 C C . ARG A 49 ? 0.2484 0.2617 0.2393 -0.0013 -0.0044 -0.0023 131 ARG A C 389 O O . ARG A 49 ? 0.2207 0.2322 0.2099 -0.0022 -0.0042 -0.0027 131 ARG A O 390 C CB . ARG A 49 ? 0.2276 0.2399 0.2181 0.0003 -0.0046 -0.0014 131 ARG A CB 391 C CG . ARG A 49 ? 0.2705 0.2830 0.2613 0.0020 -0.0044 -0.0007 131 ARG A CG 392 C CD . ARG A 49 ? 0.2763 0.2877 0.2661 0.0019 -0.0048 -0.0002 131 ARG A CD 393 N NE . ARG A 49 ? 0.2950 0.3088 0.2859 0.0011 -0.0058 -0.0002 131 ARG A NE 394 C CZ . ARG A 49 ? 0.3291 0.3457 0.3216 0.0018 -0.0064 0.0002 131 ARG A CZ 395 N NH1 . ARG A 49 ? 0.3188 0.3365 0.3121 0.0033 -0.0062 0.0007 131 ARG A NH1 396 N NH2 . ARG A 49 ? 0.3266 0.3450 0.3198 0.0009 -0.0072 0.0000 131 ARG A NH2 397 N N . PHE A 50 ? 0.2501 0.2661 0.2429 -0.0016 -0.0050 -0.0021 132 PHE A N 398 C CA . PHE A 50 ? 0.2032 0.2199 0.1963 -0.0028 -0.0055 -0.0024 132 PHE A CA 399 C C . PHE A 50 ? 0.2232 0.2398 0.2163 -0.0034 -0.0063 -0.0024 132 PHE A C 400 O O . PHE A 50 ? 0.1638 0.1809 0.1573 -0.0030 -0.0066 -0.0022 132 PHE A O 401 C CB . PHE A 50 ? 0.1401 0.1592 0.1353 -0.0028 -0.0058 -0.0022 132 PHE A CB 402 C CG . PHE A 50 ? 0.2131 0.2326 0.2084 -0.0026 -0.0050 -0.0021 132 PHE A CG 403 C CD1 . PHE A 50 ? 0.1619 0.1796 0.1554 -0.0023 -0.0042 -0.0023 132 PHE A CD1 404 C CD2 . PHE A 50 ? 0.2137 0.2351 0.2107 -0.0029 -0.0051 -0.0019 132 PHE A CD2 405 C CE1 . PHE A 50 ? 0.1723 0.1906 0.1658 -0.0021 -0.0035 -0.0023 132 PHE A CE1 406 C CE2 . PHE A 50 ? 0.2265 0.2485 0.2236 -0.0028 -0.0043 -0.0018 132 PHE A CE2 407 C CZ . PHE A 50 ? 0.1843 0.2049 0.1797 -0.0024 -0.0035 -0.0020 132 PHE A CZ 408 N N . TYR A 51 ? 0.2179 0.2341 0.2103 -0.0044 -0.0065 -0.0027 133 TYR A N 409 C CA . TYR A 51 ? 0.2201 0.2364 0.2125 -0.0051 -0.0071 -0.0027 133 TYR A CA 410 C C . TYR A 51 ? 0.2786 0.2962 0.2720 -0.0056 -0.0075 -0.0028 133 TYR A C 411 O O . TYR A 51 ? 0.1476 0.1653 0.1409 -0.0058 -0.0074 -0.0027 133 TYR A O 412 C CB . TYR A 51 ? 0.2206 0.2352 0.2112 -0.0058 -0.0069 -0.0029 133 TYR A CB 413 C CG . TYR A 51 ? 0.2156 0.2283 0.2050 -0.0053 -0.0064 -0.0028 133 TYR A CG 414 C CD1 . TYR A 51 ? 0.1749 0.1863 0.1636 -0.0044 -0.0057 -0.0028 133 TYR A CD1 415 C CD2 . TYR A 51 ? 0.1792 0.1913 0.1681 -0.0055 -0.0065 -0.0026 133 TYR A CD2 416 C CE1 . TYR A 51 ? 0.1807 0.1899 0.1682 -0.0037 -0.0052 -0.0026 133 TYR A CE1 417 C CE2 . TYR A 51 ? 0.2138 0.2239 0.2014 -0.0049 -0.0060 -0.0023 133 TYR A CE2 418 C CZ . TYR A 51 ? 0.2347 0.2432 0.2217 -0.0040 -0.0053 -0.0023 133 TYR A CZ 419 O OH . TYR A 51 ? 0.2155 0.2217 0.2012 -0.0032 -0.0048 -0.0019 133 TYR A OH 420 N N . ALA A 52 ? 0.2537 0.2723 0.2478 -0.0058 -0.0080 -0.0028 134 ALA A N 421 C CA . ALA A 52 ? 0.2552 0.2747 0.2501 -0.0061 -0.0084 -0.0029 134 ALA A CA 422 C C . ALA A 52 ? 0.2375 0.2578 0.2329 -0.0062 -0.0088 -0.0030 134 ALA A C 423 O O . ALA A 52 ? 0.2566 0.2769 0.2518 -0.0060 -0.0088 -0.0031 134 ALA A O 424 C CB . ALA A 52 ? 0.1884 0.2085 0.1845 -0.0058 -0.0084 -0.0027 134 ALA A CB 425 N N . LEU A 53 ? 0.2052 0.2262 0.2012 -0.0063 -0.0090 -0.0030 135 LEU A N 426 C CA . LEU A 53 ? 0.2530 0.2749 0.2496 -0.0062 -0.0092 -0.0033 135 LEU A CA 427 C C . LEU A 53 ? 0.1856 0.2077 0.1833 -0.0058 -0.0094 -0.0035 135 LEU A C 428 O O . LEU A 53 ? 0.2209 0.2428 0.2192 -0.0056 -0.0094 -0.0034 135 LEU A O 429 C CB . LEU A 53 ? 0.1974 0.2202 0.1942 -0.0064 -0.0094 -0.0031 135 LEU A CB 430 C CG . LEU A 53 ? 0.2305 0.2535 0.2263 -0.0071 -0.0094 -0.0031 135 LEU A CG 431 C CD1 . LEU A 53 ? 0.1429 0.1675 0.1392 -0.0072 -0.0097 -0.0029 135 LEU A CD1 432 C CD2 . LEU A 53 ? 0.2297 0.2526 0.2249 -0.0074 -0.0092 -0.0032 135 LEU A CD2 433 N N . SER A 54 ? 0.1667 0.1891 0.1645 -0.0056 -0.0094 -0.0039 136 SER A N 434 C CA . SER A 54 ? 0.1942 0.2167 0.1928 -0.0055 -0.0096 -0.0043 136 SER A CA 435 C C . SER A 54 ? 0.1526 0.1753 0.1516 -0.0052 -0.0096 -0.0047 136 SER A C 436 O O . SER A 54 ? 0.2318 0.2551 0.2306 -0.0051 -0.0095 -0.0045 136 SER A O 437 C CB . SER A 54 ? 0.1737 0.1968 0.1720 -0.0054 -0.0097 -0.0046 136 SER A CB 438 O OG . SER A 54 ? 0.1786 0.2019 0.1774 -0.0054 -0.0099 -0.0053 136 SER A OG 439 N N . GLN A 55 ? 0.1788 0.2010 0.1784 -0.0051 -0.0096 -0.0051 137 GLN A N 440 C CA . GLN A 55 ? 0.1716 0.1937 0.1715 -0.0047 -0.0095 -0.0055 137 GLN A CA 441 C C . GLN A 55 ? 0.2191 0.2414 0.2188 -0.0047 -0.0096 -0.0065 137 GLN A C 442 O O . GLN A 55 ? 0.2216 0.2435 0.2215 -0.0043 -0.0094 -0.0071 137 GLN A O 443 C CB . GLN A 55 ? 0.1882 0.2089 0.1887 -0.0045 -0.0094 -0.0053 137 GLN A CB 444 C CG . GLN A 55 ? 0.1666 0.1872 0.1671 -0.0043 -0.0094 -0.0044 137 GLN A CG 445 C CD . GLN A 55 ? 0.1962 0.2175 0.1969 -0.0036 -0.0094 -0.0042 137 GLN A CD 446 O OE1 . GLN A 55 ? 0.2577 0.2799 0.2584 -0.0033 -0.0093 -0.0047 137 GLN A OE1 447 N NE2 . GLN A 55 ? 0.1917 0.2130 0.1925 -0.0033 -0.0095 -0.0033 137 GLN A NE2 448 N N . GLY A 56 ? 0.1710 0.1939 0.1702 -0.0051 -0.0098 -0.0066 138 GLY A N 449 C CA . GLY A 56 ? 0.2156 0.2391 0.2144 -0.0051 -0.0099 -0.0074 138 GLY A CA 450 C C . GLY A 56 ? 0.2372 0.2599 0.2363 -0.0055 -0.0100 -0.0083 138 GLY A C 451 O O . GLY A 56 ? 0.2070 0.2295 0.2057 -0.0054 -0.0099 -0.0093 138 GLY A O 452 N N . THR A 57 ? 0.1989 0.2210 0.1987 -0.0060 -0.0102 -0.0081 139 THR A N 453 C CA . THR A 57 ? 0.2329 0.2541 0.2332 -0.0066 -0.0102 -0.0088 139 THR A CA 454 C C . THR A 57 ? 0.2429 0.2642 0.2441 -0.0072 -0.0103 -0.0082 139 THR A C 455 O O . THR A 57 ? 0.2322 0.2537 0.2335 -0.0069 -0.0102 -0.0072 139 THR A O 456 C CB . THR A 57 ? 0.2767 0.2958 0.2771 -0.0062 -0.0098 -0.0092 139 THR A CB 457 O OG1 . THR A 57 ? 0.2285 0.2462 0.2292 -0.0071 -0.0098 -0.0099 139 THR A OG1 458 C CG2 . THR A 57 ? 0.2505 0.2688 0.2513 -0.0057 -0.0095 -0.0080 139 THR A CG2 459 N N . THR A 58 ? 0.1921 0.2135 0.1937 -0.0081 -0.0106 -0.0088 140 THR A N 460 C CA . THR A 58 ? 0.2164 0.2380 0.2190 -0.0088 -0.0105 -0.0082 140 THR A CA 461 C C . THR A 58 ? 0.1799 0.1991 0.1828 -0.0091 -0.0100 -0.0080 140 THR A C 462 O O . THR A 58 ? 0.1858 0.2032 0.1883 -0.0088 -0.0098 -0.0085 140 THR A O 463 C CB . THR A 58 ? 0.1710 0.1944 0.1743 -0.0099 -0.0109 -0.0088 140 THR A CB 464 O OG1 . THR A 58 ? 0.2233 0.2456 0.2265 -0.0108 -0.0111 -0.0100 140 THR A OG1 465 C CG2 . THR A 58 ? 0.1814 0.2073 0.1844 -0.0094 -0.0115 -0.0087 140 THR A CG2 466 N N . ILE A 59 ? 0.2526 0.2719 0.2564 -0.0096 -0.0098 -0.0073 141 ILE A N 467 C CA . ILE A 59 ? 0.2786 0.2955 0.2825 -0.0099 -0.0093 -0.0068 141 ILE A CA 468 C C . ILE A 59 ? 0.2560 0.2711 0.2600 -0.0110 -0.0092 -0.0078 141 ILE A C 469 O O . ILE A 59 ? 0.2688 0.2811 0.2723 -0.0107 -0.0088 -0.0078 141 ILE A O 470 C CB . ILE A 59 ? 0.3373 0.3548 0.3418 -0.0104 -0.0089 -0.0057 141 ILE A CB 471 C CG1 . ILE A 59 ? 0.3290 0.3485 0.3333 -0.0095 -0.0090 -0.0050 141 ILE A CG1 472 C CG2 . ILE A 59 ? 0.3135 0.3285 0.3177 -0.0103 -0.0084 -0.0049 141 ILE A CG2 473 C CD1 . ILE A 59 ? 0.3591 0.3793 0.3639 -0.0098 -0.0085 -0.0041 141 ILE A CD1 474 N N . ARG A 60 ? 0.1928 0.2094 0.1974 -0.0122 -0.0096 -0.0086 142 ARG A N 475 C CA . ARG A 60 ? 0.2708 0.2857 0.2754 -0.0135 -0.0096 -0.0098 142 ARG A CA 476 C C . ARG A 60 ? 0.2699 0.2836 0.2733 -0.0130 -0.0097 -0.0111 142 ARG A C 477 O O . ARG A 60 ? 0.3310 0.3421 0.3339 -0.0137 -0.0095 -0.0121 142 ARG A O 478 C CB . ARG A 60 ? 0.2129 0.2303 0.2185 -0.0152 -0.0100 -0.0103 142 ARG A CB 479 C CG . ARG A 60 ? 0.2675 0.2853 0.2743 -0.0162 -0.0096 -0.0093 142 ARG A CG 480 C CD . ARG A 60 ? 0.2901 0.3039 0.2965 -0.0169 -0.0088 -0.0091 142 ARG A CD 481 N NE . ARG A 60 ? 0.2662 0.2803 0.2738 -0.0185 -0.0084 -0.0085 142 ARG A NE 482 C CZ . ARG A 60 ? 0.3343 0.3451 0.3417 -0.0195 -0.0077 -0.0081 142 ARG A CZ 483 N NH1 . ARG A 60 ? 0.2932 0.3000 0.2993 -0.0187 -0.0074 -0.0083 142 ARG A NH1 484 N NH2 . ARG A 60 ? 0.2972 0.3086 0.3056 -0.0211 -0.0073 -0.0076 142 ARG A NH2 485 N N . GLY A 61 ? 0.2854 0.3008 0.2883 -0.0118 -0.0100 -0.0111 143 GLY A N 486 C CA . GLY A 61 ? 0.2128 0.2274 0.2145 -0.0112 -0.0101 -0.0122 143 GLY A CA 487 C C . GLY A 61 ? 0.2819 0.2933 0.2831 -0.0103 -0.0094 -0.0123 143 GLY A C 488 O O . GLY A 61 ? 0.2290 0.2395 0.2305 -0.0095 -0.0090 -0.0110 143 GLY A O 489 N N . LYS A 62 ? 0.2462 0.2558 0.2464 -0.0103 -0.0092 -0.0137 144 LYS A N 490 C CA . LYS A 62 ? 0.2551 0.2614 0.2548 -0.0092 -0.0085 -0.0138 144 LYS A CA 491 C C . LYS A 62 ? 0.2275 0.2349 0.2273 -0.0073 -0.0083 -0.0128 144 LYS A C 492 O O . LYS A 62 ? 0.2176 0.2230 0.2174 -0.0061 -0.0078 -0.0122 144 LYS A O 493 C CB . LYS A 62 ? 0.2528 0.2570 0.2514 -0.0095 -0.0082 -0.0157 144 LYS A CB 494 C CG . LYS A 62 ? 0.2968 0.2988 0.2953 -0.0115 -0.0082 -0.0168 144 LYS A CG 495 C CD . LYS A 62 ? 0.2472 0.2470 0.2441 -0.0118 -0.0080 -0.0190 144 LYS A CD 496 C CE . LYS A 62 ? 0.3241 0.3222 0.3208 -0.0142 -0.0082 -0.0203 144 LYS A CE 497 N NZ . LYS A 62 ? 0.2835 0.2799 0.2785 -0.0147 -0.0080 -0.0226 144 LYS A NZ 498 N N . HIS A 63 ? 0.1946 0.2050 0.1942 -0.0070 -0.0087 -0.0127 145 HIS A N 499 C CA . HIS A 63 ? 0.2249 0.2367 0.2246 -0.0055 -0.0086 -0.0118 145 HIS A CA 500 C C . HIS A 63 ? 0.2544 0.2666 0.2549 -0.0052 -0.0086 -0.0101 145 HIS A C 501 O O . HIS A 63 ? 0.2410 0.2544 0.2416 -0.0041 -0.0085 -0.0093 145 HIS A O 502 C CB . HIS A 63 ? 0.1976 0.2123 0.1968 -0.0054 -0.0089 -0.0121 145 HIS A CB 503 C CG . HIS A 63 ? 0.2356 0.2502 0.2337 -0.0054 -0.0088 -0.0137 145 HIS A CG 504 N ND1 . HIS A 63 ? 0.2768 0.2923 0.2744 -0.0066 -0.0093 -0.0147 145 HIS A ND1 505 C CD2 . HIS A 63 ? 0.2279 0.2420 0.2254 -0.0044 -0.0082 -0.0145 145 HIS A CD2 506 C CE1 . HIS A 63 ? 0.2067 0.2219 0.2031 -0.0064 -0.0091 -0.0161 145 HIS A CE1 507 N NE2 . HIS A 63 ? 0.2208 0.2351 0.2171 -0.0050 -0.0084 -0.0160 145 HIS A NE2 508 N N . SER A 64 ? 0.2170 0.2285 0.2180 -0.0062 -0.0087 -0.0096 146 SER A N 509 C CA . SER A 64 ? 0.2687 0.2803 0.2702 -0.0059 -0.0086 -0.0080 146 SER A CA 510 C C . SER A 64 ? 0.2384 0.2478 0.2398 -0.0048 -0.0082 -0.0074 146 SER A C 511 O O . SER A 64 ? 0.2463 0.2561 0.2479 -0.0042 -0.0081 -0.0061 146 SER A O 512 C CB . SER A 64 ? 0.2649 0.2765 0.2669 -0.0072 -0.0087 -0.0076 146 SER A CB 513 O OG . SER A 64 ? 0.2407 0.2497 0.2428 -0.0080 -0.0084 -0.0081 146 SER A OG 514 N N . ASN A 65 ? 0.1646 0.1716 0.1658 -0.0046 -0.0078 -0.0084 147 ASN A N 515 C CA . ASN A 65 ? 0.2215 0.2262 0.2225 -0.0032 -0.0073 -0.0079 147 ASN A CA 516 C C . ASN A 65 ? 0.2164 0.2233 0.2177 -0.0016 -0.0073 -0.0072 147 ASN A C 517 O O . ASN A 65 ? 0.2553 0.2636 0.2564 -0.0011 -0.0073 -0.0081 147 ASN A O 518 C CB . ASN A 65 ? 0.2236 0.2253 0.2240 -0.0031 -0.0068 -0.0093 147 ASN A CB 519 C CG . ASN A 65 ? 0.3165 0.3147 0.3168 -0.0018 -0.0061 -0.0087 147 ASN A CG 520 O OD1 . ASN A 65 ? 0.2996 0.2984 0.3003 -0.0004 -0.0061 -0.0072 147 ASN A OD1 521 N ND2 . ASN A 65 ? 0.4266 0.4211 0.4262 -0.0022 -0.0056 -0.0098 147 ASN A ND2 522 N N . GLY A 66 ? 0.2285 0.2358 0.2301 -0.0009 -0.0074 -0.0057 148 GLY A N 523 C CA . GLY A 66 ? 0.2186 0.2282 0.2206 0.0005 -0.0075 -0.0050 148 GLY A CA 524 C C . GLY A 66 ? 0.2751 0.2879 0.2771 -0.0001 -0.0081 -0.0045 148 GLY A C 525 O O . GLY A 66 ? 0.2600 0.2751 0.2623 0.0007 -0.0082 -0.0041 148 GLY A O 526 N N . THR A 67 ? 0.1781 0.1911 0.1800 -0.0015 -0.0083 -0.0044 149 THR A N 527 C CA . THR A 67 ? 0.2708 0.2862 0.2725 -0.0020 -0.0087 -0.0040 149 THR A CA 528 C C . THR A 67 ? 0.2447 0.2610 0.2464 -0.0017 -0.0089 -0.0026 149 THR A C 529 O O . THR A 67 ? 0.2175 0.2353 0.2189 -0.0024 -0.0092 -0.0023 149 THR A O 530 C CB . THR A 67 ? 0.2634 0.2789 0.2650 -0.0034 -0.0088 -0.0043 149 THR A CB 531 O OG1 . THR A 67 ? 0.2473 0.2606 0.2490 -0.0039 -0.0086 -0.0042 149 THR A OG1 532 C CG2 . THR A 67 ? 0.2532 0.2694 0.2547 -0.0037 -0.0089 -0.0056 149 THR A CG2 533 N N . ILE A 68 ? 0.2798 0.2950 0.2816 -0.0007 -0.0088 -0.0018 150 ILE A N 534 C CA . ILE A 68 ? 0.2694 0.2861 0.2712 -0.0003 -0.0091 -0.0006 150 ILE A CA 535 C C . ILE A 68 ? 0.2326 0.2521 0.2347 0.0002 -0.0094 -0.0007 150 ILE A C 536 O O . ILE A 68 ? 0.3060 0.3276 0.3079 0.0000 -0.0098 -0.0001 150 ILE A O 537 C CB . ILE A 68 ? 0.2136 0.2286 0.2153 0.0009 -0.0089 0.0006 150 ILE A CB 538 C CG1 . ILE A 68 ? 0.2366 0.2532 0.2380 0.0010 -0.0094 0.0020 150 ILE A CG1 539 C CG2 . ILE A 68 ? 0.2191 0.2340 0.2216 0.0025 -0.0087 0.0003 150 ILE A CG2 540 C CD1 . ILE A 68 ? 0.3745 0.3898 0.3757 0.0024 -0.0093 0.0034 150 ILE A CD1 541 N N . HIS A 69 ? 0.2958 0.3156 0.2983 0.0006 -0.0091 -0.0017 151 HIS A N 542 C CA . HIS A 69 ? 0.3511 0.3738 0.3541 0.0010 -0.0093 -0.0020 151 HIS A CA 543 C C . HIS A 69 ? 0.2627 0.2872 0.2652 -0.0004 -0.0096 -0.0020 151 HIS A C 544 O O . HIS A 69 ? 0.2899 0.3135 0.2918 -0.0014 -0.0095 -0.0026 151 HIS A O 545 C CB . HIS A 69 ? 0.3064 0.3288 0.3097 0.0014 -0.0088 -0.0032 151 HIS A CB 546 C CG . HIS A 69 ? 0.4832 0.5084 0.4871 0.0021 -0.0087 -0.0033 151 HIS A CG 547 N ND1 . HIS A 69 ? 0.4916 0.5184 0.4952 0.0014 -0.0086 -0.0041 151 HIS A ND1 548 C CD2 . HIS A 69 ? 0.5283 0.5553 0.5332 0.0035 -0.0086 -0.0028 151 HIS A CD2 549 C CE1 . HIS A 69 ? 0.3915 0.4209 0.3960 0.0021 -0.0084 -0.0040 151 HIS A CE1 550 N NE2 . HIS A 69 ? 0.4869 0.5167 0.4923 0.0035 -0.0085 -0.0033 151 HIS A NE2 551 N N . ASP A 70 ? 0.2924 0.3195 0.2952 -0.0004 -0.0099 -0.0015 152 ASP A N 552 C CA . ASP A 70 ? 0.2618 0.2902 0.2638 -0.0017 -0.0102 -0.0015 152 ASP A CA 553 C C . ASP A 70 ? 0.2122 0.2416 0.2141 -0.0024 -0.0100 -0.0023 152 ASP A C 554 O O . ASP A 70 ? 0.2022 0.2311 0.2033 -0.0035 -0.0100 -0.0026 152 ASP A O 555 C CB . ASP A 70 ? 0.2770 0.3078 0.2792 -0.0017 -0.0107 -0.0007 152 ASP A CB 556 C CG . ASP A 70 ? 0.3021 0.3320 0.3036 -0.0018 -0.0110 0.0001 152 ASP A CG 557 O OD1 . ASP A 70 ? 0.2194 0.2471 0.2201 -0.0024 -0.0108 0.0000 152 ASP A OD1 558 O OD2 . ASP A 70 ? 0.2194 0.2510 0.2212 -0.0013 -0.0115 0.0010 152 ASP A OD2 559 N N . ARG A 71 ? 0.2177 0.2486 0.2205 -0.0017 -0.0097 -0.0027 153 ARG A N 560 C CA . ARG A 71 ? 0.2542 0.2865 0.2568 -0.0024 -0.0095 -0.0032 153 ARG A CA 561 C C . ARG A 71 ? 0.2487 0.2809 0.2516 -0.0016 -0.0090 -0.0040 153 ARG A C 562 O O . ARG A 71 ? 0.4507 0.4846 0.4545 -0.0007 -0.0087 -0.0041 153 ARG A O 563 C CB . ARG A 71 ? 0.1837 0.2193 0.1870 -0.0027 -0.0097 -0.0027 153 ARG A CB 564 C CG . ARG A 71 ? 0.1965 0.2325 0.1992 -0.0037 -0.0103 -0.0021 153 ARG A CG 565 C CD . ARG A 71 ? 0.2130 0.2526 0.2165 -0.0041 -0.0105 -0.0018 153 ARG A CD 566 N NE . ARG A 71 ? 0.1904 0.2321 0.1956 -0.0025 -0.0105 -0.0014 153 ARG A NE 567 C CZ . ARG A 71 ? 0.2223 0.2643 0.2280 -0.0014 -0.0110 -0.0006 153 ARG A CZ 568 N NH1 . ARG A 71 ? 0.2045 0.2449 0.2090 -0.0020 -0.0114 -0.0002 153 ARG A NH1 569 N NH2 . ARG A 71 ? 0.2098 0.2536 0.2169 0.0003 -0.0109 -0.0002 153 ARG A NH2 570 N N . SER A 72 ? 0.2757 0.3061 0.2777 -0.0021 -0.0088 -0.0046 154 SER A N 571 C CA . SER A 72 ? 0.2937 0.3238 0.2955 -0.0016 -0.0084 -0.0055 154 SER A CA 572 C C . SER A 72 ? 0.3233 0.3539 0.3242 -0.0026 -0.0083 -0.0058 154 SER A C 573 O O . SER A 72 ? 0.2597 0.2902 0.2600 -0.0036 -0.0085 -0.0053 154 SER A O 574 C CB . SER A 72 ? 0.2410 0.2685 0.2426 -0.0012 -0.0083 -0.0061 154 SER A CB 575 O OG . SER A 72 ? 0.2298 0.2562 0.2306 -0.0023 -0.0086 -0.0062 154 SER A OG 576 N N . GLN A 73 ? 0.2686 0.2996 0.2691 -0.0023 -0.0078 -0.0065 155 GLN A N 577 C CA . GLN A 73 ? 0.2393 0.2708 0.2386 -0.0031 -0.0077 -0.0067 155 GLN A CA 578 C C . GLN A 73 ? 0.2303 0.2599 0.2287 -0.0036 -0.0081 -0.0069 155 GLN A C 579 O O . GLN A 73 ? 0.2127 0.2424 0.2100 -0.0041 -0.0080 -0.0069 155 GLN A O 580 C CB . GLN A 73 ? 0.2287 0.2615 0.2279 -0.0026 -0.0071 -0.0074 155 GLN A CB 581 C CG . GLN A 73 ? 0.2048 0.2402 0.2050 -0.0021 -0.0066 -0.0071 155 GLN A CG 582 C CD . GLN A 73 ? 0.2621 0.2974 0.2635 -0.0006 -0.0064 -0.0076 155 GLN A CD 583 O OE1 . GLN A 73 ? 0.2318 0.2651 0.2334 -0.0001 -0.0067 -0.0075 155 GLN A OE1 584 N NE2 . GLN A 73 ? 0.3005 0.3381 0.3026 0.0003 -0.0057 -0.0079 155 GLN A NE2 585 N N . TYR A 74 ? 0.2099 0.2378 0.2087 -0.0034 -0.0084 -0.0069 156 TYR A N 586 C CA . TYR A 74 ? 0.2524 0.2790 0.2507 -0.0038 -0.0087 -0.0072 156 TYR A CA 587 C C . TYR A 74 ? 0.2650 0.2909 0.2632 -0.0043 -0.0091 -0.0064 156 TYR A C 588 O O . TYR A 74 ? 0.2804 0.3055 0.2785 -0.0046 -0.0093 -0.0065 156 TYR A O 589 C CB . TYR A 74 ? 0.2245 0.2498 0.2231 -0.0034 -0.0087 -0.0080 156 TYR A CB 590 C CG . TYR A 74 ? 0.2480 0.2737 0.2467 -0.0025 -0.0082 -0.0088 156 TYR A CG 591 C CD1 . TYR A 74 ? 0.2815 0.3084 0.2793 -0.0025 -0.0079 -0.0094 156 TYR A CD1 592 C CD2 . TYR A 74 ? 0.2340 0.2589 0.2335 -0.0017 -0.0080 -0.0088 156 TYR A CD2 593 C CE1 . TYR A 74 ? 0.1914 0.2189 0.1893 -0.0017 -0.0073 -0.0101 156 TYR A CE1 594 C CE2 . TYR A 74 ? 0.2211 0.2464 0.2208 -0.0007 -0.0074 -0.0095 156 TYR A CE2 595 C CZ . TYR A 74 ? 0.2615 0.2881 0.2604 -0.0007 -0.0070 -0.0102 156 TYR A CZ 596 O OH . TYR A 74 ? 0.2987 0.3259 0.2977 0.0004 -0.0063 -0.0110 156 TYR A OH 597 N N . ARG A 75 ? 0.1879 0.2143 0.1863 -0.0045 -0.0090 -0.0057 157 ARG A N 598 C CA . ARG A 75 ? 0.1769 0.2026 0.1751 -0.0050 -0.0092 -0.0051 157 ARG A CA 599 C C . ARG A 75 ? 0.1882 0.2140 0.1854 -0.0056 -0.0091 -0.0047 157 ARG A C 600 O O . ARG A 75 ? 0.1781 0.2047 0.1747 -0.0058 -0.0089 -0.0048 157 ARG A O 601 C CB . ARG A 75 ? 0.2108 0.2369 0.2095 -0.0050 -0.0093 -0.0046 157 ARG A CB 602 C CG . ARG A 75 ? 0.1988 0.2246 0.1985 -0.0043 -0.0093 -0.0046 157 ARG A CG 603 C CD . ARG A 75 ? 0.2770 0.3027 0.2768 -0.0043 -0.0095 -0.0039 157 ARG A CD 604 N NE . ARG A 75 ? 0.2325 0.2568 0.2319 -0.0047 -0.0096 -0.0037 157 ARG A NE 605 C CZ . ARG A 75 ? 0.2837 0.3076 0.2831 -0.0048 -0.0097 -0.0031 157 ARG A CZ 606 N NH1 . ARG A 75 ? 0.1893 0.2121 0.1883 -0.0051 -0.0097 -0.0029 157 ARG A NH1 607 N NH2 . ARG A 75 ? 0.2208 0.2457 0.2204 -0.0045 -0.0099 -0.0026 157 ARG A NH2 608 N N . ALA A 76 ? 0.1923 0.2169 0.1890 -0.0058 -0.0092 -0.0044 158 ALA A N 609 C CA . ALA A 76 ? 0.1918 0.2159 0.1874 -0.0062 -0.0091 -0.0040 158 ALA A CA 610 C C . ALA A 76 ? 0.2259 0.2487 0.2211 -0.0063 -0.0091 -0.0036 158 ALA A C 611 O O . ALA A 76 ? 0.1525 0.1751 0.1484 -0.0060 -0.0092 -0.0037 158 ALA A O 612 C CB . ALA A 76 ? 0.2259 0.2501 0.2210 -0.0059 -0.0091 -0.0041 158 ALA A CB 613 N N . LEU A 77 ? 0.2195 0.2414 0.2137 -0.0068 -0.0088 -0.0033 159 LEU A N 614 C CA . LEU A 77 ? 0.2627 0.2831 0.2562 -0.0067 -0.0087 -0.0031 159 LEU A CA 615 C C . LEU A 77 ? 0.2716 0.2916 0.2650 -0.0060 -0.0086 -0.0029 159 LEU A C 616 O O . LEU A 77 ? 0.2245 0.2443 0.2172 -0.0059 -0.0085 -0.0026 159 LEU A O 617 C CB . LEU A 77 ? 0.2319 0.2511 0.2241 -0.0075 -0.0083 -0.0029 159 LEU A CB 618 C CG . LEU A 77 ? 0.2141 0.2313 0.2053 -0.0074 -0.0080 -0.0028 159 LEU A CG 619 C CD1 . LEU A 77 ? 0.1782 0.1955 0.1698 -0.0073 -0.0080 -0.0029 159 LEU A CD1 620 C CD2 . LEU A 77 ? 0.1692 0.1846 0.1587 -0.0083 -0.0076 -0.0027 159 LEU A CD2 621 N N . ILE A 78 ? 0.2369 0.2570 0.2310 -0.0056 -0.0087 -0.0029 160 ILE A N 622 C CA . ILE A 78 ? 0.2405 0.2607 0.2348 -0.0048 -0.0087 -0.0027 160 ILE A CA 623 C C . ILE A 78 ? 0.2368 0.2557 0.2306 -0.0045 -0.0082 -0.0024 160 ILE A C 624 O O . ILE A 78 ? 0.1769 0.1952 0.1706 -0.0049 -0.0080 -0.0026 160 ILE A O 625 C CB . ILE A 78 ? 0.1850 0.2067 0.1807 -0.0046 -0.0091 -0.0030 160 ILE A CB 626 C CG1 . ILE A 78 ? 0.1874 0.2092 0.1840 -0.0049 -0.0091 -0.0032 160 ILE A CG1 627 C CG2 . ILE A 78 ? 0.1977 0.2205 0.1936 -0.0048 -0.0095 -0.0034 160 ILE A CG2 628 C CD1 . ILE A 78 ? 0.1330 0.1559 0.1310 -0.0049 -0.0094 -0.0035 160 ILE A CD1 629 N N . SER A 79 ? 0.1792 0.1979 0.1728 -0.0036 -0.0081 -0.0020 161 SER A N 630 C CA . SER A 79 ? 0.1775 0.1953 0.1708 -0.0030 -0.0075 -0.0019 161 SER A CA 631 C C . SER A 79 ? 0.2342 0.2538 0.2288 -0.0021 -0.0077 -0.0016 161 SER A C 632 O O . SER A 79 ? 0.2420 0.2629 0.2371 -0.0018 -0.0082 -0.0014 161 SER A O 633 C CB . SER A 79 ? 0.2087 0.2240 0.2002 -0.0027 -0.0070 -0.0016 161 SER A CB 634 O OG . SER A 79 ? 0.2302 0.2454 0.2213 -0.0019 -0.0070 -0.0010 161 SER A OG 635 N N . TRP A 80 ? 0.2834 0.3033 0.2786 -0.0016 -0.0073 -0.0016 162 TRP A N 636 C CA . TRP A 80 ? 0.2565 0.2786 0.2533 -0.0008 -0.0074 -0.0013 162 TRP A CA 637 C C . TRP A 80 ? 0.2422 0.2641 0.2391 0.0001 -0.0066 -0.0011 162 TRP A C 638 O O . TRP A 80 ? 0.2437 0.2636 0.2394 -0.0001 -0.0060 -0.0013 162 TRP A O 639 C CB . TRP A 80 ? 0.2291 0.2534 0.2276 -0.0017 -0.0080 -0.0017 162 TRP A CB 640 C CG . TRP A 80 ? 0.2163 0.2403 0.2152 -0.0024 -0.0077 -0.0020 162 TRP A CG 641 C CD1 . TRP A 80 ? 0.1983 0.2234 0.1983 -0.0023 -0.0073 -0.0019 162 TRP A CD1 642 C CD2 . TRP A 80 ? 0.1838 0.2064 0.1820 -0.0033 -0.0077 -0.0023 162 TRP A CD2 643 N NE1 . TRP A 80 ? 0.1999 0.2243 0.1997 -0.0031 -0.0071 -0.0020 162 TRP A NE1 644 C CE2 . TRP A 80 ? 0.2187 0.2416 0.2174 -0.0037 -0.0074 -0.0022 162 TRP A CE2 645 C CE3 . TRP A 80 ? 0.2106 0.2321 0.2078 -0.0038 -0.0080 -0.0025 162 TRP A CE3 646 C CZ2 . TRP A 80 ? 0.1566 0.1786 0.1549 -0.0044 -0.0074 -0.0023 162 TRP A CZ2 647 C CZ3 . TRP A 80 ? 0.1981 0.2191 0.1951 -0.0045 -0.0080 -0.0026 162 TRP A CZ3 648 C CH2 . TRP A 80 ? 0.2386 0.2597 0.2360 -0.0047 -0.0077 -0.0025 162 TRP A CH2 649 N N . PRO A 81 ? 0.2605 0.2845 0.2587 0.0012 -0.0066 -0.0007 163 PRO A N 650 C CA . PRO A 81 ? 0.2872 0.3110 0.2854 0.0024 -0.0057 -0.0004 163 PRO A CA 651 C C . PRO A 81 ? 0.2628 0.2867 0.2613 0.0017 -0.0051 -0.0008 163 PRO A C 652 O O . PRO A 81 ? 0.2267 0.2521 0.2264 0.0006 -0.0055 -0.0010 163 PRO A O 653 C CB . PRO A 81 ? 0.3231 0.3502 0.3232 0.0035 -0.0060 0.0001 163 PRO A CB 654 C CG . PRO A 81 ? 0.2563 0.2841 0.2563 0.0033 -0.0070 0.0003 163 PRO A CG 655 C CD . PRO A 81 ? 0.2351 0.2616 0.2344 0.0016 -0.0074 -0.0004 163 PRO A CD 656 N N . LEU A 82 ? 0.2919 0.3140 0.2892 0.0025 -0.0041 -0.0009 164 LEU A N 657 C CA . LEU A 82 ? 0.2535 0.2753 0.2506 0.0019 -0.0034 -0.0012 164 LEU A CA 658 C C . LEU A 82 ? 0.2262 0.2514 0.2256 0.0015 -0.0035 -0.0011 164 LEU A C 659 O O . LEU A 82 ? 0.2142 0.2420 0.2154 0.0025 -0.0034 -0.0007 164 LEU A O 660 C CB . LEU A 82 ? 0.2920 0.3119 0.2876 0.0032 -0.0022 -0.0013 164 LEU A CB 661 C CG . LEU A 82 ? 0.3088 0.3273 0.3029 0.0025 -0.0014 -0.0019 164 LEU A CG 662 C CD1 . LEU A 82 ? 0.3188 0.3344 0.3108 0.0013 -0.0018 -0.0024 164 LEU A CD1 663 C CD2 . LEU A 82 ? 0.3313 0.3488 0.3245 0.0040 -0.0001 -0.0020 164 LEU A CD2 664 N N . SER A 83 ? 0.2456 0.2709 0.2451 0.0001 -0.0036 -0.0013 165 SER A N 665 C CA . SER A 83 ? 0.2245 0.2523 0.2259 -0.0006 -0.0035 -0.0011 165 SER A CA 666 C C . SER A 83 ? 0.2157 0.2461 0.2193 -0.0011 -0.0044 -0.0010 165 SER A C 667 O O . SER A 83 ? 0.2039 0.2363 0.2091 -0.0020 -0.0044 -0.0009 165 SER A O 668 C CB . SER A 83 ? 0.2513 0.2804 0.2532 0.0004 -0.0024 -0.0009 165 SER A CB 669 O OG . SER A 83 ? 0.2090 0.2358 0.2087 0.0005 -0.0015 -0.0012 165 SER A OG 670 N N A SER A 84 ? 0.1881 0.2186 0.1917 -0.0007 -0.0052 -0.0010 166 SER A N 671 N N B SER A 84 ? 0.1894 0.2199 0.1930 -0.0007 -0.0052 -0.0010 166 SER A N 672 C CA A SER A 84 ? 0.2078 0.2401 0.2129 -0.0015 -0.0062 -0.0012 166 SER A CA 673 C CA B SER A 84 ? 0.2077 0.2402 0.2129 -0.0016 -0.0061 -0.0011 166 SER A CA 674 C C A SER A 84 ? 0.1847 0.2151 0.1889 -0.0029 -0.0066 -0.0016 166 SER A C 675 C C B SER A 84 ? 0.1829 0.2134 0.1872 -0.0028 -0.0066 -0.0016 166 SER A C 676 O O A SER A 84 ? 0.1697 0.1976 0.1722 -0.0029 -0.0064 -0.0016 166 SER A O 677 O O B SER A 84 ? 0.1702 0.1982 0.1727 -0.0028 -0.0064 -0.0016 166 SER A O 678 C CB A SER A 84 ? 0.2100 0.2430 0.2150 -0.0006 -0.0068 -0.0010 166 SER A CB 679 C CB B SER A 84 ? 0.2097 0.2432 0.2151 -0.0006 -0.0068 -0.0010 166 SER A CB 680 O OG A SER A 84 ? 0.1611 0.1966 0.1674 0.0007 -0.0066 -0.0005 166 SER A OG 681 O OG B SER A 84 ? 0.2044 0.2353 0.2078 -0.0004 -0.0071 -0.0011 166 SER A OG 682 N N . PRO A 85 ? 0.2080 0.2396 0.2135 -0.0039 -0.0073 -0.0019 167 PRO A N 683 C CA . PRO A 85 ? 0.1734 0.2030 0.1780 -0.0049 -0.0076 -0.0022 167 PRO A CA 684 C C . PRO A 85 ? 0.1874 0.2162 0.1911 -0.0046 -0.0083 -0.0025 167 PRO A C 685 O O . PRO A 85 ? 0.1559 0.1861 0.1598 -0.0039 -0.0086 -0.0025 167 PRO A O 686 C CB . PRO A 85 ? 0.1884 0.2193 0.1946 -0.0061 -0.0079 -0.0025 167 PRO A CB 687 C CG . PRO A 85 ? 0.2168 0.2506 0.2244 -0.0059 -0.0082 -0.0025 167 PRO A CG 688 C CD . PRO A 85 ? 0.2076 0.2422 0.2151 -0.0045 -0.0076 -0.0019 167 PRO A CD 689 N N . PRO A 86 ? 0.2458 0.2728 0.2484 -0.0050 -0.0085 -0.0028 168 PRO A N 690 C CA . PRO A 86 ? 0.1976 0.2242 0.1994 -0.0048 -0.0090 -0.0031 168 PRO A CA 691 C C . PRO A 86 ? 0.2300 0.2579 0.2327 -0.0054 -0.0097 -0.0036 168 PRO A C 692 O O . PRO A 86 ? 0.2820 0.3091 0.2849 -0.0061 -0.0098 -0.0041 168 PRO A O 693 C CB . PRO A 86 ? 0.2655 0.2901 0.2662 -0.0051 -0.0089 -0.0032 168 PRO A CB 694 C CG . PRO A 86 ? 0.2025 0.2267 0.2038 -0.0057 -0.0086 -0.0030 168 PRO A CG 695 C CD . PRO A 86 ? 0.2476 0.2730 0.2497 -0.0055 -0.0082 -0.0027 168 PRO A CD 696 N N . THR A 87 ? 0.2443 0.2740 0.2475 -0.0050 -0.0101 -0.0036 169 THR A N 697 C CA . THR A 87 ? 0.2477 0.2790 0.2516 -0.0057 -0.0108 -0.0042 169 THR A CA 698 C C . THR A 87 ? 0.2268 0.2578 0.2293 -0.0053 -0.0112 -0.0045 169 THR A C 699 O O . THR A 87 ? 0.1917 0.2218 0.1931 -0.0045 -0.0110 -0.0040 169 THR A O 700 C CB . THR A 87 ? 0.2937 0.3278 0.2990 -0.0056 -0.0111 -0.0041 169 THR A CB 701 O OG1 . THR A 87 ? 0.2176 0.2530 0.2224 -0.0044 -0.0113 -0.0035 169 THR A OG1 702 C CG2 . THR A 87 ? 0.2315 0.2662 0.2380 -0.0058 -0.0104 -0.0037 169 THR A CG2 703 N N . VAL A 88 ? 0.2251 0.2568 0.2277 -0.0060 -0.0118 -0.0053 170 VAL A N 704 C CA . VAL A 88 ? 0.2343 0.2661 0.2356 -0.0058 -0.0122 -0.0056 170 VAL A CA 705 C C . VAL A 88 ? 0.2357 0.2692 0.2366 -0.0048 -0.0125 -0.0048 170 VAL A C 706 O O . VAL A 88 ? 0.3009 0.3339 0.3004 -0.0042 -0.0125 -0.0045 170 VAL A O 707 C CB . VAL A 88 ? 0.2830 0.3155 0.2845 -0.0068 -0.0127 -0.0068 170 VAL A CB 708 C CG1 . VAL A 88 ? 0.2326 0.2658 0.2326 -0.0065 -0.0131 -0.0072 170 VAL A CG1 709 C CG2 . VAL A 88 ? 0.1749 0.2052 0.1765 -0.0075 -0.0123 -0.0075 170 VAL A CG2 710 N N . TYR A 89 ? 0.2161 0.2516 0.2182 -0.0046 -0.0127 -0.0044 171 TYR A N 711 C CA . TYR A 89 ? 0.2294 0.2670 0.2315 -0.0035 -0.0131 -0.0036 171 TYR A CA 712 C C . TYR A 89 ? 0.2903 0.3269 0.2920 -0.0021 -0.0124 -0.0025 171 TYR A C 713 O O . TYR A 89 ? 0.3436 0.3811 0.3448 -0.0009 -0.0126 -0.0017 171 TYR A O 714 C CB . TYR A 89 ? 0.2104 0.2515 0.2141 -0.0040 -0.0138 -0.0039 171 TYR A CB 715 C CG . TYR A 89 ? 0.2164 0.2579 0.2206 -0.0056 -0.0143 -0.0053 171 TYR A CG 716 C CD1 . TYR A 89 ? 0.2116 0.2525 0.2142 -0.0061 -0.0147 -0.0061 171 TYR A CD1 717 C CD2 . TYR A 89 ? 0.1767 0.2189 0.1826 -0.0068 -0.0142 -0.0057 171 TYR A CD2 718 C CE1 . TYR A 89 ? 0.2054 0.2463 0.2082 -0.0076 -0.0150 -0.0074 171 TYR A CE1 719 C CE2 . TYR A 89 ? 0.1903 0.2322 0.1963 -0.0084 -0.0145 -0.0070 171 TYR A CE2 720 C CZ . TYR A 89 ? 0.2068 0.2480 0.2113 -0.0088 -0.0149 -0.0079 171 TYR A CZ 721 O OH . TYR A 89 ? 0.2244 0.2648 0.2288 -0.0103 -0.0151 -0.0093 171 TYR A OH 722 N N . ASN A 90 ? 0.2961 0.3307 0.2980 -0.0022 -0.0116 -0.0024 172 ASN A N 723 C CA . ASN A 90 ? 0.3387 0.3721 0.3401 -0.0010 -0.0109 -0.0015 172 ASN A CA 724 C C . ASN A 90 ? 0.3733 0.4033 0.3730 -0.0011 -0.0103 -0.0015 172 ASN A C 725 O O . ASN A 90 ? 0.4591 0.4874 0.4580 -0.0002 -0.0096 -0.0010 172 ASN A O 726 C CB . ASN A 90 ? 0.3501 0.3846 0.3532 -0.0008 -0.0105 -0.0014 172 ASN A CB 727 C CG . ASN A 90 ? 0.4687 0.5015 0.4719 -0.0019 -0.0099 -0.0019 172 ASN A CG 728 O OD1 . ASN A 90 ? 0.4225 0.4542 0.4253 -0.0029 -0.0102 -0.0025 172 ASN A OD1 729 N ND2 . ASN A 90 ? 0.2955 0.3281 0.2992 -0.0016 -0.0092 -0.0017 172 ASN A ND2 730 N N . SER A 91 ? 0.1884 0.2175 0.1877 -0.0021 -0.0104 -0.0022 173 SER A N 731 C CA . SER A 91 ? 0.2594 0.2859 0.2573 -0.0024 -0.0099 -0.0022 173 SER A CA 732 C C . SER A 91 ? 0.3656 0.3911 0.3619 -0.0021 -0.0100 -0.0018 173 SER A C 733 O O . SER A 91 ? 0.3659 0.3926 0.3620 -0.0023 -0.0105 -0.0020 173 SER A O 734 C CB . SER A 91 ? 0.2584 0.2846 0.2568 -0.0034 -0.0100 -0.0029 173 SER A CB 735 O OG . SER A 91 ? 0.2643 0.2908 0.2639 -0.0038 -0.0099 -0.0031 173 SER A OG 736 N N . ARG A 92 ? 0.1716 0.1950 0.1666 -0.0018 -0.0094 -0.0014 174 ARG A N 737 C CA . ARG A 92 ? 0.2584 0.2806 0.2518 -0.0018 -0.0093 -0.0009 174 ARG A CA 738 C C . ARG A 92 ? 0.2189 0.2399 0.2117 -0.0029 -0.0090 -0.0013 174 ARG A C 739 O O . ARG A 92 ? 0.2580 0.2778 0.2508 -0.0033 -0.0087 -0.0016 174 ARG A O 740 C CB . ARG A 92 ? 0.2298 0.2499 0.2220 -0.0008 -0.0087 -0.0001 174 ARG A CB 741 C CG . ARG A 92 ? 0.3491 0.3673 0.3393 -0.0009 -0.0084 0.0006 174 ARG A CG 742 C CD . ARG A 92 ? 0.4358 0.4519 0.4250 0.0004 -0.0078 0.0014 174 ARG A CD 743 N NE . ARG A 92 ? 0.4116 0.4253 0.4003 0.0001 -0.0071 0.0011 174 ARG A NE 744 C CZ . ARG A 92 ? 0.4716 0.4839 0.4600 0.0013 -0.0065 0.0014 174 ARG A CZ 745 N NH1 . ARG A 92 ? 0.3804 0.3936 0.3691 0.0030 -0.0066 0.0023 174 ARG A NH1 746 N NH2 . ARG A 92 ? 0.3151 0.3252 0.3028 0.0009 -0.0058 0.0009 174 ARG A NH2 747 N N . VAL A 93 ? 0.2630 0.2845 0.2552 -0.0033 -0.0092 -0.0015 175 VAL A N 748 C CA . VAL A 93 ? 0.2262 0.2472 0.2181 -0.0043 -0.0090 -0.0018 175 VAL A CA 749 C C . VAL A 93 ? 0.2837 0.3026 0.2740 -0.0046 -0.0084 -0.0013 175 VAL A C 750 O O . VAL A 93 ? 0.2419 0.2601 0.2309 -0.0043 -0.0082 -0.0006 175 VAL A O 751 C CB . VAL A 93 ? 0.2477 0.2702 0.2396 -0.0046 -0.0092 -0.0023 175 VAL A CB 752 C CG1 . VAL A 93 ? 0.2191 0.2415 0.2109 -0.0054 -0.0089 -0.0025 175 VAL A CG1 753 C CG2 . VAL A 93 ? 0.1787 0.2028 0.1720 -0.0045 -0.0097 -0.0030 175 VAL A CG2 754 N N . GLU A 94 ? 0.2701 0.2879 0.2603 -0.0053 -0.0081 -0.0015 176 GLU A N 755 C CA . GLU A 94 ? 0.2336 0.2493 0.2224 -0.0060 -0.0075 -0.0012 176 GLU A CA 756 C C . GLU A 94 ? 0.2543 0.2708 0.2428 -0.0071 -0.0075 -0.0012 176 GLU A C 757 O O . GLU A 94 ? 0.2684 0.2837 0.2555 -0.0076 -0.0071 -0.0007 176 GLU A O 758 C CB . GLU A 94 ? 0.3100 0.3243 0.2985 -0.0064 -0.0073 -0.0015 176 GLU A CB 759 C CG . GLU A 94 ? 0.2942 0.3080 0.2831 -0.0053 -0.0072 -0.0015 176 GLU A CG 760 C CD . GLU A 94 ? 0.3937 0.4054 0.3814 -0.0044 -0.0068 -0.0008 176 GLU A CD 761 O OE1 . GLU A 94 ? 0.4000 0.4096 0.3861 -0.0048 -0.0063 -0.0005 176 GLU A OE1 762 O OE2 . GLU A 94 ? 0.3168 0.3292 0.3052 -0.0032 -0.0068 -0.0006 176 GLU A OE2 763 N N . CYS A 95 ? 0.2182 0.2368 0.2080 -0.0074 -0.0078 -0.0018 177 CYS A N 764 C CA . CYS A 95 ? 0.2162 0.2362 0.2061 -0.0082 -0.0077 -0.0019 177 CYS A CA 765 C C . CYS A 95 ? 0.2439 0.2661 0.2355 -0.0079 -0.0080 -0.0026 177 CYS A C 766 O O . CYS A 95 ? 0.2374 0.2596 0.2299 -0.0074 -0.0084 -0.0029 177 CYS A O 767 C CB . CYS A 95 ? 0.2099 0.2291 0.1991 -0.0095 -0.0073 -0.0018 177 CYS A CB 768 S SG . CYS A 95 ? 0.3441 0.3621 0.3333 -0.0100 -0.0074 -0.0022 177 CYS A SG 769 N N . ILE A 96 ? 0.2130 0.2370 0.2049 -0.0082 -0.0079 -0.0028 178 ILE A N 770 C CA . ILE A 96 ? 0.1707 0.1965 0.1641 -0.0077 -0.0081 -0.0034 178 ILE A CA 771 C C . ILE A 96 ? 0.2658 0.2927 0.2601 -0.0083 -0.0081 -0.0034 178 ILE A C 772 O O . ILE A 96 ? 0.1779 0.2054 0.1718 -0.0092 -0.0079 -0.0032 178 ILE A O 773 C CB . ILE A 96 ? 0.1695 0.1968 0.1627 -0.0075 -0.0079 -0.0036 178 ILE A CB 774 C CG1 . ILE A 96 ? 0.1855 0.2120 0.1776 -0.0071 -0.0080 -0.0034 178 ILE A CG1 775 C CG2 . ILE A 96 ? 0.1775 0.2062 0.1721 -0.0068 -0.0080 -0.0044 178 ILE A CG2 776 C CD1 . ILE A 96 ? 0.1591 0.1853 0.1518 -0.0063 -0.0085 -0.0039 178 ILE A CD1 777 N N . GLY A 97 ? 0.2315 0.2588 0.2269 -0.0077 -0.0085 -0.0037 179 GLY A N 778 C CA . GLY A 97 ? 0.2374 0.2659 0.2336 -0.0080 -0.0086 -0.0037 179 GLY A CA 779 C C . GLY A 97 ? 0.2206 0.2487 0.2176 -0.0074 -0.0090 -0.0037 179 GLY A C 780 O O . GLY A 97 ? 0.2178 0.2445 0.2146 -0.0069 -0.0091 -0.0038 179 GLY A O 781 N N . TRP A 98 ? 0.2214 0.2508 0.2190 -0.0076 -0.0092 -0.0035 180 TRP A N 782 C CA . TRP A 98 ? 0.2139 0.2430 0.2121 -0.0069 -0.0095 -0.0033 180 TRP A CA 783 C C . TRP A 98 ? 0.2480 0.2771 0.2456 -0.0077 -0.0098 -0.0030 180 TRP A C 784 O O . TRP A 98 ? 0.2179 0.2475 0.2160 -0.0073 -0.0101 -0.0027 180 TRP A O 785 C CB . TRP A 98 ? 0.2561 0.2868 0.2557 -0.0059 -0.0096 -0.0033 180 TRP A CB 786 C CG . TRP A 98 ? 0.2843 0.3177 0.2846 -0.0060 -0.0094 -0.0033 180 TRP A CG 787 C CD1 . TRP A 98 ? 0.2646 0.2990 0.2655 -0.0054 -0.0090 -0.0037 180 TRP A CD1 788 C CD2 . TRP A 98 ? 0.2526 0.2882 0.2532 -0.0068 -0.0096 -0.0030 180 TRP A CD2 789 N NE1 . TRP A 98 ? 0.2562 0.2934 0.2578 -0.0057 -0.0089 -0.0036 180 TRP A NE1 790 C CE2 . TRP A 98 ? 0.2630 0.3011 0.2645 -0.0067 -0.0093 -0.0031 180 TRP A CE2 791 C CE3 . TRP A 98 ? 0.2219 0.2577 0.2220 -0.0078 -0.0101 -0.0027 180 TRP A CE3 792 C CZ2 . TRP A 98 ? 0.2438 0.2850 0.2461 -0.0075 -0.0094 -0.0028 180 TRP A CZ2 793 C CZ3 . TRP A 98 ? 0.2404 0.2790 0.2410 -0.0087 -0.0103 -0.0025 180 TRP A CZ3 794 C CH2 . TRP A 98 ? 0.2429 0.2842 0.2447 -0.0086 -0.0100 -0.0025 180 TRP A CH2 795 N N . SER A 99 ? 0.2101 0.2388 0.2066 -0.0089 -0.0097 -0.0030 181 SER A N 796 C CA . SER A 99 ? 0.1929 0.2210 0.1884 -0.0098 -0.0099 -0.0030 181 SER A CA 797 C C . SER A 99 ? 0.2101 0.2361 0.2040 -0.0108 -0.0095 -0.0032 181 SER A C 798 O O . SER A 99 ? 0.2147 0.2408 0.2085 -0.0111 -0.0091 -0.0032 181 SER A O 799 C CB . SER A 99 ? 0.1646 0.1954 0.1607 -0.0106 -0.0103 -0.0028 181 SER A CB 800 O OG . SER A 99 ? 0.1744 0.2048 0.1693 -0.0115 -0.0106 -0.0029 181 SER A OG 801 N N . SER A 100 ? 0.2094 0.2335 0.2021 -0.0111 -0.0094 -0.0033 182 SER A N 802 C CA . SER A 100 ? 0.1795 0.2010 0.1706 -0.0115 -0.0088 -0.0034 182 SER A CA 803 C C . SER A 100 ? 0.2184 0.2379 0.2078 -0.0123 -0.0087 -0.0037 182 SER A C 804 O O . SER A 100 ? 0.1998 0.2198 0.1890 -0.0124 -0.0089 -0.0038 182 SER A O 805 C CB . SER A 100 ? 0.2190 0.2393 0.2104 -0.0103 -0.0086 -0.0033 182 SER A CB 806 O OG . SER A 100 ? 0.2406 0.2599 0.2318 -0.0096 -0.0086 -0.0033 182 SER A OG 807 N N . THR A 101 ? 0.1814 0.1984 0.1693 -0.0128 -0.0081 -0.0038 183 THR A N 808 C CA . THR A 101 ? 0.1872 0.2015 0.1732 -0.0131 -0.0077 -0.0042 183 THR A CA 809 C C . THR A 101 ? 0.2263 0.2378 0.2113 -0.0126 -0.0070 -0.0040 183 THR A C 810 O O . THR A 101 ? 0.2163 0.2283 0.2019 -0.0124 -0.0070 -0.0036 183 THR A O 811 C CB . THR A 101 ? 0.2684 0.2823 0.2530 -0.0150 -0.0078 -0.0047 183 THR A CB 812 O OG1 . THR A 101 ? 0.2509 0.2620 0.2335 -0.0152 -0.0073 -0.0053 183 THR A OG1 813 C CG2 . THR A 101 ? 0.2483 0.2615 0.2323 -0.0164 -0.0075 -0.0047 183 THR A CG2 814 N N . SER A 102 ? 0.2685 0.2773 0.2521 -0.0122 -0.0065 -0.0042 184 SER A N 815 C CA . SER A 102 ? 0.2059 0.2120 0.1886 -0.0114 -0.0058 -0.0039 184 SER A CA 816 C C . SER A 102 ? 0.2669 0.2697 0.2475 -0.0113 -0.0051 -0.0044 184 SER A C 817 O O . SER A 102 ? 0.2788 0.2819 0.2592 -0.0112 -0.0051 -0.0048 184 SER A O 818 C CB . SER A 102 ? 0.1983 0.2056 0.1824 -0.0095 -0.0059 -0.0033 184 SER A CB 819 O OG . SER A 102 ? 0.1899 0.1954 0.1734 -0.0087 -0.0055 -0.0028 184 SER A OG 820 N N . CYS A 103 ? 0.2840 0.2835 0.2629 -0.0114 -0.0044 -0.0043 185 CYS A N 821 C CA . CYS A 103 ? 0.2292 0.2250 0.2060 -0.0110 -0.0035 -0.0047 185 CYS A CA 822 C C . CYS A 103 ? 0.2183 0.2105 0.1937 -0.0103 -0.0027 -0.0042 185 CYS A C 823 O O . CYS A 103 ? 0.2676 0.2597 0.2430 -0.0110 -0.0028 -0.0036 185 CYS A O 824 C CB . CYS A 103 ? 0.2490 0.2435 0.2241 -0.0130 -0.0034 -0.0058 185 CYS A CB 825 S SG . CYS A 103 ? 0.2686 0.2635 0.2432 -0.0157 -0.0038 -0.0059 185 CYS A SG 826 N N . HIS A 104 ? 0.2665 0.2560 0.2408 -0.0088 -0.0019 -0.0042 186 HIS A N 827 C CA . HIS A 104 ? 0.2226 0.2081 0.1953 -0.0079 -0.0010 -0.0036 186 HIS A CA 828 C C . HIS A 104 ? 0.2794 0.2602 0.2491 -0.0093 -0.0002 -0.0045 186 HIS A C 829 O O . HIS A 104 ? 0.2471 0.2272 0.2158 -0.0099 0.0001 -0.0057 186 HIS A O 830 C CB . HIS A 104 ? 0.2415 0.2269 0.2149 -0.0052 -0.0006 -0.0031 186 HIS A CB 831 C CG . HIS A 104 ? 0.2900 0.2731 0.2627 -0.0036 -0.0001 -0.0019 186 HIS A CG 832 N ND1 . HIS A 104 ? 0.3156 0.2935 0.2857 -0.0034 0.0010 -0.0019 186 HIS A ND1 833 C CD2 . HIS A 104 ? 0.3108 0.2961 0.2850 -0.0023 -0.0006 -0.0007 186 HIS A CD2 834 C CE1 . HIS A 104 ? 0.2904 0.2674 0.2605 -0.0017 0.0012 -0.0005 186 HIS A CE1 835 N NE2 . HIS A 104 ? 0.2791 0.2608 0.2516 -0.0011 0.0002 0.0002 186 HIS A NE2 836 N N . ASP A 105 ? 0.3007 0.2780 0.2687 -0.0101 0.0004 -0.0041 187 ASP A N 837 C CA . ASP A 105 ? 0.2519 0.2243 0.2170 -0.0117 0.0012 -0.0050 187 ASP A CA 838 C C . ASP A 105 ? 0.2981 0.2652 0.2610 -0.0097 0.0026 -0.0049 187 ASP A C 839 O O . ASP A 105 ? 0.3104 0.2725 0.2706 -0.0108 0.0035 -0.0056 187 ASP A O 840 C CB . ASP A 105 ? 0.2531 0.2244 0.2173 -0.0142 0.0012 -0.0047 187 ASP A CB 841 C CG . ASP A 105 ? 0.2648 0.2351 0.2291 -0.0131 0.0014 -0.0031 187 ASP A CG 842 O OD1 . ASP A 105 ? 0.2576 0.2269 0.2220 -0.0104 0.0018 -0.0022 187 ASP A OD1 843 O OD2 . ASP A 105 ? 0.3023 0.2732 0.2666 -0.0150 0.0012 -0.0026 187 ASP A OD2 844 N N . GLY A 106 ? 0.2997 0.2680 0.2640 -0.0068 0.0027 -0.0039 188 GLY A N 845 C CA . GLY A 106 ? 0.2379 0.2020 0.2006 -0.0045 0.0039 -0.0036 188 GLY A CA 846 C C . GLY A 106 ? 0.3126 0.2755 0.2754 -0.0031 0.0040 -0.0018 188 GLY A C 847 O O . GLY A 106 ? 0.3465 0.3082 0.3093 -0.0003 0.0046 -0.0009 188 GLY A O 848 N N . LYS A 107 ? 0.3446 0.3079 0.3073 -0.0050 0.0035 -0.0012 189 LYS A N 849 C CA . LYS A 107 ? 0.4013 0.3642 0.3641 -0.0039 0.0035 0.0006 189 LYS A CA 850 C C . LYS A 107 ? 0.3568 0.3260 0.3226 -0.0036 0.0022 0.0014 189 LYS A C 851 O O . LYS A 107 ? 0.3201 0.2910 0.2870 -0.0012 0.0019 0.0026 189 LYS A O 852 C CB . LYS A 107 ? 0.3104 0.2693 0.2708 -0.0063 0.0040 0.0009 189 LYS A CB 853 C CG . LYS A 107 ? 0.3469 0.2985 0.3039 -0.0066 0.0055 0.0004 189 LYS A CG 854 C CD . LYS A 107 ? 0.4469 0.3950 0.4019 -0.0091 0.0059 0.0009 189 LYS A CD 855 C CE . LYS A 107 ? 0.5003 0.4404 0.4516 -0.0095 0.0075 0.0005 189 LYS A CE 856 N NZ . LYS A 107 ? 0.4536 0.3902 0.4029 -0.0124 0.0080 0.0010 189 LYS A NZ 857 N N . SER A 108 ? 0.2996 0.2722 0.2665 -0.0058 0.0013 0.0006 190 SER A N 858 C CA . SER A 108 ? 0.3045 0.2827 0.2741 -0.0056 0.0001 0.0011 190 SER A CA 859 C C . SER A 108 ? 0.2903 0.2724 0.2617 -0.0071 -0.0007 -0.0001 190 SER A C 860 O O . SER A 108 ? 0.2668 0.2475 0.2371 -0.0088 -0.0004 -0.0013 190 SER A O 861 C CB . SER A 108 ? 0.2893 0.2679 0.2586 -0.0065 0.0000 0.0022 190 SER A CB 862 O OG . SER A 108 ? 0.4344 0.4113 0.4029 -0.0045 0.0003 0.0037 190 SER A OG 863 N N . ARG A 109 ? 0.3065 0.2934 0.2803 -0.0066 -0.0016 0.0001 191 ARG A N 864 C CA . ARG A 109 ? 0.2504 0.2410 0.2260 -0.0076 -0.0024 -0.0008 191 ARG A CA 865 C C . ARG A 109 ? 0.2952 0.2879 0.2713 -0.0097 -0.0029 -0.0009 191 ARG A C 866 O O . ARG A 109 ? 0.2491 0.2426 0.2254 -0.0097 -0.0030 0.0000 191 ARG A O 867 C CB . ARG A 109 ? 0.2299 0.2242 0.2078 -0.0059 -0.0030 -0.0006 191 ARG A CB 868 C CG . ARG A 109 ? 0.2641 0.2622 0.2439 -0.0069 -0.0038 -0.0014 191 ARG A CG 869 C CD . ARG A 109 ? 0.2294 0.2300 0.2111 -0.0053 -0.0042 -0.0014 191 ARG A CD 870 N NE . ARG A 109 ? 0.2159 0.2147 0.1968 -0.0045 -0.0036 -0.0018 191 ARG A NE 871 C CZ . ARG A 109 ? 0.2494 0.2483 0.2302 -0.0052 -0.0035 -0.0026 191 ARG A CZ 872 N NH1 . ARG A 109 ? 0.1936 0.1944 0.1749 -0.0068 -0.0041 -0.0031 191 ARG A NH1 873 N NH2 . ARG A 109 ? 0.2673 0.2645 0.2472 -0.0044 -0.0028 -0.0030 191 ARG A NH2 874 N N . MET A 110 ? 0.2052 0.1988 0.1814 -0.0114 -0.0031 -0.0019 192 MET A N 875 C CA . MET A 110 ? 0.2490 0.2456 0.2263 -0.0131 -0.0037 -0.0020 192 MET A CA 876 C C . MET A 110 ? 0.2559 0.2568 0.2356 -0.0124 -0.0046 -0.0023 192 MET A C 877 O O . MET A 110 ? 0.2470 0.2482 0.2270 -0.0120 -0.0047 -0.0029 192 MET A O 878 C CB . MET A 110 ? 0.2228 0.2182 0.1988 -0.0155 -0.0035 -0.0028 192 MET A CB 879 C CG . MET A 110 ? 0.2464 0.2456 0.2239 -0.0172 -0.0041 -0.0029 192 MET A CG 880 S SD . MET A 110 ? 0.2699 0.2687 0.2463 -0.0202 -0.0041 -0.0039 192 MET A SD 881 C CE . MET A 110 ? 0.2422 0.2416 0.2186 -0.0195 -0.0046 -0.0049 192 MET A CE 882 N N . SER A 111 ? 0.2797 0.2837 0.2610 -0.0123 -0.0050 -0.0019 193 SER A N 883 C CA . SER A 111 ? 0.2419 0.2496 0.2253 -0.0119 -0.0058 -0.0022 193 SER A CA 884 C C . SER A 111 ? 0.2586 0.2690 0.2429 -0.0133 -0.0061 -0.0023 193 SER A C 885 O O . SER A 111 ? 0.2824 0.2928 0.2662 -0.0139 -0.0058 -0.0019 193 SER A O 886 C CB . SER A 111 ? 0.2211 0.2302 0.2058 -0.0101 -0.0061 -0.0018 193 SER A CB 887 O OG . SER A 111 ? 0.2431 0.2505 0.2274 -0.0088 -0.0058 -0.0018 193 SER A OG 888 N N . ILE A 112 ? 0.2770 0.2899 0.2626 -0.0137 -0.0066 -0.0028 194 ILE A N 889 C CA . ILE A 112 ? 0.2281 0.2440 0.2148 -0.0147 -0.0069 -0.0029 194 ILE A CA 890 C C . ILE A 112 ? 0.2699 0.2888 0.2587 -0.0135 -0.0075 -0.0030 194 ILE A C 891 O O . ILE A 112 ? 0.2875 0.3065 0.2767 -0.0129 -0.0079 -0.0032 194 ILE A O 892 C CB . ILE A 112 ? 0.2614 0.2776 0.2475 -0.0165 -0.0071 -0.0034 194 ILE A CB 893 C CG1 . ILE A 112 ? 0.2938 0.3063 0.2776 -0.0179 -0.0064 -0.0035 194 ILE A CG1 894 C CG2 . ILE A 112 ? 0.2339 0.2538 0.2215 -0.0175 -0.0074 -0.0033 194 ILE A CG2 895 C CD1 . ILE A 112 ? 0.1516 0.1642 0.1346 -0.0200 -0.0065 -0.0041 194 ILE A CD1 896 N N . CYS A 113 ? 0.1933 0.2144 0.1832 -0.0132 -0.0076 -0.0028 195 CYS A N 897 C CA . CYS A 113 ? 0.2432 0.2668 0.2349 -0.0121 -0.0080 -0.0029 195 CYS A CA 898 C C . CYS A 113 ? 0.2767 0.3034 0.2696 -0.0128 -0.0081 -0.0029 195 CYS A C 899 O O . CYS A 113 ? 0.2062 0.2333 0.1986 -0.0137 -0.0077 -0.0028 195 CYS A O 900 C CB . CYS A 113 ? 0.2528 0.2763 0.2448 -0.0108 -0.0079 -0.0028 195 CYS A CB 901 S SG . CYS A 113 ? 0.3638 0.3849 0.3552 -0.0097 -0.0080 -0.0028 195 CYS A SG 902 N N . ILE A 114 ? 0.2069 0.2357 0.2012 -0.0123 -0.0085 -0.0031 196 ILE A N 903 C CA . ILE A 114 ? 0.1991 0.2313 0.1948 -0.0125 -0.0086 -0.0031 196 ILE A CA 904 C C . ILE A 114 ? 0.1971 0.2306 0.1941 -0.0108 -0.0086 -0.0032 196 ILE A C 905 O O . ILE A 114 ? 0.2393 0.2715 0.2365 -0.0097 -0.0088 -0.0033 196 ILE A O 906 C CB . ILE A 114 ? 0.1805 0.2145 0.1769 -0.0131 -0.0092 -0.0030 196 ILE A CB 907 C CG1 . ILE A 114 ? 0.1854 0.2180 0.1801 -0.0150 -0.0091 -0.0032 196 ILE A CG1 908 C CG2 . ILE A 114 ? 0.1948 0.2329 0.1929 -0.0130 -0.0093 -0.0029 196 ILE A CG2 909 C CD1 . ILE A 114 ? 0.1974 0.2309 0.1921 -0.0156 -0.0098 -0.0033 196 ILE A CD1 910 N N . SER A 115 ? 0.2045 0.2403 0.2023 -0.0108 -0.0082 -0.0032 197 SER A N 911 C CA . SER A 115 ? 0.2059 0.2428 0.2048 -0.0092 -0.0081 -0.0035 197 SER A CA 912 C C . SER A 115 ? 0.2237 0.2643 0.2241 -0.0091 -0.0078 -0.0034 197 SER A C 913 O O . SER A 115 ? 0.2663 0.3088 0.2669 -0.0105 -0.0078 -0.0032 197 SER A O 914 C CB . SER A 115 ? 0.1975 0.2329 0.1954 -0.0087 -0.0077 -0.0037 197 SER A CB 915 O OG . SER A 115 ? 0.2339 0.2707 0.2315 -0.0094 -0.0071 -0.0036 197 SER A OG 916 N N . GLY A 116 ? 0.1923 0.2340 0.1938 -0.0076 -0.0076 -0.0037 198 GLY A N 917 C CA . GLY A 116 ? 0.2627 0.3081 0.2657 -0.0071 -0.0072 -0.0037 198 GLY A CA 918 C C . GLY A 116 ? 0.2605 0.3072 0.2652 -0.0055 -0.0076 -0.0036 198 GLY A C 919 O O . GLY A 116 ? 0.2627 0.3073 0.2672 -0.0049 -0.0081 -0.0035 198 GLY A O 920 N N . PRO A 117 ? 0.2337 0.2838 0.2400 -0.0046 -0.0072 -0.0036 199 PRO A N 921 C CA . PRO A 117 ? 0.2248 0.2764 0.2327 -0.0029 -0.0075 -0.0033 199 PRO A CA 922 C C . PRO A 117 ? 0.2673 0.3212 0.2760 -0.0039 -0.0083 -0.0026 199 PRO A C 923 O O . PRO A 117 ? 0.1880 0.2425 0.1960 -0.0060 -0.0084 -0.0025 199 PRO A O 924 C CB . PRO A 117 ? 0.2878 0.3427 0.2972 -0.0018 -0.0067 -0.0036 199 PRO A CB 925 C CG . PRO A 117 ? 0.1991 0.2560 0.2081 -0.0036 -0.0062 -0.0036 199 PRO A CG 926 C CD . PRO A 117 ? 0.1853 0.2382 0.1920 -0.0051 -0.0064 -0.0037 199 PRO A CD 927 N N . ASN A 118 ? 0.2541 0.3090 0.2639 -0.0025 -0.0088 -0.0021 200 ASN A N 928 C CA . ASN A 118 ? 0.2753 0.3323 0.2856 -0.0033 -0.0097 -0.0014 200 ASN A CA 929 C C . ASN A 118 ? 0.2624 0.3239 0.2736 -0.0050 -0.0098 -0.0012 200 ASN A C 930 O O . ASN A 118 ? 0.2874 0.3495 0.2980 -0.0069 -0.0104 -0.0010 200 ASN A O 931 C CB . ASN A 118 ? 0.2626 0.3207 0.2741 -0.0012 -0.0102 -0.0006 200 ASN A CB 932 C CG . ASN A 118 ? 0.3047 0.3582 0.3151 -0.0001 -0.0103 -0.0006 200 ASN A CG 933 O OD1 . ASN A 118 ? 0.2908 0.3406 0.2996 -0.0008 -0.0100 -0.0013 200 ASN A OD1 934 N ND2 . ASN A 118 ? 0.4039 0.4576 0.4149 0.0015 -0.0107 0.0002 200 ASN A ND2 935 N N . ASN A 119 ? 0.1964 0.2610 0.2091 -0.0044 -0.0090 -0.0013 201 ASN A N 936 C CA . ASN A 119 ? 0.2463 0.3157 0.2603 -0.0059 -0.0090 -0.0011 201 ASN A CA 937 C C . ASN A 119 ? 0.2499 0.3189 0.2629 -0.0081 -0.0083 -0.0016 201 ASN A C 938 O O . ASN A 119 ? 0.2607 0.3335 0.2747 -0.0096 -0.0081 -0.0014 201 ASN A O 939 C CB . ASN A 119 ? 0.2995 0.3739 0.3162 -0.0039 -0.0086 -0.0008 201 ASN A CB 940 C CG . ASN A 119 ? 0.3878 0.4612 0.4046 -0.0023 -0.0074 -0.0014 201 ASN A CG 941 O OD1 . ASN A 119 ? 0.2475 0.3171 0.2624 -0.0029 -0.0069 -0.0020 201 ASN A OD1 942 N ND2 . ASN A 119 ? 0.2611 0.3382 0.2801 -0.0002 -0.0069 -0.0012 201 ASN A ND2 943 N N . ASN A 120 ? 0.2619 0.3261 0.2727 -0.0083 -0.0079 -0.0020 202 ASN A N 944 C CA . ASN A 120 ? 0.1965 0.2598 0.2060 -0.0101 -0.0071 -0.0023 202 ASN A CA 945 C C . ASN A 120 ? 0.2753 0.3332 0.2823 -0.0109 -0.0072 -0.0025 202 ASN A C 946 O O . ASN A 120 ? 0.2577 0.3136 0.2634 -0.0112 -0.0066 -0.0027 202 ASN A O 947 C CB . ASN A 120 ? 0.2163 0.2810 0.2265 -0.0088 -0.0060 -0.0026 202 ASN A CB 948 C CG . ASN A 120 ? 0.2411 0.3103 0.2524 -0.0102 -0.0053 -0.0024 202 ASN A CG 949 O OD1 . ASN A 120 ? 0.2901 0.3606 0.3014 -0.0126 -0.0056 -0.0020 202 ASN A OD1 950 N ND2 . ASN A 120 ? 0.2766 0.3483 0.2890 -0.0088 -0.0043 -0.0026 202 ASN A ND2 951 N N . ALA A 121 ? 0.2440 0.2998 0.2502 -0.0113 -0.0081 -0.0024 203 ALA A N 952 C CA . ALA A 121 ? 0.2155 0.2664 0.2194 -0.0119 -0.0082 -0.0026 203 ALA A CA 953 C C . ALA A 121 ? 0.2403 0.2900 0.2427 -0.0143 -0.0079 -0.0026 203 ALA A C 954 O O . ALA A 121 ? 0.2399 0.2922 0.2428 -0.0160 -0.0079 -0.0024 203 ALA A O 955 C CB . ALA A 121 ? 0.1798 0.2290 0.1834 -0.0114 -0.0090 -0.0025 203 ALA A CB 956 N N . SER A 122 ? 0.2221 0.2676 0.2225 -0.0144 -0.0076 -0.0027 204 SER A N 957 C CA . SER A 122 ? 0.2393 0.2827 0.2379 -0.0165 -0.0073 -0.0026 204 SER A CA 958 C C . SER A 122 ? 0.2643 0.3030 0.2610 -0.0163 -0.0074 -0.0026 204 SER A C 959 O O . SER A 122 ? 0.2512 0.2883 0.2477 -0.0146 -0.0075 -0.0028 204 SER A O 960 C CB . SER A 122 ? 0.2130 0.2570 0.2112 -0.0169 -0.0064 -0.0023 204 SER A CB 961 O OG . SER A 122 ? 0.2472 0.2894 0.2448 -0.0152 -0.0061 -0.0024 204 SER A OG 962 N N . ALA A 123 ? 0.2050 0.2416 0.2001 -0.0180 -0.0074 -0.0026 205 ALA A N 963 C CA . ALA A 123 ? 0.2187 0.2509 0.2119 -0.0178 -0.0074 -0.0027 205 ALA A CA 964 C C . ALA A 123 ? 0.2919 0.3216 0.2835 -0.0183 -0.0066 -0.0023 205 ALA A C 965 O O . ALA A 123 ? 0.2558 0.2862 0.2470 -0.0199 -0.0061 -0.0021 205 ALA A O 966 C CB . ALA A 123 ? 0.2147 0.2456 0.2069 -0.0193 -0.0077 -0.0030 205 ALA A CB 967 N N . VAL A 124 ? 0.1791 0.2059 0.1696 -0.0170 -0.0065 -0.0022 206 VAL A N 968 C CA . VAL A 124 ? 0.1953 0.2193 0.1840 -0.0173 -0.0059 -0.0017 206 VAL A CA 969 C C . VAL A 124 ? 0.2339 0.2538 0.2210 -0.0172 -0.0059 -0.0017 206 VAL A C 970 O O . VAL A 124 ? 0.1960 0.2152 0.1833 -0.0159 -0.0063 -0.0019 206 VAL A O 971 C CB . VAL A 124 ? 0.2344 0.2588 0.2232 -0.0157 -0.0058 -0.0014 206 VAL A CB 972 C CG1 . VAL A 124 ? 0.2122 0.2339 0.1990 -0.0160 -0.0052 -0.0006 206 VAL A CG1 973 C CG2 . VAL A 124 ? 0.1490 0.1774 0.1394 -0.0155 -0.0057 -0.0015 206 VAL A CG2 974 N N . VAL A 125 ? 0.2552 0.2724 0.2404 -0.0187 -0.0053 -0.0014 207 VAL A N 975 C CA . VAL A 125 ? 0.2631 0.2761 0.2465 -0.0186 -0.0051 -0.0015 207 VAL A CA 976 C C . VAL A 125 ? 0.2803 0.2904 0.2623 -0.0174 -0.0046 -0.0007 207 VAL A C 977 O O . VAL A 125 ? 0.2853 0.2945 0.2662 -0.0181 -0.0040 0.0000 207 VAL A O 978 C CB . VAL A 125 ? 0.2538 0.2648 0.2357 -0.0210 -0.0047 -0.0018 207 VAL A CB 979 C CG1 . VAL A 125 ? 0.2954 0.3016 0.2752 -0.0207 -0.0044 -0.0020 207 VAL A CG1 980 C CG2 . VAL A 125 ? 0.2651 0.2795 0.2485 -0.0222 -0.0054 -0.0025 207 VAL A CG2 981 N N . TRP A 126 ? 0.2620 0.2710 0.2440 -0.0155 -0.0049 -0.0007 208 TRP A N 982 C CA . TRP A 126 ? 0.2265 0.2331 0.2074 -0.0141 -0.0045 0.0001 208 TRP A CA 983 C C . TRP A 126 ? 0.2631 0.2653 0.2420 -0.0140 -0.0040 0.0002 208 TRP A C 984 O O . TRP A 126 ? 0.2551 0.2567 0.2341 -0.0141 -0.0041 -0.0006 208 TRP A O 985 C CB . TRP A 126 ? 0.2665 0.2750 0.2487 -0.0120 -0.0051 0.0001 208 TRP A CB 986 C CG . TRP A 126 ? 0.2524 0.2647 0.2362 -0.0119 -0.0055 0.0000 208 TRP A CG 987 C CD1 . TRP A 126 ? 0.2312 0.2464 0.2166 -0.0126 -0.0058 -0.0006 208 TRP A CD1 988 C CD2 . TRP A 126 ? 0.2825 0.2959 0.2663 -0.0108 -0.0057 0.0005 208 TRP A CD2 989 N NE1 . TRP A 126 ? 0.2327 0.2505 0.2190 -0.0120 -0.0060 -0.0006 208 TRP A NE1 990 C CE2 . TRP A 126 ? 0.2796 0.2964 0.2649 -0.0110 -0.0059 0.0000 208 TRP A CE2 991 C CE3 . TRP A 126 ? 0.3236 0.3357 0.3063 -0.0096 -0.0056 0.0013 208 TRP A CE3 992 C CZ2 . TRP A 126 ? 0.2401 0.2587 0.2256 -0.0102 -0.0061 0.0001 208 TRP A CZ2 993 C CZ3 . TRP A 126 ? 0.2318 0.2461 0.2148 -0.0089 -0.0058 0.0015 208 TRP A CZ3 994 C CH2 . TRP A 126 ? 0.2295 0.2469 0.2137 -0.0093 -0.0061 0.0009 208 TRP A CH2 995 N N . TYR A 127 ? 0.2798 0.2789 0.2569 -0.0138 -0.0033 0.0011 209 TYR A N 996 C CA . TYR A 127 ? 0.2556 0.2499 0.2307 -0.0133 -0.0027 0.0013 209 TYR A CA 997 C C . TYR A 127 ? 0.2976 0.2907 0.2720 -0.0112 -0.0025 0.0025 209 TYR A C 998 O O . TYR A 127 ? 0.2239 0.2173 0.1977 -0.0113 -0.0023 0.0035 209 TYR A O 999 C CB . TYR A 127 ? 0.3188 0.3096 0.2918 -0.0155 -0.0019 0.0012 209 TYR A CB 1000 C CG . TYR A 127 ? 0.3290 0.3146 0.2998 -0.0150 -0.0011 0.0010 209 TYR A CG 1001 C CD1 . TYR A 127 ? 0.2318 0.2169 0.2028 -0.0150 -0.0012 -0.0002 209 TYR A CD1 1002 C CD2 . TYR A 127 ? 0.2732 0.2544 0.2418 -0.0145 -0.0002 0.0021 209 TYR A CD2 1003 C CE1 . TYR A 127 ? 0.2892 0.2695 0.2580 -0.0144 -0.0004 -0.0004 209 TYR A CE1 1004 C CE2 . TYR A 127 ? 0.2454 0.2215 0.2120 -0.0139 0.0006 0.0019 209 TYR A CE2 1005 C CZ . TYR A 127 ? 0.2781 0.2538 0.2448 -0.0138 0.0005 0.0006 209 TYR A CZ 1006 O OH . TYR A 127 ? 0.3110 0.2816 0.2755 -0.0131 0.0014 0.0002 209 TYR A OH 1007 N N . ASN A 128 ? 0.2558 0.2476 0.2302 -0.0093 -0.0025 0.0025 210 ASN A N 1008 C CA . ASN A 128 ? 0.2962 0.2874 0.2703 -0.0070 -0.0024 0.0037 210 ASN A CA 1009 C C . ASN A 128 ? 0.2977 0.2931 0.2732 -0.0064 -0.0032 0.0041 210 ASN A C 1010 O O . ASN A 128 ? 0.3035 0.2986 0.2780 -0.0058 -0.0032 0.0053 210 ASN A O 1011 C CB . ASN A 128 ? 0.2698 0.2562 0.2412 -0.0069 -0.0015 0.0048 210 ASN A CB 1012 C CG . ASN A 128 ? 0.3666 0.3519 0.3375 -0.0042 -0.0014 0.0061 210 ASN A CG 1013 O OD1 . ASN A 128 ? 0.3835 0.3706 0.3558 -0.0024 -0.0018 0.0058 210 ASN A OD1 1014 N ND2 . ASN A 128 ? 0.3757 0.3584 0.3447 -0.0039 -0.0009 0.0076 210 ASN A ND2 1015 N N . ARG A 129 ? 0.3151 0.3143 0.2928 -0.0067 -0.0040 0.0032 211 ARG A N 1016 C CA . ARG A 129 ? 0.3635 0.3668 0.3427 -0.0062 -0.0048 0.0032 211 ARG A CA 1017 C C . ARG A 129 ? 0.3479 0.3523 0.3264 -0.0073 -0.0046 0.0037 211 ARG A C 1018 O O . ARG A 129 ? 0.3419 0.3489 0.3210 -0.0066 -0.0051 0.0040 211 ARG A O 1019 C CB . ARG A 129 ? 0.3996 0.4037 0.3791 -0.0040 -0.0052 0.0039 211 ARG A CB 1020 C CG . ARG A 129 ? 0.5493 0.5519 0.5291 -0.0027 -0.0050 0.0037 211 ARG A CG 1021 C CD . ARG A 129 ? 0.5021 0.5077 0.4837 -0.0011 -0.0057 0.0038 211 ARG A CD 1022 N NE . ARG A 129 ? 0.6645 0.6720 0.6480 -0.0014 -0.0060 0.0026 211 ARG A NE 1023 C CZ . ARG A 129 ? 0.6149 0.6252 0.5998 -0.0023 -0.0066 0.0018 211 ARG A CZ 1024 N NH1 . ARG A 129 ? 0.6438 0.6556 0.6285 -0.0029 -0.0070 0.0019 211 ARG A NH1 1025 N NH2 . ARG A 129 ? 0.5143 0.5258 0.5007 -0.0026 -0.0068 0.0009 211 ARG A NH2 1026 N N . ARG A 130 ? 0.2624 0.2650 0.2398 -0.0091 -0.0040 0.0037 212 ARG A N 1027 C CA . ARG A 130 ? 0.2421 0.2462 0.2192 -0.0104 -0.0038 0.0041 212 ARG A CA 1028 C C . ARG A 130 ? 0.2635 0.2687 0.2414 -0.0125 -0.0036 0.0031 212 ARG A C 1029 O O . ARG A 130 ? 0.2540 0.2571 0.2316 -0.0135 -0.0034 0.0026 212 ARG A O 1030 C CB . ARG A 130 ? 0.2968 0.2975 0.2714 -0.0108 -0.0030 0.0054 212 ARG A CB 1031 C CG . ARG A 130 ? 0.3073 0.3067 0.2808 -0.0087 -0.0030 0.0067 212 ARG A CG 1032 C CD . ARG A 130 ? 0.2595 0.2552 0.2303 -0.0092 -0.0021 0.0082 212 ARG A CD 1033 N NE . ARG A 130 ? 0.3032 0.2983 0.2729 -0.0071 -0.0023 0.0096 212 ARG A NE 1034 C CZ . ARG A 130 ? 0.3912 0.3829 0.3598 -0.0054 -0.0020 0.0104 212 ARG A CZ 1035 N NH1 . ARG A 130 ? 0.2737 0.2621 0.2420 -0.0057 -0.0015 0.0098 212 ARG A NH1 1036 N NH2 . ARG A 130 ? 0.3304 0.3222 0.2981 -0.0034 -0.0023 0.0119 212 ARG A NH2 1037 N N . PRO A 131 ? 0.3178 0.3265 0.2968 -0.0132 -0.0038 0.0029 213 PRO A N 1038 C CA . PRO A 131 ? 0.2651 0.2756 0.2451 -0.0151 -0.0037 0.0022 213 PRO A CA 1039 C C . PRO A 131 ? 0.3129 0.3210 0.2913 -0.0171 -0.0028 0.0027 213 PRO A C 1040 O O . PRO A 131 ? 0.2604 0.2673 0.2372 -0.0173 -0.0023 0.0038 213 PRO A O 1041 C CB . PRO A 131 ? 0.2622 0.2769 0.2436 -0.0149 -0.0039 0.0020 213 PRO A CB 1042 C CG . PRO A 131 ? 0.2864 0.3006 0.2664 -0.0138 -0.0037 0.0029 213 PRO A CG 1043 C CD . PRO A 131 ? 0.2762 0.2875 0.2554 -0.0123 -0.0040 0.0033 213 PRO A CD 1044 N N . VAL A 132 ? 0.1784 0.1857 0.1569 -0.0187 -0.0028 0.0020 214 VAL A N 1045 C CA . VAL A 132 ? 0.2553 0.2597 0.2320 -0.0209 -0.0020 0.0024 214 VAL A CA 1046 C C . VAL A 132 ? 0.2418 0.2493 0.2197 -0.0233 -0.0019 0.0018 214 VAL A C 1047 O O . VAL A 132 ? 0.3113 0.3190 0.2885 -0.0251 -0.0013 0.0024 214 VAL A O 1048 C CB . VAL A 132 ? 0.2244 0.2239 0.1994 -0.0210 -0.0017 0.0021 214 VAL A CB 1049 C CG1 . VAL A 132 ? 0.3112 0.3079 0.2845 -0.0238 -0.0010 0.0020 214 VAL A CG1 1050 C CG2 . VAL A 132 ? 0.3289 0.3250 0.3023 -0.0189 -0.0014 0.0030 214 VAL A CG2 1051 N N . ALA A 133 ? 0.2652 0.2755 0.2449 -0.0233 -0.0027 0.0007 215 ALA A N 1052 C CA . ALA A 133 ? 0.2515 0.2653 0.2327 -0.0253 -0.0028 0.0002 215 ALA A CA 1053 C C . ALA A 133 ? 0.3106 0.3294 0.2946 -0.0240 -0.0037 -0.0004 215 ALA A C 1054 O O . ALA A 133 ? 0.2527 0.2712 0.2371 -0.0220 -0.0042 -0.0006 215 ALA A O 1055 C CB . ALA A 133 ? 0.2882 0.2998 0.2684 -0.0273 -0.0029 -0.0006 215 ALA A CB 1056 N N . GLU A 134 ? 0.2111 0.2341 0.1967 -0.0253 -0.0037 -0.0006 216 GLU A N 1057 C CA . GLU A 134 ? 0.2958 0.3235 0.2840 -0.0240 -0.0044 -0.0010 216 GLU A CA 1058 C C . GLU A 134 ? 0.2902 0.3212 0.2799 -0.0258 -0.0048 -0.0015 216 GLU A C 1059 O O . GLU A 134 ? 0.2589 0.2902 0.2481 -0.0282 -0.0044 -0.0014 216 GLU A O 1060 C CB . GLU A 134 ? 0.2526 0.2832 0.2418 -0.0232 -0.0039 -0.0006 216 GLU A CB 1061 C CG . GLU A 134 ? 0.2548 0.2828 0.2424 -0.0218 -0.0035 0.0000 216 GLU A CG 1062 C CD . GLU A 134 ? 0.2989 0.3238 0.2842 -0.0234 -0.0026 0.0009 216 GLU A CD 1063 O OE1 . GLU A 134 ? 0.3181 0.3446 0.3036 -0.0255 -0.0021 0.0011 216 GLU A OE1 1064 O OE2 . GLU A 134 ? 0.3420 0.3628 0.3254 -0.0226 -0.0025 0.0014 216 GLU A OE2 1065 N N . ILE A 135 ? 0.2585 0.2921 0.2499 -0.0246 -0.0056 -0.0020 217 ILE A N 1066 C CA . ILE A 135 ? 0.2681 0.3053 0.2609 -0.0260 -0.0062 -0.0024 217 ILE A CA 1067 C C . ILE A 135 ? 0.2834 0.3255 0.2790 -0.0242 -0.0066 -0.0024 217 ILE A C 1068 O O . ILE A 135 ? 0.2608 0.3025 0.2569 -0.0220 -0.0070 -0.0025 217 ILE A O 1069 C CB . ILE A 135 ? 0.2791 0.3141 0.2709 -0.0264 -0.0069 -0.0030 217 ILE A CB 1070 C CG1 . ILE A 135 ? 0.2959 0.3255 0.2849 -0.0278 -0.0063 -0.0031 217 ILE A CG1 1071 C CG2 . ILE A 135 ? 0.2447 0.2838 0.2378 -0.0280 -0.0076 -0.0034 217 ILE A CG2 1072 C CD1 . ILE A 135 ? 0.3270 0.3537 0.3145 -0.0277 -0.0068 -0.0037 217 ILE A CD1 1073 N N . ASN A 136 ? 0.2984 0.3452 0.2958 -0.0253 -0.0065 -0.0022 218 ASN A N 1074 C CA . ASN A 136 ? 0.2301 0.2816 0.2301 -0.0235 -0.0068 -0.0022 218 ASN A CA 1075 C C . ASN A 136 ? 0.2411 0.2951 0.2424 -0.0234 -0.0079 -0.0024 218 ASN A C 1076 O O . ASN A 136 ? 0.2229 0.2765 0.2233 -0.0255 -0.0083 -0.0027 218 ASN A O 1077 C CB . ASN A 136 ? 0.1829 0.2387 0.1845 -0.0242 -0.0061 -0.0019 218 ASN A CB 1078 C CG . ASN A 136 ? 0.3294 0.3889 0.3332 -0.0217 -0.0060 -0.0018 218 ASN A CG 1079 O OD1 . ASN A 136 ? 0.2909 0.3483 0.2944 -0.0194 -0.0060 -0.0020 218 ASN A OD1 1080 N ND2 . ASN A 136 ? 0.2958 0.3610 0.3020 -0.0221 -0.0058 -0.0017 218 ASN A ND2 1081 N N . THR A 137 ? 0.2206 0.2768 0.2236 -0.0210 -0.0083 -0.0023 219 THR A N 1082 C CA . THR A 137 ? 0.2453 0.3045 0.2497 -0.0206 -0.0094 -0.0023 219 THR A CA 1083 C C . THR A 137 ? 0.2428 0.3068 0.2485 -0.0228 -0.0096 -0.0022 219 THR A C 1084 O O . THR A 137 ? 0.2558 0.3228 0.2627 -0.0236 -0.0090 -0.0020 219 THR A O 1085 C CB . THR A 137 ? 0.2006 0.2618 0.2069 -0.0175 -0.0095 -0.0020 219 THR A CB 1086 O OG1 . THR A 137 ? 0.2227 0.2868 0.2302 -0.0170 -0.0105 -0.0018 219 THR A OG1 1087 C CG2 . THR A 137 ? 0.2163 0.2811 0.2244 -0.0168 -0.0087 -0.0019 219 THR A CG2 1088 N N . TRP A 138 ? 0.2863 0.3510 0.2916 -0.0240 -0.0106 -0.0024 220 TRP A N 1089 C CA . TRP A 138 ? 0.2914 0.3610 0.2980 -0.0263 -0.0111 -0.0024 220 TRP A CA 1090 C C . TRP A 138 ? 0.2976 0.3726 0.3066 -0.0249 -0.0122 -0.0020 220 TRP A C 1091 O O . TRP A 138 ? 0.3247 0.4052 0.3355 -0.0263 -0.0126 -0.0018 220 TRP A O 1092 C CB . TRP A 138 ? 0.2513 0.3180 0.2554 -0.0293 -0.0114 -0.0031 220 TRP A CB 1093 C CG . TRP A 138 ? 0.2800 0.3431 0.2822 -0.0287 -0.0122 -0.0034 220 TRP A CG 1094 C CD1 . TRP A 138 ? 0.2516 0.3171 0.2542 -0.0284 -0.0134 -0.0034 220 TRP A CD1 1095 C CD2 . TRP A 138 ? 0.2151 0.2717 0.2147 -0.0282 -0.0117 -0.0037 220 TRP A CD2 1096 N NE1 . TRP A 138 ? 0.2808 0.3417 0.2810 -0.0278 -0.0136 -0.0037 220 TRP A NE1 1097 C CE2 . TRP A 138 ? 0.2180 0.2734 0.2164 -0.0276 -0.0126 -0.0040 220 TRP A CE2 1098 C CE3 . TRP A 138 ? 0.2255 0.2774 0.2235 -0.0281 -0.0106 -0.0038 220 TRP A CE3 1099 C CZ2 . TRP A 138 ? 0.1914 0.2412 0.1874 -0.0270 -0.0123 -0.0043 220 TRP A CZ2 1100 C CZ3 . TRP A 138 ? 0.1799 0.2263 0.1755 -0.0273 -0.0105 -0.0041 220 TRP A CZ3 1101 C CH2 . TRP A 138 ? 0.2623 0.3078 0.2571 -0.0268 -0.0113 -0.0044 220 TRP A CH2 1102 N N . ALA A 139 ? 0.2407 0.3144 0.2499 -0.0220 -0.0125 -0.0017 221 ALA A N 1103 C CA . ALA A 139 ? 0.3057 0.3838 0.3169 -0.0202 -0.0135 -0.0010 221 ALA A CA 1104 C C . ALA A 139 ? 0.3077 0.3864 0.3206 -0.0168 -0.0130 -0.0005 221 ALA A C 1105 O O . ALA A 139 ? 0.3077 0.3900 0.3225 -0.0148 -0.0136 0.0001 221 ALA A O 1106 C CB . ALA A 139 ? 0.2982 0.3743 0.3077 -0.0202 -0.0146 -0.0011 221 ALA A CB 1107 N N . ARG A 140 ? 0.3046 0.3795 0.3166 -0.0161 -0.0119 -0.0009 222 ARG A N 1108 C CA . ARG A 140 ? 0.3032 0.3780 0.3165 -0.0131 -0.0112 -0.0006 222 ARG A CA 1109 C C . ARG A 140 ? 0.2610 0.3344 0.2744 -0.0106 -0.0119 -0.0002 222 ARG A C 1110 O O . ARG A 140 ? 0.2510 0.3266 0.2662 -0.0081 -0.0117 0.0002 222 ARG A O 1111 C CB . ARG A 140 ? 0.2893 0.3701 0.3054 -0.0126 -0.0108 -0.0003 222 ARG A CB 1112 C CG . ARG A 140 ? 0.3956 0.4787 0.4118 -0.0156 -0.0103 -0.0006 222 ARG A CG 1113 C CD . ARG A 140 ? 0.5021 0.5877 0.5197 -0.0148 -0.0090 -0.0006 222 ARG A CD 1114 N NE . ARG A 140 ? 0.7864 0.8691 0.8022 -0.0170 -0.0081 -0.0010 222 ARG A NE 1115 C CZ . ARG A 140 ? 0.7295 0.8142 0.7459 -0.0173 -0.0069 -0.0010 222 ARG A CZ 1116 N NH1 . ARG A 140 ? 0.8703 0.9601 0.8893 -0.0157 -0.0064 -0.0008 222 ARG A NH1 1117 N NH2 . ARG A 140 ? 0.5892 0.6707 0.6035 -0.0193 -0.0061 -0.0012 222 ARG A NH2 1118 N N . ASN A 141 ? 0.1913 0.2610 0.2027 -0.0111 -0.0124 -0.0003 223 ASN A N 1119 C CA . ASN A 141 ? 0.2187 0.2866 0.2299 -0.0090 -0.0129 0.0002 223 ASN A CA 1120 C C . ASN A 141 ? 0.2736 0.3359 0.2822 -0.0095 -0.0129 -0.0002 223 ASN A C 1121 O O . ASN A 141 ? 0.2459 0.3073 0.2532 -0.0105 -0.0137 -0.0001 223 ASN A O 1122 C CB . ASN A 141 ? 0.2741 0.3463 0.2863 -0.0088 -0.0141 0.0009 223 ASN A CB 1123 C CG . ASN A 141 ? 0.3171 0.3879 0.3293 -0.0064 -0.0146 0.0017 223 ASN A CG 1124 O OD1 . ASN A 141 ? 0.2717 0.3384 0.2833 -0.0048 -0.0140 0.0016 223 ASN A OD1 1125 N ND2 . ASN A 141 ? 0.3012 0.3753 0.3140 -0.0062 -0.0157 0.0025 223 ASN A ND2 1126 N N . ILE A 142 ? 0.2649 0.3236 0.2728 -0.0087 -0.0121 -0.0006 224 ILE A N 1127 C CA . ILE A 142 ? 0.3086 0.3621 0.3144 -0.0089 -0.0119 -0.0010 224 ILE A CA 1128 C C . ILE A 142 ? 0.2396 0.2914 0.2434 -0.0113 -0.0121 -0.0014 224 ILE A C 1129 O O . ILE A 142 ? 0.2365 0.2871 0.2392 -0.0118 -0.0126 -0.0013 224 ILE A O 1130 C CB . ILE A 142 ? 0.2871 0.3389 0.2927 -0.0072 -0.0124 -0.0005 224 ILE A CB 1131 C CG1 . ILE A 142 ? 0.3189 0.3724 0.3264 -0.0048 -0.0122 0.0000 224 ILE A CG1 1132 C CG2 . ILE A 142 ? 0.1699 0.2168 0.1738 -0.0072 -0.0120 -0.0009 224 ILE A CG2 1133 C CD1 . ILE A 142 ? 0.2855 0.3369 0.2927 -0.0031 -0.0125 0.0006 224 ILE A CD1 1134 N N . LEU A 143 ? 0.2388 0.2905 0.2423 -0.0129 -0.0115 -0.0018 225 LEU A N 1135 C CA . LEU A 143 ? 0.2745 0.3234 0.2758 -0.0150 -0.0114 -0.0023 225 LEU A CA 1136 C C . LEU A 143 ? 0.2566 0.3010 0.2563 -0.0141 -0.0113 -0.0024 225 LEU A C 1137 O O . LEU A 143 ? 0.1836 0.2262 0.1835 -0.0127 -0.0109 -0.0024 225 LEU A O 1138 C CB . LEU A 143 ? 0.2353 0.2840 0.2363 -0.0163 -0.0106 -0.0025 225 LEU A CB 1139 C CG . LEU A 143 ? 0.2445 0.2891 0.2431 -0.0181 -0.0102 -0.0029 225 LEU A CG 1140 C CD1 . LEU A 143 ? 0.2146 0.2595 0.2122 -0.0202 -0.0107 -0.0032 225 LEU A CD1 1141 C CD2 . LEU A 143 ? 0.2659 0.3104 0.2643 -0.0189 -0.0093 -0.0029 225 LEU A CD2 1142 N N . ARG A 144 ? 0.2325 0.2751 0.2306 -0.0151 -0.0117 -0.0026 226 ARG A N 1143 C CA . ARG A 144 ? 0.1773 0.2162 0.1741 -0.0142 -0.0116 -0.0027 226 ARG A CA 1144 C C . ARG A 144 ? 0.2176 0.2540 0.2121 -0.0157 -0.0116 -0.0032 226 ARG A C 1145 O O . ARG A 144 ? 0.2646 0.3022 0.2585 -0.0175 -0.0119 -0.0035 226 ARG A O 1146 C CB . ARG A 144 ? 0.2033 0.2434 0.2011 -0.0125 -0.0121 -0.0022 226 ARG A CB 1147 C CG . ARG A 144 ? 0.1958 0.2389 0.1937 -0.0131 -0.0130 -0.0018 226 ARG A CG 1148 C CD . ARG A 144 ? 0.2171 0.2620 0.2164 -0.0112 -0.0134 -0.0010 226 ARG A CD 1149 N NE . ARG A 144 ? 0.1989 0.2469 0.1983 -0.0115 -0.0144 -0.0005 226 ARG A NE 1150 C CZ . ARG A 144 ? 0.2843 0.3368 0.2854 -0.0116 -0.0149 -0.0002 226 ARG A CZ 1151 N NH1 . ARG A 144 ? 0.1934 0.2477 0.1961 -0.0115 -0.0144 -0.0003 226 ARG A NH1 1152 N NH2 . ARG A 144 ? 0.2330 0.2884 0.2340 -0.0118 -0.0159 0.0003 226 ARG A NH2 1153 N N . THR A 145 ? 0.2256 0.2584 0.2189 -0.0150 -0.0112 -0.0033 227 THR A N 1154 C CA . THR A 145 ? 0.1843 0.2142 0.1753 -0.0162 -0.0109 -0.0039 227 THR A CA 1155 C C . THR A 145 ? 0.1734 0.2012 0.1635 -0.0152 -0.0109 -0.0038 227 THR A C 1156 O O . THR A 145 ? 0.2492 0.2784 0.2403 -0.0140 -0.0113 -0.0033 227 THR A O 1157 C CB . THR A 145 ? 0.2388 0.2660 0.2288 -0.0170 -0.0101 -0.0042 227 THR A CB 1158 O OG1 . THR A 145 ? 0.2159 0.2403 0.2036 -0.0183 -0.0099 -0.0048 227 THR A OG1 1159 C CG2 . THR A 145 ? 0.1981 0.2233 0.1884 -0.0153 -0.0096 -0.0039 227 THR A CG2 1160 N N . GLN A 146 ? 0.2258 0.2504 0.2140 -0.0157 -0.0103 -0.0043 228 GLN A N 1161 C CA . GLN A 146 ? 0.1814 0.2043 0.1682 -0.0153 -0.0102 -0.0045 228 GLN A CA 1162 C C . GLN A 146 ? 0.2148 0.2373 0.2026 -0.0134 -0.0101 -0.0040 228 GLN A C 1163 O O . GLN A 146 ? 0.2133 0.2363 0.2007 -0.0131 -0.0103 -0.0038 228 GLN A O 1164 C CB . GLN A 146 ? 0.1825 0.2019 0.1669 -0.0161 -0.0095 -0.0052 228 GLN A CB 1165 C CG . GLN A 146 ? 0.2137 0.2330 0.1967 -0.0183 -0.0097 -0.0059 228 GLN A CG 1166 C CD . GLN A 146 ? 0.2845 0.2997 0.2650 -0.0190 -0.0088 -0.0067 228 GLN A CD 1167 O OE1 . GLN A 146 ? 0.2943 0.3085 0.2734 -0.0209 -0.0088 -0.0074 228 GLN A OE1 1168 N NE2 . GLN A 146 ? 0.2563 0.2690 0.2362 -0.0176 -0.0082 -0.0067 228 GLN A NE2 1169 N N . GLU A 147 ? 0.2012 0.2229 0.1900 -0.0125 -0.0097 -0.0038 229 GLU A N 1170 C CA . GLU A 147 ? 0.2074 0.2284 0.1969 -0.0110 -0.0095 -0.0034 229 GLU A CA 1171 C C . GLU A 147 ? 0.2378 0.2566 0.2259 -0.0108 -0.0089 -0.0037 229 GLU A C 1172 O O . GLU A 147 ? 0.2623 0.2809 0.2509 -0.0099 -0.0087 -0.0034 229 GLU A O 1173 C CB . GLU A 147 ? 0.2311 0.2540 0.2220 -0.0102 -0.0100 -0.0028 229 GLU A CB 1174 C CG . GLU A 147 ? 0.2297 0.2553 0.2218 -0.0103 -0.0106 -0.0026 229 GLU A CG 1175 C CD . GLU A 147 ? 0.2315 0.2576 0.2249 -0.0100 -0.0104 -0.0026 229 GLU A CD 1176 O OE1 . GLU A 147 ? 0.2317 0.2562 0.2249 -0.0098 -0.0099 -0.0029 229 GLU A OE1 1177 O OE2 . GLU A 147 ? 0.2143 0.2427 0.2089 -0.0098 -0.0108 -0.0024 229 GLU A OE2 1178 N N . SER A 148 ? 0.1969 0.2138 0.1832 -0.0117 -0.0085 -0.0043 230 SER A N 1179 C CA . SER A 148 ? 0.2147 0.2290 0.1996 -0.0113 -0.0077 -0.0046 230 SER A CA 1180 C C . SER A 148 ? 0.2218 0.2337 0.2051 -0.0120 -0.0072 -0.0051 230 SER A C 1181 O O . SER A 148 ? 0.1962 0.2085 0.1795 -0.0131 -0.0075 -0.0052 230 SER A O 1182 C CB . SER A 148 ? 0.1920 0.2062 0.1756 -0.0114 -0.0076 -0.0048 230 SER A CB 1183 O OG . SER A 148 ? 0.2222 0.2368 0.2043 -0.0129 -0.0080 -0.0053 230 SER A OG 1184 N N . GLU A 149 ? 0.2270 0.2362 0.2090 -0.0114 -0.0064 -0.0054 231 GLU A N 1185 C CA . GLU A 149 ? 0.2253 0.2316 0.2058 -0.0118 -0.0058 -0.0057 231 GLU A CA 1186 C C . GLU A 149 ? 0.2909 0.2961 0.2695 -0.0138 -0.0058 -0.0065 231 GLU A C 1187 O O . GLU A 149 ? 0.2337 0.2397 0.2114 -0.0146 -0.0061 -0.0070 231 GLU A O 1188 C CB . GLU A 149 ? 0.2097 0.2134 0.1893 -0.0105 -0.0048 -0.0058 231 GLU A CB 1189 C CG . GLU A 149 ? 0.2234 0.2251 0.2007 -0.0108 -0.0042 -0.0067 231 GLU A CG 1190 C CD . GLU A 149 ? 0.2958 0.2945 0.2720 -0.0093 -0.0030 -0.0068 231 GLU A CD 1191 O OE1 . GLU A 149 ? 0.2529 0.2516 0.2304 -0.0080 -0.0029 -0.0061 231 GLU A OE1 1192 O OE2 . GLU A 149 ? 0.2628 0.2593 0.2370 -0.0095 -0.0023 -0.0076 231 GLU A OE2 1193 N N . CYS A 150 ? 0.2326 0.2359 0.2104 -0.0146 -0.0056 -0.0065 232 CYS A N 1194 C CA . CYS A 150 ? 0.2865 0.2881 0.2623 -0.0167 -0.0054 -0.0073 232 CYS A CA 1195 C C . CYS A 150 ? 0.2747 0.2717 0.2480 -0.0163 -0.0043 -0.0080 232 CYS A C 1196 O O . CYS A 150 ? 0.2545 0.2506 0.2280 -0.0143 -0.0038 -0.0077 232 CYS A O 1197 C CB . CYS A 150 ? 0.2906 0.2924 0.2667 -0.0180 -0.0056 -0.0070 232 CYS A CB 1198 S SG . CYS A 150 ? 0.3041 0.3054 0.2815 -0.0164 -0.0052 -0.0059 232 CYS A SG 1199 N N . VAL A 151 ? 0.2128 0.2070 0.1837 -0.0181 -0.0040 -0.0089 233 VAL A N 1200 C CA . VAL A 151 ? 0.2742 0.2636 0.2424 -0.0178 -0.0028 -0.0097 233 VAL A CA 1201 C C . VAL A 151 ? 0.3103 0.2960 0.2766 -0.0194 -0.0023 -0.0099 233 VAL A C 1202 O O . VAL A 151 ? 0.3271 0.3142 0.2935 -0.0216 -0.0029 -0.0101 233 VAL A O 1203 C CB . VAL A 151 ? 0.2921 0.2809 0.2582 -0.0185 -0.0027 -0.0109 233 VAL A CB 1204 C CG1 . VAL A 151 ? 0.2910 0.2746 0.2544 -0.0177 -0.0013 -0.0118 233 VAL A CG1 1205 C CG2 . VAL A 151 ? 0.3068 0.2994 0.2747 -0.0172 -0.0033 -0.0105 233 VAL A CG2 1206 N N . CYS A 152 ? 0.2501 0.2311 0.2148 -0.0183 -0.0011 -0.0099 234 CYS A N 1207 C CA . CYS A 152 ? 0.2788 0.2557 0.2415 -0.0198 -0.0005 -0.0100 234 CYS A CA 1208 C C . CYS A 152 ? 0.3469 0.3182 0.3061 -0.0204 0.0007 -0.0114 234 CYS A C 1209 O O . CYS A 152 ? 0.2789 0.2489 0.2372 -0.0188 0.0013 -0.0119 234 CYS A O 1210 C CB . CYS A 152 ? 0.2985 0.2743 0.2622 -0.0180 0.0000 -0.0085 234 CYS A CB 1211 S SG . CYS A 152 ? 0.3073 0.2892 0.2747 -0.0173 -0.0013 -0.0071 234 CYS A SG 1212 N N . HIS A 153 ? 0.2638 0.2319 0.2210 -0.0229 0.0010 -0.0119 235 HIS A N 1213 C CA . HIS A 153 ? 0.3026 0.2642 0.2561 -0.0235 0.0023 -0.0132 235 HIS A CA 1214 C C . HIS A 153 ? 0.2761 0.2333 0.2281 -0.0249 0.0030 -0.0128 235 HIS A C 1215 O O . HIS A 153 ? 0.2938 0.2524 0.2461 -0.0277 0.0024 -0.0128 235 HIS A O 1216 C CB . HIS A 153 ? 0.2986 0.2605 0.2502 -0.0259 0.0019 -0.0151 235 HIS A CB 1217 C CG . HIS A 153 ? 0.3448 0.2998 0.2923 -0.0269 0.0033 -0.0167 235 HIS A CG 1218 N ND1 . HIS A 153 ? 0.3478 0.2993 0.2935 -0.0247 0.0045 -0.0174 235 HIS A ND1 1219 C CD2 . HIS A 153 ? 0.3793 0.3304 0.3243 -0.0299 0.0037 -0.0177 235 HIS A CD2 1220 C CE1 . HIS A 153 ? 0.3868 0.3320 0.3287 -0.0262 0.0056 -0.0189 235 HIS A CE1 1221 N NE2 . HIS A 153 ? 0.3993 0.3440 0.3406 -0.0295 0.0051 -0.0191 235 HIS A NE2 1222 N N . ASN A 154 ? 0.2972 0.2489 0.2475 -0.0229 0.0044 -0.0123 236 ASN A N 1223 C CA . ASN A 154 ? 0.3481 0.2949 0.2967 -0.0238 0.0052 -0.0116 236 ASN A CA 1224 C C . ASN A 154 ? 0.3508 0.3014 0.3019 -0.0246 0.0044 -0.0099 236 ASN A C 1225 O O . ASN A 154 ? 0.3055 0.2543 0.2556 -0.0272 0.0046 -0.0098 236 ASN A O 1226 C CB . ASN A 154 ? 0.3536 0.2953 0.2988 -0.0270 0.0059 -0.0132 236 ASN A CB 1227 C CG . ASN A 154 ? 0.4586 0.3932 0.4012 -0.0272 0.0073 -0.0126 236 ASN A CG 1228 O OD1 . ASN A 154 ? 0.4111 0.3435 0.3539 -0.0242 0.0080 -0.0111 236 ASN A OD1 1229 N ND2 . ASN A 154 ? 0.4864 0.4173 0.4265 -0.0308 0.0077 -0.0137 236 ASN A ND2 1230 N N . GLY A 155 ? 0.3620 0.3181 0.3163 -0.0225 0.0035 -0.0088 237 GLY A N 1231 C CA . GLY A 155 ? 0.3518 0.3117 0.3084 -0.0229 0.0028 -0.0073 237 GLY A CA 1232 C C . GLY A 155 ? 0.3428 0.3088 0.3016 -0.0251 0.0015 -0.0078 237 GLY A C 1233 O O . GLY A 155 ? 0.3489 0.3191 0.3101 -0.0249 0.0008 -0.0067 237 GLY A O 1234 N N . VAL A 156 ? 0.2832 0.2497 0.2411 -0.0271 0.0011 -0.0094 238 VAL A N 1235 C CA . VAL A 156 ? 0.3177 0.2899 0.2776 -0.0292 -0.0001 -0.0097 238 VAL A CA 1236 C C . VAL A 156 ? 0.2740 0.2512 0.2362 -0.0274 -0.0011 -0.0098 238 VAL A C 1237 O O . VAL A 156 ? 0.2388 0.2150 0.1998 -0.0267 -0.0010 -0.0108 238 VAL A O 1238 C CB . VAL A 156 ? 0.3065 0.2774 0.2643 -0.0326 -0.0002 -0.0114 238 VAL A CB 1239 C CG1 . VAL A 156 ? 0.2314 0.2090 0.1915 -0.0344 -0.0016 -0.0117 238 VAL A CG1 1240 C CG2 . VAL A 156 ? 0.3490 0.3150 0.3046 -0.0349 0.0008 -0.0113 238 VAL A CG2 1241 N N . CYS A 157 ? 0.3077 0.2901 0.2728 -0.0267 -0.0020 -0.0088 239 CYS A N 1242 C CA . CYS A 157 ? 0.2860 0.2728 0.2533 -0.0249 -0.0028 -0.0087 239 CYS A CA 1243 C C . CYS A 157 ? 0.2857 0.2780 0.2550 -0.0265 -0.0040 -0.0088 239 CYS A C 1244 O O . CYS A 157 ? 0.2609 0.2566 0.2324 -0.0265 -0.0045 -0.0079 239 CYS A O 1245 C CB . CYS A 157 ? 0.2666 0.2548 0.2359 -0.0222 -0.0028 -0.0073 239 CYS A CB 1246 S SG . CYS A 157 ? 0.3193 0.3018 0.2868 -0.0202 -0.0015 -0.0066 239 CYS A SG 1247 N N . PRO A 158 ? 0.3132 0.3067 0.2817 -0.0277 -0.0046 -0.0099 240 PRO A N 1248 C CA . PRO A 158 ? 0.2940 0.2930 0.2644 -0.0290 -0.0058 -0.0100 240 PRO A CA 1249 C C . PRO A 158 ? 0.2480 0.2513 0.2212 -0.0267 -0.0065 -0.0091 240 PRO A C 1250 O O . PRO A 158 ? 0.2530 0.2551 0.2262 -0.0245 -0.0062 -0.0089 240 PRO A O 1251 C CB . PRO A 158 ? 0.2483 0.2467 0.2166 -0.0305 -0.0061 -0.0114 240 PRO A CB 1252 C CG . PRO A 158 ? 0.3668 0.3587 0.3318 -0.0309 -0.0048 -0.0123 240 PRO A CG 1253 C CD . PRO A 158 ? 0.3211 0.3105 0.2866 -0.0281 -0.0040 -0.0112 240 PRO A CD 1254 N N . VAL A 159 ? 0.2523 0.2604 0.2279 -0.0271 -0.0073 -0.0085 241 VAL A N 1255 C CA . VAL A 159 ? 0.2567 0.2687 0.2349 -0.0251 -0.0080 -0.0077 241 VAL A CA 1256 C C . VAL A 159 ? 0.2516 0.2688 0.2313 -0.0262 -0.0091 -0.0077 241 VAL A C 1257 O O . VAL A 159 ? 0.2600 0.2790 0.2401 -0.0282 -0.0093 -0.0079 241 VAL A O 1258 C CB . VAL A 159 ? 0.2630 0.2758 0.2430 -0.0237 -0.0077 -0.0067 241 VAL A CB 1259 C CG1 . VAL A 159 ? 0.1947 0.2112 0.1772 -0.0218 -0.0084 -0.0060 241 VAL A CG1 1260 C CG2 . VAL A 159 ? 0.1979 0.2063 0.1767 -0.0225 -0.0068 -0.0064 241 VAL A CG2 1261 N N . VAL A 160 ? 0.2524 0.2720 0.2331 -0.0248 -0.0098 -0.0075 242 VAL A N 1262 C CA . VAL A 160 ? 0.1836 0.2082 0.1658 -0.0255 -0.0109 -0.0073 242 VAL A CA 1263 C C . VAL A 160 ? 0.2950 0.3230 0.2802 -0.0238 -0.0112 -0.0062 242 VAL A C 1264 O O . VAL A 160 ? 0.2433 0.2703 0.2293 -0.0217 -0.0109 -0.0057 242 VAL A O 1265 C CB . VAL A 160 ? 0.2281 0.2535 0.2094 -0.0250 -0.0115 -0.0075 242 VAL A CB 1266 C CG1 . VAL A 160 ? 0.2407 0.2713 0.2233 -0.0258 -0.0127 -0.0072 242 VAL A CG1 1267 C CG2 . VAL A 160 ? 0.1907 0.2121 0.1687 -0.0264 -0.0110 -0.0087 242 VAL A CG2 1268 N N . PHE A 161 ? 0.2099 0.2419 0.1968 -0.0248 -0.0117 -0.0060 243 PHE A N 1269 C CA . PHE A 161 ? 0.2327 0.2682 0.2224 -0.0232 -0.0119 -0.0051 243 PHE A CA 1270 C C . PHE A 161 ? 0.2988 0.3393 0.2900 -0.0233 -0.0130 -0.0048 243 PHE A C 1271 O O . PHE A 161 ? 0.3186 0.3608 0.3091 -0.0253 -0.0135 -0.0052 243 PHE A O 1272 C CB . PHE A 161 ? 0.2429 0.2791 0.2335 -0.0240 -0.0113 -0.0049 243 PHE A CB 1273 C CG . PHE A 161 ? 0.2823 0.3141 0.2717 -0.0237 -0.0103 -0.0050 243 PHE A CG 1274 C CD1 . PHE A 161 ? 0.3088 0.3367 0.2957 -0.0255 -0.0097 -0.0056 243 PHE A CD1 1275 C CD2 . PHE A 161 ? 0.2852 0.3166 0.2757 -0.0218 -0.0099 -0.0044 243 PHE A CD2 1276 C CE1 . PHE A 161 ? 0.2355 0.2594 0.2212 -0.0250 -0.0088 -0.0054 243 PHE A CE1 1277 C CE2 . PHE A 161 ? 0.3397 0.3674 0.3289 -0.0214 -0.0091 -0.0044 243 PHE A CE2 1278 C CZ . PHE A 161 ? 0.2677 0.2917 0.2546 -0.0230 -0.0085 -0.0048 243 PHE A CZ 1279 N N . THR A 162 ? 0.2328 0.2757 0.2261 -0.0212 -0.0133 -0.0040 244 THR A N 1280 C CA . THR A 162 ? 0.1869 0.2351 0.1821 -0.0209 -0.0142 -0.0034 244 THR A CA 1281 C C . THR A 162 ? 0.2849 0.3358 0.2828 -0.0195 -0.0139 -0.0028 244 THR A C 1282 O O . THR A 162 ? 0.2726 0.3212 0.2707 -0.0180 -0.0132 -0.0026 244 THR A O 1283 C CB . THR A 162 ? 0.2290 0.2776 0.2239 -0.0193 -0.0149 -0.0029 244 THR A CB 1284 O OG1 . THR A 162 ? 0.2083 0.2547 0.2007 -0.0207 -0.0151 -0.0035 244 THR A OG1 1285 C CG2 . THR A 162 ? 0.2634 0.3175 0.2603 -0.0187 -0.0159 -0.0021 244 THR A CG2 1286 N N . ASP A 163 ? 0.2618 0.3177 0.2615 -0.0201 -0.0145 -0.0025 245 ASP A N 1287 C CA . ASP A 163 ? 0.2753 0.3344 0.2776 -0.0186 -0.0142 -0.0019 245 ASP A CA 1288 C C . ASP A 163 ? 0.2717 0.3365 0.2759 -0.0181 -0.0152 -0.0013 245 ASP A C 1289 O O . ASP A 163 ? 0.2763 0.3440 0.2804 -0.0202 -0.0159 -0.0015 245 ASP A O 1290 C CB . ASP A 163 ? 0.1852 0.2447 0.1879 -0.0202 -0.0134 -0.0023 245 ASP A CB 1291 C CG . ASP A 163 ? 0.2915 0.3531 0.2963 -0.0183 -0.0127 -0.0019 245 ASP A CG 1292 O OD1 . ASP A 163 ? 0.2742 0.3375 0.2806 -0.0159 -0.0130 -0.0013 245 ASP A OD1 1293 O OD2 . ASP A 163 ? 0.2390 0.3004 0.2440 -0.0193 -0.0119 -0.0021 245 ASP A OD2 1294 N N . GLY A 164 ? 0.2173 0.2838 0.2234 -0.0154 -0.0153 -0.0005 246 GLY A N 1295 C CA . GLY A 164 ? 0.2863 0.3580 0.2942 -0.0144 -0.0163 0.0004 246 GLY A CA 1296 C C . GLY A 164 ? 0.3496 0.4199 0.3572 -0.0120 -0.0167 0.0012 246 GLY A C 1297 O O . GLY A 164 ? 0.2323 0.2979 0.2389 -0.0108 -0.0161 0.0011 246 GLY A O 1298 N N . SER A 165 ? 0.2617 0.3361 0.2702 -0.0114 -0.0178 0.0020 247 SER A N 1299 C CA . SER A 165 ? 0.3093 0.3829 0.3178 -0.0089 -0.0182 0.0031 247 SER A CA 1300 C C . SER A 165 ? 0.3205 0.3891 0.3260 -0.0093 -0.0183 0.0029 247 SER A C 1301 O O . SER A 165 ? 0.3481 0.4152 0.3515 -0.0117 -0.0184 0.0021 247 SER A O 1302 C CB . SER A 165 ? 0.3054 0.3849 0.3153 -0.0082 -0.0195 0.0042 247 SER A CB 1303 O OG . SER A 165 ? 0.3719 0.4504 0.3817 -0.0056 -0.0198 0.0055 247 SER A OG 1304 N N . ALA A 166 ? 0.3450 0.4109 0.3503 -0.0071 -0.0180 0.0037 248 ALA A N 1305 C CA . ALA A 166 ? 0.3995 0.4614 0.4025 -0.0071 -0.0181 0.0038 248 ALA A CA 1306 C C . ALA A 166 ? 0.4041 0.4684 0.4066 -0.0063 -0.0192 0.0050 248 ALA A C 1307 O O . ALA A 166 ? 0.3601 0.4220 0.3604 -0.0066 -0.0193 0.0053 248 ALA A O 1308 C CB . ALA A 166 ? 0.2964 0.3537 0.2992 -0.0054 -0.0171 0.0039 248 ALA A CB 1309 N N . THR A 167 ? 0.3084 0.3778 0.3130 -0.0052 -0.0199 0.0060 249 THR A N 1310 C CA . THR A 167 ? 0.4397 0.5119 0.4441 -0.0040 -0.0210 0.0075 249 THR A CA 1311 C C . THR A 167 ? 0.4566 0.5352 0.4619 -0.0053 -0.0223 0.0076 249 THR A C 1312 O O . THR A 167 ? 0.4408 0.5237 0.4473 -0.0038 -0.0233 0.0090 249 THR A O 1313 C CB . THR A 167 ? 0.3632 0.4354 0.3694 -0.0006 -0.0208 0.0089 249 THR A CB 1314 O OG1 . THR A 167 ? 0.4116 0.4875 0.4207 0.0003 -0.0206 0.0089 249 THR A OG1 1315 C CG2 . THR A 167 ? 0.3990 0.4650 0.4044 0.0004 -0.0195 0.0087 249 THR A CG2 1316 N N . GLY A 168 ? 0.3632 0.4426 0.3680 -0.0082 -0.0223 0.0061 250 GLY A N 1317 C CA . GLY A 168 ? 0.3778 0.4632 0.3835 -0.0101 -0.0234 0.0059 250 GLY A CA 1318 C C . GLY A 168 ? 0.4188 0.5027 0.4231 -0.0135 -0.0230 0.0041 250 GLY A C 1319 O O . GLY A 168 ? 0.4036 0.4818 0.4063 -0.0141 -0.0219 0.0031 250 GLY A O 1320 N N . PRO A 169 ? 0.3307 0.4196 0.3356 -0.0159 -0.0239 0.0036 251 PRO A N 1321 C CA . PRO A 169 ? 0.4051 0.4924 0.4087 -0.0193 -0.0235 0.0019 251 PRO A CA 1322 C C . PRO A 169 ? 0.3611 0.4455 0.3658 -0.0192 -0.0220 0.0013 251 PRO A C 1323 O O . PRO A 169 ? 0.2490 0.3363 0.2566 -0.0176 -0.0217 0.0019 251 PRO A O 1324 C CB . PRO A 169 ? 0.3065 0.4011 0.3117 -0.0212 -0.0247 0.0019 251 PRO A CB 1325 C CG . PRO A 169 ? 0.3602 0.4589 0.3658 -0.0194 -0.0262 0.0033 251 PRO A CG 1326 C CD . PRO A 169 ? 0.3127 0.4086 0.3192 -0.0155 -0.0254 0.0046 251 PRO A CD 1327 N N . ALA A 170 ? 0.3468 0.4255 0.3491 -0.0207 -0.0211 0.0001 252 ALA A N 1328 C CA . ALA A 170 ? 0.3458 0.4212 0.3487 -0.0207 -0.0197 -0.0005 252 ALA A CA 1329 C C . ALA A 170 ? 0.2848 0.3585 0.2861 -0.0240 -0.0192 -0.0018 252 ALA A C 1330 O O . ALA A 170 ? 0.2202 0.2944 0.2197 -0.0264 -0.0199 -0.0025 252 ALA A O 1331 C CB . ALA A 170 ? 0.1916 0.2611 0.1932 -0.0187 -0.0188 -0.0004 252 ALA A CB 1332 N N . ASP A 171 ? 0.3088 0.3804 0.3107 -0.0243 -0.0181 -0.0022 253 ASP A N 1333 C CA . ASP A 171 ? 0.3411 0.4107 0.3415 -0.0274 -0.0175 -0.0033 253 ASP A CA 1334 C C . ASP A 171 ? 0.3588 0.4212 0.3564 -0.0275 -0.0165 -0.0040 253 ASP A C 1335 O O . ASP A 171 ? 0.3003 0.3597 0.2981 -0.0263 -0.0155 -0.0038 253 ASP A O 1336 C CB . ASP A 171 ? 0.3089 0.3813 0.3116 -0.0279 -0.0168 -0.0031 253 ASP A CB 1337 C CG . ASP A 171 ? 0.4943 0.5744 0.5002 -0.0278 -0.0176 -0.0024 253 ASP A CG 1338 O OD1 . ASP A 171 ? 0.5045 0.5881 0.5102 -0.0295 -0.0188 -0.0026 253 ASP A OD1 1339 O OD2 . ASP A 171 ? 0.6864 0.7692 0.6948 -0.0259 -0.0172 -0.0017 253 ASP A OD2 1340 N N . THR A 172 ? 0.2816 0.3413 0.2764 -0.0289 -0.0169 -0.0047 254 THR A N 1341 C CA . THR A 172 ? 0.2415 0.2946 0.2336 -0.0289 -0.0159 -0.0054 254 THR A CA 1342 C C . THR A 172 ? 0.2481 0.2986 0.2385 -0.0318 -0.0153 -0.0064 254 THR A C 1343 O O . THR A 172 ? 0.2836 0.3366 0.2737 -0.0345 -0.0159 -0.0070 254 THR A O 1344 C CB . THR A 172 ? 0.2413 0.2926 0.2311 -0.0284 -0.0165 -0.0056 254 THR A CB 1345 O OG1 . THR A 172 ? 0.2535 0.3061 0.2448 -0.0255 -0.0168 -0.0045 254 THR A OG1 1346 C CG2 . THR A 172 ? 0.1850 0.2299 0.1720 -0.0287 -0.0155 -0.0065 254 THR A CG2 1347 N N . ARG A 173 ? 0.2200 0.2655 0.2094 -0.0314 -0.0141 -0.0066 255 ARG A N 1348 C CA . ARG A 173 ? 0.3024 0.3444 0.2899 -0.0338 -0.0133 -0.0074 255 ARG A CA 1349 C C . ARG A 173 ? 0.2919 0.3272 0.2765 -0.0332 -0.0124 -0.0079 255 ARG A C 1350 O O . ARG A 173 ? 0.2158 0.2494 0.2007 -0.0306 -0.0121 -0.0074 255 ARG A O 1351 C CB . ARG A 173 ? 0.2837 0.3265 0.2729 -0.0339 -0.0125 -0.0068 255 ARG A CB 1352 C CG . ARG A 173 ? 0.2629 0.3123 0.2549 -0.0348 -0.0131 -0.0064 255 ARG A CG 1353 C CD . ARG A 173 ? 0.2089 0.2584 0.2020 -0.0352 -0.0120 -0.0059 255 ARG A CD 1354 N NE . ARG A 173 ? 0.2354 0.2915 0.2314 -0.0361 -0.0124 -0.0055 255 ARG A NE 1355 C CZ . ARG A 173 ? 0.2941 0.3517 0.2914 -0.0367 -0.0116 -0.0051 255 ARG A CZ 1356 N NH1 . ARG A 173 ? 0.2179 0.2708 0.2137 -0.0365 -0.0104 -0.0049 255 ARG A NH1 1357 N NH2 . ARG A 173 ? 0.2632 0.3273 0.2633 -0.0374 -0.0119 -0.0047 255 ARG A NH2 1358 N N . ILE A 174 ? 0.2704 0.3021 0.2524 -0.0356 -0.0119 -0.0090 256 ILE A N 1359 C CA . ILE A 174 ? 0.2748 0.3000 0.2541 -0.0350 -0.0109 -0.0095 256 ILE A CA 1360 C C . ILE A 174 ? 0.3770 0.3990 0.3558 -0.0360 -0.0098 -0.0093 256 ILE A C 1361 O O . ILE A 174 ? 0.3405 0.3626 0.3186 -0.0388 -0.0097 -0.0098 256 ILE A O 1362 C CB . ILE A 174 ? 0.3212 0.3435 0.2973 -0.0366 -0.0110 -0.0108 256 ILE A CB 1363 C CG1 . ILE A 174 ? 0.3667 0.3915 0.3429 -0.0353 -0.0119 -0.0108 256 ILE A CG1 1364 C CG2 . ILE A 174 ? 0.2566 0.2720 0.2300 -0.0361 -0.0097 -0.0113 256 ILE A CG2 1365 C CD1 . ILE A 174 ? 0.3790 0.4101 0.3567 -0.0365 -0.0134 -0.0107 256 ILE A CD1 1366 N N . TYR A 175 ? 0.3469 0.3663 0.3260 -0.0337 -0.0090 -0.0086 257 TYR A N 1367 C CA . TYR A 175 ? 0.3160 0.3321 0.2944 -0.0343 -0.0079 -0.0082 257 TYR A CA 1368 C C . TYR A 175 ? 0.3192 0.3287 0.2945 -0.0341 -0.0070 -0.0087 257 TYR A C 1369 O O . TYR A 175 ? 0.2915 0.2991 0.2659 -0.0323 -0.0070 -0.0090 257 TYR A O 1370 C CB . TYR A 175 ? 0.2969 0.3147 0.2774 -0.0320 -0.0077 -0.0070 257 TYR A CB 1371 C CG . TYR A 175 ? 0.2903 0.3135 0.2734 -0.0328 -0.0081 -0.0064 257 TYR A CG 1372 C CD1 . TYR A 175 ? 0.2746 0.3033 0.2601 -0.0323 -0.0091 -0.0064 257 TYR A CD1 1373 C CD2 . TYR A 175 ? 0.2602 0.2831 0.2435 -0.0339 -0.0073 -0.0059 257 TYR A CD2 1374 C CE1 . TYR A 175 ? 0.2621 0.2959 0.2501 -0.0328 -0.0094 -0.0058 257 TYR A CE1 1375 C CE2 . TYR A 175 ? 0.2370 0.2651 0.2227 -0.0346 -0.0075 -0.0054 257 TYR A CE2 1376 C CZ . TYR A 175 ? 0.3100 0.3436 0.2981 -0.0339 -0.0085 -0.0054 257 TYR A CZ 1377 O OH . TYR A 175 ? 0.3103 0.3494 0.3010 -0.0343 -0.0087 -0.0050 257 TYR A OH 1378 N N . TYR A 176 ? 0.3003 0.3061 0.2739 -0.0359 -0.0061 -0.0088 258 TYR A N 1379 C CA . TYR A 176 ? 0.2209 0.2200 0.1915 -0.0356 -0.0050 -0.0092 258 TYR A CA 1380 C C . TYR A 176 ? 0.3497 0.3463 0.3203 -0.0345 -0.0041 -0.0080 258 TYR A C 1381 O O . TYR A 176 ? 0.3449 0.3415 0.3155 -0.0364 -0.0037 -0.0076 258 TYR A O 1382 C CB . TYR A 176 ? 0.2905 0.2865 0.2584 -0.0389 -0.0047 -0.0105 258 TYR A CB 1383 C CG . TYR A 176 ? 0.2240 0.2225 0.1915 -0.0400 -0.0057 -0.0118 258 TYR A CG 1384 C CD1 . TYR A 176 ? 0.2881 0.2925 0.2574 -0.0420 -0.0068 -0.0120 258 TYR A CD1 1385 C CD2 . TYR A 176 ? 0.3125 0.3078 0.2779 -0.0390 -0.0055 -0.0127 258 TYR A CD2 1386 C CE1 . TYR A 176 ? 0.2732 0.2800 0.2420 -0.0429 -0.0078 -0.0130 258 TYR A CE1 1387 C CE2 . TYR A 176 ? 0.3030 0.3005 0.2677 -0.0400 -0.0064 -0.0139 258 TYR A CE2 1388 C CZ . TYR A 176 ? 0.2418 0.2451 0.2082 -0.0420 -0.0076 -0.0140 258 TYR A CZ 1389 O OH . TYR A 176 ? 0.2984 0.3041 0.2640 -0.0430 -0.0086 -0.0150 258 TYR A OH 1390 N N . PHE A 177 ? 0.3200 0.3148 0.2907 -0.0315 -0.0038 -0.0074 259 PHE A N 1391 C CA . PHE A 177 ? 0.2737 0.2666 0.2444 -0.0302 -0.0030 -0.0061 259 PHE A CA 1392 C C . PHE A 177 ? 0.2998 0.2859 0.2676 -0.0296 -0.0019 -0.0061 259 PHE A C 1393 O O . PHE A 177 ? 0.3679 0.3512 0.3341 -0.0289 -0.0017 -0.0070 259 PHE A O 1394 C CB . PHE A 177 ? 0.2429 0.2389 0.2159 -0.0272 -0.0035 -0.0053 259 PHE A CB 1395 C CG . PHE A 177 ? 0.2467 0.2489 0.2226 -0.0273 -0.0045 -0.0052 259 PHE A CG 1396 C CD1 . PHE A 177 ? 0.2347 0.2398 0.2120 -0.0280 -0.0045 -0.0045 259 PHE A CD1 1397 C CD2 . PHE A 177 ? 0.2145 0.2196 0.1916 -0.0265 -0.0054 -0.0058 259 PHE A CD2 1398 C CE1 . PHE A 177 ? 0.2239 0.2347 0.2039 -0.0278 -0.0053 -0.0044 259 PHE A CE1 1399 C CE2 . PHE A 177 ? 0.2701 0.2805 0.2498 -0.0263 -0.0062 -0.0056 259 PHE A CE2 1400 C CZ . PHE A 177 ? 0.2536 0.2669 0.2348 -0.0269 -0.0062 -0.0049 259 PHE A CZ 1401 N N . LYS A 178 ? 0.2913 0.2749 0.2582 -0.0298 -0.0011 -0.0051 260 LYS A N 1402 C CA . LYS A 178 ? 0.3076 0.2849 0.2720 -0.0283 0.0000 -0.0046 260 LYS A CA 1403 C C . LYS A 178 ? 0.2813 0.2589 0.2464 -0.0266 0.0003 -0.0029 260 LYS A C 1404 O O . LYS A 178 ? 0.3574 0.3367 0.3231 -0.0280 0.0004 -0.0021 260 LYS A O 1405 C CB . LYS A 178 ? 0.3440 0.3157 0.3054 -0.0308 0.0010 -0.0052 260 LYS A CB 1406 C CG . LYS A 178 ? 0.2873 0.2523 0.2461 -0.0291 0.0022 -0.0046 260 LYS A CG 1407 C CD . LYS A 178 ? 0.3846 0.3434 0.3400 -0.0316 0.0032 -0.0057 260 LYS A CD 1408 C CE . LYS A 178 ? 0.3952 0.3469 0.3479 -0.0296 0.0045 -0.0052 260 LYS A CE 1409 N NZ . LYS A 178 ? 0.6365 0.5821 0.5858 -0.0315 0.0055 -0.0067 260 LYS A NZ 1410 N N . GLU A 179 ? 0.3629 0.3394 0.3282 -0.0235 0.0004 -0.0023 261 GLU A N 1411 C CA . GLU A 179 ? 0.3298 0.3073 0.2958 -0.0216 0.0004 -0.0007 261 GLU A CA 1412 C C . GLU A 179 ? 0.2729 0.2565 0.2416 -0.0221 -0.0004 -0.0004 261 GLU A C 1413 O O . GLU A 179 ? 0.3372 0.3216 0.3060 -0.0220 -0.0002 0.0008 261 GLU A O 1414 C CB . GLU A 179 ? 0.3198 0.2921 0.2833 -0.0220 0.0016 0.0004 261 GLU A CB 1415 C CG . GLU A 179 ? 0.3557 0.3217 0.3166 -0.0210 0.0025 0.0002 261 GLU A CG 1416 C CD . GLU A 179 ? 0.4663 0.4266 0.4245 -0.0210 0.0037 0.0015 261 GLU A CD 1417 O OE1 . GLU A 179 ? 0.5613 0.5204 0.5184 -0.0238 0.0041 0.0017 261 GLU A OE1 1418 O OE2 . GLU A 179 ? 0.6445 0.6016 0.6016 -0.0184 0.0042 0.0023 261 GLU A OE2 1419 N N . GLY A 180 ? 0.2965 0.2842 0.2671 -0.0226 -0.0013 -0.0014 262 GLY A N 1420 C CA . GLY A 180 ? 0.2453 0.2387 0.2184 -0.0229 -0.0020 -0.0012 262 GLY A CA 1421 C C . GLY A 180 ? 0.3079 0.3033 0.2814 -0.0257 -0.0019 -0.0013 262 GLY A C 1422 O O . GLY A 180 ? 0.2728 0.2732 0.2485 -0.0260 -0.0025 -0.0014 262 GLY A O 1423 N N . LYS A 181 ? 0.2722 0.2636 0.2434 -0.0279 -0.0012 -0.0014 263 LYS A N 1424 C CA . LYS A 181 ? 0.2953 0.2887 0.2668 -0.0309 -0.0010 -0.0016 263 LYS A CA 1425 C C . LYS A 181 ? 0.3081 0.3033 0.2801 -0.0329 -0.0017 -0.0030 263 LYS A C 1426 O O . LYS A 181 ? 0.2644 0.2568 0.2350 -0.0326 -0.0017 -0.0039 263 LYS A O 1427 C CB . LYS A 181 ? 0.3956 0.3838 0.3644 -0.0326 0.0002 -0.0009 263 LYS A CB 1428 C CG . LYS A 181 ? 0.3767 0.3636 0.3449 -0.0308 0.0008 0.0008 263 LYS A CG 1429 C CD . LYS A 181 ? 0.6575 0.6411 0.6237 -0.0330 0.0019 0.0018 263 LYS A CD 1430 C CE . LYS A 181 ? 0.8501 0.8262 0.8130 -0.0332 0.0029 0.0019 263 LYS A CE 1431 N NZ . LYS A 181 ? 0.9657 0.9382 0.9264 -0.0351 0.0040 0.0031 263 LYS A NZ 1432 N N . ILE A 182 ? 0.3171 0.3172 0.2910 -0.0348 -0.0021 -0.0032 264 ILE A N 1433 C CA . ILE A 182 ? 0.2948 0.2977 0.2694 -0.0368 -0.0029 -0.0044 264 ILE A CA 1434 C C . ILE A 182 ? 0.3803 0.3793 0.3524 -0.0401 -0.0022 -0.0051 264 ILE A C 1435 O O . ILE A 182 ? 0.3161 0.3149 0.2878 -0.0423 -0.0016 -0.0046 264 ILE A O 1436 C CB . ILE A 182 ? 0.2427 0.2527 0.2204 -0.0374 -0.0036 -0.0042 264 ILE A CB 1437 C CG1 . ILE A 182 ? 0.2063 0.2197 0.1862 -0.0342 -0.0041 -0.0037 264 ILE A CG1 1438 C CG2 . ILE A 182 ? 0.2133 0.2265 0.1917 -0.0395 -0.0044 -0.0054 264 ILE A CG2 1439 C CD1 . ILE A 182 ? 0.2821 0.3019 0.2650 -0.0344 -0.0045 -0.0033 264 ILE A CD1 1440 N N . LEU A 183 ? 0.3167 0.3123 0.2868 -0.0405 -0.0024 -0.0063 265 LEU A N 1441 C CA . LEU A 183 ? 0.3644 0.3561 0.3320 -0.0437 -0.0018 -0.0073 265 LEU A CA 1442 C C . LEU A 183 ? 0.3147 0.3116 0.2836 -0.0466 -0.0028 -0.0082 265 LEU A C 1443 O O . LEU A 183 ? 0.3865 0.3828 0.3546 -0.0500 -0.0024 -0.0086 265 LEU A O 1444 C CB . LEU A 183 ? 0.3396 0.3255 0.3043 -0.0429 -0.0015 -0.0083 265 LEU A CB 1445 C CG . LEU A 183 ? 0.4475 0.4277 0.4104 -0.0401 -0.0004 -0.0075 265 LEU A CG 1446 C CD1 . LEU A 183 ? 0.3662 0.3411 0.3264 -0.0395 0.0000 -0.0087 265 LEU A CD1 1447 C CD2 . LEU A 183 ? 0.4187 0.3951 0.3802 -0.0413 0.0007 -0.0064 265 LEU A CD2 1448 N N . LYS A 184 ? 0.3130 0.3151 0.2842 -0.0451 -0.0040 -0.0085 266 LYS A N 1449 C CA . LYS A 184 ? 0.2925 0.2995 0.2648 -0.0474 -0.0051 -0.0095 266 LYS A CA 1450 C C . LYS A 184 ? 0.2888 0.3011 0.2637 -0.0448 -0.0063 -0.0093 266 LYS A C 1451 O O . LYS A 184 ? 0.2754 0.2858 0.2500 -0.0417 -0.0062 -0.0090 266 LYS A O 1452 C CB . LYS A 184 ? 0.2895 0.2923 0.2587 -0.0496 -0.0050 -0.0111 266 LYS A CB 1453 C CG . LYS A 184 ? 0.2865 0.2942 0.2564 -0.0518 -0.0063 -0.0123 266 LYS A CG 1454 C CD . LYS A 184 ? 0.3311 0.3338 0.2973 -0.0537 -0.0062 -0.0140 266 LYS A CD 1455 C CE . LYS A 184 ? 0.3823 0.3901 0.3490 -0.0560 -0.0076 -0.0152 266 LYS A CE 1456 N NZ . LYS A 184 ? 0.3541 0.3571 0.3169 -0.0581 -0.0074 -0.0171 266 LYS A NZ 1457 N N . TRP A 185 ? 0.2210 0.2399 0.1983 -0.0459 -0.0073 -0.0093 267 TRP A N 1458 C CA . TRP A 185 ? 0.3323 0.3557 0.3114 -0.0439 -0.0085 -0.0093 267 TRP A CA 1459 C C . TRP A 185 ? 0.3340 0.3619 0.3136 -0.0465 -0.0097 -0.0102 267 TRP A C 1460 O O . TRP A 185 ? 0.2416 0.2707 0.2211 -0.0497 -0.0096 -0.0106 267 TRP A O 1461 C CB . TRP A 185 ? 0.2702 0.2982 0.2527 -0.0414 -0.0087 -0.0080 267 TRP A CB 1462 C CG . TRP A 185 ? 0.3074 0.3408 0.2923 -0.0429 -0.0088 -0.0075 267 TRP A CG 1463 C CD1 . TRP A 185 ? 0.2482 0.2812 0.2336 -0.0435 -0.0078 -0.0067 267 TRP A CD1 1464 C CD2 . TRP A 185 ? 0.2945 0.3348 0.2819 -0.0439 -0.0099 -0.0076 267 TRP A CD2 1465 N NE1 . TRP A 185 ? 0.3201 0.3594 0.3081 -0.0449 -0.0081 -0.0064 267 TRP A NE1 1466 C CE2 . TRP A 185 ? 0.2511 0.2951 0.2405 -0.0451 -0.0095 -0.0069 267 TRP A CE2 1467 C CE3 . TRP A 185 ? 0.2735 0.3175 0.2616 -0.0438 -0.0112 -0.0080 267 TRP A CE3 1468 C CZ2 . TRP A 185 ? 0.2339 0.2853 0.2262 -0.0461 -0.0103 -0.0067 267 TRP A CZ2 1469 C CZ3 . TRP A 185 ? 0.3072 0.3585 0.2981 -0.0448 -0.0121 -0.0078 267 TRP A CZ3 1470 C CH2 . TRP A 185 ? 0.2645 0.3195 0.2575 -0.0459 -0.0116 -0.0072 267 TRP A CH2 1471 N N . GLU A 186 ? 0.2594 0.2898 0.2394 -0.0452 -0.0107 -0.0105 268 GLU A N 1472 C CA . GLU A 186 ? 0.3327 0.3677 0.3131 -0.0474 -0.0120 -0.0112 268 GLU A CA 1473 C C . GLU A 186 ? 0.3228 0.3631 0.3055 -0.0448 -0.0132 -0.0105 268 GLU A C 1474 O O . GLU A 186 ? 0.3101 0.3488 0.2929 -0.0417 -0.0131 -0.0100 268 GLU A O 1475 C CB . GLU A 186 ? 0.3929 0.4233 0.3695 -0.0494 -0.0120 -0.0128 268 GLU A CB 1476 C CG . GLU A 186 ? 0.4253 0.4508 0.3997 -0.0469 -0.0116 -0.0131 268 GLU A CG 1477 C CD . GLU A 186 ? 0.4013 0.4218 0.3717 -0.0490 -0.0113 -0.0149 268 GLU A CD 1478 O OE1 . GLU A 186 ? 0.4074 0.4237 0.3758 -0.0470 -0.0108 -0.0152 268 GLU A OE1 1479 O OE2 . GLU A 186 ? 0.4044 0.4251 0.3736 -0.0525 -0.0115 -0.0159 268 GLU A OE2 1480 N N A SER A 187 ? 0.2846 0.3315 0.2693 -0.0461 -0.0144 -0.0104 269 SER A N 1481 N N B SER A 187 ? 0.2842 0.3311 0.2688 -0.0462 -0.0144 -0.0105 269 SER A N 1482 C CA A SER A 187 ? 0.3254 0.3773 0.3121 -0.0438 -0.0156 -0.0097 269 SER A CA 1483 C CA B SER A 187 ? 0.3259 0.3780 0.3125 -0.0440 -0.0157 -0.0097 269 SER A CA 1484 C C A SER A 187 ? 0.2997 0.3497 0.2838 -0.0437 -0.0163 -0.0105 269 SER A C 1485 C C B SER A 187 ? 0.2996 0.3492 0.2835 -0.0436 -0.0162 -0.0105 269 SER A C 1486 O O A SER A 187 ? 0.3149 0.3621 0.2961 -0.0463 -0.0163 -0.0119 269 SER A O 1487 O O B SER A 187 ? 0.3152 0.3615 0.2961 -0.0461 -0.0161 -0.0119 269 SER A O 1488 C CB A SER A 187 ? 0.2970 0.3569 0.2866 -0.0451 -0.0167 -0.0093 269 SER A CB 1489 C CB B SER A 187 ? 0.2973 0.3572 0.2866 -0.0455 -0.0168 -0.0094 269 SER A CB 1490 O OG A SER A 187 ? 0.3219 0.3828 0.3102 -0.0490 -0.0172 -0.0104 269 SER A OG 1491 O OG B SER A 187 ? 0.2660 0.3290 0.2583 -0.0450 -0.0163 -0.0085 269 SER A OG 1492 N N . LEU A 188 ? 0.2991 0.3503 0.2839 -0.0406 -0.0168 -0.0097 270 LEU A N 1493 C CA . LEU A 188 ? 0.2995 0.3492 0.2820 -0.0401 -0.0173 -0.0102 270 LEU A CA 1494 C C . LEU A 188 ? 0.3185 0.3720 0.3000 -0.0428 -0.0187 -0.0110 270 LEU A C 1495 O O . LEU A 188 ? 0.2541 0.3141 0.2381 -0.0435 -0.0197 -0.0105 270 LEU A O 1496 C CB . LEU A 188 ? 0.2225 0.2743 0.2067 -0.0365 -0.0178 -0.0088 270 LEU A CB 1497 C CG . LEU A 188 ? 0.3029 0.3548 0.2852 -0.0359 -0.0186 -0.0089 270 LEU A CG 1498 C CD1 . LEU A 188 ? 0.1810 0.2262 0.1600 -0.0356 -0.0175 -0.0099 270 LEU A CD1 1499 C CD2 . LEU A 188 ? 0.2309 0.2861 0.2154 -0.0327 -0.0192 -0.0073 270 LEU A CD2 1500 N N . THR A 189 ? 0.3360 0.3855 0.3138 -0.0444 -0.0185 -0.0124 271 THR A N 1501 C CA . THR A 189 ? 0.3926 0.4452 0.3688 -0.0471 -0.0198 -0.0135 271 THR A CA 1502 C C . THR A 189 ? 0.4012 0.4524 0.3748 -0.0457 -0.0202 -0.0138 271 THR A C 1503 O O . THR A 189 ? 0.3012 0.3488 0.2744 -0.0430 -0.0194 -0.0132 271 THR A O 1504 C CB . THR A 189 ? 0.3434 0.3925 0.3170 -0.0510 -0.0193 -0.0153 271 THR A CB 1505 O OG1 . THR A 189 ? 0.5829 0.6370 0.5561 -0.0541 -0.0208 -0.0162 271 THR A OG1 1506 C CG2 . THR A 189 ? 0.4070 0.4482 0.3764 -0.0510 -0.0181 -0.0167 271 THR A CG2 1507 N N . GLY A 190 ? 0.3117 0.3661 0.2837 -0.0478 -0.0216 -0.0146 272 GLY A N 1508 C CA . GLY A 190 ? 0.2944 0.3477 0.2637 -0.0468 -0.0219 -0.0149 272 GLY A CA 1509 C C . GLY A 190 ? 0.2755 0.3349 0.2468 -0.0445 -0.0234 -0.0131 272 GLY A C 1510 O O . GLY A 190 ? 0.2891 0.3546 0.2637 -0.0444 -0.0244 -0.0120 272 GLY A O 1511 N N . THR A 191 ? 0.3036 0.3616 0.2731 -0.0426 -0.0234 -0.0128 273 THR A N 1512 C CA . THR A 191 ? 0.3178 0.3813 0.2884 -0.0407 -0.0248 -0.0111 273 THR A CA 1513 C C . THR A 191 ? 0.2981 0.3612 0.2711 -0.0368 -0.0243 -0.0091 273 THR A C 1514 O O . THR A 191 ? 0.2952 0.3625 0.2694 -0.0349 -0.0253 -0.0075 273 THR A O 1515 C CB . THR A 191 ? 0.3205 0.3842 0.2872 -0.0417 -0.0256 -0.0120 273 THR A CB 1516 O OG1 . THR A 191 ? 0.2897 0.3470 0.2536 -0.0404 -0.0241 -0.0125 273 THR A OG1 1517 C CG2 . THR A 191 ? 0.2895 0.3539 0.2539 -0.0458 -0.0262 -0.0141 273 THR A CG2 1518 N N . ALA A 192 ? 0.2395 0.2974 0.2130 -0.0355 -0.0227 -0.0092 274 ALA A N 1519 C CA . ALA A 192 ? 0.2396 0.2970 0.2154 -0.0320 -0.0221 -0.0074 274 ALA A CA 1520 C C . ALA A 192 ? 0.2886 0.3515 0.2685 -0.0311 -0.0229 -0.0060 274 ALA A C 1521 O O . ALA A 192 ? 0.2665 0.3307 0.2479 -0.0328 -0.0229 -0.0066 274 ALA A O 1522 C CB . ALA A 192 ? 0.2331 0.2844 0.2088 -0.0311 -0.0204 -0.0078 274 ALA A CB 1523 N N . LYS A 193 ? 0.2223 0.2881 0.2039 -0.0285 -0.0236 -0.0042 275 LYS A N 1524 C CA . LYS A 193 ? 0.2764 0.3479 0.2617 -0.0274 -0.0244 -0.0029 275 LYS A CA 1525 C C . LYS A 193 ? 0.3465 0.4163 0.3347 -0.0249 -0.0233 -0.0019 275 LYS A C 1526 O O . LYS A 193 ? 0.2787 0.3525 0.2700 -0.0240 -0.0236 -0.0011 275 LYS A O 1527 C CB . LYS A 193 ? 0.2549 0.3313 0.2405 -0.0260 -0.0259 -0.0014 275 LYS A CB 1528 C CG . LYS A 193 ? 0.2884 0.3676 0.2713 -0.0286 -0.0272 -0.0022 275 LYS A CG 1529 C CD . LYS A 193 ? 0.2947 0.3766 0.2782 -0.0319 -0.0277 -0.0037 275 LYS A CD 1530 C CE . LYS A 193 ? 0.2116 0.2976 0.1929 -0.0345 -0.0293 -0.0045 275 LYS A CE 1531 N NZ . LYS A 193 ? 0.2291 0.3103 0.2057 -0.0358 -0.0289 -0.0058 275 LYS A NZ 1532 N N . HIS A 194 ? 0.3111 0.3752 0.2980 -0.0236 -0.0221 -0.0021 276 HIS A N 1533 C CA . HIS A 194 ? 0.2482 0.3102 0.2374 -0.0215 -0.0210 -0.0014 276 HIS A CA 1534 C C . HIS A 194 ? 0.2929 0.3485 0.2802 -0.0214 -0.0196 -0.0023 276 HIS A C 1535 O O . HIS A 194 ? 0.2779 0.3308 0.2627 -0.0213 -0.0194 -0.0025 276 HIS A O 1536 C CB . HIS A 194 ? 0.2255 0.2894 0.2164 -0.0185 -0.0214 0.0004 276 HIS A CB 1537 C CG . HIS A 194 ? 0.3553 0.4185 0.3490 -0.0166 -0.0206 0.0010 276 HIS A CG 1538 N ND1 . HIS A 194 ? 0.2675 0.3266 0.2612 -0.0147 -0.0196 0.0013 276 HIS A ND1 1539 C CD2 . HIS A 194 ? 0.2967 0.3630 0.2931 -0.0163 -0.0205 0.0011 276 HIS A CD2 1540 C CE1 . HIS A 194 ? 0.3396 0.3990 0.3357 -0.0133 -0.0191 0.0017 276 HIS A CE1 1541 N NE2 . HIS A 194 ? 0.2922 0.3560 0.2900 -0.0142 -0.0196 0.0016 276 HIS A NE2 1542 N N . ILE A 195 ? 0.2320 0.2854 0.2205 -0.0214 -0.0186 -0.0027 277 ILE A N 1543 C CA . ILE A 195 ? 0.2149 0.2626 0.2018 -0.0214 -0.0173 -0.0035 277 ILE A CA 1544 C C . ILE A 195 ? 0.3336 0.3795 0.3224 -0.0193 -0.0165 -0.0028 277 ILE A C 1545 O O . ILE A 195 ? 0.2565 0.3042 0.2475 -0.0190 -0.0164 -0.0026 277 ILE A O 1546 C CB . ILE A 195 ? 0.2609 0.3067 0.2464 -0.0240 -0.0169 -0.0049 277 ILE A CB 1547 C CG1 . ILE A 195 ? 0.2543 0.3011 0.2374 -0.0263 -0.0176 -0.0059 277 ILE A CG1 1548 C CG2 . ILE A 195 ? 0.1487 0.1889 0.1330 -0.0236 -0.0155 -0.0055 277 ILE A CG2 1549 C CD1 . ILE A 195 ? 0.2685 0.3120 0.2487 -0.0260 -0.0173 -0.0063 277 ILE A CD1 1550 N N . GLU A 196 ? 0.2812 0.3237 0.2692 -0.0178 -0.0158 -0.0026 278 GLU A N 1551 C CA . GLU A 196 ? 0.1879 0.2283 0.1773 -0.0161 -0.0150 -0.0022 278 GLU A CA 1552 C C . GLU A 196 ? 0.2917 0.3274 0.2793 -0.0161 -0.0140 -0.0029 278 GLU A C 1553 O O . GLU A 196 ? 0.2582 0.2927 0.2438 -0.0164 -0.0140 -0.0031 278 GLU A O 1554 C CB . GLU A 196 ? 0.1927 0.2343 0.1836 -0.0139 -0.0153 -0.0010 278 GLU A CB 1555 C CG . GLU A 196 ? 0.2208 0.2670 0.2137 -0.0133 -0.0162 -0.0001 278 GLU A CG 1556 C CD . GLU A 196 ? 0.2667 0.3143 0.2620 -0.0128 -0.0159 -0.0001 278 GLU A CD 1557 O OE1 . GLU A 196 ? 0.2888 0.3397 0.2860 -0.0116 -0.0164 0.0008 278 GLU A OE1 1558 O OE2 . GLU A 196 ? 0.2932 0.3385 0.2883 -0.0134 -0.0151 -0.0009 278 GLU A OE2 1559 N N . GLU A 197 ? 0.2351 0.2686 0.2234 -0.0156 -0.0132 -0.0031 279 GLU A N 1560 C CA . GLU A 197 ? 0.2118 0.2416 0.1992 -0.0148 -0.0124 -0.0033 279 GLU A CA 1561 C C . GLU A 197 ? 0.2326 0.2599 0.2173 -0.0158 -0.0120 -0.0041 279 GLU A C 1562 O O . GLU A 197 ? 0.1661 0.1924 0.1499 -0.0151 -0.0117 -0.0039 279 GLU A O 1563 C CB . GLU A 197 ? 0.2010 0.2310 0.1896 -0.0129 -0.0123 -0.0023 279 GLU A CB 1564 C CG . GLU A 197 ? 0.1795 0.2112 0.1706 -0.0118 -0.0125 -0.0017 279 GLU A CG 1565 C CD . GLU A 197 ? 0.2897 0.3214 0.2817 -0.0101 -0.0126 -0.0008 279 GLU A CD 1566 O OE1 . GLU A 197 ? 0.2658 0.2980 0.2570 -0.0099 -0.0129 -0.0002 279 GLU A OE1 1567 O OE2 . GLU A 197 ? 0.2607 0.2918 0.2542 -0.0091 -0.0122 -0.0006 279 GLU A OE2 1568 N N . CYS A 198 ? 0.2355 0.2617 0.2189 -0.0175 -0.0118 -0.0050 280 CYS A N 1569 C CA . CYS A 198 ? 0.2455 0.2690 0.2260 -0.0184 -0.0113 -0.0060 280 CYS A CA 1570 C C . CYS A 198 ? 0.2605 0.2804 0.2404 -0.0173 -0.0102 -0.0061 280 CYS A C 1571 O O . CYS A 198 ? 0.1942 0.2128 0.1752 -0.0166 -0.0097 -0.0059 280 CYS A O 1572 C CB . CYS A 198 ? 0.1976 0.2205 0.1768 -0.0207 -0.0113 -0.0070 280 CYS A CB 1573 S SG . CYS A 198 ? 0.3681 0.3957 0.3477 -0.0225 -0.0127 -0.0070 280 CYS A SG 1574 N N . SER A 199 ? 0.2131 0.2317 0.1912 -0.0170 -0.0099 -0.0064 281 SER A N 1575 C CA . SER A 199 ? 0.2155 0.2308 0.1927 -0.0160 -0.0087 -0.0068 281 SER A CA 1576 C C . SER A 199 ? 0.2636 0.2760 0.2379 -0.0173 -0.0081 -0.0081 281 SER A C 1577 O O . SER A 199 ? 0.2805 0.2933 0.2528 -0.0184 -0.0084 -0.0087 281 SER A O 1578 C CB . SER A 199 ? 0.2344 0.2503 0.2116 -0.0148 -0.0085 -0.0062 281 SER A CB 1579 O OG . SER A 199 ? 0.2334 0.2515 0.2130 -0.0137 -0.0090 -0.0050 281 SER A OG 1580 N N . CYS A 200 ? 0.2280 0.2373 0.2018 -0.0172 -0.0073 -0.0085 282 CYS A N 1581 C CA . CYS A 200 ? 0.2704 0.2763 0.2413 -0.0185 -0.0066 -0.0098 282 CYS A CA 1582 C C . CYS A 200 ? 0.2579 0.2599 0.2274 -0.0172 -0.0053 -0.0102 282 CYS A C 1583 O O . CYS A 200 ? 0.2266 0.2287 0.1978 -0.0153 -0.0049 -0.0094 282 CYS A O 1584 C CB . CYS A 200 ? 0.2253 0.2305 0.1964 -0.0200 -0.0068 -0.0100 282 CYS A CB 1585 S SG . CYS A 200 ? 0.2849 0.2950 0.2582 -0.0212 -0.0083 -0.0093 282 CYS A SG 1586 N N . TYR A 201 ? 0.1972 0.1961 0.1637 -0.0182 -0.0046 -0.0115 283 TYR A N 1587 C CA . TYR A 201 ? 0.2502 0.2450 0.2150 -0.0170 -0.0032 -0.0121 283 TYR A CA 1588 C C . TYR A 201 ? 0.2945 0.2854 0.2562 -0.0187 -0.0026 -0.0135 283 TYR A C 1589 O O . TYR A 201 ? 0.2734 0.2652 0.2339 -0.0210 -0.0034 -0.0143 283 TYR A O 1590 C CB . TYR A 201 ? 0.2535 0.2489 0.2177 -0.0156 -0.0026 -0.0122 283 TYR A CB 1591 C CG . TYR A 201 ? 0.2483 0.2439 0.2098 -0.0171 -0.0028 -0.0133 283 TYR A CG 1592 C CD1 . TYR A 201 ? 0.2235 0.2232 0.1858 -0.0179 -0.0040 -0.0128 283 TYR A CD1 1593 C CD2 . TYR A 201 ? 0.3066 0.2984 0.2647 -0.0176 -0.0018 -0.0149 283 TYR A CD2 1594 C CE1 . TYR A 201 ? 0.2307 0.2310 0.1904 -0.0192 -0.0043 -0.0137 283 TYR A CE1 1595 C CE2 . TYR A 201 ? 0.2303 0.2225 0.1856 -0.0191 -0.0020 -0.0160 283 TYR A CE2 1596 C CZ . TYR A 201 ? 0.2404 0.2371 0.1967 -0.0199 -0.0034 -0.0153 283 TYR A CZ 1597 O OH . TYR A 201 ? 0.3266 0.3240 0.2801 -0.0213 -0.0037 -0.0163 283 TYR A OH 1598 N N . GLY A 202 ? 0.2314 0.2178 0.1917 -0.0177 -0.0013 -0.0140 284 GLY A N 1599 C CA . GLY A 202 ? 0.2717 0.2535 0.2288 -0.0194 -0.0006 -0.0154 284 GLY A CA 1600 C C . GLY A 202 ? 0.3415 0.3193 0.2957 -0.0184 0.0008 -0.0166 284 GLY A C 1601 O O . GLY A 202 ? 0.2699 0.2474 0.2248 -0.0159 0.0017 -0.0160 284 GLY A O 1602 N N . GLU A 203 ? 0.3646 0.3393 0.3153 -0.0204 0.0012 -0.0183 285 GLU A N 1603 C CA . GLU A 203 ? 0.3574 0.3273 0.3049 -0.0196 0.0028 -0.0197 285 GLU A CA 1604 C C . GLU A 203 ? 0.3759 0.3414 0.3200 -0.0223 0.0030 -0.0214 285 GLU A C 1605 O O . GLU A 203 ? 0.4328 0.3997 0.3775 -0.0247 0.0020 -0.0213 285 GLU A O 1606 C CB . GLU A 203 ? 0.3223 0.2945 0.2689 -0.0188 0.0029 -0.0202 285 GLU A CB 1607 C CG . GLU A 203 ? 0.3896 0.3662 0.3361 -0.0211 0.0014 -0.0205 285 GLU A CG 1608 C CD . GLU A 203 ? 0.5384 0.5128 0.4806 -0.0227 0.0018 -0.0226 285 GLU A CD 1609 O OE1 . GLU A 203 ? 0.4940 0.4630 0.4333 -0.0224 0.0033 -0.0240 285 GLU A OE1 1610 O OE2 . GLU A 203 ? 0.7412 0.7194 0.6829 -0.0241 0.0007 -0.0229 285 GLU A OE2 1611 N N . ARG A 204 ? 0.4016 0.3618 0.3421 -0.0220 0.0046 -0.0230 286 ARG A N 1612 C CA . ARG A 204 ? 0.4662 0.4210 0.4032 -0.0246 0.0051 -0.0247 286 ARG A CA 1613 C C . ARG A 204 ? 0.4516 0.4090 0.3877 -0.0284 0.0036 -0.0257 286 ARG A C 1614 O O . ARG A 204 ? 0.4637 0.4183 0.3983 -0.0309 0.0035 -0.0264 286 ARG A O 1615 C CB . ARG A 204 ? 0.4406 0.3897 0.3737 -0.0236 0.0069 -0.0265 286 ARG A CB 1616 C CG . ARG A 204 ? 0.4167 0.3684 0.3486 -0.0230 0.0070 -0.0274 286 ARG A CG 1617 C CD . ARG A 204 ? 0.4229 0.3688 0.3510 -0.0217 0.0091 -0.0292 286 ARG A CD 1618 N NE . ARG A 204 ? 0.4248 0.3736 0.3522 -0.0205 0.0094 -0.0297 286 ARG A NE 1619 C CZ . ARG A 204 ? 0.4516 0.3978 0.3776 -0.0178 0.0112 -0.0303 286 ARG A CZ 1620 N NH1 . ARG A 204 ? 0.4120 0.3524 0.3371 -0.0160 0.0129 -0.0305 286 ARG A NH1 1621 N NH2 . ARG A 204 ? 0.5091 0.4583 0.4345 -0.0169 0.0115 -0.0307 286 ARG A NH2 1622 N N . THR A 205 ? 0.8504 0.8134 0.7875 -0.0287 0.0024 -0.0255 287 THR A N 1623 C CA . THR A 205 ? 0.8869 0.8532 0.8232 -0.0320 0.0008 -0.0263 287 THR A CA 1624 C C . THR A 205 ? 0.9419 0.9124 0.8818 -0.0333 -0.0007 -0.0248 287 THR A C 1625 O O . THR A 205 ? 0.9108 0.8842 0.8504 -0.0361 -0.0020 -0.0253 287 THR A O 1626 C CB . THR A 205 ? 0.9932 0.9643 0.9292 -0.0318 0.0000 -0.0265 287 THR A CB 1627 O OG1 . THR A 205 ? 0.9833 0.9599 0.9234 -0.0298 -0.0009 -0.0244 287 THR A OG1 1628 C CG2 . THR A 205 ? 0.8510 0.8185 0.7837 -0.0303 0.0016 -0.0279 287 THR A CG2 1629 N N . GLY A 206 ? 0.6717 0.6427 0.6147 -0.0311 -0.0004 -0.0230 288 GLY A N 1630 C CA . GLY A 206 ? 0.5043 0.4791 0.4506 -0.0318 -0.0016 -0.0215 288 GLY A CA 1631 C C . GLY A 206 ? 0.4921 0.4716 0.4423 -0.0292 -0.0022 -0.0195 288 GLY A C 1632 O O . GLY A 206 ? 0.4561 0.4347 0.4067 -0.0264 -0.0014 -0.0190 288 GLY A O 1633 N N . ILE A 207 ? 0.3583 0.3426 0.3114 -0.0299 -0.0035 -0.0184 289 ILE A N 1634 C CA . ILE A 207 ? 0.2895 0.2782 0.2462 -0.0277 -0.0042 -0.0166 289 ILE A CA 1635 C C . ILE A 207 ? 0.2882 0.2824 0.2458 -0.0283 -0.0056 -0.0164 289 ILE A C 1636 O O . ILE A 207 ? 0.3056 0.3022 0.2629 -0.0307 -0.0066 -0.0169 289 ILE A O 1637 C CB . ILE A 207 ? 0.2465 0.2364 0.2059 -0.0276 -0.0044 -0.0153 289 ILE A CB 1638 C CG1 . ILE A 207 ? 0.2699 0.2543 0.2283 -0.0266 -0.0030 -0.0152 289 ILE A CG1 1639 C CG2 . ILE A 207 ? 0.2504 0.2450 0.2134 -0.0256 -0.0052 -0.0137 289 ILE A CG2 1640 C CD1 . ILE A 207 ? 0.2723 0.2574 0.2329 -0.0266 -0.0032 -0.0139 289 ILE A CD1 1641 N N . THR A 208 ? 0.2776 0.2737 0.2362 -0.0261 -0.0056 -0.0157 290 THR A N 1642 C CA . THR A 208 ? 0.2199 0.2209 0.1793 -0.0263 -0.0068 -0.0152 290 THR A CA 1643 C C . THR A 208 ? 0.2914 0.2962 0.2546 -0.0245 -0.0075 -0.0133 290 THR A C 1644 O O . THR A 208 ? 0.2846 0.2883 0.2491 -0.0223 -0.0067 -0.0126 290 THR A O 1645 C CB . THR A 208 ? 0.2455 0.2458 0.2025 -0.0256 -0.0064 -0.0159 290 THR A CB 1646 O OG1 . THR A 208 ? 0.2960 0.2923 0.2491 -0.0273 -0.0056 -0.0178 290 THR A OG1 1647 C CG2 . THR A 208 ? 0.2838 0.2891 0.2413 -0.0260 -0.0077 -0.0153 290 THR A CG2 1648 N N . CYS A 209 ? 0.2833 0.2925 0.2482 -0.0253 -0.0088 -0.0127 291 CYS A N 1649 C CA . CYS A 209 ? 0.2882 0.3009 0.2565 -0.0237 -0.0094 -0.0110 291 CYS A CA 1650 C C . CYS A 209 ? 0.3009 0.3177 0.2696 -0.0234 -0.0105 -0.0104 291 CYS A C 1651 O O . CYS A 209 ? 0.3239 0.3432 0.2918 -0.0251 -0.0115 -0.0107 291 CYS A O 1652 C CB . CYS A 209 ? 0.2743 0.2890 0.2449 -0.0245 -0.0100 -0.0105 291 CYS A CB 1653 S SG . CYS A 209 ? 0.3207 0.3310 0.2911 -0.0246 -0.0088 -0.0109 291 CYS A SG 1654 N N . THR A 210 ? 0.2411 0.2584 0.2109 -0.0213 -0.0103 -0.0093 292 THR A N 1655 C CA . THR A 210 ? 0.2499 0.2708 0.2203 -0.0207 -0.0112 -0.0084 292 THR A CA 1656 C C . THR A 210 ? 0.2320 0.2556 0.2058 -0.0195 -0.0118 -0.0069 292 THR A C 1657 O O . THR A 210 ? 0.2748 0.2971 0.2503 -0.0180 -0.0111 -0.0063 292 THR A O 1658 C CB . THR A 210 ? 0.2262 0.2458 0.1953 -0.0194 -0.0104 -0.0081 292 THR A CB 1659 O OG1 . THR A 210 ? 0.2826 0.2992 0.2486 -0.0203 -0.0095 -0.0096 292 THR A OG1 1660 C CG2 . THR A 210 ? 0.2190 0.2421 0.1881 -0.0191 -0.0114 -0.0071 292 THR A CG2 1661 N N . CYS A 211 ? 0.2591 0.2866 0.2341 -0.0200 -0.0130 -0.0063 293 CYS A N 1662 C CA . CYS A 211 ? 0.1977 0.2276 0.1758 -0.0189 -0.0135 -0.0051 293 CYS A CA 1663 C C . CYS A 211 ? 0.2392 0.2722 0.2184 -0.0176 -0.0143 -0.0037 293 CYS A C 1664 O O . CYS A 211 ? 0.2207 0.2532 0.1984 -0.0171 -0.0142 -0.0033 293 CYS A O 1665 C CB . CYS A 211 ? 0.2222 0.2543 0.2013 -0.0205 -0.0141 -0.0055 293 CYS A CB 1666 S SG . CYS A 211 ? 0.2742 0.3025 0.2512 -0.0226 -0.0133 -0.0072 293 CYS A SG 1667 N N . LYS A 212 ? 0.2370 0.2729 0.2188 -0.0170 -0.0150 -0.0028 294 LYS A N 1668 C CA . LYS A 212 ? 0.2067 0.2452 0.1898 -0.0154 -0.0157 -0.0013 294 LYS A CA 1669 C C . LYS A 212 ? 0.2497 0.2928 0.2341 -0.0159 -0.0169 -0.0009 294 LYS A C 1670 O O . LYS A 212 ? 0.2503 0.2946 0.2364 -0.0164 -0.0169 -0.0012 294 LYS A O 1671 C CB . LYS A 212 ? 0.2592 0.2964 0.2444 -0.0135 -0.0151 -0.0005 294 LYS A CB 1672 C CG . LYS A 212 ? 0.2238 0.2631 0.2104 -0.0118 -0.0156 0.0011 294 LYS A CG 1673 C CD . LYS A 212 ? 0.3173 0.3551 0.3061 -0.0101 -0.0150 0.0017 294 LYS A CD 1674 C CE . LYS A 212 ? 0.3085 0.3485 0.2996 -0.0097 -0.0153 0.0017 294 LYS A CE 1675 N NZ . LYS A 212 ? 0.3501 0.3890 0.3431 -0.0079 -0.0149 0.0024 294 LYS A NZ 1676 N N . ASP A 213 ? 0.2092 0.2551 0.1929 -0.0158 -0.0179 -0.0001 295 ASP A N 1677 C CA . ASP A 213 ? 0.2374 0.2883 0.2227 -0.0158 -0.0191 0.0006 295 ASP A CA 1678 C C . ASP A 213 ? 0.2813 0.3330 0.2686 -0.0132 -0.0192 0.0024 295 ASP A C 1679 O O . ASP A 213 ? 0.2536 0.3050 0.2399 -0.0121 -0.0193 0.0034 295 ASP A O 1680 C CB . ASP A 213 ? 0.2927 0.3464 0.2758 -0.0170 -0.0202 0.0006 295 ASP A CB 1681 C CG . ASP A 213 ? 0.2800 0.3395 0.2649 -0.0167 -0.0217 0.0017 295 ASP A CG 1682 O OD1 . ASP A 213 ? 0.2253 0.2866 0.2128 -0.0146 -0.0219 0.0031 295 ASP A OD1 1683 O OD2 . ASP A 213 ? 0.2935 0.3561 0.2772 -0.0187 -0.0227 0.0010 295 ASP A OD2 1684 N N . ASN A 214 ? 0.2848 0.3373 0.2749 -0.0121 -0.0189 0.0027 296 ASN A N 1685 C CA . ASN A 214 ? 0.3544 0.4071 0.3463 -0.0096 -0.0188 0.0041 296 ASN A CA 1686 C C . ASN A 214 ? 0.4089 0.4663 0.4019 -0.0085 -0.0201 0.0056 296 ASN A C 1687 O O . ASN A 214 ? 0.3882 0.4456 0.3820 -0.0063 -0.0201 0.0070 296 ASN A O 1688 C CB . ASN A 214 ? 0.2507 0.3021 0.2448 -0.0087 -0.0180 0.0038 296 ASN A CB 1689 C CG . ASN A 214 ? 0.3192 0.3689 0.3145 -0.0063 -0.0176 0.0050 296 ASN A CG 1690 O OD1 . ASN A 214 ? 0.2751 0.3212 0.2694 -0.0058 -0.0169 0.0051 296 ASN A OD1 1691 N ND2 . ASN A 214 ? 0.2934 0.3459 0.2910 -0.0048 -0.0179 0.0058 296 ASN A ND2 1692 N N . TRP A 215 ? 0.3299 0.3914 0.3230 -0.0100 -0.0210 0.0051 297 TRP A N 1693 C CA . TRP A 215 ? 0.2921 0.3592 0.2869 -0.0091 -0.0223 0.0064 297 TRP A CA 1694 C C . TRP A 215 ? 0.3162 0.3846 0.3092 -0.0084 -0.0232 0.0077 297 TRP A C 1695 O O . TRP A 215 ? 0.2992 0.3685 0.2932 -0.0060 -0.0235 0.0095 297 TRP A O 1696 C CB . TRP A 215 ? 0.3195 0.3907 0.3151 -0.0113 -0.0230 0.0053 297 TRP A CB 1697 C CG . TRP A 215 ? 0.3607 0.4386 0.3581 -0.0108 -0.0244 0.0064 297 TRP A CG 1698 C CD1 . TRP A 215 ? 0.3630 0.4435 0.3620 -0.0080 -0.0249 0.0083 297 TRP A CD1 1699 C CD2 . TRP A 215 ? 0.3308 0.4136 0.3285 -0.0132 -0.0254 0.0057 297 TRP A CD2 1700 N NE1 . TRP A 215 ? 0.2905 0.3777 0.2910 -0.0084 -0.0263 0.0089 297 TRP A NE1 1701 C CE2 . TRP A 215 ? 0.3833 0.4721 0.3830 -0.0116 -0.0267 0.0073 297 TRP A CE2 1702 C CE3 . TRP A 215 ? 0.3203 0.4030 0.3167 -0.0165 -0.0254 0.0039 297 TRP A CE3 1703 C CZ2 . TRP A 215 ? 0.3307 0.4260 0.3314 -0.0134 -0.0280 0.0071 297 TRP A CZ2 1704 C CZ3 . TRP A 215 ? 0.3333 0.4218 0.3305 -0.0184 -0.0267 0.0036 297 TRP A CZ3 1705 C CH2 . TRP A 215 ? 0.3827 0.4777 0.3821 -0.0170 -0.0280 0.0052 297 TRP A CH2 1706 N N . GLN A 216 ? 0.3927 0.4612 0.3829 -0.0105 -0.0237 0.0069 298 GLN A N 1707 C CA . GLN A 216 ? 0.3744 0.4449 0.3627 -0.0100 -0.0248 0.0082 298 GLN A CA 1708 C C . GLN A 216 ? 0.4020 0.4687 0.3866 -0.0110 -0.0243 0.0076 298 GLN A C 1709 O O . GLN A 216 ? 0.3794 0.4468 0.3623 -0.0102 -0.0248 0.0089 298 GLN A O 1710 C CB . GLN A 216 ? 0.4444 0.5210 0.4328 -0.0115 -0.0264 0.0080 298 GLN A CB 1711 C CG . GLN A 216 ? 0.4426 0.5244 0.4345 -0.0102 -0.0272 0.0091 298 GLN A CG 1712 C CD . GLN A 216 ? 0.5685 0.6567 0.5606 -0.0122 -0.0288 0.0087 298 GLN A CD 1713 O OE1 . GLN A 216 ? 0.5792 0.6725 0.5723 -0.0109 -0.0301 0.0103 298 GLN A OE1 1714 N NE2 . GLN A 216 ? 0.4251 0.5128 0.4161 -0.0153 -0.0287 0.0066 298 GLN A NE2 1715 N N . GLY A 217 ? 0.3057 0.3687 0.2890 -0.0128 -0.0233 0.0058 299 GLY A N 1716 C CA . GLY A 217 ? 0.3506 0.4108 0.3303 -0.0140 -0.0229 0.0050 299 GLY A CA 1717 C C . GLY A 217 ? 0.3522 0.4071 0.3310 -0.0131 -0.0213 0.0050 299 GLY A C 1718 O O . GLY A 217 ? 0.3891 0.4410 0.3692 -0.0130 -0.0203 0.0042 299 GLY A O 1719 N N . SER A 218 ? 0.3364 0.3906 0.3129 -0.0126 -0.0213 0.0059 300 SER A N 1720 C CA . SER A 218 ? 0.2850 0.3345 0.2604 -0.0119 -0.0198 0.0059 300 SER A CA 1721 C C . SER A 218 ? 0.3453 0.3924 0.3178 -0.0138 -0.0191 0.0040 300 SER A C 1722 O O . SER A 218 ? 0.3424 0.3859 0.3140 -0.0134 -0.0177 0.0038 300 SER A O 1723 C CB . SER A 218 ? 0.3097 0.3593 0.2844 -0.0103 -0.0199 0.0080 300 SER A CB 1724 O OG . SER A 218 ? 0.2957 0.3467 0.2731 -0.0083 -0.0203 0.0097 300 SER A OG 1725 N N . ASN A 219 ? 0.2996 0.3486 0.2706 -0.0158 -0.0198 0.0027 301 ASN A N 1726 C CA . ASN A 219 ? 0.3146 0.3607 0.2832 -0.0176 -0.0190 0.0005 301 ASN A CA 1727 C C . ASN A 219 ? 0.2965 0.3408 0.2672 -0.0181 -0.0184 -0.0007 301 ASN A C 1728 O O . ASN A 219 ? 0.2861 0.3324 0.2597 -0.0175 -0.0189 0.0000 301 ASN A O 1729 C CB . ASN A 219 ? 0.2233 0.2716 0.1889 -0.0197 -0.0200 -0.0006 301 ASN A CB 1730 C CG . ASN A 219 ? 0.2920 0.3452 0.2592 -0.0206 -0.0217 -0.0004 301 ASN A CG 1731 O OD1 . ASN A 219 ? 0.2921 0.3475 0.2625 -0.0191 -0.0222 0.0011 301 ASN A OD1 1732 N ND2 . ASN A 219 ? 0.2527 0.3077 0.2177 -0.0229 -0.0225 -0.0018 301 ASN A ND2 1733 N N . ARG A 220 ? 0.2967 0.3372 0.2660 -0.0191 -0.0172 -0.0023 302 ARG A N 1734 C CA . ARG A 220 ? 0.2401 0.2787 0.2112 -0.0194 -0.0166 -0.0032 302 ARG A CA 1735 C C . ARG A 220 ? 0.2163 0.2553 0.1863 -0.0219 -0.0170 -0.0049 302 ARG A C 1736 O O . ARG A 220 ? 0.2375 0.2755 0.2044 -0.0234 -0.0169 -0.0062 302 ARG A O 1737 C CB . ARG A 220 ? 0.2024 0.2364 0.1733 -0.0186 -0.0150 -0.0037 302 ARG A CB 1738 C CG . ARG A 220 ? 0.2959 0.3294 0.2685 -0.0164 -0.0145 -0.0021 302 ARG A CG 1739 C CD . ARG A 220 ? 0.2155 0.2452 0.1887 -0.0157 -0.0130 -0.0026 302 ARG A CD 1740 N NE . ARG A 220 ? 0.2496 0.2791 0.2247 -0.0139 -0.0126 -0.0012 302 ARG A NE 1741 C CZ . ARG A 220 ? 0.2485 0.2787 0.2265 -0.0129 -0.0128 -0.0004 302 ARG A CZ 1742 N NH1 . ARG A 220 ? 0.1838 0.2151 0.1631 -0.0134 -0.0134 -0.0009 302 ARG A NH1 1743 N NH2 . ARG A 220 ? 0.1897 0.2192 0.1690 -0.0115 -0.0124 0.0007 302 ARG A NH2 1744 N N . PRO A 221 ? 0.2440 0.2843 0.2165 -0.0223 -0.0173 -0.0049 303 PRO A N 1745 C CA . PRO A 221 ? 0.2750 0.3152 0.2467 -0.0247 -0.0175 -0.0065 303 PRO A CA 1746 C C . PRO A 221 ? 0.3229 0.3577 0.2931 -0.0252 -0.0160 -0.0079 303 PRO A C 1747 O O . PRO A 221 ? 0.2882 0.3202 0.2593 -0.0235 -0.0150 -0.0074 303 PRO A O 1748 C CB . PRO A 221 ? 0.3051 0.3483 0.2803 -0.0245 -0.0181 -0.0057 303 PRO A CB 1749 C CG . PRO A 221 ? 0.2913 0.3340 0.2689 -0.0218 -0.0176 -0.0043 303 PRO A CG 1750 C CD . PRO A 221 ? 0.2662 0.3084 0.2423 -0.0205 -0.0176 -0.0035 303 PRO A CD 1751 N N . VAL A 222 ? 0.2463 0.2796 0.2140 -0.0276 -0.0159 -0.0096 304 VAL A N 1752 C CA . VAL A 222 ? 0.2126 0.2407 0.1785 -0.0282 -0.0145 -0.0110 304 VAL A CA 1753 C C . VAL A 222 ? 0.3582 0.3859 0.3244 -0.0305 -0.0146 -0.0119 304 VAL A C 1754 O O . VAL A 222 ? 0.3066 0.3375 0.2724 -0.0326 -0.0157 -0.0124 304 VAL A O 1755 C CB . VAL A 222 ? 0.2641 0.2894 0.2260 -0.0289 -0.0140 -0.0123 304 VAL A CB 1756 C CG1 . VAL A 222 ? 0.2155 0.2351 0.1753 -0.0296 -0.0125 -0.0139 304 VAL A CG1 1757 C CG2 . VAL A 222 ? 0.2592 0.2846 0.2209 -0.0267 -0.0136 -0.0113 304 VAL A CG2 1758 N N . ILE A 223 ? 0.3099 0.3338 0.2766 -0.0301 -0.0135 -0.0121 305 ILE A N 1759 C CA . ILE A 223 ? 0.2315 0.2541 0.1980 -0.0323 -0.0133 -0.0131 305 ILE A CA 1760 C C . ILE A 223 ? 0.2814 0.2976 0.2449 -0.0326 -0.0118 -0.0144 305 ILE A C 1761 O O . ILE A 223 ? 0.2575 0.2707 0.2213 -0.0305 -0.0107 -0.0140 305 ILE A O 1762 C CB . ILE A 223 ? 0.2723 0.2961 0.2422 -0.0314 -0.0132 -0.0119 305 ILE A CB 1763 C CG1 . ILE A 223 ? 0.2256 0.2557 0.1984 -0.0311 -0.0146 -0.0107 305 ILE A CG1 1764 C CG2 . ILE A 223 ? 0.2291 0.2504 0.1984 -0.0335 -0.0126 -0.0128 305 ILE A CG2 1765 C CD1 . ILE A 223 ? 0.2856 0.3173 0.2618 -0.0299 -0.0144 -0.0096 305 ILE A CD1 1766 N N . GLN A 224 ? 0.3010 0.3154 0.2618 -0.0353 -0.0117 -0.0161 306 GLN A N 1767 C CA . GLN A 224 ? 0.2745 0.2824 0.2322 -0.0358 -0.0103 -0.0175 306 GLN A CA 1768 C C . GLN A 224 ? 0.3379 0.3434 0.2958 -0.0376 -0.0098 -0.0179 306 GLN A C 1769 O O . GLN A 224 ? 0.2873 0.2950 0.2451 -0.0403 -0.0106 -0.0184 306 GLN A O 1770 C CB . GLN A 224 ? 0.3353 0.3419 0.2891 -0.0374 -0.0103 -0.0193 306 GLN A CB 1771 C CG . GLN A 224 ? 0.5272 0.5349 0.4802 -0.0354 -0.0103 -0.0189 306 GLN A CG 1772 C CD . GLN A 224 ? 0.5502 0.5578 0.4994 -0.0371 -0.0107 -0.0205 306 GLN A CD 1773 O OE1 . GLN A 224 ? 0.5510 0.5627 0.5000 -0.0392 -0.0121 -0.0208 306 GLN A OE1 1774 N NE2 . GLN A 224 ? 0.6324 0.6355 0.5786 -0.0363 -0.0093 -0.0216 306 GLN A NE2 1775 N N . ILE A 225 ? 0.3321 0.3332 0.2901 -0.0361 -0.0085 -0.0175 307 ILE A N 1776 C CA . ILE A 225 ? 0.3194 0.3183 0.2778 -0.0375 -0.0080 -0.0175 307 ILE A CA 1777 C C . ILE A 225 ? 0.2871 0.2789 0.2421 -0.0383 -0.0065 -0.0188 307 ILE A C 1778 O O . ILE A 225 ? 0.3332 0.3211 0.2869 -0.0361 -0.0054 -0.0189 307 ILE A O 1779 C CB . ILE A 225 ? 0.2777 0.2775 0.2394 -0.0350 -0.0077 -0.0157 307 ILE A CB 1780 C CG1 . ILE A 225 ? 0.2503 0.2568 0.2155 -0.0341 -0.0090 -0.0143 307 ILE A CG1 1781 C CG2 . ILE A 225 ? 0.2498 0.2473 0.2117 -0.0363 -0.0070 -0.0154 307 ILE A CG2 1782 C CD1 . ILE A 225 ? 0.2160 0.2233 0.1840 -0.0313 -0.0087 -0.0128 307 ILE A CD1 1783 N N . ASP A 226 ? 0.3283 0.3184 0.2818 -0.0415 -0.0064 -0.0199 308 ASP A N 1784 C CA . ASP A 226 ? 0.3489 0.3317 0.2992 -0.0424 -0.0049 -0.0209 308 ASP A CA 1785 C C . ASP A 226 ? 0.3616 0.3428 0.3138 -0.0416 -0.0042 -0.0195 308 ASP A C 1786 O O . ASP A 226 ? 0.3614 0.3453 0.3152 -0.0436 -0.0048 -0.0189 308 ASP A O 1787 C CB . ASP A 226 ? 0.3676 0.3490 0.3152 -0.0465 -0.0052 -0.0228 308 ASP A CB 1788 C CG . ASP A 226 ? 0.4009 0.3740 0.3447 -0.0476 -0.0035 -0.0241 308 ASP A CG 1789 O OD1 . ASP A 226 ? 0.3580 0.3267 0.3018 -0.0454 -0.0022 -0.0232 308 ASP A OD1 1790 O OD2 . ASP A 226 ? 0.4503 0.4212 0.3910 -0.0506 -0.0035 -0.0261 308 ASP A OD2 1791 N N . PRO A 227 ? 0.3633 0.3403 0.3151 -0.0388 -0.0030 -0.0188 309 PRO A N 1792 C CA . PRO A 227 ? 0.4256 0.4014 0.3791 -0.0377 -0.0024 -0.0172 309 PRO A CA 1793 C C . PRO A 227 ? 0.3046 0.2746 0.2557 -0.0399 -0.0013 -0.0177 309 PRO A C 1794 O O . PRO A 227 ? 0.3853 0.3545 0.3375 -0.0396 -0.0009 -0.0164 309 PRO A O 1795 C CB . PRO A 227 ? 0.3043 0.2783 0.2583 -0.0338 -0.0016 -0.0164 309 PRO A CB 1796 C CG . PRO A 227 ? 0.3913 0.3620 0.3423 -0.0335 -0.0010 -0.0180 309 PRO A CG 1797 C CD . PRO A 227 ? 0.3841 0.3583 0.3344 -0.0362 -0.0022 -0.0192 309 PRO A CD 1798 N N . VAL A 228 ? 0.4028 0.3684 0.3503 -0.0420 -0.0007 -0.0196 310 VAL A N 1799 C CA . VAL A 228 ? 0.3985 0.3579 0.3433 -0.0444 0.0004 -0.0202 310 VAL A CA 1800 C C . VAL A 228 ? 0.3989 0.3619 0.3445 -0.0485 -0.0006 -0.0206 310 VAL A C 1801 O O . VAL A 228 ? 0.4647 0.4268 0.4110 -0.0498 -0.0002 -0.0196 310 VAL A O 1802 C CB . VAL A 228 ? 0.4705 0.4229 0.4108 -0.0449 0.0016 -0.0222 310 VAL A CB 1803 C CG1 . VAL A 228 ? 0.4244 0.3704 0.3619 -0.0479 0.0027 -0.0229 310 VAL A CG1 1804 C CG2 . VAL A 228 ? 0.3859 0.3348 0.3256 -0.0408 0.0027 -0.0218 310 VAL A CG2 1805 N N . ALA A 229 ? 0.3813 0.3484 0.3268 -0.0504 -0.0018 -0.0219 311 ALA A N 1806 C CA . ALA A 229 ? 0.3604 0.3320 0.3069 -0.0543 -0.0029 -0.0223 311 ALA A CA 1807 C C . ALA A 229 ? 0.3796 0.3588 0.3307 -0.0533 -0.0040 -0.0203 311 ALA A C 1808 O O . ALA A 229 ? 0.3792 0.3621 0.3319 -0.0560 -0.0047 -0.0201 311 ALA A O 1809 C CB . ALA A 229 ? 0.3308 0.3048 0.2756 -0.0564 -0.0040 -0.0242 311 ALA A CB 1810 N N . MET A 230 ? 0.2599 0.2413 0.2131 -0.0495 -0.0042 -0.0191 312 MET A N 1811 C CA . MET A 230 ? 0.2974 0.2857 0.2549 -0.0480 -0.0052 -0.0174 312 MET A CA 1812 C C . MET A 230 ? 0.3050 0.3004 0.2641 -0.0498 -0.0069 -0.0178 312 MET A C 1813 O O . MET A 230 ? 0.2720 0.2723 0.2337 -0.0512 -0.0076 -0.0170 312 MET A O 1814 C CB . MET A 230 ? 0.2513 0.2391 0.2102 -0.0485 -0.0046 -0.0160 312 MET A CB 1815 C CG . MET A 230 ? 0.2899 0.2712 0.2473 -0.0462 -0.0031 -0.0153 312 MET A CG 1816 S SD . MET A 230 ? 0.3500 0.3318 0.3094 -0.0458 -0.0025 -0.0133 312 MET A SD 1817 C CE . MET A 230 ? 0.3075 0.2878 0.2653 -0.0508 -0.0021 -0.0141 312 MET A CE 1818 N N . THR A 231 ? 0.3603 0.3563 0.3179 -0.0497 -0.0075 -0.0189 313 THR A N 1819 C CA . THR A 231 ? 0.3413 0.3442 0.3003 -0.0510 -0.0092 -0.0192 313 THR A CA 1820 C C . THR A 231 ? 0.2788 0.2832 0.2379 -0.0482 -0.0097 -0.0190 313 THR A C 1821 O O . THR A 231 ? 0.3274 0.3274 0.2852 -0.0457 -0.0087 -0.0189 313 THR A O 1822 C CB . THR A 231 ? 0.4060 0.4083 0.3624 -0.0552 -0.0096 -0.0211 313 THR A CB 1823 O OG1 . THR A 231 ? 0.3450 0.3405 0.2971 -0.0553 -0.0086 -0.0228 313 THR A OG1 1824 C CG2 . THR A 231 ? 0.3937 0.3954 0.3503 -0.0584 -0.0093 -0.0212 313 THR A CG2 1825 N N . HIS A 232 ? 0.3279 0.3386 0.2884 -0.0485 -0.0112 -0.0188 314 HIS A N 1826 C CA . HIS A 232 ? 0.3311 0.3439 0.2920 -0.0458 -0.0118 -0.0183 314 HIS A CA 1827 C C . HIS A 232 ? 0.3840 0.4023 0.3447 -0.0473 -0.0134 -0.0189 314 HIS A C 1828 O O . HIS A 232 ? 0.2871 0.3087 0.2482 -0.0503 -0.0143 -0.0193 314 HIS A O 1829 C CB . HIS A 232 ? 0.2928 0.3087 0.2575 -0.0426 -0.0119 -0.0163 314 HIS A CB 1830 C CG . HIS A 232 ? 0.3063 0.3293 0.2744 -0.0432 -0.0132 -0.0153 314 HIS A CG 1831 N ND1 . HIS A 232 ? 0.2993 0.3239 0.2691 -0.0448 -0.0132 -0.0149 314 HIS A ND1 1832 C CD2 . HIS A 232 ? 0.3097 0.3387 0.2797 -0.0423 -0.0146 -0.0145 314 HIS A CD2 1833 C CE1 . HIS A 232 ? 0.3473 0.3786 0.3201 -0.0448 -0.0144 -0.0140 314 HIS A CE1 1834 N NE2 . HIS A 232 ? 0.3016 0.3357 0.2746 -0.0432 -0.0153 -0.0137 314 HIS A NE2 1835 N N . THR A 233 ? 0.3334 0.3527 0.2933 -0.0454 -0.0138 -0.0187 315 THR A N 1836 C CA . THR A 233 ? 0.3082 0.3334 0.2684 -0.0462 -0.0155 -0.0186 315 THR A CA 1837 C C . THR A 233 ? 0.2862 0.3143 0.2486 -0.0426 -0.0159 -0.0169 315 THR A C 1838 O O . THR A 233 ? 0.2693 0.2941 0.2323 -0.0400 -0.0148 -0.0161 315 THR A O 1839 C CB . THR A 233 ? 0.4019 0.4250 0.3577 -0.0480 -0.0156 -0.0206 315 THR A CB 1840 O OG1 . THR A 233 ? 0.3960 0.4133 0.3494 -0.0459 -0.0142 -0.0210 315 THR A OG1 1841 C CG2 . THR A 233 ? 0.4379 0.4585 0.3915 -0.0520 -0.0154 -0.0225 315 THR A CG2 1842 N N . SER A 234 ? 0.3082 0.3423 0.2717 -0.0424 -0.0174 -0.0161 316 SER A N 1843 C CA . SER A 234 ? 0.2676 0.3038 0.2327 -0.0392 -0.0177 -0.0144 316 SER A CA 1844 C C . SER A 234 ? 0.3358 0.3758 0.2995 -0.0394 -0.0190 -0.0144 316 SER A C 1845 O O . SER A 234 ? 0.3162 0.3594 0.2788 -0.0420 -0.0202 -0.0152 316 SER A O 1846 C CB . SER A 234 ? 0.2595 0.2996 0.2291 -0.0374 -0.0181 -0.0126 316 SER A CB 1847 O OG . SER A 234 ? 0.2756 0.3224 0.2471 -0.0383 -0.0197 -0.0119 316 SER A OG 1848 N N . GLN A 235 ? 0.2937 0.3332 0.2571 -0.0368 -0.0188 -0.0134 317 GLN A N 1849 C CA . GLN A 235 ? 0.2734 0.3167 0.2357 -0.0363 -0.0200 -0.0128 317 GLN A CA 1850 C C . GLN A 235 ? 0.2687 0.3114 0.2322 -0.0329 -0.0195 -0.0110 317 GLN A C 1851 O O . GLN A 235 ? 0.2932 0.3344 0.2593 -0.0311 -0.0187 -0.0101 317 GLN A O 1852 C CB . GLN A 235 ? 0.2673 0.3083 0.2250 -0.0383 -0.0199 -0.0147 317 GLN A CB 1853 C CG . GLN A 235 ? 0.2851 0.3196 0.2401 -0.0372 -0.0181 -0.0156 317 GLN A CG 1854 C CD . GLN A 235 ? 0.4514 0.4841 0.4017 -0.0389 -0.0180 -0.0174 317 GLN A CD 1855 O OE1 . GLN A 235 ? 0.3588 0.3889 0.3067 -0.0415 -0.0177 -0.0195 317 GLN A OE1 1856 N NE2 . GLN A 235 ? 0.2720 0.3058 0.2208 -0.0374 -0.0181 -0.0167 317 GLN A NE2 1857 N N . TYR A 236 ? 0.2645 0.3087 0.2263 -0.0321 -0.0200 -0.0105 318 TYR A N 1858 C CA . TYR A 236 ? 0.2387 0.2819 0.2011 -0.0292 -0.0194 -0.0089 318 TYR A CA 1859 C C . TYR A 236 ? 0.3221 0.3612 0.2808 -0.0292 -0.0183 -0.0100 318 TYR A C 1860 O O . TYR A 236 ? 0.2585 0.2963 0.2140 -0.0313 -0.0182 -0.0118 318 TYR A O 1861 C CB . TYR A 236 ? 0.2604 0.3089 0.2240 -0.0280 -0.0209 -0.0070 318 TYR A CB 1862 C CG . TYR A 236 ? 0.2258 0.2781 0.1936 -0.0270 -0.0217 -0.0055 318 TYR A CG 1863 C CD1 . TYR A 236 ? 0.2579 0.3144 0.2269 -0.0289 -0.0229 -0.0059 318 TYR A CD1 1864 C CD2 . TYR A 236 ? 0.2959 0.3477 0.2664 -0.0243 -0.0212 -0.0038 318 TYR A CD2 1865 C CE1 . TYR A 236 ? 0.2710 0.3312 0.2438 -0.0278 -0.0236 -0.0046 318 TYR A CE1 1866 C CE2 . TYR A 236 ? 0.2450 0.3001 0.2192 -0.0232 -0.0218 -0.0026 318 TYR A CE2 1867 C CZ . TYR A 236 ? 0.2883 0.3478 0.2637 -0.0249 -0.0230 -0.0030 318 TYR A CZ 1868 O OH . TYR A 236 ? 0.2939 0.3570 0.2730 -0.0238 -0.0235 -0.0018 318 TYR A OH 1869 N N . ILE A 237 ? 0.2709 0.3080 0.2301 -0.0269 -0.0172 -0.0089 319 ILE A N 1870 C CA . ILE A 237 ? 0.2661 0.3004 0.2219 -0.0266 -0.0162 -0.0096 319 ILE A CA 1871 C C . ILE A 237 ? 0.2375 0.2758 0.1913 -0.0271 -0.0175 -0.0090 319 ILE A C 1872 O O . ILE A 237 ? 0.2638 0.3055 0.2194 -0.0257 -0.0185 -0.0069 319 ILE A O 1873 C CB . ILE A 237 ? 0.2795 0.3115 0.2367 -0.0240 -0.0149 -0.0084 319 ILE A CB 1874 C CG1 . ILE A 237 ? 0.2818 0.3104 0.2411 -0.0235 -0.0138 -0.0089 319 ILE A CG1 1875 C CG2 . ILE A 237 ? 0.2295 0.2593 0.1834 -0.0237 -0.0138 -0.0089 319 ILE A CG2 1876 C CD1 . ILE A 237 ? 0.2619 0.2888 0.2232 -0.0211 -0.0127 -0.0076 319 ILE A CD1 1877 N N . CYS A 238 ? 0.2306 0.2681 0.1804 -0.0290 -0.0176 -0.0107 320 CYS A N 1878 C CA . CYS A 238 ? 0.2776 0.3192 0.2251 -0.0298 -0.0190 -0.0104 320 CYS A CA 1879 C C . CYS A 238 ? 0.2567 0.2986 0.2033 -0.0276 -0.0186 -0.0086 320 CYS A C 1880 O O . CYS A 238 ? 0.3036 0.3497 0.2498 -0.0273 -0.0199 -0.0071 320 CYS A O 1881 C CB . CYS A 238 ? 0.2171 0.2572 0.1600 -0.0324 -0.0190 -0.0129 320 CYS A CB 1882 S SG . CYS A 238 ? 0.3679 0.4080 0.3107 -0.0358 -0.0197 -0.0151 320 CYS A SG 1883 N N . SER A 239 ? 0.3167 0.3546 0.2633 -0.0262 -0.0168 -0.0087 321 SER A N 1884 C CA . SER A 239 ? 0.2449 0.2826 0.1902 -0.0245 -0.0160 -0.0073 321 SER A CA 1885 C C . SER A 239 ? 0.2587 0.3000 0.2065 -0.0228 -0.0171 -0.0044 321 SER A C 1886 O O . SER A 239 ? 0.3162 0.3586 0.2678 -0.0219 -0.0176 -0.0034 321 SER A O 1887 C CB . SER A 239 ? 0.2871 0.3202 0.2330 -0.0231 -0.0139 -0.0076 321 SER A CB 1888 O OG . SER A 239 ? 0.2663 0.2994 0.2111 -0.0217 -0.0131 -0.0063 321 SER A OG 1889 N N . PRO A 240 ? 0.2787 0.3217 0.2242 -0.0222 -0.0173 -0.0032 322 PRO A N 1890 C CA . PRO A 240 ? 0.2357 0.2812 0.1831 -0.0203 -0.0181 -0.0003 322 PRO A CA 1891 C C . PRO A 240 ? 0.2798 0.3223 0.2293 -0.0183 -0.0165 0.0009 322 PRO A C 1892 O O . PRO A 240 ? 0.2518 0.2956 0.2032 -0.0167 -0.0168 0.0033 322 PRO A O 1893 C CB . PRO A 240 ? 0.2868 0.3345 0.2302 -0.0206 -0.0186 0.0003 322 PRO A CB 1894 C CG . PRO A 240 ? 0.3096 0.3543 0.2492 -0.0220 -0.0173 -0.0021 322 PRO A CG 1895 C CD . PRO A 240 ? 0.2662 0.3090 0.2068 -0.0235 -0.0172 -0.0045 322 PRO A CD 1896 N N . VAL A 241 ? 0.2629 0.3016 0.2123 -0.0185 -0.0148 -0.0006 323 VAL A N 1897 C CA . VAL A 241 ? 0.2989 0.3351 0.2510 -0.0168 -0.0134 0.0003 323 VAL A CA 1898 C C . VAL A 241 ? 0.2801 0.3163 0.2363 -0.0164 -0.0140 0.0005 323 VAL A C 1899 O O . VAL A 241 ? 0.2711 0.3055 0.2281 -0.0171 -0.0136 -0.0011 323 VAL A O 1900 C CB . VAL A 241 ? 0.3171 0.3496 0.2678 -0.0170 -0.0114 -0.0013 323 VAL A CB 1901 C CG1 . VAL A 241 ? 0.3188 0.3492 0.2725 -0.0154 -0.0102 -0.0004 323 VAL A CG1 1902 C CG2 . VAL A 241 ? 0.2688 0.3013 0.2153 -0.0174 -0.0108 -0.0016 323 VAL A CG2 1903 N N . LEU A 242 ? 0.2341 0.2725 0.1927 -0.0151 -0.0149 0.0026 324 LEU A N 1904 C CA . LEU A 242 ? 0.2571 0.2962 0.2193 -0.0147 -0.0156 0.0029 324 LEU A CA 1905 C C . LEU A 242 ? 0.2793 0.3153 0.2441 -0.0136 -0.0142 0.0030 324 LEU A C 1906 O O . LEU A 242 ? 0.2406 0.2751 0.2054 -0.0126 -0.0132 0.0040 324 LEU A O 1907 C CB . LEU A 242 ? 0.2763 0.3187 0.2398 -0.0136 -0.0170 0.0051 324 LEU A CB 1908 C CG . LEU A 242 ? 0.3102 0.3564 0.2713 -0.0144 -0.0185 0.0054 324 LEU A CG 1909 C CD1 . LEU A 242 ? 0.2819 0.3314 0.2448 -0.0129 -0.0198 0.0077 324 LEU A CD1 1910 C CD2 . LEU A 242 ? 0.3176 0.3651 0.2780 -0.0165 -0.0192 0.0032 324 LEU A CD2 1911 N N . THR A 243 ? 0.2822 0.3175 0.2492 -0.0138 -0.0142 0.0020 325 THR A N 1912 C CA . THR A 243 ? 0.2431 0.2755 0.2122 -0.0131 -0.0130 0.0017 325 THR A CA 1913 C C . THR A 243 ? 0.2484 0.2811 0.2211 -0.0122 -0.0133 0.0023 325 THR A C 1914 O O . THR A 243 ? 0.2304 0.2608 0.2046 -0.0117 -0.0124 0.0018 325 THR A O 1915 C CB . THR A 243 ? 0.2433 0.2730 0.2109 -0.0141 -0.0120 -0.0004 325 THR A CB 1916 O OG1 . THR A 243 ? 0.1973 0.2278 0.1648 -0.0155 -0.0127 -0.0017 325 THR A OG1 1917 C CG2 . THR A 243 ? 0.2112 0.2401 0.1754 -0.0146 -0.0112 -0.0010 325 THR A CG2 1918 N N . ASP A 244 ? 0.2865 0.3219 0.2604 -0.0118 -0.0146 0.0033 326 ASP A N 1919 C CA . ASP A 244 ? 0.2708 0.3065 0.2479 -0.0108 -0.0148 0.0039 326 ASP A CA 1920 C C . ASP A 244 ? 0.2842 0.3191 0.2621 -0.0091 -0.0144 0.0058 326 ASP A C 1921 O O . ASP A 244 ? 0.2793 0.3136 0.2553 -0.0090 -0.0140 0.0065 326 ASP A O 1922 C CB . ASP A 244 ? 0.2667 0.3059 0.2450 -0.0110 -0.0161 0.0040 326 ASP A CB 1923 C CG . ASP A 244 ? 0.3349 0.3741 0.3163 -0.0102 -0.0161 0.0040 326 ASP A CG 1924 O OD1 . ASP A 244 ? 0.3634 0.4002 0.3462 -0.0092 -0.0152 0.0043 326 ASP A OD1 1925 O OD2 . ASP A 244 ? 0.3736 0.4155 0.3561 -0.0107 -0.0169 0.0037 326 ASP A OD2 1926 N N . ASN A 245 ? 0.2318 0.2665 0.2125 -0.0079 -0.0144 0.0064 327 ASN A N 1927 C CA . ASN A 245 ? 0.2999 0.3335 0.2815 -0.0064 -0.0141 0.0081 327 ASN A CA 1928 C C . ASN A 245 ? 0.2620 0.2966 0.2462 -0.0052 -0.0147 0.0087 327 ASN A C 1929 O O . ASN A 245 ? 0.2400 0.2745 0.2259 -0.0054 -0.0145 0.0076 327 ASN A O 1930 C CB . ASN A 245 ? 0.2164 0.2467 0.1983 -0.0064 -0.0127 0.0078 327 ASN A CB 1931 C CG . ASN A 245 ? 0.2435 0.2724 0.2265 -0.0052 -0.0123 0.0094 327 ASN A CG 1932 O OD1 . ASN A 245 ? 0.2723 0.3003 0.2575 -0.0044 -0.0123 0.0094 327 ASN A OD1 1933 N ND2 . ASN A 245 ? 0.2699 0.2984 0.2512 -0.0050 -0.0121 0.0107 327 ASN A ND2 1934 N N . PRO A 246 ? 0.2402 0.2759 0.2246 -0.0039 -0.0152 0.0105 328 PRO A N 1935 C CA . PRO A 246 ? 0.2818 0.3179 0.2641 -0.0035 -0.0155 0.0121 328 PRO A CA 1936 C C . PRO A 246 ? 0.3484 0.3878 0.3286 -0.0046 -0.0165 0.0118 328 PRO A C 1937 O O . PRO A 246 ? 0.2845 0.3258 0.2653 -0.0055 -0.0171 0.0105 328 PRO A O 1938 C CB . PRO A 246 ? 0.3322 0.3688 0.3160 -0.0015 -0.0159 0.0140 328 PRO A CB 1939 C CG . PRO A 246 ? 0.2982 0.3364 0.2844 -0.0011 -0.0164 0.0132 328 PRO A CG 1940 C CD . PRO A 246 ? 0.3261 0.3625 0.3130 -0.0023 -0.0156 0.0112 328 PRO A CD 1941 N N . ARG A 247 ? 0.2888 0.3287 0.2666 -0.0046 -0.0167 0.0129 329 ARG A N 1942 C CA . ARG A 247 ? 0.2479 0.2906 0.2232 -0.0059 -0.0176 0.0124 329 ARG A CA 1943 C C . ARG A 247 ? 0.3301 0.3740 0.3031 -0.0052 -0.0180 0.0144 329 ARG A C 1944 O O . ARG A 247 ? 0.2630 0.3044 0.2356 -0.0043 -0.0172 0.0158 329 ARG A O 1945 C CB . ARG A 247 ? 0.2332 0.2742 0.2067 -0.0077 -0.0167 0.0103 329 ARG A CB 1946 C CG . ARG A 247 ? 0.2672 0.3050 0.2393 -0.0076 -0.0153 0.0106 329 ARG A CG 1947 C CD . ARG A 247 ? 0.2950 0.3315 0.2649 -0.0092 -0.0145 0.0087 329 ARG A CD 1948 N NE . ARG A 247 ? 0.2408 0.2750 0.2094 -0.0091 -0.0131 0.0091 329 ARG A NE 1949 C CZ . ARG A 247 ? 0.2394 0.2710 0.2095 -0.0088 -0.0118 0.0087 329 ARG A CZ 1950 N NH1 . ARG A 247 ? 0.2024 0.2331 0.1751 -0.0087 -0.0117 0.0078 329 ARG A NH1 1951 N NH2 . ARG A 247 ? 0.2597 0.2898 0.2286 -0.0088 -0.0105 0.0092 329 ARG A NH2 1952 N N . PRO A 248 ? 0.2920 0.3396 0.2632 -0.0059 -0.0194 0.0145 330 PRO A N 1953 C CA . PRO A 248 ? 0.3098 0.3586 0.2782 -0.0055 -0.0198 0.0162 330 PRO A CA 1954 C C . PRO A 248 ? 0.3088 0.3552 0.2742 -0.0067 -0.0186 0.0155 330 PRO A C 1955 O O . PRO A 248 ? 0.3022 0.3464 0.2677 -0.0078 -0.0176 0.0135 330 PRO A O 1956 C CB . PRO A 248 ? 0.3411 0.3949 0.3084 -0.0064 -0.0216 0.0159 330 PRO A CB 1957 C CG . PRO A 248 ? 0.3294 0.3847 0.2997 -0.0066 -0.0222 0.0146 330 PRO A CG 1958 C CD . PRO A 248 ? 0.2839 0.3350 0.2556 -0.0071 -0.0206 0.0131 330 PRO A CD 1959 N N . ASN A 249 ? 0.3363 0.3832 0.2989 -0.0063 -0.0187 0.0171 331 ASN A N 1960 C CA . ASN A 249 ? 0.3410 0.3862 0.3005 -0.0075 -0.0176 0.0164 331 ASN A CA 1961 C C . ASN A 249 ? 0.2730 0.3200 0.2301 -0.0094 -0.0181 0.0141 331 ASN A C 1962 O O . ASN A 249 ? 0.2482 0.2985 0.2055 -0.0099 -0.0196 0.0136 331 ASN A O 1963 C CB . ASN A 249 ? 0.3550 0.4004 0.3120 -0.0066 -0.0175 0.0189 331 ASN A CB 1964 C CG . ASN A 249 ? 0.4067 0.4491 0.3655 -0.0050 -0.0164 0.0209 331 ASN A CG 1965 O OD1 . ASN A 249 ? 0.4191 0.4584 0.3797 -0.0052 -0.0150 0.0200 331 ASN A OD1 1966 N ND2 . ASN A 249 ? 0.3677 0.4109 0.3261 -0.0035 -0.0171 0.0236 331 ASN A ND2 1967 N N . ASP A 250 ? 0.2724 0.3172 0.2274 -0.0106 -0.0167 0.0125 332 ASP A N 1968 C CA . ASP A 250 ? 0.3268 0.3724 0.2792 -0.0125 -0.0170 0.0101 332 ASP A CA 1969 C C . ASP A 250 ? 0.3533 0.4024 0.3022 -0.0131 -0.0183 0.0108 332 ASP A C 1970 O O . ASP A 250 ? 0.3456 0.3946 0.2918 -0.0127 -0.0179 0.0121 332 ASP A O 1971 C CB . ASP A 250 ? 0.3116 0.3539 0.2623 -0.0133 -0.0151 0.0084 332 ASP A CB 1972 C CG . ASP A 250 ? 0.3710 0.4102 0.3248 -0.0130 -0.0139 0.0073 332 ASP A CG 1973 O OD1 . ASP A 250 ? 0.2715 0.3112 0.2285 -0.0126 -0.0146 0.0073 332 ASP A OD1 1974 O OD2 . ASP A 250 ? 0.3041 0.3406 0.2572 -0.0130 -0.0122 0.0065 332 ASP A OD2 1975 N N . PRO A 251 ? 0.2767 0.3291 0.2254 -0.0142 -0.0200 0.0098 333 PRO A N 1976 C CA . PRO A 251 ? 0.2367 0.2928 0.1819 -0.0151 -0.0214 0.0100 333 PRO A CA 1977 C C . PRO A 251 ? 0.2648 0.3194 0.2061 -0.0171 -0.0206 0.0074 333 PRO A C 1978 O O . PRO A 251 ? 0.2774 0.3280 0.2187 -0.0173 -0.0188 0.0061 333 PRO A O 1979 C CB . PRO A 251 ? 0.2233 0.2833 0.1707 -0.0157 -0.0234 0.0096 333 PRO A CB 1980 C CG . PRO A 251 ? 0.2949 0.3521 0.2450 -0.0164 -0.0225 0.0076 333 PRO A CG 1981 C CD . PRO A 251 ? 0.2273 0.2802 0.1791 -0.0147 -0.0206 0.0084 333 PRO A CD 1982 N N . ASN A 252 ? 0.3019 0.3596 0.2398 -0.0186 -0.0219 0.0067 334 ASN A N 1983 C CA . ASN A 252 ? 0.2830 0.3392 0.2168 -0.0206 -0.0212 0.0041 334 ASN A CA 1984 C C . ASN A 252 ? 0.3232 0.3804 0.2569 -0.0229 -0.0221 0.0014 334 ASN A C 1985 O O . ASN A 252 ? 0.3494 0.4046 0.2799 -0.0247 -0.0214 -0.0012 334 ASN A O 1986 C CB . ASN A 252 ? 0.3343 0.3927 0.2633 -0.0209 -0.0216 0.0049 334 ASN A CB 1987 C CG . ASN A 252 ? 0.4089 0.4654 0.3373 -0.0191 -0.0201 0.0071 334 ASN A CG 1988 O OD1 . ASN A 252 ? 0.3487 0.4015 0.2793 -0.0181 -0.0183 0.0072 334 ASN A OD1 1989 N ND2 . ASN A 252 ? 0.3508 0.4099 0.2759 -0.0188 -0.0208 0.0088 334 ASN A ND2 1990 N N . ILE A 253 ? 0.3482 0.4085 0.2852 -0.0229 -0.0237 0.0020 335 ILE A N 1991 C CA . ILE A 253 ? 0.2994 0.3606 0.2370 -0.0251 -0.0245 -0.0003 335 ILE A CA 1992 C C . ILE A 253 ? 0.3315 0.3919 0.2742 -0.0242 -0.0244 0.0001 335 ILE A C 1993 O O . ILE A 253 ? 0.3246 0.3877 0.2705 -0.0224 -0.0253 0.0024 335 ILE A O 1994 C CB . ILE A 253 ? 0.3345 0.4016 0.2707 -0.0266 -0.0270 -0.0002 335 ILE A CB 1995 C CG1 . ILE A 253 ? 0.3636 0.4319 0.2945 -0.0274 -0.0273 -0.0004 335 ILE A CG1 1996 C CG2 . ILE A 253 ? 0.2934 0.3612 0.2302 -0.0292 -0.0277 -0.0028 335 ILE A CG2 1997 C CD1 . ILE A 253 ? 0.3983 0.4729 0.3277 -0.0288 -0.0298 -0.0001 335 ILE A CD1 1998 N N . GLY A 254 ? 0.2888 0.3454 0.2321 -0.0253 -0.0232 -0.0021 336 GLY A N 1999 C CA . GLY A 254 ? 0.2714 0.3272 0.2193 -0.0246 -0.0230 -0.0019 336 GLY A CA 2000 C C . GLY A 254 ? 0.3427 0.4020 0.2919 -0.0264 -0.0245 -0.0029 336 GLY A C 2001 O O . GLY A 254 ? 0.2987 0.3619 0.2458 -0.0279 -0.0261 -0.0032 336 GLY A O 2002 N N . LYS A 255 ? 0.3366 0.3947 0.2891 -0.0265 -0.0242 -0.0034 337 LYS A N 2003 C CA . LYS A 255 ? 0.3108 0.3723 0.2649 -0.0284 -0.0255 -0.0043 337 LYS A CA 2004 C C . LYS A 255 ? 0.3333 0.3908 0.2880 -0.0299 -0.0243 -0.0064 337 LYS A C 2005 O O . LYS A 255 ? 0.2924 0.3464 0.2493 -0.0284 -0.0229 -0.0061 337 LYS A O 2006 C CB . LYS A 255 ? 0.3385 0.4046 0.2969 -0.0267 -0.0267 -0.0020 337 LYS A CB 2007 C CG . LYS A 255 ? 0.3220 0.3933 0.2799 -0.0256 -0.0283 0.0001 337 LYS A CG 2008 C CD . LYS A 255 ? 0.4358 0.5126 0.3925 -0.0280 -0.0303 -0.0007 337 LYS A CD 2009 C CE . LYS A 255 ? 0.4418 0.5240 0.4028 -0.0274 -0.0317 0.0005 337 LYS A CE 2010 N NZ . LYS A 255 ? 0.4586 0.5463 0.4190 -0.0303 -0.0335 -0.0006 337 LYS A NZ 2011 N N . CYS A 256 ? 0.2752 0.3329 0.2277 -0.0329 -0.0248 -0.0086 338 CYS A N 2012 C CA . CYS A 256 ? 0.3187 0.3721 0.2711 -0.0346 -0.0236 -0.0107 338 CYS A CA 2013 C C . CYS A 256 ? 0.2950 0.3507 0.2513 -0.0353 -0.0242 -0.0105 338 CYS A C 2014 O O . CYS A 256 ? 0.3320 0.3838 0.2895 -0.0354 -0.0229 -0.0112 338 CYS A O 2015 C CB . CYS A 256 ? 0.2555 0.3075 0.2035 -0.0378 -0.0237 -0.0133 338 CYS A CB 2016 S SG . CYS A 256 ? 0.4468 0.4957 0.3895 -0.0374 -0.0228 -0.0142 338 CYS A SG 2017 N N . ASN A 257 ? 0.3037 0.3658 0.2619 -0.0356 -0.0260 -0.0094 339 ASN A N 2018 C CA . ASN A 257 ? 0.2937 0.3586 0.2550 -0.0369 -0.0266 -0.0095 339 ASN A CA 2019 C C . ASN A 257 ? 0.2498 0.3201 0.2155 -0.0347 -0.0276 -0.0071 339 ASN A C 2020 O O . ASN A 257 ? 0.2903 0.3646 0.2587 -0.0357 -0.0284 -0.0070 339 ASN A O 2021 C CB . ASN A 257 ? 0.2793 0.3471 0.2386 -0.0407 -0.0279 -0.0114 339 ASN A CB 2022 C CG . ASN A 257 ? 0.3651 0.4270 0.3205 -0.0431 -0.0267 -0.0140 339 ASN A CG 2023 O OD1 . ASN A 257 ? 0.4632 0.5201 0.4192 -0.0433 -0.0251 -0.0149 339 ASN A OD1 2024 N ND2 . ASN A 257 ? 0.3589 0.4211 0.3102 -0.0449 -0.0273 -0.0153 339 ASN A ND2 2025 N N . ASP A 258 ? 0.3153 0.3854 0.2816 -0.0316 -0.0275 -0.0052 340 ASP A N 2026 C CA . ASP A 258 ? 0.3004 0.3745 0.2706 -0.0290 -0.0281 -0.0028 340 ASP A CA 2027 C C . ASP A 258 ? 0.3062 0.3766 0.2768 -0.0259 -0.0269 -0.0013 340 ASP A C 2028 O O . ASP A 258 ? 0.3175 0.3839 0.2852 -0.0258 -0.0260 -0.0018 340 ASP A O 2029 C CB . ASP A 258 ? 0.3187 0.3999 0.2892 -0.0291 -0.0302 -0.0016 340 ASP A CB 2030 C CG . ASP A 258 ? 0.3805 0.4672 0.3536 -0.0310 -0.0314 -0.0021 340 ASP A CG 2031 O OD1 . ASP A 258 ? 0.3076 0.3940 0.2840 -0.0306 -0.0307 -0.0020 340 ASP A OD1 2032 O OD2 . ASP A 258 ? 0.4073 0.4986 0.3790 -0.0331 -0.0330 -0.0026 340 ASP A OD2 2033 N N . PRO A 259 ? 0.3125 0.3842 0.2867 -0.0234 -0.0269 0.0005 341 PRO A N 2034 C CA . PRO A 259 ? 0.3195 0.3881 0.2943 -0.0206 -0.0259 0.0020 341 PRO A CA 2035 C C . PRO A 259 ? 0.3407 0.4104 0.3133 -0.0194 -0.0265 0.0035 341 PRO A C 2036 O O . PRO A 259 ? 0.3262 0.4012 0.2988 -0.0193 -0.0281 0.0045 341 PRO A O 2037 C CB . PRO A 259 ? 0.2691 0.3401 0.2481 -0.0185 -0.0261 0.0034 341 PRO A CB 2038 C CG . PRO A 259 ? 0.2881 0.3652 0.2686 -0.0198 -0.0276 0.0033 341 PRO A CG 2039 C CD . PRO A 259 ? 0.2436 0.3196 0.2216 -0.0233 -0.0276 0.0010 341 PRO A CD 2040 N N . TYR A 260 ? 0.3187 0.3839 0.2893 -0.0184 -0.0253 0.0037 342 TYR A N 2041 C CA . TYR A 260 ? 0.2743 0.3404 0.2432 -0.0168 -0.0257 0.0056 342 TYR A CA 2042 C C . TYR A 260 ? 0.2918 0.3589 0.2640 -0.0139 -0.0258 0.0080 342 TYR A C 2043 O O . TYR A 260 ? 0.2600 0.3237 0.2342 -0.0127 -0.0246 0.0080 342 TYR A O 2044 C CB . TYR A 260 ? 0.3304 0.3917 0.2962 -0.0169 -0.0243 0.0051 342 TYR A CB 2045 C CG . TYR A 260 ? 0.3397 0.4026 0.3031 -0.0160 -0.0249 0.0068 342 TYR A CG 2046 C CD1 . TYR A 260 ? 0.2993 0.3611 0.2637 -0.0134 -0.0244 0.0092 342 TYR A CD1 2047 C CD2 . TYR A 260 ? 0.3657 0.4310 0.3256 -0.0177 -0.0259 0.0061 342 TYR A CD2 2048 C CE1 . TYR A 260 ? 0.3727 0.4358 0.3347 -0.0126 -0.0249 0.0110 342 TYR A CE1 2049 C CE2 . TYR A 260 ? 0.3734 0.4403 0.3308 -0.0168 -0.0264 0.0079 342 TYR A CE2 2050 C CZ . TYR A 260 ? 0.4016 0.4674 0.3602 -0.0142 -0.0259 0.0104 342 TYR A CZ 2051 O OH . TYR A 260 ? 0.4970 0.5642 0.4530 -0.0133 -0.0264 0.0123 342 TYR A OH 2052 N N . PRO A 261 ? 0.2977 0.3693 0.2701 -0.0127 -0.0272 0.0099 343 PRO A N 2053 C CA . PRO A 261 ? 0.3004 0.3735 0.2761 -0.0099 -0.0275 0.0122 343 PRO A CA 2054 C C . PRO A 261 ? 0.3013 0.3707 0.2763 -0.0076 -0.0266 0.0141 343 PRO A C 2055 O O . PRO A 261 ? 0.2893 0.3565 0.2611 -0.0081 -0.0261 0.0142 343 PRO A O 2056 C CB . PRO A 261 ? 0.3107 0.3904 0.2865 -0.0097 -0.0295 0.0134 343 PRO A CB 2057 C CG . PRO A 261 ? 0.3589 0.4393 0.3305 -0.0116 -0.0302 0.0127 343 PRO A CG 2058 C CD . PRO A 261 ? 0.2555 0.3312 0.2252 -0.0140 -0.0288 0.0100 343 PRO A CD 2059 N N . GLY A 262 ? 0.3225 0.3914 0.3004 -0.0051 -0.0262 0.0156 344 GLY A N 2060 C CA . GLY A 262 ? 0.3139 0.3794 0.2914 -0.0030 -0.0254 0.0176 344 GLY A CA 2061 C C . GLY A 262 ? 0.3560 0.4181 0.3366 -0.0014 -0.0242 0.0177 344 GLY A C 2062 O O . GLY A 262 ? 0.3539 0.4149 0.3354 0.0010 -0.0240 0.0197 344 GLY A O 2063 N N . ASN A 263 ? 0.2967 0.3569 0.2784 -0.0027 -0.0234 0.0156 345 ASN A N 2064 C CA . ASN A 263 ? 0.3499 0.4071 0.3343 -0.0015 -0.0223 0.0154 345 ASN A CA 2065 C C . ASN A 263 ? 0.2842 0.3438 0.2710 -0.0023 -0.0226 0.0139 345 ASN A C 2066 O O . ASN A 263 ? 0.3552 0.4151 0.3412 -0.0046 -0.0226 0.0120 345 ASN A O 2067 C CB . ASN A 263 ? 0.2827 0.3345 0.2661 -0.0022 -0.0207 0.0144 345 ASN A CB 2068 C CG . ASN A 263 ? 0.3513 0.4007 0.3325 -0.0015 -0.0202 0.0160 345 ASN A CG 2069 O OD1 . ASN A 263 ? 0.3962 0.4462 0.3745 -0.0026 -0.0204 0.0160 345 ASN A OD1 2070 N ND2 . ASN A 263 ? 0.3362 0.3826 0.3186 0.0002 -0.0194 0.0173 345 ASN A ND2 2071 N N . ASN A 264 ? 0.3127 0.3740 0.3024 -0.0004 -0.0227 0.0148 346 ASN A N 2072 C CA . ASN A 264 ? 0.4113 0.4753 0.4036 -0.0009 -0.0230 0.0136 346 ASN A CA 2073 C C . ASN A 264 ? 0.3954 0.4558 0.3896 -0.0001 -0.0216 0.0128 346 ASN A C 2074 O O . ASN A 264 ? 0.3540 0.4107 0.3483 0.0015 -0.0208 0.0137 346 ASN A O 2075 C CB . ASN A 264 ? 0.4444 0.5141 0.4387 0.0006 -0.0242 0.0150 346 ASN A CB 2076 C CG . ASN A 264 ? 0.5640 0.6381 0.5564 -0.0003 -0.0258 0.0157 346 ASN A CG 2077 O OD1 . ASN A 264 ? 0.4933 0.5681 0.4838 -0.0030 -0.0262 0.0142 346 ASN A OD1 2078 N ND2 . ASN A 264 ? 0.6469 0.7238 0.6397 0.0019 -0.0267 0.0179 346 ASN A ND2 2079 N N . ASN A 265 ? 0.3446 0.4059 0.3401 -0.0014 -0.0214 0.0112 347 ASN A N 2080 C CA . ASN A 265 ? 0.2596 0.3185 0.2571 -0.0006 -0.0203 0.0106 347 ASN A CA 2081 C C . ASN A 265 ? 0.2871 0.3402 0.2836 -0.0004 -0.0190 0.0102 347 ASN A C 2082 O O . ASN A 265 ? 0.2576 0.3084 0.2554 0.0013 -0.0183 0.0106 347 ASN A O 2083 C CB . ASN A 265 ? 0.3037 0.3648 0.3038 0.0021 -0.0205 0.0119 347 ASN A CB 2084 C CG . ASN A 265 ? 0.4382 0.5058 0.4399 0.0020 -0.0217 0.0123 347 ASN A CG 2085 O OD1 . ASN A 265 ? 0.3858 0.4561 0.3872 -0.0003 -0.0222 0.0111 347 ASN A OD1 2086 N ND2 . ASN A 265 ? 0.4541 0.5243 0.4575 0.0046 -0.0221 0.0140 347 ASN A ND2 2087 N N . ASN A 266 ? 0.2550 0.3058 0.2492 -0.0021 -0.0187 0.0094 348 ASN A N 2088 C CA . ASN A 266 ? 0.4054 0.4513 0.3989 -0.0022 -0.0175 0.0089 348 ASN A CA 2089 C C . ASN A 266 ? 0.4322 0.4767 0.4234 -0.0044 -0.0173 0.0076 348 ASN A C 2090 O O . ASN A 266 ? 0.3161 0.3631 0.3062 -0.0058 -0.0180 0.0071 348 ASN A O 2091 C CB . ASN A 266 ? 0.3364 0.3799 0.3293 -0.0006 -0.0172 0.0105 348 ASN A CB 2092 C CG . ASN A 266 ? 0.5265 0.5722 0.5178 -0.0002 -0.0181 0.0121 348 ASN A CG 2093 O OD1 . ASN A 266 ? 0.5430 0.5908 0.5326 -0.0017 -0.0188 0.0116 348 ASN A OD1 2094 N ND2 . ASN A 266 ? 0.5904 0.6356 0.5821 0.0018 -0.0182 0.0139 348 ASN A ND2 2095 N N . GLY A 267 ? 0.3118 0.3525 0.3024 -0.0047 -0.0162 0.0070 349 GLY A N 2096 C CA . GLY A 267 ? 0.2981 0.3373 0.2866 -0.0064 -0.0158 0.0058 349 GLY A CA 2097 C C . GLY A 267 ? 0.2946 0.3303 0.2836 -0.0065 -0.0146 0.0049 349 GLY A C 2098 O O . GLY A 267 ? 0.2504 0.2851 0.2412 -0.0055 -0.0143 0.0051 349 GLY A O 2099 N N . VAL A 268 ? 0.1961 0.2300 0.1833 -0.0077 -0.0141 0.0039 350 VAL A N 2100 C CA . VAL A 268 ? 0.2332 0.2642 0.2208 -0.0078 -0.0130 0.0031 350 VAL A CA 2101 C C . VAL A 268 ? 0.2333 0.2637 0.2197 -0.0093 -0.0128 0.0016 350 VAL A C 2102 O O . VAL A 268 ? 0.2602 0.2914 0.2446 -0.0103 -0.0131 0.0012 350 VAL A O 2103 C CB . VAL A 268 ? 0.2097 0.2385 0.1967 -0.0073 -0.0122 0.0037 350 VAL A CB 2104 C CG1 . VAL A 268 ? 0.2030 0.2313 0.1874 -0.0083 -0.0119 0.0033 350 VAL A CG1 2105 C CG2 . VAL A 268 ? 0.1766 0.2032 0.1650 -0.0070 -0.0114 0.0032 350 VAL A CG2 2106 N N . LYS A 269 ? 0.2559 0.2847 0.2432 -0.0094 -0.0122 0.0008 351 LYS A N 2107 C CA . LYS A 269 ? 0.2724 0.2999 0.2584 -0.0105 -0.0118 -0.0005 351 LYS A CA 2108 C C . LYS A 269 ? 0.2694 0.2950 0.2534 -0.0107 -0.0110 -0.0007 351 LYS A C 2109 O O . LYS A 269 ? 0.2075 0.2322 0.1921 -0.0098 -0.0105 -0.0001 351 LYS A O 2110 C CB . LYS A 269 ? 0.2247 0.2508 0.2121 -0.0104 -0.0112 -0.0011 351 LYS A CB 2111 C CG . LYS A 269 ? 0.2248 0.2489 0.2107 -0.0113 -0.0106 -0.0022 351 LYS A CG 2112 C CD . LYS A 269 ? 0.1984 0.2212 0.1855 -0.0109 -0.0102 -0.0025 351 LYS A CD 2113 C CE . LYS A 269 ? 0.2154 0.2356 0.2009 -0.0114 -0.0094 -0.0034 351 LYS A CE 2114 N NZ . LYS A 269 ? 0.2538 0.2739 0.2378 -0.0130 -0.0096 -0.0042 351 LYS A NZ 2115 N N . GLY A 270 ? 0.1956 0.2209 0.1775 -0.0119 -0.0110 -0.0016 352 GLY A N 2116 C CA . GLY A 270 ? 0.1841 0.2076 0.1638 -0.0120 -0.0102 -0.0020 352 GLY A CA 2117 C C . GLY A 270 ? 0.2590 0.2808 0.2366 -0.0132 -0.0098 -0.0035 352 GLY A C 2118 O O . GLY A 270 ? 0.2144 0.2359 0.1925 -0.0139 -0.0100 -0.0041 352 GLY A O 2119 N N . PHE A 271 ? 0.2224 0.2428 0.1977 -0.0134 -0.0091 -0.0041 353 PHE A N 2120 C CA . PHE A 271 ? 0.2286 0.2466 0.2017 -0.0143 -0.0084 -0.0056 353 PHE A CA 2121 C C . PHE A 271 ? 0.2344 0.2518 0.2044 -0.0149 -0.0081 -0.0062 353 PHE A C 2122 O O . PHE A 271 ? 0.2787 0.2976 0.2484 -0.0144 -0.0081 -0.0054 353 PHE A O 2123 C CB . PHE A 271 ? 0.2066 0.2221 0.1806 -0.0133 -0.0073 -0.0058 353 PHE A CB 2124 C CG . PHE A 271 ? 0.2513 0.2659 0.2246 -0.0123 -0.0062 -0.0057 353 PHE A CG 2125 C CD1 . PHE A 271 ? 0.2782 0.2943 0.2534 -0.0112 -0.0062 -0.0044 353 PHE A CD1 2126 C CD2 . PHE A 271 ? 0.2665 0.2790 0.2374 -0.0124 -0.0052 -0.0068 353 PHE A CD2 2127 C CE1 . PHE A 271 ? 0.2573 0.2730 0.2321 -0.0104 -0.0052 -0.0042 353 PHE A CE1 2128 C CE2 . PHE A 271 ? 0.2251 0.2372 0.1955 -0.0114 -0.0041 -0.0066 353 PHE A CE2 2129 C CZ . PHE A 271 ? 0.2801 0.2940 0.2525 -0.0105 -0.0041 -0.0053 353 PHE A CZ 2130 N N . SER A 272 ? 0.2396 0.2548 0.2072 -0.0159 -0.0075 -0.0077 354 SER A N 2131 C CA . SER A 272 ? 0.2660 0.2800 0.2304 -0.0163 -0.0068 -0.0086 354 SER A CA 2132 C C . SER A 272 ? 0.3112 0.3214 0.2738 -0.0167 -0.0057 -0.0103 354 SER A C 2133 O O . SER A 272 ? 0.2913 0.3001 0.2547 -0.0171 -0.0058 -0.0106 354 SER A O 2134 C CB . SER A 272 ? 0.2377 0.2539 0.2001 -0.0178 -0.0080 -0.0089 354 SER A CB 2135 O OG . SER A 272 ? 0.2837 0.2995 0.2452 -0.0196 -0.0086 -0.0100 354 SER A OG 2136 N N . TYR A 273 ? 0.2908 0.2991 0.2507 -0.0164 -0.0046 -0.0112 355 TYR A N 2137 C CA . TYR A 273 ? 0.2643 0.2687 0.2217 -0.0169 -0.0035 -0.0129 355 TYR A CA 2138 C C . TYR A 273 ? 0.3570 0.3611 0.3105 -0.0186 -0.0038 -0.0143 355 TYR A C 2139 O O . TYR A 273 ? 0.3150 0.3200 0.2668 -0.0183 -0.0033 -0.0143 355 TYR A O 2140 C CB . TYR A 273 ? 0.3018 0.3038 0.2592 -0.0150 -0.0018 -0.0130 355 TYR A CB 2141 C CG . TYR A 273 ? 0.2413 0.2427 0.2019 -0.0137 -0.0016 -0.0122 355 TYR A CG 2142 C CD1 . TYR A 273 ? 0.2460 0.2440 0.2060 -0.0138 -0.0011 -0.0130 355 TYR A CD1 2143 C CD2 . TYR A 273 ? 0.2092 0.2131 0.1730 -0.0124 -0.0018 -0.0106 355 TYR A CD2 2144 C CE1 . TYR A 273 ? 0.1796 0.1771 0.1422 -0.0126 -0.0009 -0.0122 355 TYR A CE1 2145 C CE2 . TYR A 273 ? 0.2460 0.2495 0.2124 -0.0113 -0.0017 -0.0100 355 TYR A CE2 2146 C CZ . TYR A 273 ? 0.2042 0.2047 0.1700 -0.0113 -0.0013 -0.0107 355 TYR A CZ 2147 O OH . TYR A 273 ? 0.2435 0.2437 0.2118 -0.0102 -0.0012 -0.0100 355 TYR A OH 2148 N N . LEU A 274 ? 0.2784 0.2817 0.2307 -0.0206 -0.0045 -0.0154 356 LEU A N 2149 C CA . LEU A 274 ? 0.3241 0.3277 0.2729 -0.0227 -0.0050 -0.0167 356 LEU A CA 2150 C C . LEU A 274 ? 0.3413 0.3400 0.2866 -0.0235 -0.0037 -0.0189 356 LEU A C 2151 O O . LEU A 274 ? 0.3206 0.3165 0.2657 -0.0246 -0.0036 -0.0197 356 LEU A O 2152 C CB . LEU A 274 ? 0.2868 0.2934 0.2366 -0.0247 -0.0068 -0.0165 356 LEU A CB 2153 C CG . LEU A 274 ? 0.3121 0.3233 0.2656 -0.0237 -0.0081 -0.0143 356 LEU A CG 2154 C CD1 . LEU A 274 ? 0.3111 0.3251 0.2661 -0.0254 -0.0096 -0.0141 356 LEU A CD1 2155 C CD2 . LEU A 274 ? 0.2303 0.2444 0.1830 -0.0230 -0.0085 -0.0134 356 LEU A CD2 2156 N N . ASP A 275 ? 0.3438 0.3410 0.2862 -0.0229 -0.0026 -0.0198 357 ASP A N 2157 C CA . ASP A 275 ? 0.3807 0.3727 0.3199 -0.0229 -0.0009 -0.0218 357 ASP A CA 2158 C C . ASP A 275 ? 0.3674 0.3589 0.3023 -0.0235 -0.0003 -0.0233 357 ASP A C 2159 O O . ASP A 275 ? 0.3352 0.3247 0.2689 -0.0218 0.0014 -0.0237 357 ASP A O 2160 C CB . ASP A 275 ? 0.3879 0.3776 0.3291 -0.0202 0.0007 -0.0211 357 ASP A CB 2161 C CG . ASP A 275 ? 0.3502 0.3340 0.2886 -0.0198 0.0025 -0.0230 357 ASP A CG 2162 O OD1 . ASP A 275 ? 0.4357 0.4166 0.3717 -0.0219 0.0023 -0.0245 357 ASP A OD1 2163 O OD2 . ASP A 275 ? 0.3993 0.3815 0.3379 -0.0175 0.0041 -0.0228 357 ASP A OD2 2164 N N . GLY A 276 ? 0.3906 0.3841 0.3233 -0.0259 -0.0016 -0.0241 358 GLY A N 2165 C CA . GLY A 276 ? 0.2889 0.2823 0.2172 -0.0267 -0.0013 -0.0255 358 GLY A CA 2166 C C . GLY A 276 ? 0.3142 0.3100 0.2429 -0.0246 -0.0005 -0.0242 358 GLY A C 2167 O O . GLY A 276 ? 0.3241 0.3241 0.2558 -0.0237 -0.0015 -0.0220 358 GLY A O 2168 N N . ALA A 277 ? 0.2894 0.2823 0.2149 -0.0237 0.0013 -0.0256 359 ALA A N 2169 C CA . ALA A 277 ? 0.3652 0.3602 0.2909 -0.0217 0.0023 -0.0245 359 ALA A CA 2170 C C . ALA A 277 ? 0.3676 0.3631 0.2978 -0.0191 0.0031 -0.0226 359 ALA A C 2171 O O . ALA A 277 ? 0.3605 0.3583 0.2917 -0.0176 0.0037 -0.0212 359 ALA A O 2172 C CB . ALA A 277 ? 0.3138 0.3058 0.2349 -0.0215 0.0042 -0.0266 359 ALA A CB 2173 N N . ASN A 278 ? 0.3471 0.3404 0.2798 -0.0188 0.0031 -0.0225 360 ASN A N 2174 C CA . ASN A 278 ? 0.3574 0.3512 0.2943 -0.0165 0.0037 -0.0208 360 ASN A CA 2175 C C . ASN A 278 ? 0.3553 0.3527 0.2963 -0.0168 0.0019 -0.0187 360 ASN A C 2176 O O . ASN A 278 ? 0.3464 0.3437 0.2908 -0.0155 0.0019 -0.0176 360 ASN A O 2177 C CB . ASN A 278 ? 0.3192 0.3083 0.2563 -0.0155 0.0050 -0.0218 360 ASN A CB 2178 C CG . ASN A 278 ? 0.3648 0.3544 0.3056 -0.0128 0.0060 -0.0203 360 ASN A CG 2179 O OD1 . ASN A 278 ? 0.3230 0.3149 0.2645 -0.0114 0.0068 -0.0194 360 ASN A OD1 2180 N ND2 . ASN A 278 ? 0.3286 0.3162 0.2716 -0.0122 0.0060 -0.0200 360 ASN A ND2 2181 N N . THR A 279 ? 0.2700 0.2706 0.2103 -0.0183 0.0002 -0.0182 361 THR A N 2182 C CA . THR A 279 ? 0.2747 0.2788 0.2186 -0.0185 -0.0015 -0.0163 361 THR A CA 2183 C C . THR A 279 ? 0.2771 0.2842 0.2238 -0.0168 -0.0014 -0.0141 361 THR A C 2184 O O . THR A 279 ? 0.2551 0.2636 0.2002 -0.0165 -0.0010 -0.0137 361 THR A O 2185 C CB . THR A 279 ? 0.2334 0.2401 0.1757 -0.0207 -0.0034 -0.0165 361 THR A CB 2186 O OG1 . THR A 279 ? 0.2663 0.2706 0.2069 -0.0226 -0.0036 -0.0184 361 THR A OG1 2187 C CG2 . THR A 279 ? 0.2570 0.2676 0.2030 -0.0206 -0.0050 -0.0144 361 THR A CG2 2188 N N . TRP A 280 ? 0.2949 0.3027 0.2456 -0.0159 -0.0018 -0.0128 362 TRP A N 2189 C CA . TRP A 280 ? 0.3090 0.3196 0.2626 -0.0146 -0.0020 -0.0107 362 TRP A CA 2190 C C . TRP A 280 ? 0.3127 0.3255 0.2693 -0.0149 -0.0037 -0.0094 362 TRP A C 2191 O O . TRP A 280 ? 0.2720 0.2839 0.2301 -0.0153 -0.0041 -0.0098 362 TRP A O 2192 C CB . TRP A 280 ? 0.3239 0.3332 0.2796 -0.0128 -0.0005 -0.0104 362 TRP A CB 2193 C CG . TRP A 280 ? 0.3511 0.3592 0.3046 -0.0119 0.0013 -0.0111 362 TRP A CG 2194 C CD1 . TRP A 280 ? 0.2863 0.2913 0.2367 -0.0121 0.0024 -0.0131 362 TRP A CD1 2195 C CD2 . TRP A 280 ? 0.2546 0.2644 0.2086 -0.0109 0.0022 -0.0100 362 TRP A CD2 2196 N NE1 . TRP A 280 ? 0.2183 0.2232 0.1673 -0.0110 0.0041 -0.0132 362 TRP A NE1 2197 C CE2 . TRP A 280 ? 0.2881 0.2962 0.2395 -0.0103 0.0040 -0.0113 362 TRP A CE2 2198 C CE3 . TRP A 280 ? 0.2995 0.3121 0.2560 -0.0104 0.0019 -0.0080 362 TRP A CE3 2199 C CZ2 . TRP A 280 ? 0.3083 0.3178 0.2596 -0.0093 0.0054 -0.0107 362 TRP A CZ2 2200 C CZ3 . TRP A 280 ? 0.3425 0.3562 0.2989 -0.0095 0.0032 -0.0074 362 TRP A CZ3 2201 C CH2 . TRP A 280 ? 0.2921 0.3045 0.2459 -0.0090 0.0049 -0.0087 362 TRP A CH2 2202 N N . LEU A 281 ? 0.2757 0.2914 0.2332 -0.0147 -0.0044 -0.0077 363 LEU A N 2203 C CA . LEU A 281 ? 0.2349 0.2529 0.1953 -0.0147 -0.0059 -0.0064 363 LEU A CA 2204 C C . LEU A 281 ? 0.2761 0.2949 0.2395 -0.0132 -0.0056 -0.0047 363 LEU A C 2205 O O . LEU A 281 ? 0.2453 0.2643 0.2081 -0.0126 -0.0047 -0.0040 363 LEU A O 2206 C CB . LEU A 281 ? 0.2363 0.2571 0.1951 -0.0157 -0.0074 -0.0058 363 LEU A CB 2207 C CG . LEU A 281 ? 0.3100 0.3307 0.2652 -0.0174 -0.0078 -0.0073 363 LEU A CG 2208 C CD1 . LEU A 281 ? 0.2109 0.2353 0.1653 -0.0180 -0.0094 -0.0063 363 LEU A CD1 2209 C CD2 . LEU A 281 ? 0.2278 0.2468 0.1829 -0.0186 -0.0080 -0.0090 363 LEU A CD2 2210 N N . GLY A 282 ? 0.2484 0.2675 0.2148 -0.0128 -0.0062 -0.0041 364 GLY A N 2211 C CA . GLY A 282 ? 0.2065 0.2264 0.1758 -0.0117 -0.0061 -0.0026 364 GLY A CA 2212 C C . GLY A 282 ? 0.2277 0.2499 0.1980 -0.0117 -0.0074 -0.0011 364 GLY A C 2213 O O . GLY A 282 ? 0.1965 0.2199 0.1667 -0.0124 -0.0086 -0.0013 364 GLY A O 2214 N N . ARG A 283 ? 0.2041 0.2269 0.1754 -0.0109 -0.0072 0.0004 365 ARG A N 2215 C CA . ARG A 283 ? 0.1911 0.2156 0.1638 -0.0105 -0.0083 0.0019 365 ARG A CA 2216 C C . ARG A 283 ? 0.2184 0.2425 0.1929 -0.0096 -0.0077 0.0034 365 ARG A C 2217 O O . ARG A 283 ? 0.2325 0.2556 0.2067 -0.0094 -0.0065 0.0034 365 ARG A O 2218 C CB . ARG A 283 ? 0.2108 0.2372 0.1810 -0.0110 -0.0091 0.0025 365 ARG A CB 2219 C CG . ARG A 283 ? 0.2038 0.2301 0.1716 -0.0109 -0.0083 0.0032 365 ARG A CG 2220 C CD . ARG A 283 ? 0.2984 0.3268 0.2637 -0.0114 -0.0094 0.0038 365 ARG A CD 2221 N NE . ARG A 283 ? 0.2933 0.3220 0.2561 -0.0114 -0.0087 0.0046 365 ARG A NE 2222 C CZ . ARG A 283 ? 0.2734 0.3041 0.2336 -0.0117 -0.0096 0.0054 365 ARG A CZ 2223 N NH1 . ARG A 283 ? 0.2420 0.2748 0.2023 -0.0120 -0.0112 0.0055 365 ARG A NH1 2224 N NH2 . ARG A 283 ? 0.2391 0.2699 0.1969 -0.0117 -0.0088 0.0062 365 ARG A NH2 2225 N N . THR A 284 ? 0.1902 0.2149 0.1665 -0.0090 -0.0085 0.0046 366 THR A N 2226 C CA . THR A 284 ? 0.2167 0.2407 0.1943 -0.0083 -0.0080 0.0060 366 THR A CA 2227 C C . THR A 284 ? 0.2476 0.2721 0.2229 -0.0083 -0.0077 0.0072 366 THR A C 2228 O O . THR A 284 ? 0.2468 0.2727 0.2198 -0.0087 -0.0083 0.0072 366 THR A O 2229 C CB . THR A 284 ? 0.2320 0.2564 0.2117 -0.0075 -0.0090 0.0070 366 THR A CB 2230 O OG1 . THR A 284 ? 0.2434 0.2698 0.2219 -0.0074 -0.0101 0.0077 366 THR A OG1 2231 C CG2 . THR A 284 ? 0.1635 0.1877 0.1454 -0.0075 -0.0092 0.0058 366 THR A CG2 2232 N N . ILE A 285 ? 0.2692 0.2928 0.2450 -0.0081 -0.0067 0.0083 367 ILE A N 2233 C CA . ILE A 285 ? 0.2755 0.2995 0.2491 -0.0081 -0.0064 0.0097 367 ILE A CA 2234 C C . ILE A 285 ? 0.2691 0.2938 0.2425 -0.0075 -0.0075 0.0115 367 ILE A C 2235 O O . ILE A 285 ? 0.3443 0.3705 0.3154 -0.0075 -0.0082 0.0121 367 ILE A O 2236 C CB . ILE A 285 ? 0.3059 0.3287 0.2800 -0.0083 -0.0049 0.0104 367 ILE A CB 2237 C CG1 . ILE A 285 ? 0.2945 0.3173 0.2681 -0.0087 -0.0038 0.0088 367 ILE A CG1 2238 C CG2 . ILE A 285 ? 0.2610 0.2840 0.2329 -0.0083 -0.0046 0.0123 367 ILE A CG2 2239 C CD1 . ILE A 285 ? 0.2655 0.2877 0.2404 -0.0089 -0.0023 0.0092 367 ILE A CD1 2240 N N . SER A 286 ? 0.3492 0.3729 0.3251 -0.0068 -0.0078 0.0122 368 SER A N 2241 C CA . SER A 286 ? 0.3800 0.4041 0.3561 -0.0058 -0.0088 0.0139 368 SER A CA 2242 C C . SER A 286 ? 0.3566 0.3832 0.3323 -0.0056 -0.0102 0.0134 368 SER A C 2243 O O . SER A 286 ? 0.2681 0.2952 0.2444 -0.0062 -0.0105 0.0116 368 SER A O 2244 C CB . SER A 286 ? 0.3121 0.3343 0.2909 -0.0051 -0.0087 0.0144 368 SER A CB 2245 O OG . SER A 286 ? 0.4243 0.4470 0.4035 -0.0039 -0.0097 0.0158 368 SER A OG 2246 N N . THR A 287 ? 0.2734 0.3015 0.2479 -0.0049 -0.0112 0.0150 369 THR A N 2247 C CA . THR A 287 ? 0.2971 0.3280 0.2715 -0.0047 -0.0127 0.0148 369 THR A CA 2248 C C . THR A 287 ? 0.2729 0.3038 0.2501 -0.0033 -0.0133 0.0156 369 THR A C 2249 O O . THR A 287 ? 0.2946 0.3280 0.2725 -0.0030 -0.0145 0.0153 369 THR A O 2250 C CB . THR A 287 ? 0.2917 0.3250 0.2635 -0.0045 -0.0136 0.0162 369 THR A CB 2251 O OG1 . THR A 287 ? 0.2068 0.2390 0.1784 -0.0033 -0.0134 0.0187 369 THR A OG1 2252 C CG2 . THR A 287 ? 0.2947 0.3282 0.2634 -0.0059 -0.0130 0.0153 369 THR A CG2 2253 N N . ALA A 288 ? 0.3005 0.3286 0.2791 -0.0025 -0.0125 0.0164 370 ALA A N 2254 C CA . ALA A 288 ? 0.3118 0.3393 0.2927 -0.0010 -0.0129 0.0172 370 ALA A CA 2255 C C . ALA A 288 ? 0.2854 0.3114 0.2688 -0.0012 -0.0124 0.0156 370 ALA A C 2256 O O . ALA A 288 ? 0.2969 0.3237 0.2822 -0.0003 -0.0129 0.0153 370 ALA A O 2257 C CB . ALA A 288 ? 0.3013 0.3265 0.2818 0.0001 -0.0124 0.0195 370 ALA A CB 2258 N N . SER A 289 ? 0.2950 0.3191 0.2784 -0.0023 -0.0113 0.0145 371 SER A N 2259 C CA . SER A 289 ? 0.2465 0.2692 0.2322 -0.0025 -0.0108 0.0130 371 SER A CA 2260 C C . SER A 289 ? 0.2979 0.3204 0.2835 -0.0039 -0.0102 0.0113 371 SER A C 2261 O O . SER A 289 ? 0.2044 0.2274 0.1880 -0.0047 -0.0099 0.0111 371 SER A O 2262 C CB . SER A 289 ? 0.3141 0.3337 0.3009 -0.0019 -0.0101 0.0139 371 SER A CB 2263 O OG . SER A 289 ? 0.4363 0.4542 0.4220 -0.0028 -0.0091 0.0144 371 SER A OG 2264 N N . ARG A 290 ? 0.2578 0.2796 0.2453 -0.0040 -0.0100 0.0100 372 ARG A N 2265 C CA . ARG A 290 ? 0.2819 0.3034 0.2695 -0.0050 -0.0094 0.0084 372 ARG A CA 2266 C C . ARG A 290 ? 0.2614 0.2812 0.2490 -0.0055 -0.0083 0.0086 372 ARG A C 2267 O O . ARG A 290 ? 0.2929 0.3115 0.2821 -0.0057 -0.0078 0.0079 372 ARG A O 2268 C CB . ARG A 290 ? 0.2142 0.2358 0.2037 -0.0048 -0.0097 0.0072 372 ARG A CB 2269 C CG . ARG A 290 ? 0.2054 0.2291 0.1951 -0.0045 -0.0107 0.0070 372 ARG A CG 2270 C CD . ARG A 290 ? 0.2413 0.2650 0.2328 -0.0043 -0.0109 0.0059 372 ARG A CD 2271 N NE . ARG A 290 ? 0.2148 0.2410 0.2065 -0.0043 -0.0117 0.0056 372 ARG A NE 2272 C CZ . ARG A 290 ? 0.2702 0.2970 0.2633 -0.0042 -0.0119 0.0047 372 ARG A CZ 2273 N NH1 . ARG A 290 ? 0.2382 0.2634 0.2325 -0.0040 -0.0113 0.0041 372 ARG A NH1 2274 N NH2 . ARG A 290 ? 0.1983 0.2276 0.1915 -0.0044 -0.0126 0.0045 372 ARG A NH2 2275 N N . SER A 291 ? 0.2840 0.3039 0.2697 -0.0058 -0.0079 0.0095 373 SER A N 2276 C CA . SER A 291 ? 0.3024 0.3212 0.2881 -0.0064 -0.0067 0.0097 373 SER A CA 2277 C C . SER A 291 ? 0.2441 0.2639 0.2278 -0.0070 -0.0062 0.0094 373 SER A C 2278 O O . SER A 291 ? 0.2397 0.2607 0.2213 -0.0070 -0.0067 0.0096 373 SER A O 2279 C CB . SER A 291 ? 0.3480 0.3652 0.3336 -0.0061 -0.0064 0.0116 373 SER A CB 2280 O OG . SER A 291 ? 0.4577 0.4757 0.4413 -0.0057 -0.0068 0.0130 373 SER A OG 2281 N N . GLY A 292 ? 0.2277 0.2472 0.2120 -0.0076 -0.0052 0.0086 374 GLY A N 2282 C CA . GLY A 292 ? 0.2019 0.2222 0.1844 -0.0080 -0.0044 0.0081 374 GLY A CA 2283 C C . GLY A 292 ? 0.1853 0.2062 0.1669 -0.0080 -0.0049 0.0065 374 GLY A C 2284 O O . GLY A 292 ? 0.2139 0.2351 0.1960 -0.0078 -0.0059 0.0061 374 GLY A O 2285 N N . TYR A 293 ? 0.2346 0.2558 0.2149 -0.0083 -0.0040 0.0057 375 TYR A N 2286 C CA . TYR A 293 ? 0.2348 0.2562 0.2138 -0.0085 -0.0043 0.0042 375 TYR A CA 2287 C C . TYR A 293 ? 0.2473 0.2687 0.2239 -0.0087 -0.0032 0.0037 375 TYR A C 2288 O O . TYR A 293 ? 0.2538 0.2752 0.2310 -0.0086 -0.0020 0.0039 375 TYR A O 2289 C CB . TYR A 293 ? 0.2391 0.2598 0.2200 -0.0083 -0.0043 0.0030 375 TYR A CB 2290 C CG . TYR A 293 ? 0.2079 0.2285 0.1878 -0.0085 -0.0050 0.0018 375 TYR A CG 2291 C CD1 . TYR A 293 ? 0.2037 0.2248 0.1842 -0.0086 -0.0063 0.0020 375 TYR A CD1 2292 C CD2 . TYR A 293 ? 0.2049 0.2249 0.1830 -0.0087 -0.0044 0.0006 375 TYR A CD2 2293 C CE1 . TYR A 293 ? 0.2663 0.2875 0.2458 -0.0091 -0.0069 0.0010 375 TYR A CE1 2294 C CE2 . TYR A 293 ? 0.2102 0.2297 0.1871 -0.0092 -0.0050 -0.0005 375 TYR A CE2 2295 C CZ . TYR A 293 ? 0.2397 0.2600 0.2175 -0.0095 -0.0063 -0.0003 375 TYR A CZ 2296 O OH . TYR A 293 ? 0.2529 0.2729 0.2295 -0.0102 -0.0068 -0.0014 375 TYR A OH 2297 N N . GLU A 294 ? 0.2528 0.2744 0.2268 -0.0091 -0.0036 0.0030 376 GLU A N 2298 C CA . GLU A 294 ? 0.2403 0.2618 0.2116 -0.0093 -0.0025 0.0022 376 GLU A CA 2299 C C . GLU A 294 ? 0.2437 0.2644 0.2132 -0.0097 -0.0028 0.0004 376 GLU A C 2300 O O . GLU A 294 ? 0.2544 0.2754 0.2241 -0.0101 -0.0040 0.0002 376 GLU A O 2301 C CB . GLU A 294 ? 0.2385 0.2610 0.2074 -0.0096 -0.0025 0.0034 376 GLU A CB 2302 C CG . GLU A 294 ? 0.2313 0.2548 0.1987 -0.0100 -0.0040 0.0038 376 GLU A CG 2303 C CD . GLU A 294 ? 0.3184 0.3430 0.2835 -0.0101 -0.0041 0.0053 376 GLU A CD 2304 O OE1 . GLU A 294 ? 0.3078 0.3323 0.2719 -0.0101 -0.0028 0.0058 376 GLU A OE1 2305 O OE2 . GLU A 294 ? 0.3406 0.3664 0.3048 -0.0103 -0.0055 0.0059 376 GLU A OE2 2306 N N . MET A 295 ? 0.2197 0.2395 0.1876 -0.0096 -0.0015 -0.0008 377 MET A N 2307 C CA . MET A 295 ? 0.2696 0.2881 0.2349 -0.0102 -0.0016 -0.0025 377 MET A CA 2308 C C . MET A 295 ? 0.3180 0.3370 0.2795 -0.0108 -0.0013 -0.0028 377 MET A C 2309 O O . MET A 295 ? 0.2743 0.2939 0.2351 -0.0104 -0.0002 -0.0021 377 MET A O 2310 C CB . MET A 295 ? 0.2435 0.2603 0.2093 -0.0095 -0.0003 -0.0038 377 MET A CB 2311 C CG . MET A 295 ? 0.2564 0.2726 0.2255 -0.0089 -0.0006 -0.0037 377 MET A CG 2312 S SD . MET A 295 ? 0.2900 0.3060 0.2597 -0.0098 -0.0024 -0.0039 377 MET A SD 2313 C CE . MET A 295 ? 0.2277 0.2415 0.1939 -0.0106 -0.0020 -0.0060 377 MET A CE 2314 N N . LEU A 296 ? 0.3268 0.3457 0.2860 -0.0118 -0.0022 -0.0037 378 LEU A N 2315 C CA . LEU A 296 ? 0.2878 0.3073 0.2431 -0.0125 -0.0021 -0.0041 378 LEU A CA 2316 C C . LEU A 296 ? 0.2819 0.2994 0.2343 -0.0134 -0.0018 -0.0064 378 LEU A C 2317 O O . LEU A 296 ? 0.2553 0.2721 0.2081 -0.0142 -0.0028 -0.0073 378 LEU A O 2318 C CB . LEU A 296 ? 0.2698 0.2918 0.2245 -0.0131 -0.0037 -0.0028 378 LEU A CB 2319 C CG . LEU A 296 ? 0.2731 0.2966 0.2300 -0.0123 -0.0039 -0.0004 378 LEU A CG 2320 C CD1 . LEU A 296 ? 0.2123 0.2380 0.1688 -0.0127 -0.0057 0.0010 378 LEU A CD1 2321 C CD2 . LEU A 296 ? 0.2473 0.2709 0.2029 -0.0119 -0.0024 0.0003 378 LEU A CD2 2322 N N . LYS A 297 ? 0.2347 0.2512 0.1841 -0.0133 -0.0004 -0.0075 379 LYS A N 2323 C CA . LYS A 297 ? 0.3005 0.3147 0.2466 -0.0142 0.0000 -0.0098 379 LYS A CA 2324 C C . LYS A 297 ? 0.2875 0.3032 0.2303 -0.0158 -0.0013 -0.0102 379 LYS A C 2325 O O . LYS A 297 ? 0.3206 0.3379 0.2611 -0.0159 -0.0011 -0.0097 379 LYS A O 2326 C CB . LYS A 297 ? 0.3048 0.3172 0.2489 -0.0133 0.0022 -0.0109 379 LYS A CB 2327 C CG . LYS A 297 ? 0.3478 0.3569 0.2886 -0.0140 0.0029 -0.0135 379 LYS A CG 2328 C CD . LYS A 297 ? 0.3447 0.3521 0.2834 -0.0128 0.0052 -0.0146 379 LYS A CD 2329 C CE . LYS A 297 ? 0.3247 0.3283 0.2598 -0.0134 0.0060 -0.0173 379 LYS A CE 2330 N NZ . LYS A 297 ? 0.3107 0.3128 0.2436 -0.0121 0.0083 -0.0184 379 LYS A NZ 2331 N N . VAL A 298 ? 0.2638 0.2793 0.2067 -0.0171 -0.0027 -0.0110 380 VAL A N 2332 C CA . VAL A 298 ? 0.2611 0.2787 0.2013 -0.0188 -0.0043 -0.0113 380 VAL A CA 2333 C C . VAL A 298 ? 0.3338 0.3490 0.2713 -0.0206 -0.0043 -0.0139 380 VAL A C 2334 O O . VAL A 298 ? 0.2828 0.2975 0.2219 -0.0214 -0.0052 -0.0144 380 VAL A O 2335 C CB . VAL A 298 ? 0.2435 0.2642 0.1867 -0.0191 -0.0063 -0.0095 380 VAL A CB 2336 C CG1 . VAL A 298 ? 0.2706 0.2942 0.2112 -0.0206 -0.0080 -0.0096 380 VAL A CG1 2337 C CG2 . VAL A 298 ? 0.2982 0.3205 0.2442 -0.0174 -0.0061 -0.0071 380 VAL A CG2 2338 N N . PRO A 299 ? 0.3219 0.3354 0.2551 -0.0211 -0.0033 -0.0156 381 PRO A N 2339 C CA . PRO A 299 ? 0.3542 0.3646 0.2844 -0.0228 -0.0030 -0.0183 381 PRO A CA 2340 C C . PRO A 299 ? 0.2977 0.3099 0.2277 -0.0250 -0.0051 -0.0187 381 PRO A C 2341 O O . PRO A 299 ? 0.3136 0.3297 0.2427 -0.0258 -0.0067 -0.0178 381 PRO A O 2342 C CB . PRO A 299 ? 0.2866 0.2963 0.2119 -0.0231 -0.0019 -0.0197 381 PRO A CB 2343 C CG . PRO A 299 ? 0.3211 0.3323 0.2476 -0.0210 -0.0008 -0.0178 381 PRO A CG 2344 C CD . PRO A 299 ? 0.3080 0.3226 0.2387 -0.0204 -0.0023 -0.0151 381 PRO A CD 2345 N N . ASN A 300 ? 0.3022 0.3118 0.2330 -0.0260 -0.0052 -0.0200 382 ASN A N 2346 C CA . ASN A 300 ? 0.2678 0.2789 0.1984 -0.0284 -0.0070 -0.0207 382 ASN A CA 2347 C C . ASN A 300 ? 0.2892 0.3055 0.2232 -0.0283 -0.0090 -0.0184 382 ASN A C 2348 O O . ASN A 300 ? 0.3074 0.3268 0.2405 -0.0302 -0.0107 -0.0186 382 ASN A O 2349 C CB . ASN A 300 ? 0.3157 0.3268 0.2412 -0.0307 -0.0074 -0.0228 382 ASN A CB 2350 C CG . ASN A 300 ? 0.3705 0.3760 0.2922 -0.0309 -0.0054 -0.0253 382 ASN A CG 2351 O OD1 . ASN A 300 ? 0.4266 0.4278 0.3488 -0.0309 -0.0044 -0.0264 382 ASN A OD1 2352 N ND2 . ASN A 300 ? 0.4607 0.4662 0.3785 -0.0309 -0.0047 -0.0262 382 ASN A ND2 2353 N N . ALA A 301 ? 0.2826 0.2998 0.2204 -0.0261 -0.0088 -0.0163 383 ALA A N 2354 C CA . ALA A 301 ? 0.2735 0.2952 0.2146 -0.0256 -0.0104 -0.0140 383 ALA A CA 2355 C C . ALA A 301 ? 0.2990 0.3224 0.2416 -0.0274 -0.0120 -0.0143 383 ALA A C 2356 O O . ALA A 301 ? 0.2988 0.3268 0.2424 -0.0279 -0.0137 -0.0132 383 ALA A O 2357 C CB . ALA A 301 ? 0.2514 0.2726 0.1964 -0.0232 -0.0096 -0.0122 383 ALA A CB 2358 N N . LEU A 302 ? 0.3392 0.3594 0.2822 -0.0282 -0.0113 -0.0158 384 LEU A N 2359 C CA . LEU A 302 ? 0.2777 0.2991 0.2221 -0.0301 -0.0125 -0.0162 384 LEU A CA 2360 C C . LEU A 302 ? 0.3392 0.3637 0.2811 -0.0327 -0.0141 -0.0172 384 LEU A C 2361 O O . LEU A 302 ? 0.3273 0.3560 0.2712 -0.0336 -0.0157 -0.0164 384 LEU A O 2362 C CB . LEU A 302 ? 0.2226 0.2391 0.1669 -0.0307 -0.0113 -0.0178 384 LEU A CB 2363 C CG . LEU A 302 ? 0.3388 0.3561 0.2841 -0.0330 -0.0123 -0.0184 384 LEU A CG 2364 C CD1 . LEU A 302 ? 0.2752 0.2970 0.2250 -0.0321 -0.0135 -0.0163 384 LEU A CD1 2365 C CD2 . LEU A 302 ? 0.3067 0.3185 0.2514 -0.0336 -0.0109 -0.0199 384 LEU A CD2 2366 N N . THR A 303 ? 0.2614 0.2841 0.1989 -0.0338 -0.0136 -0.0190 385 THR A N 2367 C CA . THR A 303 ? 0.3112 0.3362 0.2457 -0.0367 -0.0149 -0.0204 385 THR A CA 2368 C C . THR A 303 ? 0.2957 0.3245 0.2277 -0.0366 -0.0159 -0.0198 385 THR A C 2369 O O . THR A 303 ? 0.3115 0.3439 0.2419 -0.0388 -0.0176 -0.0203 385 THR A O 2370 C CB . THR A 303 ? 0.3872 0.4069 0.3178 -0.0388 -0.0138 -0.0235 385 THR A CB 2371 O OG1 . THR A 303 ? 0.3181 0.3337 0.2460 -0.0373 -0.0119 -0.0242 385 THR A OG1 2372 C CG2 . THR A 303 ? 0.2850 0.3013 0.2178 -0.0394 -0.0131 -0.0240 385 THR A CG2 2373 N N . ASP A 304 ? 0.2914 0.3196 0.2230 -0.0343 -0.0149 -0.0186 386 ASP A N 2374 C CA . ASP A 304 ? 0.3377 0.3689 0.2666 -0.0341 -0.0155 -0.0179 386 ASP A CA 2375 C C . ASP A 304 ? 0.3311 0.3671 0.2631 -0.0322 -0.0168 -0.0148 386 ASP A C 2376 O O . ASP A 304 ? 0.3372 0.3722 0.2715 -0.0298 -0.0158 -0.0131 386 ASP A O 2377 C CB . ASP A 304 ? 0.3430 0.3702 0.2688 -0.0328 -0.0134 -0.0187 386 ASP A CB 2378 C CG . ASP A 304 ? 0.4242 0.4542 0.3465 -0.0327 -0.0138 -0.0181 386 ASP A CG 2379 O OD1 . ASP A 304 ? 0.3452 0.3803 0.2677 -0.0332 -0.0158 -0.0168 386 ASP A OD1 2380 O OD2 . ASP A 304 ? 0.4357 0.4628 0.3550 -0.0320 -0.0121 -0.0190 386 ASP A OD2 2381 N N . ASP A 305 ? 0.3328 0.3740 0.2647 -0.0333 -0.0189 -0.0141 387 ASP A N 2382 C CA . ASP A 305 ? 0.3141 0.3599 0.2490 -0.0314 -0.0202 -0.0110 387 ASP A CA 2383 C C . ASP A 305 ? 0.3294 0.3763 0.2621 -0.0298 -0.0199 -0.0094 387 ASP A C 2384 O O . ASP A 305 ? 0.3492 0.3997 0.2837 -0.0283 -0.0210 -0.0068 387 ASP A O 2385 C CB . ASP A 305 ? 0.2929 0.3444 0.2292 -0.0328 -0.0226 -0.0105 387 ASP A CB 2386 C CG . ASP A 305 ? 0.3770 0.4315 0.3089 -0.0351 -0.0239 -0.0116 387 ASP A CG 2387 O OD1 . ASP A 305 ? 0.3503 0.4028 0.2779 -0.0353 -0.0231 -0.0126 387 ASP A OD1 2388 O OD2 . ASP A 305 ? 0.3679 0.4272 0.3007 -0.0366 -0.0259 -0.0116 387 ASP A OD2 2389 N N . ARG A 306 ? 0.3365 0.3801 0.2653 -0.0301 -0.0184 -0.0108 388 ARG A N 2390 C CA . ARG A 306 ? 0.3250 0.3692 0.2516 -0.0286 -0.0178 -0.0093 388 ARG A CA 2391 C C . ARG A 306 ? 0.3511 0.3909 0.2785 -0.0268 -0.0154 -0.0091 388 ARG A C 2392 O O . ARG A 306 ? 0.3277 0.3675 0.2537 -0.0255 -0.0145 -0.0078 388 ARG A O 2393 C CB . ARG A 306 ? 0.3633 0.4081 0.2842 -0.0305 -0.0180 -0.0110 388 ARG A CB 2394 C CG . ARG A 306 ? 0.3499 0.3991 0.2694 -0.0328 -0.0204 -0.0117 388 ARG A CG 2395 C CD . ARG A 306 ? 0.3267 0.3816 0.2488 -0.0316 -0.0224 -0.0087 388 ARG A CD 2396 N NE . ARG A 306 ? 0.4030 0.4624 0.3246 -0.0338 -0.0248 -0.0094 388 ARG A NE 2397 C CZ . ARG A 306 ? 0.4351 0.4986 0.3531 -0.0352 -0.0263 -0.0095 388 ARG A CZ 2398 N NH1 . ARG A 306 ? 0.3943 0.4575 0.3084 -0.0344 -0.0257 -0.0089 388 ARG A NH1 2399 N NH2 . ARG A 306 ? 0.4126 0.4806 0.3309 -0.0373 -0.0285 -0.0102 388 ARG A NH2 2400 N N . SER A 307 ? 0.2336 0.2696 0.1631 -0.0268 -0.0142 -0.0104 389 SER A N 2401 C CA . SER A 307 ? 0.2840 0.3158 0.2138 -0.0253 -0.0119 -0.0108 389 SER A CA 2402 C C . SER A 307 ? 0.3289 0.3613 0.2618 -0.0229 -0.0113 -0.0081 389 SER A C 2403 O O . SER A 307 ? 0.2944 0.3288 0.2310 -0.0221 -0.0123 -0.0063 389 SER A O 2404 C CB . SER A 307 ? 0.3132 0.3412 0.2446 -0.0258 -0.0110 -0.0127 389 SER A CB 2405 O OG . SER A 307 ? 0.3151 0.3445 0.2506 -0.0258 -0.0122 -0.0118 389 SER A OG 2406 N N . LYS A 308 ? 0.2726 0.3031 0.2039 -0.0219 -0.0095 -0.0080 390 LYS A N 2407 C CA . LYS A 308 ? 0.3529 0.3838 0.2866 -0.0199 -0.0086 -0.0056 390 LYS A CA 2408 C C . LYS A 308 ? 0.3087 0.3359 0.2433 -0.0189 -0.0063 -0.0065 390 LYS A C 2409 O O . LYS A 308 ? 0.3442 0.3688 0.2769 -0.0196 -0.0054 -0.0089 390 LYS A O 2410 C CB . LYS A 308 ? 0.3110 0.3442 0.2415 -0.0198 -0.0088 -0.0041 390 LYS A CB 2411 C CG . LYS A 308 ? 0.3169 0.3542 0.2473 -0.0202 -0.0111 -0.0025 390 LYS A CG 2412 C CD . LYS A 308 ? 0.3012 0.3396 0.2364 -0.0189 -0.0120 -0.0003 390 LYS A CD 2413 C CE . LYS A 308 ? 0.4617 0.5043 0.3968 -0.0189 -0.0142 0.0016 390 LYS A CE 2414 N NZ . LYS A 308 ? 0.4418 0.4861 0.3736 -0.0185 -0.0142 0.0032 390 LYS A NZ 2415 N N . PRO A 309 ? 0.3761 0.4032 0.3135 -0.0173 -0.0055 -0.0046 391 PRO A N 2416 C CA . PRO A 309 ? 0.2857 0.3101 0.2244 -0.0163 -0.0034 -0.0053 391 PRO A CA 2417 C C . PRO A 309 ? 0.3275 0.3510 0.2627 -0.0161 -0.0016 -0.0062 391 PRO A C 2418 O O . PRO A 309 ? 0.3637 0.3891 0.2962 -0.0163 -0.0017 -0.0052 391 PRO A O 2419 C CB . PRO A 309 ? 0.2629 0.2881 0.2056 -0.0149 -0.0033 -0.0029 391 PRO A CB 2420 C CG . PRO A 309 ? 0.3473 0.3749 0.2914 -0.0152 -0.0054 -0.0013 391 PRO A CG 2421 C CD . PRO A 309 ? 0.3050 0.3344 0.2452 -0.0164 -0.0065 -0.0018 391 PRO A CD 2422 N N . ILE A 310 ? 0.2536 0.2743 0.1886 -0.0157 0.0001 -0.0080 392 ILE A N 2423 C CA . ILE A 310 ? 0.3280 0.3477 0.2601 -0.0152 0.0022 -0.0089 392 ILE A CA 2424 C C . ILE A 310 ? 0.3469 0.3658 0.2822 -0.0135 0.0040 -0.0083 392 ILE A C 2425 O O . ILE A 310 ? 0.3496 0.3683 0.2835 -0.0128 0.0059 -0.0085 392 ILE A O 2426 C CB . ILE A 310 ? 0.3727 0.3898 0.3009 -0.0160 0.0029 -0.0119 392 ILE A CB 2427 C CG1 . ILE A 310 ? 0.3203 0.3342 0.2506 -0.0156 0.0034 -0.0134 392 ILE A CG1 2428 C CG2 . ILE A 310 ? 0.3207 0.3391 0.2456 -0.0180 0.0010 -0.0126 392 ILE A CG2 2429 C CD1 . ILE A 310 ? 0.2849 0.2955 0.2113 -0.0163 0.0044 -0.0163 392 ILE A CD1 2430 N N . GLN A 311 ? 0.3277 0.3463 0.2673 -0.0129 0.0034 -0.0075 393 GLN A N 2431 C CA . GLN A 311 ? 0.3324 0.3507 0.2756 -0.0115 0.0048 -0.0068 393 GLN A CA 2432 C C . GLN A 311 ? 0.3393 0.3582 0.2869 -0.0113 0.0035 -0.0054 393 GLN A C 2433 O O . GLN A 311 ? 0.3240 0.3429 0.2719 -0.0121 0.0018 -0.0054 393 GLN A O 2434 C CB . GLN A 311 ? 0.3567 0.3722 0.2994 -0.0108 0.0064 -0.0089 393 GLN A CB 2435 C CG . GLN A 311 ? 0.2604 0.2762 0.2058 -0.0091 0.0082 -0.0084 393 GLN A CG 2436 C CD . GLN A 311 ? 0.3964 0.4094 0.3421 -0.0081 0.0095 -0.0102 393 GLN A CD 2437 O OE1 . GLN A 311 ? 0.3047 0.3152 0.2471 -0.0085 0.0098 -0.0122 393 GLN A OE1 2438 N NE2 . GLN A 311 ? 0.2715 0.2849 0.2210 -0.0067 0.0102 -0.0095 393 GLN A NE2 2439 N N . GLY A 312 ? 0.3351 0.3546 0.2860 -0.0103 0.0043 -0.0041 394 GLY A N 2440 C CA . GLY A 312 ? 0.2771 0.2971 0.2320 -0.0101 0.0032 -0.0028 394 GLY A CA 2441 C C . GLY A 312 ? 0.3639 0.3840 0.3224 -0.0090 0.0043 -0.0022 394 GLY A C 2442 O O . GLY A 312 ? 0.3001 0.3204 0.2583 -0.0084 0.0060 -0.0025 394 GLY A O 2443 N N . GLN A 313 ? 0.3026 0.3229 0.2645 -0.0089 0.0032 -0.0014 395 GLN A N 2444 C CA . GLN A 313 ? 0.2788 0.2997 0.2443 -0.0081 0.0040 -0.0007 395 GLN A CA 2445 C C . GLN A 313 ? 0.3294 0.3508 0.2978 -0.0084 0.0027 0.0007 395 GLN A C 2446 O O . GLN A 313 ? 0.2717 0.2924 0.2407 -0.0086 0.0013 0.0003 395 GLN A O 2447 C CB . GLN A 313 ? 0.2764 0.2959 0.2430 -0.0073 0.0047 -0.0022 395 GLN A CB 2448 C CG . GLN A 313 ? 0.2313 0.2520 0.2015 -0.0065 0.0055 -0.0015 395 GLN A CG 2449 C CD . GLN A 313 ? 0.2781 0.2978 0.2490 -0.0053 0.0065 -0.0028 395 GLN A CD 2450 O OE1 . GLN A 313 ? 0.2455 0.2636 0.2137 -0.0050 0.0072 -0.0042 395 GLN A OE1 2451 N NE2 . GLN A 313 ? 0.2365 0.2571 0.2109 -0.0047 0.0065 -0.0024 395 GLN A NE2 2452 N N . THR A 314 ? 0.2951 0.3176 0.2651 -0.0083 0.0031 0.0022 396 THR A N 2453 C CA . THR A 314 ? 0.2472 0.2700 0.2202 -0.0085 0.0021 0.0034 396 THR A CA 2454 C C . THR A 314 ? 0.3566 0.3791 0.3327 -0.0080 0.0022 0.0027 396 THR A C 2455 O O . THR A 314 ? 0.3333 0.3563 0.3103 -0.0075 0.0034 0.0023 396 THR A O 2456 C CB . THR A 314 ? 0.3410 0.3646 0.3144 -0.0089 0.0027 0.0053 396 THR A CB 2457 O OG1 . THR A 314 ? 0.3141 0.3379 0.2846 -0.0092 0.0022 0.0062 396 THR A OG1 2458 C CG2 . THR A 314 ? 0.3248 0.3481 0.3013 -0.0090 0.0019 0.0063 396 THR A CG2 2459 N N . ILE A 315 ? 0.2636 0.2855 0.2413 -0.0080 0.0009 0.0027 397 ILE A N 2460 C CA . ILE A 315 ? 0.2722 0.2939 0.2527 -0.0076 0.0007 0.0021 397 ILE A CA 2461 C C . ILE A 315 ? 0.2662 0.2884 0.2494 -0.0078 0.0003 0.0032 397 ILE A C 2462 O O . ILE A 315 ? 0.2447 0.2676 0.2302 -0.0077 0.0009 0.0032 397 ILE A O 2463 C CB . ILE A 315 ? 0.2428 0.2633 0.2229 -0.0075 -0.0004 0.0011 397 ILE A CB 2464 C CG1 . ILE A 315 ? 0.2574 0.2770 0.2344 -0.0076 -0.0001 -0.0001 397 ILE A CG1 2465 C CG2 . ILE A 315 ? 0.2301 0.2504 0.2127 -0.0070 -0.0004 0.0005 397 ILE A CG2 2466 C CD1 . ILE A 315 ? 0.2567 0.2761 0.2332 -0.0069 0.0014 -0.0011 397 ILE A CD1 2467 N N . VAL A 316 ? 0.1719 0.1936 0.1548 -0.0082 -0.0006 0.0042 398 VAL A N 2468 C CA . VAL A 316 ? 0.2548 0.2764 0.2399 -0.0085 -0.0009 0.0053 398 VAL A CA 2469 C C . VAL A 316 ? 0.3273 0.3487 0.3109 -0.0088 -0.0009 0.0068 398 VAL A C 2470 O O . VAL A 316 ? 0.2438 0.2651 0.2251 -0.0087 -0.0015 0.0070 398 VAL A O 2471 C CB . VAL A 316 ? 0.2357 0.2565 0.2220 -0.0083 -0.0022 0.0049 398 VAL A CB 2472 C CG1 . VAL A 316 ? 0.2207 0.2409 0.2090 -0.0085 -0.0025 0.0059 398 VAL A CG1 2473 C CG2 . VAL A 316 ? 0.2390 0.2599 0.2265 -0.0079 -0.0023 0.0035 398 VAL A CG2 2474 N N . LEU A 317 ? 0.2161 0.2375 0.2007 -0.0093 -0.0002 0.0079 399 LEU A N 2475 C CA . LEU A 317 ? 0.2745 0.2954 0.2576 -0.0096 0.0000 0.0097 399 LEU A CA 2476 C C . LEU A 317 ? 0.3414 0.3611 0.3245 -0.0092 -0.0014 0.0104 399 LEU A C 2477 O O . LEU A 317 ? 0.2642 0.2833 0.2492 -0.0090 -0.0021 0.0098 399 LEU A O 2478 C CB . LEU A 317 ? 0.2905 0.3113 0.2750 -0.0104 0.0011 0.0107 399 LEU A CB 2479 C CG . LEU A 317 ? 0.3010 0.3235 0.2858 -0.0108 0.0026 0.0103 399 LEU A CG 2480 C CD1 . LEU A 317 ? 0.3474 0.3700 0.3341 -0.0118 0.0035 0.0114 399 LEU A CD1 2481 C CD2 . LEU A 317 ? 0.3022 0.3256 0.2839 -0.0107 0.0033 0.0106 399 LEU A CD2 2482 N N . ASN A 318 ? 0.2664 0.2859 0.2474 -0.0091 -0.0016 0.0118 400 ASN A N 2483 C CA . ASN A 318 ? 0.2325 0.2511 0.2133 -0.0085 -0.0028 0.0127 400 ASN A CA 2484 C C . ASN A 318 ? 0.2783 0.2951 0.2614 -0.0085 -0.0028 0.0135 400 ASN A C 2485 O O . ASN A 318 ? 0.3501 0.3660 0.3340 -0.0078 -0.0037 0.0137 400 ASN A O 2486 C CB . ASN A 318 ? 0.2967 0.3157 0.2747 -0.0083 -0.0030 0.0143 400 ASN A CB 2487 C CG . ASN A 318 ? 0.4362 0.4548 0.4141 -0.0074 -0.0044 0.0153 400 ASN A CG 2488 O OD1 . ASN A 318 ? 0.4054 0.4248 0.3839 -0.0069 -0.0054 0.0143 400 ASN A OD1 2489 N ND2 . ASN A 318 ? 0.4873 0.5048 0.4645 -0.0070 -0.0043 0.0174 400 ASN A ND2 2490 N N . ALA A 319 ? 0.3230 0.3391 0.3070 -0.0094 -0.0016 0.0139 401 ALA A N 2491 C CA . ALA A 319 ? 0.3563 0.3704 0.3424 -0.0097 -0.0015 0.0143 401 ALA A CA 2492 C C . ALA A 319 ? 0.3702 0.3842 0.3586 -0.0096 -0.0020 0.0127 401 ALA A C 2493 O O . ALA A 319 ? 0.3940 0.4062 0.3839 -0.0097 -0.0022 0.0127 401 ALA A O 2494 C CB . ALA A 319 ? 0.3595 0.3734 0.3460 -0.0110 -0.0001 0.0150 401 ALA A CB 2495 N N . ASP A 320 ? 0.2774 0.2932 0.2660 -0.0094 -0.0023 0.0111 402 ASP A N 2496 C CA . ASP A 320 ? 0.2807 0.2968 0.2714 -0.0093 -0.0028 0.0096 402 ASP A CA 2497 C C . ASP A 320 ? 0.3292 0.3455 0.3195 -0.0084 -0.0039 0.0088 402 ASP A C 2498 O O . ASP A 320 ? 0.2985 0.3157 0.2870 -0.0080 -0.0043 0.0089 402 ASP A O 2499 C CB . ASP A 320 ? 0.3137 0.3315 0.3051 -0.0097 -0.0021 0.0084 402 ASP A CB 2500 C CG . ASP A 320 ? 0.3522 0.3703 0.3448 -0.0108 -0.0009 0.0089 402 ASP A CG 2501 O OD1 . ASP A 320 ? 0.3876 0.4044 0.3816 -0.0114 -0.0010 0.0092 402 ASP A OD1 2502 O OD2 . ASP A 320 ? 0.2829 0.3025 0.2749 -0.0110 0.0000 0.0090 402 ASP A OD2 2503 N N . TRP A 321 ? 0.2730 0.2886 0.2650 -0.0081 -0.0045 0.0081 403 TRP A N 2504 C CA . TRP A 321 ? 0.2354 0.2514 0.2274 -0.0073 -0.0055 0.0075 403 TRP A CA 2505 C C . TRP A 321 ? 0.2542 0.2717 0.2458 -0.0074 -0.0057 0.0061 403 TRP A C 2506 O O . TRP A 321 ? 0.2317 0.2497 0.2242 -0.0078 -0.0051 0.0053 403 TRP A O 2507 C CB . TRP A 321 ? 0.2571 0.2719 0.2508 -0.0070 -0.0060 0.0070 403 TRP A CB 2508 C CG . TRP A 321 ? 0.3138 0.3265 0.3076 -0.0069 -0.0058 0.0082 403 TRP A CG 2509 C CD1 . TRP A 321 ? 0.3025 0.3135 0.2976 -0.0075 -0.0053 0.0082 403 TRP A CD1 2510 C CD2 . TRP A 321 ? 0.3244 0.3364 0.3171 -0.0060 -0.0061 0.0097 403 TRP A CD2 2511 N NE1 . TRP A 321 ? 0.3268 0.3355 0.3213 -0.0071 -0.0051 0.0095 403 TRP A NE1 2512 C CE2 . TRP A 321 ? 0.3943 0.4036 0.3874 -0.0061 -0.0057 0.0106 403 TRP A CE2 2513 C CE3 . TRP A 321 ? 0.3412 0.3545 0.3324 -0.0053 -0.0067 0.0104 403 TRP A CE3 2514 C CZ2 . TRP A 321 ? 0.2807 0.2885 0.2729 -0.0052 -0.0058 0.0122 403 TRP A CZ2 2515 C CZ3 . TRP A 321 ? 0.3295 0.3419 0.3199 -0.0044 -0.0070 0.0120 403 TRP A CZ3 2516 C CH2 . TRP A 321 ? 0.3909 0.4004 0.3818 -0.0042 -0.0065 0.0130 403 TRP A CH2 2517 N N . SER A 322 ? 0.2374 0.2557 0.2278 -0.0070 -0.0063 0.0060 404 SER A N 2518 C CA . SER A 322 ? 0.2231 0.2423 0.2131 -0.0071 -0.0065 0.0047 404 SER A CA 2519 C C . SER A 322 ? 0.2102 0.2297 0.2010 -0.0067 -0.0074 0.0041 404 SER A C 2520 O O . SER A 322 ? 0.2354 0.2543 0.2278 -0.0064 -0.0076 0.0041 404 SER A O 2521 C CB . SER A 322 ? 0.2346 0.2545 0.2223 -0.0073 -0.0064 0.0046 404 SER A CB 2522 O OG . SER A 322 ? 0.2308 0.2513 0.2173 -0.0071 -0.0071 0.0056 404 SER A OG 2523 N N . GLY A 323 ? 0.2006 0.2210 0.1904 -0.0068 -0.0079 0.0036 405 GLY A N 2524 C CA . GLY A 323 ? 0.1609 0.1819 0.1514 -0.0066 -0.0086 0.0030 405 GLY A CA 2525 C C . GLY A 323 ? 0.2456 0.2672 0.2348 -0.0071 -0.0089 0.0021 405 GLY A C 2526 O O . GLY A 323 ? 0.2648 0.2867 0.2521 -0.0076 -0.0088 0.0021 405 GLY A O 2527 N N . TYR A 324 ? 0.2126 0.2344 0.2027 -0.0072 -0.0091 0.0012 406 TYR A N 2528 C CA . TYR A 324 ? 0.2048 0.2268 0.1936 -0.0079 -0.0092 0.0003 406 TYR A CA 2529 C C . TYR A 324 ? 0.2264 0.2472 0.2139 -0.0082 -0.0084 -0.0003 406 TYR A C 2530 O O . TYR A 324 ? 0.2058 0.2258 0.1938 -0.0078 -0.0077 -0.0001 406 TYR A O 2531 C CB . TYR A 324 ? 0.2026 0.2246 0.1926 -0.0079 -0.0094 -0.0004 406 TYR A CB 2532 C CG . TYR A 324 ? 0.2303 0.2539 0.2213 -0.0078 -0.0102 -0.0001 406 TYR A CG 2533 C CD1 . TYR A 324 ? 0.2725 0.2973 0.2637 -0.0073 -0.0107 0.0008 406 TYR A CD1 2534 C CD2 . TYR A 324 ? 0.2226 0.2467 0.2142 -0.0081 -0.0104 -0.0007 406 TYR A CD2 2535 C CE1 . TYR A 324 ? 0.2994 0.3261 0.2917 -0.0070 -0.0114 0.0011 406 TYR A CE1 2536 C CE2 . TYR A 324 ? 0.1794 0.2053 0.1720 -0.0080 -0.0110 -0.0005 406 TYR A CE2 2537 C CZ . TYR A 324 ? 0.2435 0.2707 0.2364 -0.0074 -0.0115 0.0004 406 TYR A CZ 2538 O OH . TYR A 324 ? 0.2360 0.2654 0.2301 -0.0070 -0.0120 0.0006 406 TYR A OH 2539 N N . SER A 325 ? 0.2237 0.2443 0.2093 -0.0089 -0.0084 -0.0009 407 SER A N 2540 C CA . SER A 325 ? 0.2641 0.2832 0.2481 -0.0091 -0.0075 -0.0017 407 SER A CA 2541 C C . SER A 325 ? 0.2726 0.2910 0.2553 -0.0099 -0.0077 -0.0027 407 SER A C 2542 O O . SER A 325 ? 0.2557 0.2752 0.2381 -0.0106 -0.0085 -0.0028 407 SER A O 2543 C CB . SER A 325 ? 0.1945 0.2139 0.1768 -0.0092 -0.0072 -0.0013 407 SER A CB 2544 O OG . SER A 325 ? 0.2462 0.2667 0.2270 -0.0099 -0.0080 -0.0012 407 SER A OG 2545 N N . GLY A 326 ? 0.2127 0.2292 0.1947 -0.0098 -0.0069 -0.0035 408 GLY A N 2546 C CA . GLY A 326 ? 0.1922 0.2074 0.1729 -0.0106 -0.0069 -0.0044 408 GLY A CA 2547 C C . GLY A 326 ? 0.2265 0.2392 0.2056 -0.0103 -0.0058 -0.0052 408 GLY A C 2548 O O . GLY A 326 ? 0.2019 0.2143 0.1814 -0.0093 -0.0050 -0.0050 408 GLY A O 2549 N N . SER A 327 ? 0.2190 0.2299 0.1963 -0.0113 -0.0056 -0.0062 409 SER A N 2550 C CA . SER A 327 ? 0.2706 0.2785 0.2460 -0.0109 -0.0045 -0.0071 409 SER A CA 2551 C C . SER A 327 ? 0.2347 0.2407 0.2108 -0.0103 -0.0040 -0.0071 409 SER A C 2552 O O . SER A 327 ? 0.2263 0.2328 0.2036 -0.0107 -0.0047 -0.0068 409 SER A O 2553 C CB . SER A 327 ? 0.2628 0.2693 0.2352 -0.0124 -0.0044 -0.0082 409 SER A CB 2554 O OG . SER A 327 ? 0.1973 0.2044 0.1696 -0.0139 -0.0054 -0.0084 409 SER A OG 2555 N N . PHE A 328 ? 0.1739 0.1777 0.1491 -0.0092 -0.0029 -0.0075 410 PHE A N 2556 C CA . PHE A 328 ? 0.2353 0.2366 0.2105 -0.0084 -0.0023 -0.0075 410 PHE A CA 2557 C C . PHE A 328 ? 0.2366 0.2354 0.2100 -0.0074 -0.0010 -0.0082 410 PHE A C 2558 O O . PHE A 328 ? 0.2388 0.2385 0.2117 -0.0070 -0.0005 -0.0084 410 PHE A O 2559 C CB . PHE A 328 ? 0.2529 0.2560 0.2309 -0.0072 -0.0026 -0.0065 410 PHE A CB 2560 C CG . PHE A 328 ? 0.2171 0.2217 0.1966 -0.0057 -0.0020 -0.0060 410 PHE A CG 2561 C CD1 . PHE A 328 ? 0.1920 0.1993 0.1726 -0.0059 -0.0024 -0.0056 410 PHE A CD1 2562 C CD2 . PHE A 328 ? 0.2192 0.2226 0.1988 -0.0041 -0.0011 -0.0060 410 PHE A CD2 2563 C CE1 . PHE A 328 ? 0.2572 0.2660 0.2392 -0.0047 -0.0019 -0.0051 410 PHE A CE1 2564 C CE2 . PHE A 328 ? 0.2595 0.2647 0.2405 -0.0028 -0.0006 -0.0055 410 PHE A CE2 2565 C CZ . PHE A 328 ? 0.2649 0.2729 0.2472 -0.0033 -0.0010 -0.0051 410 PHE A CZ 2566 N N . MET A 329 ? 0.2928 0.2883 0.2650 -0.0069 -0.0002 -0.0086 411 MET A N 2567 C CA . MET A 329 ? 0.2805 0.2734 0.2512 -0.0054 0.0012 -0.0091 411 MET A CA 2568 C C . MET A 329 ? 0.3176 0.3086 0.2890 -0.0039 0.0017 -0.0085 411 MET A C 2569 O O . MET A 329 ? 0.2733 0.2637 0.2452 -0.0045 0.0011 -0.0081 411 MET A O 2570 C CB . MET A 329 ? 0.2604 0.2498 0.2275 -0.0066 0.0018 -0.0106 411 MET A CB 2571 C CG . MET A 329 ? 0.3057 0.2970 0.2717 -0.0081 0.0014 -0.0112 411 MET A CG 2572 S SD . MET A 329 ? 0.2975 0.2850 0.2591 -0.0090 0.0025 -0.0131 411 MET A SD 2573 C CE . MET A 329 ? 0.2023 0.1866 0.1621 -0.0113 0.0019 -0.0139 411 MET A CE 2574 N N . ASP A 330 ? 0.2921 0.2825 0.2638 -0.0018 0.0028 -0.0084 412 ASP A N 2575 C CA . ASP A 330 ? 0.2568 0.2451 0.2286 -0.0001 0.0034 -0.0078 412 ASP A CA 2576 C C . ASP A 330 ? 0.3106 0.2933 0.2790 -0.0004 0.0044 -0.0089 412 ASP A C 2577 O O . ASP A 330 ? 0.2676 0.2480 0.2343 0.0008 0.0058 -0.0096 412 ASP A O 2578 C CB . ASP A 330 ? 0.2421 0.2323 0.2157 0.0024 0.0042 -0.0072 412 ASP A CB 2579 C CG . ASP A 330 ? 0.2856 0.2745 0.2599 0.0044 0.0046 -0.0063 412 ASP A CG 2580 O OD1 . ASP A 330 ? 0.2414 0.2272 0.2144 0.0039 0.0044 -0.0062 412 ASP A OD1 2581 O OD2 . ASP A 330 ? 0.3411 0.3322 0.3173 0.0065 0.0051 -0.0057 412 ASP A OD2 2582 N N . TYR A 331 ? 0.3016 0.2823 0.2690 -0.0020 0.0039 -0.0089 413 TYR A N 2583 C CA . TYR A 331 ? 0.3494 0.3245 0.3134 -0.0028 0.0048 -0.0099 413 TYR A CA 2584 C C . TYR A 331 ? 0.3981 0.3693 0.3611 -0.0004 0.0061 -0.0095 413 TYR A C 2585 O O . TYR A 331 ? 0.3555 0.3215 0.3155 -0.0006 0.0072 -0.0104 413 TYR A O 2586 C CB . TYR A 331 ? 0.3148 0.2890 0.2780 -0.0054 0.0039 -0.0100 413 TYR A CB 2587 C CG . TYR A 331 ? 0.2846 0.2621 0.2482 -0.0076 0.0027 -0.0106 413 TYR A CG 2588 C CD1 . TYR A 331 ? 0.2528 0.2287 0.2138 -0.0093 0.0030 -0.0121 413 TYR A CD1 2589 C CD2 . TYR A 331 ? 0.2760 0.2584 0.2426 -0.0080 0.0014 -0.0096 413 TYR A CD2 2590 C CE1 . TYR A 331 ? 0.2237 0.2031 0.1851 -0.0112 0.0018 -0.0125 413 TYR A CE1 2591 C CE2 . TYR A 331 ? 0.2581 0.2435 0.2251 -0.0097 0.0004 -0.0100 413 TYR A CE2 2592 C CZ . TYR A 331 ? 0.2801 0.2642 0.2446 -0.0113 0.0006 -0.0113 413 TYR A CZ 2593 O OH . TYR A 331 ? 0.2836 0.2710 0.2485 -0.0129 -0.0005 -0.0115 413 TYR A OH 2594 N N . TRP A 332 ? 0.3095 0.2834 0.2752 0.0020 0.0061 -0.0082 414 TRP A N 2595 C CA . TRP A 332 ? 0.3480 0.3189 0.3133 0.0046 0.0072 -0.0075 414 TRP A CA 2596 C C . TRP A 332 ? 0.3679 0.3401 0.3340 0.0073 0.0083 -0.0075 414 TRP A C 2597 O O . TRP A 332 ? 0.3469 0.3182 0.3136 0.0100 0.0090 -0.0066 414 TRP A O 2598 C CB . TRP A 332 ? 0.2881 0.2605 0.2553 0.0053 0.0063 -0.0058 414 TRP A CB 2599 C CG . TRP A 332 ? 0.3084 0.2790 0.2745 0.0027 0.0056 -0.0058 414 TRP A CG 2600 C CD1 . TRP A 332 ? 0.3231 0.2885 0.2867 0.0023 0.0062 -0.0057 414 TRP A CD1 2601 C CD2 . TRP A 332 ? 0.2268 0.2007 0.1940 0.0002 0.0042 -0.0059 414 TRP A CD2 2602 N NE1 . TRP A 332 ? 0.2916 0.2572 0.2549 -0.0004 0.0053 -0.0057 414 TRP A NE1 2603 C CE2 . TRP A 332 ? 0.2872 0.2581 0.2527 -0.0016 0.0040 -0.0059 414 TRP A CE2 2604 C CE3 . TRP A 332 ? 0.2614 0.2404 0.2309 -0.0005 0.0031 -0.0060 414 TRP A CE3 2605 C CZ2 . TRP A 332 ? 0.2473 0.2207 0.2136 -0.0041 0.0029 -0.0060 414 TRP A CZ2 2606 C CZ3 . TRP A 332 ? 0.2345 0.2156 0.2046 -0.0028 0.0020 -0.0060 414 TRP A CZ3 2607 C CH2 . TRP A 332 ? 0.2254 0.2038 0.1940 -0.0046 0.0018 -0.0060 414 TRP A CH2 2608 N N . ALA A 333 ? 0.2634 0.2379 0.2296 0.0067 0.0084 -0.0085 415 ALA A N 2609 C CA . ALA A 333 ? 0.2825 0.2584 0.2494 0.0090 0.0096 -0.0086 415 ALA A CA 2610 C C . ALA A 333 ? 0.2716 0.2418 0.2351 0.0103 0.0115 -0.0098 415 ALA A C 2611 O O . ALA A 333 ? 0.3509 0.3163 0.3112 0.0087 0.0118 -0.0109 415 ALA A O 2612 C CB . ALA A 333 ? 0.2444 0.2244 0.2122 0.0078 0.0092 -0.0092 415 ALA A CB 2613 N N . GLU A 334 ? 0.4242 0.3953 0.3884 0.0131 0.0128 -0.0096 416 GLU A N 2614 C CA . GLU A 334 ? 0.5350 0.5010 0.4962 0.0147 0.0148 -0.0108 416 GLU A CA 2615 C C . GLU A 334 ? 0.4677 0.4327 0.4263 0.0130 0.0154 -0.0128 416 GLU A C 2616 O O . GLU A 334 ? 0.4076 0.3769 0.3673 0.0112 0.0144 -0.0129 416 GLU A O 2617 C CB . GLU A 334 ? 0.5652 0.5333 0.5284 0.0185 0.0160 -0.0100 416 GLU A CB 2618 C CG . GLU A 334 ? 0.7230 0.6909 0.6880 0.0208 0.0158 -0.0082 416 GLU A CG 2619 C CD . GLU A 334 ? 0.8343 0.7947 0.7959 0.0213 0.0167 -0.0085 416 GLU A CD 2620 O OE1 . GLU A 334 ? 0.8167 0.7722 0.7752 0.0222 0.0185 -0.0099 416 GLU A OE1 2621 O OE2 . GLU A 334 ? 0.8463 0.8055 0.8082 0.0208 0.0157 -0.0073 416 GLU A OE2 2622 N N . GLY A 335 ? 0.4517 0.4109 0.4065 0.0134 0.0170 -0.0143 417 GLY A N 2623 C CA . GLY A 335 ? 0.3786 0.3368 0.3305 0.0120 0.0177 -0.0163 417 GLY A CA 2624 C C . GLY A 335 ? 0.4614 0.4147 0.4093 0.0088 0.0174 -0.0179 417 GLY A C 2625 O O . GLY A 335 ? 0.4058 0.3560 0.3531 0.0077 0.0168 -0.0176 417 GLY A O 2626 N N . ASP A 336 ? 0.4147 0.3676 0.3600 0.0074 0.0179 -0.0197 418 ASP A N 2627 C CA . ASP A 336 ? 0.3777 0.3259 0.3189 0.0044 0.0178 -0.0216 418 ASP A CA 2628 C C . ASP A 336 ? 0.3797 0.3318 0.3213 0.0010 0.0157 -0.0217 418 ASP A C 2629 O O . ASP A 336 ? 0.3129 0.2622 0.2515 -0.0019 0.0154 -0.0232 418 ASP A O 2630 C CB . ASP A 336 ? 0.5024 0.4464 0.4394 0.0050 0.0197 -0.0239 418 ASP A CB 2631 C CG . ASP A 336 ? 0.6753 0.6242 0.6127 0.0053 0.0200 -0.0243 418 ASP A CG 2632 O OD1 . ASP A 336 ? 0.6596 0.6136 0.5985 0.0032 0.0184 -0.0238 418 ASP A OD1 2633 O OD2 . ASP A 336 ? 0.8337 0.7812 0.7698 0.0077 0.0220 -0.0251 418 ASP A OD2 2634 N N . CYS A 337 ? 0.3503 0.3088 0.2958 0.0012 0.0145 -0.0201 419 CYS A N 2635 C CA . CYS A 337 ? 0.3068 0.2692 0.2529 -0.0017 0.0127 -0.0200 419 CYS A CA 2636 C C . CYS A 337 ? 0.3615 0.3290 0.3121 -0.0015 0.0111 -0.0178 419 CYS A C 2637 O O . CYS A 337 ? 0.3423 0.3115 0.2957 0.0009 0.0114 -0.0165 419 CYS A O 2638 C CB . CYS A 337 ? 0.3378 0.3029 0.2827 -0.0020 0.0130 -0.0209 419 CYS A CB 2639 S SG . CYS A 337 ? 0.3634 0.3331 0.3112 0.0012 0.0141 -0.0197 419 CYS A SG 2640 N N . TYR A 338 ? 0.2797 0.2496 0.2309 -0.0041 0.0094 -0.0176 420 TYR A N 2641 C CA . TYR A 338 ? 0.3180 0.2926 0.2731 -0.0042 0.0078 -0.0158 420 TYR A CA 2642 C C . TYR A 338 ? 0.3230 0.3026 0.2797 -0.0040 0.0074 -0.0153 420 TYR A C 2643 O O . TYR A 338 ? 0.2722 0.2527 0.2271 -0.0055 0.0072 -0.0162 420 TYR A O 2644 C CB . TYR A 338 ? 0.3038 0.2786 0.2587 -0.0070 0.0063 -0.0159 420 TYR A CB 2645 C CG . TYR A 338 ? 0.3487 0.3190 0.3025 -0.0075 0.0065 -0.0160 420 TYR A CG 2646 C CD1 . TYR A 338 ? 0.2677 0.2363 0.2228 -0.0053 0.0072 -0.0150 420 TYR A CD1 2647 C CD2 . TYR A 338 ? 0.2555 0.2235 0.2069 -0.0103 0.0060 -0.0171 420 TYR A CD2 2648 C CE1 . TYR A 338 ? 0.2957 0.2601 0.2496 -0.0058 0.0074 -0.0149 420 TYR A CE1 2649 C CE2 . TYR A 338 ? 0.3546 0.3184 0.3050 -0.0110 0.0063 -0.0172 420 TYR A CE2 2650 C CZ . TYR A 338 ? 0.2836 0.2454 0.2351 -0.0087 0.0070 -0.0160 420 TYR A CZ 2651 O OH . TYR A 338 ? 0.3457 0.3032 0.2960 -0.0094 0.0073 -0.0159 420 TYR A OH 2652 N N . ARG A 339 ? 0.2513 0.2344 0.2116 -0.0023 0.0073 -0.0138 421 ARG A N 2653 C CA . ARG A 339 ? 0.2375 0.2252 0.1996 -0.0020 0.0070 -0.0131 421 ARG A CA 2654 C C . ARG A 339 ? 0.2813 0.2724 0.2453 -0.0037 0.0052 -0.0121 421 ARG A C 2655 O O . ARG A 339 ? 0.3042 0.2965 0.2708 -0.0035 0.0043 -0.0110 421 ARG A O 2656 C CB . ARG A 339 ? 0.3000 0.2897 0.2649 0.0005 0.0078 -0.0120 421 ARG A CB 2657 C CG . ARG A 339 ? 0.2915 0.2857 0.2582 0.0009 0.0079 -0.0113 421 ARG A CG 2658 C CD . ARG A 339 ? 0.3280 0.3247 0.2980 0.0031 0.0085 -0.0101 421 ARG A CD 2659 N NE . ARG A 339 ? 0.2906 0.2852 0.2594 0.0053 0.0103 -0.0108 421 ARG A NE 2660 C CZ . ARG A 339 ? 0.3295 0.3267 0.2997 0.0070 0.0115 -0.0104 421 ARG A CZ 2661 N NH1 . ARG A 339 ? 0.3025 0.3043 0.2752 0.0065 0.0110 -0.0095 421 ARG A NH1 2662 N NH2 . ARG A 339 ? 0.3624 0.3576 0.3316 0.0091 0.0132 -0.0111 421 ARG A NH2 2663 N N . ALA A 340 ? 0.2049 0.1973 0.1674 -0.0054 0.0046 -0.0126 422 ALA A N 2664 C CA . ALA A 340 ? 0.2667 0.2623 0.2309 -0.0068 0.0029 -0.0117 422 ALA A CA 2665 C C . ALA A 340 ? 0.2714 0.2706 0.2393 -0.0056 0.0026 -0.0101 422 ALA A C 2666 O O . ALA A 340 ? 0.2507 0.2513 0.2193 -0.0044 0.0035 -0.0097 422 ALA A O 2667 C CB . ALA A 340 ? 0.2879 0.2847 0.2499 -0.0083 0.0025 -0.0122 422 ALA A CB 2668 N N . CYS A 341 ? 0.2011 0.2018 0.1713 -0.0061 0.0013 -0.0092 423 CYS A N 2669 C CA . CYS A 341 ? 0.2926 0.2966 0.2662 -0.0054 0.0008 -0.0078 423 CYS A CA 2670 C C . CYS A 341 ? 0.2834 0.2895 0.2580 -0.0067 -0.0007 -0.0072 423 CYS A C 2671 O O . CYS A 341 ? 0.2389 0.2443 0.2123 -0.0080 -0.0014 -0.0077 423 CYS A O 2672 C CB . CYS A 341 ? 0.2235 0.2272 0.1991 -0.0041 0.0009 -0.0073 423 CYS A CB 2673 S SG . CYS A 341 ? 0.2700 0.2716 0.2450 -0.0020 0.0027 -0.0078 423 CYS A SG 2674 N N . PHE A 342 ? 0.2332 0.2420 0.2102 -0.0064 -0.0011 -0.0061 424 PHE A N 2675 C CA . PHE A 342 ? 0.2298 0.2405 0.2082 -0.0072 -0.0024 -0.0054 424 PHE A CA 2676 C C . PHE A 342 ? 0.2077 0.2204 0.1890 -0.0065 -0.0026 -0.0044 424 PHE A C 2677 O O . PHE A 342 ? 0.2262 0.2394 0.2084 -0.0055 -0.0018 -0.0041 424 PHE A O 2678 C CB . PHE A 342 ? 0.1836 0.1953 0.1603 -0.0082 -0.0028 -0.0053 424 PHE A CB 2679 C CG . PHE A 342 ? 0.2398 0.2528 0.2166 -0.0077 -0.0021 -0.0048 424 PHE A CG 2680 C CD1 . PHE A 342 ? 0.2488 0.2607 0.2235 -0.0073 -0.0009 -0.0054 424 PHE A CD1 2681 C CD2 . PHE A 342 ? 0.2677 0.2827 0.2463 -0.0076 -0.0026 -0.0035 424 PHE A CD2 2682 C CE1 . PHE A 342 ? 0.2193 0.2326 0.1939 -0.0069 -0.0001 -0.0048 424 PHE A CE1 2683 C CE2 . PHE A 342 ? 0.2232 0.2392 0.2017 -0.0074 -0.0019 -0.0029 424 PHE A CE2 2684 C CZ . PHE A 342 ? 0.3024 0.3179 0.2790 -0.0070 -0.0006 -0.0035 424 PHE A CZ 2685 N N . TYR A 343 ? 0.2132 0.2270 0.1960 -0.0070 -0.0037 -0.0038 425 TYR A N 2686 C CA . TYR A 343 ? 0.2069 0.2224 0.1923 -0.0065 -0.0039 -0.0030 425 TYR A CA 2687 C C . TYR A 343 ? 0.2841 0.3009 0.2696 -0.0071 -0.0046 -0.0023 425 TYR A C 2688 O O . TYR A 343 ? 0.2007 0.2174 0.1848 -0.0078 -0.0052 -0.0024 425 TYR A O 2689 C CB . TYR A 343 ? 0.1613 0.1769 0.1483 -0.0063 -0.0045 -0.0029 425 TYR A CB 2690 C CG . TYR A 343 ? 0.2038 0.2193 0.1905 -0.0071 -0.0054 -0.0030 425 TYR A CG 2691 C CD1 . TYR A 343 ? 0.2036 0.2176 0.1887 -0.0076 -0.0055 -0.0037 425 TYR A CD1 2692 C CD2 . TYR A 343 ? 0.1309 0.1479 0.1188 -0.0074 -0.0062 -0.0025 425 TYR A CD2 2693 C CE1 . TYR A 343 ? 0.2306 0.2451 0.2156 -0.0085 -0.0063 -0.0038 425 TYR A CE1 2694 C CE2 . TYR A 343 ? 0.2005 0.2179 0.1882 -0.0080 -0.0070 -0.0025 425 TYR A CE2 2695 C CZ . TYR A 343 ? 0.1748 0.1912 0.1612 -0.0086 -0.0070 -0.0032 425 TYR A CZ 2696 O OH . TYR A 343 ? 0.2280 0.2453 0.2145 -0.0093 -0.0078 -0.0032 425 TYR A OH 2697 N N . VAL A 344 ? 0.2510 0.2689 0.2381 -0.0069 -0.0046 -0.0015 426 VAL A N 2698 C CA . VAL A 344 ? 0.1948 0.2135 0.1824 -0.0072 -0.0053 -0.0006 426 VAL A CA 2699 C C . VAL A 344 ? 0.2838 0.3029 0.2737 -0.0070 -0.0057 -0.0003 426 VAL A C 2700 O O . VAL A 344 ? 0.1875 0.2068 0.1788 -0.0067 -0.0052 -0.0003 426 VAL A O 2701 C CB . VAL A 344 ? 0.2994 0.3185 0.2861 -0.0073 -0.0047 0.0001 426 VAL A CB 2702 C CG1 . VAL A 344 ? 0.2378 0.2575 0.2248 -0.0076 -0.0054 0.0011 426 VAL A CG1 2703 C CG2 . VAL A 344 ? 0.2109 0.2296 0.1950 -0.0076 -0.0041 -0.0004 426 VAL A CG2 2704 N N . GLU A 345 ? 0.2405 0.2598 0.2309 -0.0071 -0.0065 -0.0001 427 GLU A N 2705 C CA . GLU A 345 ? 0.2082 0.2277 0.2006 -0.0069 -0.0069 0.0001 427 GLU A CA 2706 C C . GLU A 345 ? 0.2320 0.2515 0.2249 -0.0069 -0.0067 0.0011 427 GLU A C 2707 O O . GLU A 345 ? 0.2389 0.2585 0.2308 -0.0070 -0.0069 0.0018 427 GLU A O 2708 C CB . GLU A 345 ? 0.1572 0.1770 0.1498 -0.0069 -0.0077 0.0000 427 GLU A CB 2709 C CG . GLU A 345 ? 0.1968 0.2166 0.1912 -0.0066 -0.0081 0.0002 427 GLU A CG 2710 C CD . GLU A 345 ? 0.2831 0.3035 0.2776 -0.0064 -0.0088 0.0002 427 GLU A CD 2711 O OE1 . GLU A 345 ? 0.2388 0.2599 0.2324 -0.0065 -0.0091 0.0005 427 GLU A OE1 2712 O OE2 . GLU A 345 ? 0.2245 0.2450 0.2201 -0.0062 -0.0090 -0.0003 427 GLU A OE2 2713 N N . LEU A 346 ? 0.1870 0.2065 0.1814 -0.0070 -0.0064 0.0012 428 LEU A N 2714 C CA . LEU A 346 ? 0.1747 0.1938 0.1697 -0.0072 -0.0061 0.0021 428 LEU A CA 2715 C C . LEU A 346 ? 0.2438 0.2623 0.2401 -0.0071 -0.0066 0.0021 428 LEU A C 2716 O O . LEU A 346 ? 0.2255 0.2439 0.2231 -0.0073 -0.0066 0.0015 428 LEU A O 2717 C CB . LEU A 346 ? 0.2080 0.2276 0.2037 -0.0076 -0.0053 0.0021 428 LEU A CB 2718 C CG . LEU A 346 ? 0.2190 0.2393 0.2136 -0.0075 -0.0046 0.0018 428 LEU A CG 2719 C CD1 . LEU A 346 ? 0.1823 0.2036 0.1779 -0.0077 -0.0037 0.0019 428 LEU A CD1 2720 C CD2 . LEU A 346 ? 0.2395 0.2595 0.2319 -0.0075 -0.0045 0.0025 428 LEU A CD2 2721 N N . ILE A 347 ? 0.1890 0.2070 0.1848 -0.0067 -0.0071 0.0026 429 ILE A N 2722 C CA . ILE A 347 ? 0.1846 0.2018 0.1814 -0.0063 -0.0076 0.0025 429 ILE A CA 2723 C C . ILE A 347 ? 0.2204 0.2361 0.2179 -0.0066 -0.0072 0.0030 429 ILE A C 2724 O O . ILE A 347 ? 0.2384 0.2534 0.2353 -0.0068 -0.0068 0.0041 429 ILE A O 2725 C CB . ILE A 347 ? 0.2381 0.2556 0.2343 -0.0056 -0.0082 0.0030 429 ILE A CB 2726 C CG1 . ILE A 347 ? 0.1849 0.2039 0.1804 -0.0057 -0.0086 0.0023 429 ILE A CG1 2727 C CG2 . ILE A 347 ? 0.1286 0.1452 0.1259 -0.0050 -0.0084 0.0029 429 ILE A CG2 2728 C CD1 . ILE A 347 ? 0.1718 0.1919 0.1669 -0.0051 -0.0093 0.0028 429 ILE A CD1 2729 N N . ARG A 348 ? 0.2022 0.2173 0.2010 -0.0069 -0.0072 0.0023 430 ARG A N 2730 C CA . ARG A 348 ? 0.2241 0.2374 0.2236 -0.0073 -0.0068 0.0026 430 ARG A CA 2731 C C . ARG A 348 ? 0.2573 0.2692 0.2572 -0.0067 -0.0072 0.0022 430 ARG A C 2732 O O . ARG A 348 ? 0.2262 0.2391 0.2263 -0.0062 -0.0076 0.0013 430 ARG A O 2733 C CB . ARG A 348 ? 0.2588 0.2726 0.2594 -0.0084 -0.0064 0.0020 430 ARG A CB 2734 C CG . ARG A 348 ? 0.2346 0.2500 0.2349 -0.0089 -0.0060 0.0023 430 ARG A CG 2735 C CD . ARG A 348 ? 0.2565 0.2713 0.2558 -0.0090 -0.0054 0.0037 430 ARG A CD 2736 N NE . ARG A 348 ? 0.2288 0.2416 0.2284 -0.0096 -0.0050 0.0044 430 ARG A NE 2737 C CZ . ARG A 348 ? 0.3053 0.3180 0.3057 -0.0109 -0.0044 0.0046 430 ARG A CZ 2738 N NH1 . ARG A 348 ? 0.1829 0.1979 0.1840 -0.0114 -0.0040 0.0041 430 ARG A NH1 2739 N NH2 . ARG A 348 ? 0.2740 0.2843 0.2744 -0.0115 -0.0040 0.0052 430 ARG A NH2 2740 N N . GLY A 349 ? 0.3067 0.3163 0.3066 -0.0067 -0.0069 0.0028 431 GLY A N 2741 C CA . GLY A 349 ? 0.2500 0.2579 0.2502 -0.0059 -0.0070 0.0024 431 GLY A CA 2742 C C . GLY A 349 ? 0.2459 0.2536 0.2454 -0.0044 -0.0073 0.0035 431 GLY A C 2743 O O . GLY A 349 ? 0.2729 0.2806 0.2716 -0.0042 -0.0072 0.0048 431 GLY A O 2744 N N . ARG A 350 ? 0.2021 0.2099 0.2019 -0.0033 -0.0076 0.0028 432 ARG A N 2745 C CA . ARG A 350 ? 0.2635 0.2713 0.2631 -0.0018 -0.0079 0.0038 432 ARG A CA 2746 C C . ARG A 350 ? 0.2527 0.2636 0.2519 -0.0014 -0.0084 0.0043 432 ARG A C 2747 O O . ARG A 350 ? 0.2180 0.2309 0.2172 -0.0022 -0.0087 0.0035 432 ARG A O 2748 C CB . ARG A 350 ? 0.2164 0.2234 0.2167 -0.0007 -0.0078 0.0029 432 ARG A CB 2749 C CG . ARG A 350 ? 0.2309 0.2340 0.2312 -0.0008 -0.0072 0.0027 432 ARG A CG 2750 C CD . ARG A 350 ? 0.2952 0.2971 0.2959 0.0005 -0.0070 0.0018 432 ARG A CD 2751 N NE . ARG A 350 ? 0.3420 0.3396 0.3424 0.0002 -0.0064 0.0017 432 ARG A NE 2752 C CZ . ARG A 350 ? 0.3710 0.3660 0.3713 0.0016 -0.0059 0.0014 432 ARG A CZ 2753 N NH1 . ARG A 350 ? 0.3860 0.3827 0.3867 0.0034 -0.0061 0.0012 432 ARG A NH1 2754 N NH2 . ARG A 350 ? 0.3331 0.3238 0.3329 0.0011 -0.0053 0.0012 432 ARG A NH2 2755 N N . PRO A 351 ? 0.2898 0.3011 0.2885 -0.0003 -0.0087 0.0057 433 PRO A N 2756 C CA . PRO A 351 ? 0.2362 0.2451 0.2347 0.0009 -0.0085 0.0069 433 PRO A CA 2757 C C . PRO A 351 ? 0.3214 0.3280 0.3190 0.0003 -0.0080 0.0082 433 PRO A C 2758 O O . PRO A 351 ? 0.2620 0.2657 0.2594 0.0011 -0.0076 0.0091 433 PRO A O 2759 C CB . PRO A 351 ? 0.2945 0.3059 0.2931 0.0024 -0.0091 0.0079 433 PRO A CB 2760 C CG . PRO A 351 ? 0.2823 0.2967 0.2802 0.0014 -0.0096 0.0077 433 PRO A CG 2761 C CD . PRO A 351 ? 0.2227 0.2371 0.2209 -0.0001 -0.0094 0.0061 433 PRO A CD 2762 N N . LYS A 352 ? 0.2697 0.2776 0.2667 -0.0010 -0.0079 0.0083 434 LYS A N 2763 C CA . LYS A 352 ? 0.2857 0.2919 0.2816 -0.0016 -0.0074 0.0097 434 LYS A CA 2764 C C . LYS A 352 ? 0.2883 0.2913 0.2846 -0.0027 -0.0066 0.0094 434 LYS A C 2765 O O . LYS A 352 ? 0.2762 0.2768 0.2718 -0.0028 -0.0060 0.0108 434 LYS A O 2766 C CB . LYS A 352 ? 0.2284 0.2370 0.2234 -0.0027 -0.0074 0.0097 434 LYS A CB 2767 C CG . LYS A 352 ? 0.2854 0.2967 0.2795 -0.0019 -0.0082 0.0104 434 LYS A CG 2768 C CD . LYS A 352 ? 0.3569 0.3673 0.3499 -0.0008 -0.0083 0.0124 434 LYS A CD 2769 C CE . LYS A 352 ? 0.3886 0.4020 0.3805 -0.0002 -0.0092 0.0132 434 LYS A CE 2770 N NZ . LYS A 352 ? 0.4464 0.4618 0.4394 0.0009 -0.0100 0.0125 434 LYS A NZ 2771 N N . GLU A 353 ? 0.2952 0.2981 0.2926 -0.0035 -0.0065 0.0077 435 GLU A N 2772 C CA . GLU A 353 ? 0.2844 0.2847 0.2823 -0.0047 -0.0058 0.0072 435 GLU A CA 2773 C C . GLU A 353 ? 0.3564 0.3550 0.3551 -0.0042 -0.0058 0.0059 435 GLU A C 2774 O O . GLU A 353 ? 0.3592 0.3590 0.3587 -0.0049 -0.0060 0.0043 435 GLU A O 2775 C CB . GLU A 353 ? 0.3829 0.3852 0.3814 -0.0065 -0.0056 0.0063 435 GLU A CB 2776 C CG . GLU A 353 ? 0.3372 0.3412 0.3347 -0.0069 -0.0054 0.0074 435 GLU A CG 2777 C CD . GLU A 353 ? 0.3696 0.3760 0.3678 -0.0081 -0.0052 0.0065 435 GLU A CD 2778 O OE1 . GLU A 353 ? 0.3404 0.3488 0.3391 -0.0079 -0.0057 0.0053 435 GLU A OE1 2779 O OE2 . GLU A 353 ? 0.3598 0.3660 0.3580 -0.0093 -0.0045 0.0071 435 GLU A OE2 2780 N N . ASP A 354 ? 0.3149 0.3107 0.3132 -0.0030 -0.0056 0.0066 436 ASP A N 2781 C CA . ASP A 354 ? 0.3131 0.3074 0.3119 -0.0020 -0.0056 0.0054 436 ASP A CA 2782 C C . ASP A 354 ? 0.3465 0.3370 0.3454 -0.0031 -0.0050 0.0044 436 ASP A C 2783 O O . ASP A 354 ? 0.3431 0.3317 0.3421 -0.0023 -0.0048 0.0034 436 ASP A O 2784 C CB . ASP A 354 ? 0.3863 0.3799 0.3847 0.0004 -0.0057 0.0066 436 ASP A CB 2785 C CG . ASP A 354 ? 0.5094 0.4993 0.5070 0.0009 -0.0052 0.0084 436 ASP A CG 2786 O OD1 . ASP A 354 ? 0.4611 0.4492 0.4582 -0.0008 -0.0046 0.0089 436 ASP A OD1 2787 O OD2 . ASP A 354 ? 0.6314 0.6202 0.6287 0.0030 -0.0052 0.0094 436 ASP A OD2 2788 N N . LYS A 355 ? 0.3501 0.3398 0.3489 -0.0051 -0.0045 0.0046 437 LYS A N 2789 C CA . LYS A 355 ? 0.3312 0.3179 0.3303 -0.0067 -0.0040 0.0034 437 LYS A CA 2790 C C . LYS A 355 ? 0.4075 0.3964 0.4074 -0.0074 -0.0045 0.0011 437 LYS A C 2791 O O . LYS A 355 ? 0.3045 0.2911 0.3044 -0.0081 -0.0043 -0.0003 437 LYS A O 2792 C CB . LYS A 355 ? 0.3738 0.3595 0.3728 -0.0088 -0.0034 0.0042 437 LYS A CB 2793 C CG . LYS A 355 ? 0.4070 0.3888 0.4048 -0.0083 -0.0027 0.0062 437 LYS A CG 2794 C CD . LYS A 355 ? 0.6768 0.6575 0.6745 -0.0106 -0.0020 0.0070 437 LYS A CD 2795 C CE . LYS A 355 ? 0.7413 0.7177 0.7377 -0.0101 -0.0012 0.0091 437 LYS A CE 2796 N NZ . LYS A 355 ? 0.6669 0.6448 0.6624 -0.0080 -0.0016 0.0111 437 LYS A NZ 2797 N N . VAL A 356 ? 0.2921 0.2853 0.2925 -0.0073 -0.0051 0.0009 438 VAL A N 2798 C CA . VAL A 356 ? 0.2390 0.2346 0.2401 -0.0075 -0.0056 -0.0009 438 VAL A CA 2799 C C . VAL A 356 ? 0.3464 0.3430 0.3473 -0.0055 -0.0060 -0.0011 438 VAL A C 2800 O O . VAL A 356 ? 0.3093 0.3058 0.3098 -0.0040 -0.0060 0.0003 438 VAL A O 2801 C CB . VAL A 356 ? 0.2612 0.2606 0.2628 -0.0085 -0.0060 -0.0010 438 VAL A CB 2802 C CG1 . VAL A 356 ? 0.3066 0.3058 0.3087 -0.0106 -0.0057 -0.0009 438 VAL A CG1 2803 C CG2 . VAL A 356 ? 0.2353 0.2369 0.2366 -0.0074 -0.0063 0.0003 438 VAL A CG2 2804 N N . TRP A 357 ? 0.2640 0.2617 0.2651 -0.0054 -0.0063 -0.0027 439 TRP A N 2805 C CA . TRP A 357 ? 0.2287 0.2273 0.2298 -0.0036 -0.0065 -0.0030 439 TRP A CA 2806 C C . TRP A 357 ? 0.2504 0.2531 0.2518 -0.0035 -0.0071 -0.0031 439 TRP A C 2807 O O . TRP A 357 ? 0.2633 0.2675 0.2648 -0.0022 -0.0073 -0.0033 439 TRP A O 2808 C CB . TRP A 357 ? 0.2956 0.2923 0.2965 -0.0035 -0.0062 -0.0047 439 TRP A CB 2809 C CG . TRP A 357 ? 0.4178 0.4099 0.4181 -0.0032 -0.0055 -0.0046 439 TRP A CG 2810 C CD1 . TRP A 357 ? 0.4253 0.4143 0.4253 -0.0048 -0.0051 -0.0049 439 TRP A CD1 2811 C CD2 . TRP A 357 ? 0.4264 0.4164 0.4264 -0.0010 -0.0050 -0.0040 439 TRP A CD2 2812 N NE1 . TRP A 357 ? 0.5534 0.5380 0.5527 -0.0039 -0.0044 -0.0046 439 TRP A NE1 2813 C CE2 . TRP A 357 ? 0.5013 0.4863 0.5006 -0.0014 -0.0043 -0.0040 439 TRP A CE2 2814 C CE3 . TRP A 357 ? 0.4342 0.4260 0.4344 0.0012 -0.0052 -0.0035 439 TRP A CE3 2815 C CZ2 . TRP A 357 ? 0.5896 0.5713 0.5884 0.0006 -0.0037 -0.0035 439 TRP A CZ2 2816 C CZ3 . TRP A 357 ? 0.5160 0.5050 0.5160 0.0032 -0.0046 -0.0030 439 TRP A CZ3 2817 C CH2 . TRP A 357 ? 0.5271 0.5109 0.5263 0.0030 -0.0038 -0.0029 439 TRP A CH2 2818 N N . TRP A 358 ? 0.2151 0.2196 0.2167 -0.0048 -0.0073 -0.0030 440 TRP A N 2819 C CA . TRP A 358 ? 0.2421 0.2500 0.2439 -0.0048 -0.0078 -0.0031 440 TRP A CA 2820 C C . TRP A 358 ? 0.2440 0.2532 0.2455 -0.0045 -0.0079 -0.0017 440 TRP A C 2821 O O . TRP A 358 ? 0.2404 0.2482 0.2416 -0.0044 -0.0077 -0.0005 440 TRP A O 2822 C CB . TRP A 358 ? 0.1998 0.2089 0.2018 -0.0062 -0.0080 -0.0040 440 TRP A CB 2823 C CG . TRP A 358 ? 0.2513 0.2597 0.2538 -0.0076 -0.0077 -0.0037 440 TRP A CG 2824 C CD1 . TRP A 358 ? 0.2767 0.2834 0.2794 -0.0087 -0.0075 -0.0045 440 TRP A CD1 2825 C CD2 . TRP A 358 ? 0.2384 0.2478 0.2410 -0.0081 -0.0076 -0.0027 440 TRP A CD2 2826 N NE1 . TRP A 358 ? 0.1825 0.1892 0.1856 -0.0100 -0.0073 -0.0039 440 TRP A NE1 2827 C CE2 . TRP A 358 ? 0.2716 0.2801 0.2747 -0.0096 -0.0073 -0.0028 440 TRP A CE2 2828 C CE3 . TRP A 358 ? 0.2212 0.2322 0.2234 -0.0076 -0.0076 -0.0017 440 TRP A CE3 2829 C CZ2 . TRP A 358 ? 0.2731 0.2825 0.2765 -0.0104 -0.0069 -0.0018 440 TRP A CZ2 2830 C CZ3 . TRP A 358 ? 0.2249 0.2365 0.2272 -0.0083 -0.0073 -0.0009 440 TRP A CZ3 2831 C CH2 . TRP A 358 ? 0.2728 0.2836 0.2757 -0.0096 -0.0069 -0.0009 440 TRP A CH2 2832 N N . THR A 359 ? 0.2378 0.2496 0.2393 -0.0044 -0.0083 -0.0018 441 THR A N 2833 C CA . THR A 359 ? 0.2297 0.2429 0.2307 -0.0045 -0.0084 -0.0008 441 THR A CA 2834 C C . THR A 359 ? 0.2230 0.2381 0.2240 -0.0052 -0.0086 -0.0014 441 THR A C 2835 O O . THR A 359 ? 0.2343 0.2504 0.2354 -0.0050 -0.0088 -0.0022 441 THR A O 2836 C CB . THR A 359 ? 0.3188 0.3332 0.3195 -0.0034 -0.0087 -0.0002 441 THR A CB 2837 O OG1 . THR A 359 ? 0.2419 0.2546 0.2426 -0.0024 -0.0086 0.0006 441 THR A OG1 2838 C CG2 . THR A 359 ? 0.2274 0.2434 0.2274 -0.0037 -0.0089 0.0005 441 THR A CG2 2839 N N . SER A 360 ? 0.2199 0.2352 0.2207 -0.0058 -0.0084 -0.0009 442 SER A N 2840 C CA . SER A 360 ? 0.1737 0.1906 0.1744 -0.0063 -0.0084 -0.0014 442 SER A CA 2841 C C . SER A 360 ? 0.2876 0.3050 0.2877 -0.0065 -0.0082 -0.0006 442 SER A C 2842 O O . SER A 360 ? 0.2892 0.3061 0.2887 -0.0062 -0.0081 0.0002 442 SER A O 2843 C CB . SER A 360 ? 0.2053 0.2225 0.2070 -0.0070 -0.0084 -0.0021 442 SER A CB 2844 O OG . SER A 360 ? 0.1998 0.2185 0.2014 -0.0070 -0.0085 -0.0025 442 SER A OG 2845 N N . ASN A 361 ? 0.2403 0.2588 0.2406 -0.0068 -0.0080 -0.0009 443 ASN A N 2846 C CA . ASN A 361 ? 0.1904 0.2092 0.1898 -0.0069 -0.0076 -0.0003 443 ASN A CA 2847 C C . ASN A 361 ? 0.2189 0.2388 0.2189 -0.0072 -0.0072 -0.0007 443 ASN A C 2848 O O . ASN A 361 ? 0.2150 0.2355 0.2158 -0.0072 -0.0075 -0.0013 443 ASN A O 2849 C CB . ASN A 361 ? 0.1596 0.1787 0.1577 -0.0065 -0.0078 -0.0003 443 ASN A CB 2850 C CG . ASN A 361 ? 0.2211 0.2408 0.2191 -0.0064 -0.0080 -0.0010 443 ASN A CG 2851 O OD1 . ASN A 361 ? 0.1812 0.2011 0.1797 -0.0062 -0.0084 -0.0015 443 ASN A OD1 2852 N ND2 . ASN A 361 ? 0.1822 0.2022 0.1796 -0.0064 -0.0076 -0.0011 443 ASN A ND2 2853 N N . SER A 362 ? 0.1725 0.1928 0.1720 -0.0073 -0.0066 -0.0002 444 SER A N 2854 C CA . SER A 362 ? 0.1839 0.2053 0.1836 -0.0071 -0.0062 -0.0005 444 SER A CA 2855 C C . SER A 362 ? 0.2394 0.2606 0.2375 -0.0067 -0.0060 -0.0004 444 SER A C 2856 O O . SER A 362 ? 0.1916 0.2119 0.1884 -0.0067 -0.0062 -0.0002 444 SER A O 2857 C CB . SER A 362 ? 0.1812 0.2036 0.1820 -0.0076 -0.0056 -0.0001 444 SER A CB 2858 O OG . SER A 362 ? 0.2686 0.2907 0.2686 -0.0078 -0.0050 0.0006 444 SER A OG 2859 N N . ILE A 363 ? 0.2056 0.2273 0.2035 -0.0063 -0.0054 -0.0007 445 ILE A N 2860 C CA . ILE A 363 ? 0.2416 0.2627 0.2377 -0.0059 -0.0051 -0.0009 445 ILE A CA 2861 C C . ILE A 363 ? 0.2450 0.2667 0.2409 -0.0057 -0.0041 -0.0006 445 ILE A C 2862 O O . ILE A 363 ? 0.2183 0.2414 0.2157 -0.0055 -0.0037 -0.0005 445 ILE A O 2863 C CB . ILE A 363 ? 0.2493 0.2699 0.2451 -0.0053 -0.0052 -0.0014 445 ILE A CB 2864 C CG1 . ILE A 363 ? 0.1757 0.1959 0.1716 -0.0055 -0.0061 -0.0016 445 ILE A CG1 2865 C CG2 . ILE A 363 ? 0.2105 0.2299 0.2042 -0.0050 -0.0047 -0.0017 445 ILE A CG2 2866 C CD1 . ILE A 363 ? 0.1659 0.1858 0.1617 -0.0050 -0.0062 -0.0020 445 ILE A CD1 2867 N N . VAL A 364 ? 0.2036 0.2246 0.1976 -0.0058 -0.0037 -0.0006 446 VAL A N 2868 C CA . VAL A 364 ? 0.2255 0.2468 0.2187 -0.0054 -0.0026 -0.0006 446 VAL A CA 2869 C C . VAL A 364 ? 0.2773 0.2970 0.2681 -0.0051 -0.0024 -0.0013 446 VAL A C 2870 O O . VAL A 364 ? 0.2215 0.2402 0.2111 -0.0056 -0.0031 -0.0015 446 VAL A O 2871 C CB . VAL A 364 ? 0.2235 0.2455 0.2164 -0.0059 -0.0020 0.0001 446 VAL A CB 2872 C CG1 . VAL A 364 ? 0.1214 0.1423 0.1122 -0.0064 -0.0024 0.0003 446 VAL A CG1 2873 C CG2 . VAL A 364 ? 0.1517 0.1744 0.1441 -0.0054 -0.0007 0.0000 446 VAL A CG2 2874 N N . SER A 365 ? 0.2173 0.2368 0.2077 -0.0042 -0.0015 -0.0018 447 SER A N 2875 C CA . SER A 365 ? 0.2413 0.2587 0.2293 -0.0040 -0.0012 -0.0026 447 SER A CA 2876 C C . SER A 365 ? 0.2181 0.2353 0.2048 -0.0033 0.0002 -0.0029 447 SER A C 2877 O O . SER A 365 ? 0.2523 0.2712 0.2405 -0.0026 0.0009 -0.0026 447 SER A O 2878 C CB . SER A 365 ? 0.1938 0.2103 0.1824 -0.0033 -0.0014 -0.0029 447 SER A CB 2879 O OG . SER A 365 ? 0.3019 0.3160 0.2882 -0.0034 -0.0013 -0.0037 447 SER A OG 2880 N N . MET A 366 ? 0.2642 0.2795 0.2480 -0.0037 0.0005 -0.0036 448 MET A N 2881 C CA . MET A 366 ? 0.1844 0.1991 0.1664 -0.0030 0.0018 -0.0042 448 MET A CA 2882 C C . MET A 366 ? 0.3084 0.3201 0.2878 -0.0028 0.0022 -0.0053 448 MET A C 2883 O O . MET A 366 ? 0.2434 0.2536 0.2219 -0.0037 0.0013 -0.0057 448 MET A O 2884 C CB . MET A 366 ? 0.1816 0.1971 0.1620 -0.0039 0.0021 -0.0039 448 MET A CB 2885 C CG . MET A 366 ? 0.2713 0.2889 0.2535 -0.0046 0.0014 -0.0027 448 MET A CG 2886 S SD . MET A 366 ? 0.3457 0.3659 0.3301 -0.0041 0.0025 -0.0019 448 MET A SD 2887 C CE . MET A 366 ? 0.2651 0.2850 0.2465 -0.0039 0.0040 -0.0023 448 MET A CE 2888 N N . CYS A 367 ? 0.2424 0.2531 0.2207 -0.0017 0.0036 -0.0060 449 CYS A N 2889 C CA . CYS A 367 ? 0.2447 0.2520 0.2199 -0.0016 0.0043 -0.0072 449 CYS A CA 2890 C C . CYS A 367 ? 0.3052 0.3121 0.2779 -0.0015 0.0055 -0.0080 449 CYS A C 2891 O O . CYS A 367 ? 0.2524 0.2618 0.2261 -0.0010 0.0062 -0.0074 449 CYS A O 2892 C CB . CYS A 367 ? 0.2712 0.2768 0.2471 0.0000 0.0049 -0.0074 449 CYS A CB 2893 S SG . CYS A 367 ? 0.3261 0.3316 0.3041 -0.0002 0.0035 -0.0068 449 CYS A SG 2894 N N . SER A 368 ? 0.2853 0.2890 0.2546 -0.0020 0.0059 -0.0093 450 SER A N 2895 C CA . SER A 368 ? 0.3227 0.3259 0.2891 -0.0021 0.0071 -0.0102 450 SER A CA 2896 C C . SER A 368 ? 0.2768 0.2793 0.2430 0.0000 0.0090 -0.0107 450 SER A C 2897 O O . SER A 368 ? 0.2436 0.2447 0.2110 0.0014 0.0094 -0.0107 450 SER A O 2898 C CB . SER A 368 ? 0.2614 0.2615 0.2239 -0.0036 0.0068 -0.0117 450 SER A CB 2899 O OG . SER A 368 ? 0.2786 0.2747 0.2398 -0.0030 0.0074 -0.0128 450 SER A OG 2900 N N . SER A 369 ? 0.3466 0.3502 0.3114 0.0002 0.0102 -0.0109 451 SER A N 2901 C CA . SER A 369 ? 0.3355 0.3386 0.2998 0.0022 0.0122 -0.0115 451 SER A CA 2902 C C . SER A 369 ? 0.3377 0.3385 0.2975 0.0018 0.0133 -0.0132 451 SER A C 2903 O O . SER A 369 ? 0.3155 0.3169 0.2734 0.0000 0.0126 -0.0133 451 SER A O 2904 C CB . SER A 369 ? 0.3062 0.3138 0.2735 0.0031 0.0129 -0.0102 451 SER A CB 2905 O OG . SER A 369 ? 0.3229 0.3307 0.2897 0.0050 0.0150 -0.0108 451 SER A OG 2906 N N . THR A 370 ? 0.2824 0.2804 0.2405 0.0034 0.0150 -0.0144 452 THR A N 2907 C CA . THR A 370 ? 0.3093 0.3050 0.2629 0.0031 0.0163 -0.0161 452 THR A CA 2908 C C . THR A 370 ? 0.3666 0.3658 0.3204 0.0039 0.0177 -0.0157 452 THR A C 2909 O O . THR A 370 ? 0.3200 0.3183 0.2702 0.0036 0.0188 -0.0169 452 THR A O 2910 C CB . THR A 370 ? 0.3097 0.3005 0.2608 0.0045 0.0178 -0.0179 452 THR A CB 2911 O OG1 . THR A 370 ? 0.3450 0.3366 0.2989 0.0073 0.0191 -0.0172 452 THR A OG1 2912 C CG2 . THR A 370 ? 0.2860 0.2728 0.2360 0.0032 0.0165 -0.0185 452 THR A CG2 2913 N N . GLU A 371 ? 0.2773 0.2806 0.2353 0.0049 0.0178 -0.0140 453 GLU A N 2914 C CA . GLU A 371 ? 0.3073 0.3145 0.2660 0.0052 0.0189 -0.0132 453 GLU A CA 2915 C C . GLU A 371 ? 0.3006 0.3100 0.2589 0.0029 0.0175 -0.0122 453 GLU A C 2916 O O . GLU A 371 ? 0.3207 0.3292 0.2790 0.0013 0.0155 -0.0119 453 GLU A O 2917 C CB . GLU A 371 ? 0.3056 0.3165 0.2690 0.0069 0.0195 -0.0118 453 GLU A CB 2918 C CG . GLU A 371 ? 0.3455 0.3547 0.3098 0.0095 0.0208 -0.0125 453 GLU A CG 2919 C CD . GLU A 371 ? 0.3737 0.3808 0.3346 0.0110 0.0231 -0.0141 453 GLU A CD 2920 O OE1 . GLU A 371 ? 0.4575 0.4672 0.4176 0.0109 0.0244 -0.0140 453 GLU A OE1 2921 O OE2 . GLU A 371 ? 0.4813 0.4842 0.4404 0.0124 0.0238 -0.0154 453 GLU A OE2 2922 N N . PHE A 372 ? 0.2874 0.2997 0.2452 0.0027 0.0185 -0.0116 454 PHE A N 2923 C CA . PHE A 372 ? 0.2595 0.2742 0.2174 0.0008 0.0173 -0.0103 454 PHE A CA 2924 C C . PHE A 372 ? 0.2894 0.3081 0.2517 0.0011 0.0173 -0.0083 454 PHE A C 2925 O O . PHE A 372 ? 0.3327 0.3542 0.2954 0.0014 0.0188 -0.0077 454 PHE A O 2926 C CB . PHE A 372 ? 0.3089 0.3238 0.2626 0.0001 0.0183 -0.0109 454 PHE A CB 2927 C CG . PHE A 372 ? 0.3656 0.3770 0.3147 -0.0008 0.0179 -0.0128 454 PHE A CG 2928 C CD1 . PHE A 372 ? 0.3322 0.3402 0.2789 0.0004 0.0192 -0.0148 454 PHE A CD1 2929 C CD2 . PHE A 372 ? 0.3828 0.3941 0.3298 -0.0028 0.0161 -0.0125 454 PHE A CD2 2930 C CE1 . PHE A 372 ? 0.3659 0.3703 0.3082 -0.0007 0.0188 -0.0167 454 PHE A CE1 2931 C CE2 . PHE A 372 ? 0.3627 0.3710 0.3056 -0.0039 0.0156 -0.0143 454 PHE A CE2 2932 C CZ . PHE A 372 ? 0.2748 0.2796 0.2152 -0.0030 0.0170 -0.0165 454 PHE A CZ 2933 N N . LEU A 373 ? 0.2664 0.2855 0.2321 0.0010 0.0159 -0.0075 455 LEU A N 2934 C CA . LEU A 373 ? 0.3060 0.3285 0.2762 0.0013 0.0158 -0.0059 455 LEU A CA 2935 C C . LEU A 373 ? 0.2736 0.2984 0.2446 -0.0004 0.0150 -0.0043 455 LEU A C 2936 O O . LEU A 373 ? 0.2690 0.2924 0.2381 -0.0018 0.0136 -0.0041 455 LEU A O 2937 C CB . LEU A 373 ? 0.2515 0.2734 0.2247 0.0017 0.0145 -0.0057 455 LEU A CB 2938 C CG . LEU A 373 ? 0.2867 0.3060 0.2595 0.0034 0.0151 -0.0070 455 LEU A CG 2939 C CD1 . LEU A 373 ? 0.2693 0.2884 0.2450 0.0036 0.0136 -0.0065 455 LEU A CD1 2940 C CD2 . LEU A 373 ? 0.2781 0.2992 0.2517 0.0055 0.0173 -0.0072 455 LEU A CD2 2941 N N . GLY A 374 ? 0.2817 0.3098 0.2554 -0.0003 0.0159 -0.0030 456 GLY A N 2942 C CA . GLY A 374 ? 0.2677 0.2976 0.2426 -0.0019 0.0152 -0.0013 456 GLY A CA 2943 C C . GLY A 374 ? 0.3369 0.3657 0.3135 -0.0028 0.0130 -0.0008 456 GLY A C 2944 O O . GLY A 374 ? 0.2821 0.3099 0.2603 -0.0021 0.0122 -0.0015 456 GLY A O 2945 N N . GLN A 375 ? 0.2586 0.2875 0.2348 -0.0043 0.0120 0.0004 457 GLN A N 2946 C CA . GLN A 375 ? 0.3102 0.3380 0.2878 -0.0050 0.0100 0.0009 457 GLN A CA 2947 C C . GLN A 375 ? 0.2648 0.2944 0.2458 -0.0058 0.0097 0.0024 457 GLN A C 2948 O O . GLN A 375 ? 0.2926 0.3240 0.2741 -0.0063 0.0108 0.0034 457 GLN A O 2949 C CB . GLN A 375 ? 0.2143 0.2403 0.1888 -0.0059 0.0089 0.0010 457 GLN A CB 2950 C CG . GLN A 375 ? 0.3134 0.3404 0.2864 -0.0069 0.0092 0.0025 457 GLN A CG 2951 C CD . GLN A 375 ? 0.3815 0.4072 0.3516 -0.0076 0.0079 0.0027 457 GLN A CD 2952 O OE1 . GLN A 375 ? 0.4193 0.4435 0.3873 -0.0074 0.0073 0.0014 457 GLN A OE1 2953 N NE2 . GLN A 375 ? 0.4955 0.5218 0.4652 -0.0084 0.0076 0.0044 457 GLN A NE2 2954 N N . TRP A 376 ? 0.2347 0.2637 0.2180 -0.0059 0.0084 0.0024 458 TRP A N 2955 C CA . TRP A 376 ? 0.2323 0.2623 0.2184 -0.0068 0.0078 0.0036 458 TRP A CA 2956 C C . TRP A 376 ? 0.2918 0.3198 0.2774 -0.0074 0.0060 0.0039 458 TRP A C 2957 O O . TRP A 376 ? 0.2984 0.3247 0.2816 -0.0072 0.0053 0.0033 458 TRP A O 2958 C CB . TRP A 376 ? 0.2638 0.2954 0.2534 -0.0063 0.0078 0.0033 458 TRP A CB 2959 C CG . TRP A 376 ? 0.2417 0.2755 0.2342 -0.0074 0.0082 0.0044 458 TRP A CG 2960 C CD1 . TRP A 376 ? 0.2556 0.2897 0.2477 -0.0087 0.0086 0.0057 458 TRP A CD1 2961 C CD2 . TRP A 376 ? 0.2676 0.3035 0.2636 -0.0074 0.0081 0.0043 458 TRP A CD2 2962 N NE1 . TRP A 376 ? 0.2482 0.2843 0.2434 -0.0096 0.0089 0.0063 458 TRP A NE1 2963 C CE2 . TRP A 376 ? 0.2835 0.3209 0.2811 -0.0089 0.0085 0.0054 458 TRP A CE2 2964 C CE3 . TRP A 376 ? 0.2406 0.2774 0.2385 -0.0063 0.0076 0.0034 458 TRP A CE3 2965 C CZ2 . TRP A 376 ? 0.2832 0.3232 0.2844 -0.0095 0.0084 0.0056 458 TRP A CZ2 2966 C CZ3 . TRP A 376 ? 0.2633 0.3027 0.2645 -0.0067 0.0075 0.0036 458 TRP A CZ3 2967 C CH2 . TRP A 376 ? 0.2552 0.2963 0.2581 -0.0084 0.0079 0.0046 458 TRP A CH2 2968 N N . ASN A 377 ? 0.2659 0.2939 0.2536 -0.0082 0.0054 0.0048 459 ASN A N 2969 C CA . ASN A 377 ? 0.2705 0.2968 0.2583 -0.0085 0.0038 0.0050 459 ASN A CA 2970 C C . ASN A 377 ? 0.2756 0.3021 0.2664 -0.0085 0.0031 0.0046 459 ASN A C 2971 O O . ASN A 377 ? 0.2865 0.3148 0.2796 -0.0088 0.0037 0.0048 459 ASN A O 2972 C CB . ASN A 377 ? 0.2272 0.2527 0.2142 -0.0094 0.0035 0.0065 459 ASN A CB 2973 C CG . ASN A 377 ? 0.2673 0.2936 0.2566 -0.0103 0.0041 0.0075 459 ASN A CG 2974 O OD1 . ASN A 377 ? 0.2530 0.2787 0.2444 -0.0108 0.0034 0.0076 459 ASN A OD1 2975 N ND2 . ASN A 377 ? 0.2777 0.3056 0.2668 -0.0108 0.0056 0.0081 459 ASN A ND2 2976 N N . TRP A 378 ? 0.2165 0.2417 0.2074 -0.0083 0.0018 0.0041 460 TRP A N 2977 C CA . TRP A 378 ? 0.2516 0.2771 0.2450 -0.0081 0.0011 0.0035 460 TRP A CA 2978 C C . TRP A 378 ? 0.2119 0.2361 0.2061 -0.0086 -0.0001 0.0038 460 TRP A C 2979 O O . TRP A 378 ? 0.2550 0.2779 0.2483 -0.0082 -0.0011 0.0034 460 TRP A O 2980 C CB . TRP A 378 ? 0.1614 0.1865 0.1541 -0.0071 0.0009 0.0023 460 TRP A CB 2981 C CG . TRP A 378 ? 0.2231 0.2492 0.2152 -0.0063 0.0022 0.0018 460 TRP A CG 2982 C CD1 . TRP A 378 ? 0.2513 0.2768 0.2407 -0.0060 0.0029 0.0015 460 TRP A CD1 2983 C CD2 . TRP A 378 ? 0.2283 0.2564 0.2225 -0.0057 0.0029 0.0016 460 TRP A CD2 2984 N NE1 . TRP A 378 ? 0.1919 0.2185 0.1815 -0.0051 0.0042 0.0010 460 TRP A NE1 2985 C CE2 . TRP A 378 ? 0.1962 0.2247 0.1889 -0.0048 0.0042 0.0011 460 TRP A CE2 2986 C CE3 . TRP A 378 ? 0.2032 0.2331 0.2004 -0.0058 0.0026 0.0017 460 TRP A CE3 2987 C CZ2 . TRP A 378 ? 0.1765 0.2070 0.1708 -0.0039 0.0052 0.0009 460 TRP A CZ2 2988 C CZ3 . TRP A 378 ? 0.2281 0.2603 0.2269 -0.0049 0.0035 0.0015 460 TRP A CZ3 2989 C CH2 . TRP A 378 ? 0.1917 0.2242 0.1891 -0.0039 0.0048 0.0011 460 TRP A CH2 2990 N N . PRO A 379 ? 0.2942 0.3186 0.2900 -0.0095 0.0000 0.0046 461 PRO A N 2991 C CA . PRO A 379 ? 0.2755 0.2983 0.2719 -0.0098 -0.0010 0.0049 461 PRO A CA 2992 C C . PRO A 379 ? 0.2526 0.2756 0.2508 -0.0097 -0.0017 0.0039 461 PRO A C 2993 O O . PRO A 379 ? 0.2347 0.2594 0.2341 -0.0094 -0.0014 0.0032 461 PRO A O 2994 C CB . PRO A 379 ? 0.2383 0.2609 0.2355 -0.0110 -0.0003 0.0059 461 PRO A CB 2995 C CG . PRO A 379 ? 0.3526 0.3770 0.3495 -0.0112 0.0010 0.0063 461 PRO A CG 2996 C CD . PRO A 379 ? 0.2455 0.2714 0.2424 -0.0102 0.0012 0.0052 461 PRO A CD 2997 N N . ASP A 380 ? 0.2447 0.2662 0.2431 -0.0097 -0.0026 0.0038 462 ASP A N 2998 C CA . ASP A 380 ? 0.2386 0.2603 0.2386 -0.0097 -0.0033 0.0029 462 ASP A CA 2999 C C . ASP A 380 ? 0.2567 0.2798 0.2588 -0.0106 -0.0029 0.0028 462 ASP A C 3000 O O . ASP A 380 ? 0.2115 0.2363 0.2149 -0.0105 -0.0030 0.0021 462 ASP A O 3001 C CB . ASP A 380 ? 0.2459 0.2657 0.2458 -0.0096 -0.0041 0.0029 462 ASP A CB 3002 C CG . ASP A 380 ? 0.2591 0.2791 0.2607 -0.0099 -0.0046 0.0020 462 ASP A CG 3003 O OD1 . ASP A 380 ? 0.2526 0.2736 0.2545 -0.0094 -0.0051 0.0012 462 ASP A OD1 3004 O OD2 . ASP A 380 ? 0.2464 0.2654 0.2488 -0.0107 -0.0046 0.0022 462 ASP A OD2 3005 N N . GLY A 381 ? 0.2109 0.2332 0.2132 -0.0116 -0.0024 0.0037 463 GLY A N 3006 C CA . GLY A 381 ? 0.2366 0.2603 0.2407 -0.0129 -0.0018 0.0038 463 GLY A CA 3007 C C . GLY A 381 ? 0.2518 0.2745 0.2572 -0.0140 -0.0023 0.0033 463 GLY A C 3008 O O . GLY A 381 ? 0.2237 0.2476 0.2308 -0.0153 -0.0019 0.0034 463 GLY A O 3009 N N . ALA A 382 ? 0.1879 0.2086 0.1928 -0.0134 -0.0032 0.0029 464 ALA A N 3010 C CA . ALA A 382 ? 0.2187 0.2379 0.2245 -0.0144 -0.0036 0.0023 464 ALA A CA 3011 C C . ALA A 382 ? 0.2282 0.2444 0.2334 -0.0152 -0.0031 0.0032 464 ALA A C 3012 O O . ALA A 382 ? 0.2377 0.2524 0.2413 -0.0145 -0.0029 0.0043 464 ALA A O 3013 C CB . ALA A 382 ? 0.1716 0.1900 0.1771 -0.0134 -0.0046 0.0013 464 ALA A CB 3014 N N . LYS A 383 ? 0.2785 0.2938 0.2847 -0.0168 -0.0030 0.0029 465 LYS A N 3015 C CA . LYS A 383 ? 0.2699 0.2816 0.2755 -0.0176 -0.0026 0.0037 465 LYS A CA 3016 C C . LYS A 383 ? 0.3112 0.3200 0.3164 -0.0171 -0.0033 0.0028 465 LYS A C 3017 O O . LYS A 383 ? 0.2612 0.2703 0.2674 -0.0179 -0.0037 0.0014 465 LYS A O 3018 C CB . LYS A 383 ? 0.3068 0.3188 0.3136 -0.0198 -0.0018 0.0039 465 LYS A CB 3019 C CG . LYS A 383 ? 0.3739 0.3895 0.3815 -0.0203 -0.0011 0.0046 465 LYS A CG 3020 C CD . LYS A 383 ? 0.5087 0.5256 0.5180 -0.0227 -0.0005 0.0045 465 LYS A CD 3021 C CE . LYS A 383 ? 0.5757 0.5894 0.5843 -0.0242 0.0005 0.0058 465 LYS A CE 3022 N NZ . LYS A 383 ? 0.7265 0.7420 0.7347 -0.0242 0.0016 0.0073 465 LYS A NZ 3023 N N . ILE A 384 ? 0.3070 0.3133 0.3107 -0.0157 -0.0034 0.0035 466 ILE A N 3024 C CA . ILE A 384 ? 0.3187 0.3223 0.3219 -0.0149 -0.0038 0.0028 466 ILE A CA 3025 C C . ILE A 384 ? 0.3059 0.3068 0.3096 -0.0165 -0.0036 0.0021 466 ILE A C 3026 O O . ILE A 384 ? 0.2940 0.2940 0.2979 -0.0163 -0.0041 0.0007 466 ILE A O 3027 C CB . ILE A 384 ? 0.3920 0.3932 0.3937 -0.0133 -0.0038 0.0042 466 ILE A CB 3028 C CG1 . ILE A 384 ? 0.4124 0.4162 0.4134 -0.0119 -0.0042 0.0047 466 ILE A CG1 3029 C CG2 . ILE A 384 ? 0.4910 0.4896 0.4924 -0.0122 -0.0042 0.0034 466 ILE A CG2 3030 C CD1 . ILE A 384 ? 0.5280 0.5338 0.5294 -0.0109 -0.0050 0.0034 466 ILE A CD1 3031 N N . GLU A 385 ? 0.2619 0.2615 0.2658 -0.0181 -0.0028 0.0029 467 GLU A N 3032 C CA . GLU A 385 ? 0.3793 0.3757 0.3834 -0.0199 -0.0024 0.0023 467 GLU A CA 3033 C C . GLU A 385 ? 0.3068 0.3052 0.3122 -0.0212 -0.0030 0.0003 467 GLU A C 3034 O O . GLU A 385 ? 0.3057 0.3015 0.3111 -0.0222 -0.0030 -0.0009 467 GLU A O 3035 C CB . GLU A 385 ? 0.3621 0.3573 0.3663 -0.0217 -0.0014 0.0037 467 GLU A CB 3036 C CG . GLU A 385 ? 0.5100 0.5097 0.5154 -0.0228 -0.0011 0.0041 467 GLU A CG 3037 C CD . GLU A 385 ? 0.6985 0.6989 0.7028 -0.0218 -0.0005 0.0060 467 GLU A CD 3038 O OE1 . GLU A 385 ? 0.6900 0.6911 0.6946 -0.0233 0.0004 0.0071 467 GLU A OE1 3039 O OE2 . GLU A 385 ? 0.5432 0.5437 0.5463 -0.0196 -0.0009 0.0065 467 GLU A OE2 3040 N N . TYR A 386 ? 0.2678 0.2709 0.2744 -0.0211 -0.0034 -0.0001 468 TYR A N 3041 C CA . TYR A 386 ? 0.3213 0.3271 0.3292 -0.0222 -0.0041 -0.0018 468 TYR A CA 3042 C C . TYR A 386 ? 0.3486 0.3534 0.3559 -0.0211 -0.0049 -0.0033 468 TYR A C 3043 O O . TYR A 386 ? 0.2591 0.2647 0.2670 -0.0222 -0.0054 -0.0049 468 TYR A O 3044 C CB . TYR A 386 ? 0.2166 0.2277 0.2258 -0.0220 -0.0043 -0.0017 468 TYR A CB 3045 C CG . TYR A 386 ? 0.3305 0.3436 0.3409 -0.0235 -0.0035 -0.0007 468 TYR A CG 3046 C CD1 . TYR A 386 ? 0.3490 0.3599 0.3596 -0.0256 -0.0028 -0.0003 468 TYR A CD1 3047 C CD2 . TYR A 386 ? 0.2671 0.2844 0.2784 -0.0228 -0.0034 -0.0002 468 TYR A CD2 3048 C CE1 . TYR A 386 ? 0.3131 0.3261 0.3248 -0.0271 -0.0020 0.0007 468 TYR A CE1 3049 C CE2 . TYR A 386 ? 0.2766 0.2962 0.2890 -0.0241 -0.0026 0.0007 468 TYR A CE2 3050 C CZ . TYR A 386 ? 0.3207 0.3384 0.3334 -0.0263 -0.0018 0.0011 468 TYR A CZ 3051 O OH . TYR A 386 ? 0.3134 0.3336 0.3273 -0.0277 -0.0009 0.0021 468 TYR A OH 3052 N N . PHE A 387 ? 0.2386 0.2422 0.2447 -0.0189 -0.0050 -0.0028 469 PHE A N 3053 C CA . PHE A 387 ? 0.2951 0.2981 0.3006 -0.0176 -0.0057 -0.0040 469 PHE A CA 3054 C C . PHE A 387 ? 0.3543 0.3525 0.3587 -0.0176 -0.0053 -0.0046 469 PHE A C 3055 O O . PHE A 387 ? 0.3790 0.3764 0.3828 -0.0164 -0.0057 -0.0056 469 PHE A O 3056 C CB . PHE A 387 ? 0.2452 0.2495 0.2501 -0.0153 -0.0059 -0.0033 469 PHE A CB 3057 C CG . PHE A 387 ? 0.2902 0.2988 0.2958 -0.0151 -0.0063 -0.0032 469 PHE A CG 3058 C CD1 . PHE A 387 ? 0.2488 0.2590 0.2547 -0.0152 -0.0059 -0.0019 469 PHE A CD1 3059 C CD2 . PHE A 387 ? 0.2557 0.2666 0.2615 -0.0145 -0.0070 -0.0043 469 PHE A CD2 3060 C CE1 . PHE A 387 ? 0.2505 0.2642 0.2569 -0.0148 -0.0061 -0.0019 469 PHE A CE1 3061 C CE2 . PHE A 387 ? 0.2965 0.3109 0.3029 -0.0141 -0.0073 -0.0041 469 PHE A CE2 3062 C CZ . PHE A 387 ? 0.2390 0.2547 0.2457 -0.0142 -0.0068 -0.0029 469 PHE A CZ 3063 N N . LEU A 388 ? 0.3576 0.3527 0.3618 -0.0188 -0.0046 -0.0038 470 LEU A N 3064 C CA . LEU A 388 ? 0.4178 0.4076 0.4208 -0.0185 -0.0041 -0.0041 470 LEU A CA 3065 C C . LEU A 388 ? 0.4787 0.4667 0.4817 -0.0205 -0.0041 -0.0060 470 LEU A C 3066 O O . LEU A 388 ? 0.4988 0.4898 0.5030 -0.0224 -0.0045 -0.0070 470 LEU A O 3067 C CB . LEU A 388 ? 0.4551 0.4417 0.4575 -0.0188 -0.0032 -0.0022 470 LEU A CB 3068 C CG . LEU A 388 ? 0.4858 0.4736 0.4877 -0.0167 -0.0031 -0.0002 470 LEU A CG 3069 C CD1 . LEU A 388 ? 0.4415 0.4253 0.4423 -0.0167 -0.0022 0.0017 470 LEU A CD1 3070 C CD2 . LEU A 388 ? 0.4240 0.4124 0.4254 -0.0142 -0.0037 -0.0006 470 LEU A CD2 3071 O OXT . LEU A 388 ? 0.5913 0.5750 0.5932 -0.0201 -0.0038 -0.0068 470 LEU A OXT 3072 C C1 . NAG B . ? 0.7053 0.6283 0.6437 -0.0171 0.0110 -0.0135 501 NAG A C1 3073 C C2 . NAG B . ? 0.7498 0.6689 0.6878 -0.0132 0.0123 -0.0119 501 NAG A C2 3074 C C3 . NAG B . ? 0.8260 0.7407 0.7628 -0.0138 0.0128 -0.0104 501 NAG A C3 3075 C C4 . NAG B . ? 0.8601 0.7686 0.7932 -0.0176 0.0136 -0.0120 501 NAG A C4 3076 C C5 . NAG B . ? 0.8640 0.7778 0.7982 -0.0214 0.0121 -0.0134 501 NAG A C5 3077 C C6 . NAG B . ? 0.7497 0.6586 0.6807 -0.0258 0.0126 -0.0149 501 NAG A C6 3078 C C7 . NAG B . ? 0.8076 0.7320 0.7494 -0.0064 0.0124 -0.0104 501 NAG A C7 3079 C C8 . NAG B . ? 0.7033 0.6345 0.6490 -0.0037 0.0115 -0.0090 501 NAG A C8 3080 N N2 . NAG B . ? 0.7255 0.6506 0.6672 -0.0100 0.0115 -0.0105 501 NAG A N2 3081 O O3 . NAG B . ? 0.8199 0.7307 0.7561 -0.0100 0.0140 -0.0090 501 NAG A O3 3082 O O4 . NAG B . ? 0.8785 0.7830 0.8105 -0.0184 0.0141 -0.0104 501 NAG A O4 3083 O O5 . NAG B . ? 0.6919 0.6094 0.6269 -0.0206 0.0116 -0.0148 501 NAG A O5 3084 O O6 . NAG B . ? 0.8634 0.7672 0.7909 -0.0264 0.0136 -0.0172 501 NAG A O6 3085 O O7 . NAG B . ? 0.8222 0.7406 0.7611 -0.0054 0.0140 -0.0115 501 NAG A O7 3086 C C1 . NAG C . ? 0.5668 0.5579 0.5661 -0.0006 -0.0049 -0.0091 502 NAG A C1 3087 C C2 . NAG C . ? 0.6299 0.6165 0.6285 -0.0021 -0.0044 -0.0101 502 NAG A C2 3088 C C3 . NAG C . ? 0.7030 0.6849 0.7010 -0.0005 -0.0035 -0.0095 502 NAG A C3 3089 C C4 . NAG C . ? 0.6742 0.6563 0.6720 0.0019 -0.0031 -0.0103 502 NAG A C4 3090 C C5 . NAG C . ? 0.7006 0.6880 0.6995 0.0031 -0.0037 -0.0094 502 NAG A C5 3091 C C6 . NAG C . ? 0.7577 0.7460 0.7565 0.0052 -0.0032 -0.0103 502 NAG A C6 3092 C C7 . NAG C . ? 0.6363 0.6231 0.6350 -0.0064 -0.0049 -0.0108 502 NAG A C7 3093 C C8 . NAG C . ? 0.5426 0.5311 0.5421 -0.0084 -0.0054 -0.0100 502 NAG A C8 3094 N N2 . NAG C . ? 0.6122 0.5990 0.6111 -0.0042 -0.0047 -0.0094 502 NAG A N2 3095 O O3 . NAG C . ? 0.7221 0.6995 0.7192 -0.0021 -0.0030 -0.0105 502 NAG A O3 3096 O O4 . NAG C . ? 0.8897 0.8677 0.8871 0.0038 -0.0022 -0.0096 502 NAG A O4 3097 O O5 . NAG C . ? 0.6255 0.6167 0.6247 0.0014 -0.0045 -0.0097 502 NAG A O5 3098 O O6 . NAG C . ? 0.7739 0.7664 0.7737 0.0066 -0.0036 -0.0091 502 NAG A O6 3099 O O7 . NAG C . ? 0.5642 0.5498 0.5622 -0.0068 -0.0048 -0.0127 502 NAG A O7 3100 C C1 . NAG D . ? 0.3744 0.4494 0.3872 -0.0106 -0.0035 -0.0024 503 NAG A C1 3101 C C2 . NAG D . ? 0.3870 0.4663 0.4021 -0.0083 -0.0027 -0.0025 503 NAG A C2 3102 C C3 . NAG D . ? 0.3503 0.4337 0.3661 -0.0094 -0.0014 -0.0024 503 NAG A C3 3103 C C4 . NAG D . ? 0.3461 0.4258 0.3590 -0.0109 -0.0007 -0.0026 503 NAG A C4 3104 C C5 . NAG D . ? 0.2913 0.3667 0.3023 -0.0130 -0.0017 -0.0023 503 NAG A C5 3105 C C6 . NAG D . ? 0.2870 0.3586 0.2950 -0.0143 -0.0011 -0.0022 503 NAG A C6 3106 C C7 . NAG D . ? 0.5023 0.5851 0.5210 -0.0044 -0.0037 -0.0023 503 NAG A C7 3107 C C8 . NAG D . ? 0.3768 0.4634 0.3978 -0.0036 -0.0046 -0.0016 503 NAG A C8 3108 N N2 . NAG D . ? 0.3268 0.4098 0.3445 -0.0073 -0.0035 -0.0021 503 NAG A N2 3109 O O3 . NAG D . ? 0.3486 0.4350 0.3660 -0.0069 -0.0005 -0.0028 503 NAG A O3 3110 O O4 . NAG D . ? 0.3902 0.4739 0.4038 -0.0124 0.0004 -0.0022 503 NAG A O4 3111 O O5 . NAG D . ? 0.3278 0.3999 0.3384 -0.0116 -0.0027 -0.0025 503 NAG A O5 3112 O O6 . NAG D . ? 0.2809 0.3505 0.2879 -0.0123 -0.0006 -0.0028 503 NAG A O6 3113 O O7 . NAG D . ? 0.4266 0.5064 0.4443 -0.0025 -0.0031 -0.0029 503 NAG A O7 3114 C C1 . NAG E . ? 0.3210 0.4042 0.3334 -0.0113 0.0017 -0.0027 504 NAG A C1 3115 C C2 . NAG E . ? 0.2627 0.3479 0.2744 -0.0138 0.0028 -0.0021 504 NAG A C2 3116 C C3 . NAG E . ? 0.2868 0.3707 0.2966 -0.0126 0.0040 -0.0025 504 NAG A C3 3117 C C4 . NAG E . ? 0.3436 0.4302 0.3550 -0.0096 0.0047 -0.0034 504 NAG A C4 3118 C C5 . NAG E . ? 0.3431 0.4278 0.3555 -0.0075 0.0034 -0.0039 504 NAG A C5 3119 C C6 . NAG E . ? 0.2751 0.3623 0.2892 -0.0043 0.0041 -0.0046 504 NAG A C6 3120 C C7 . NAG E . ? 0.3418 0.4259 0.3529 -0.0189 0.0018 -0.0010 504 NAG A C7 3121 C C8 . NAG E . ? 0.2522 0.3320 0.2610 -0.0216 0.0014 -0.0005 504 NAG A C8 3122 N N2 . NAG E . ? 0.2451 0.3270 0.2549 -0.0166 0.0022 -0.0015 504 NAG A N2 3123 O O3 . NAG E . ? 0.2825 0.3681 0.2914 -0.0148 0.0051 -0.0019 504 NAG A O3 3124 O O4 . NAG E . ? 0.2906 0.3753 0.2998 -0.0086 0.0056 -0.0040 504 NAG A O4 3125 O O5 . NAG E . ? 0.2779 0.3641 0.2921 -0.0086 0.0023 -0.0032 504 NAG A O5 3126 O O6 . NAG E . ? 0.5026 0.5962 0.5194 -0.0045 0.0051 -0.0042 504 NAG A O6 3127 O O7 . NAG E . ? 0.3236 0.4132 0.3376 -0.0188 0.0018 -0.0009 504 NAG A O7 3128 C C1 . BMA F . ? 0.3564 0.4457 0.3664 -0.0080 0.0072 -0.0042 505 BMA A C1 3129 C C2 . BMA F . ? 0.3172 0.4039 0.3248 -0.0062 0.0080 -0.0052 505 BMA A C2 3130 C C3 . BMA F . ? 0.3475 0.4386 0.3553 -0.0056 0.0099 -0.0055 505 BMA A C3 3131 C C4 . BMA F . ? 0.3346 0.4291 0.3427 -0.0084 0.0107 -0.0043 505 BMA A C4 3132 C C5 . BMA F . ? 0.3813 0.4782 0.3921 -0.0101 0.0098 -0.0033 505 BMA A C5 3133 C C6 . BMA F . ? 0.3090 0.4085 0.3196 -0.0134 0.0106 -0.0022 505 BMA A C6 3134 O O2 . BMA F . ? 0.2646 0.3467 0.2688 -0.0077 0.0075 -0.0049 505 BMA A O2 3135 O O3 . BMA F . ? 0.3447 0.4325 0.3493 -0.0046 0.0104 -0.0065 505 BMA A O3 3136 O O4 . BMA F . ? 0.3967 0.4964 0.4057 -0.0077 0.0125 -0.0045 505 BMA A O4 3137 O O5 . BMA F . ? 0.3196 0.4113 0.3293 -0.0107 0.0081 -0.0032 505 BMA A O5 3138 O O6 . BMA F . ? 0.4216 0.5247 0.4351 -0.0150 0.0100 -0.0015 505 BMA A O6 3139 C C1 . MAN G . ? 0.3723 0.4628 0.3776 -0.0021 0.0117 -0.0077 506 MAN A C1 3140 C C2 . MAN G . ? 0.3422 0.4299 0.3440 -0.0014 0.0124 -0.0087 506 MAN A C2 3141 C C3 . MAN G . ? 0.3493 0.4311 0.3492 -0.0007 0.0109 -0.0094 506 MAN A C3 3142 C C4 . MAN G . ? 0.3407 0.4219 0.3429 0.0017 0.0104 -0.0104 506 MAN A C4 3143 C C5 . MAN G . ? 0.3472 0.4316 0.3529 0.0012 0.0099 -0.0092 506 MAN A C5 3144 C C6 . MAN G . ? 0.4029 0.4871 0.4109 0.0038 0.0095 -0.0098 506 MAN A C6 3145 O O2 . MAN G . ? 0.4455 0.5364 0.4483 0.0010 0.0139 -0.0099 506 MAN A O2 3146 O O3 . MAN G . ? 0.1899 0.2688 0.1863 -0.0004 0.0112 -0.0104 506 MAN A O3 3147 O O4 . MAN G . ? 0.4100 0.4858 0.4107 0.0021 0.0090 -0.0109 506 MAN A O4 3148 O O5 . MAN G . ? 0.2878 0.3779 0.2952 0.0004 0.0112 -0.0085 506 MAN A O5 3149 O O6 . MAN G . ? 0.5291 0.6143 0.5394 0.0029 0.0082 -0.0086 506 MAN A O6 3150 C C1 . MAN H . ? 0.4257 0.5156 0.4253 0.0017 0.0151 -0.0110 507 MAN A C1 3151 C C2 . MAN H . ? 0.3772 0.4706 0.3783 0.0044 0.0168 -0.0123 507 MAN A C2 3152 C C3 . MAN H . ? 0.4221 0.5222 0.4258 0.0037 0.0182 -0.0113 507 MAN A C3 3153 C C4 . MAN H . ? 0.4215 0.5226 0.4227 0.0011 0.0189 -0.0103 507 MAN A C4 3154 C C5 . MAN H . ? 0.4840 0.5809 0.4836 -0.0015 0.0172 -0.0091 507 MAN A C5 3155 C C6 . MAN H . ? 0.3741 0.4715 0.3711 -0.0040 0.0179 -0.0079 507 MAN A C6 3156 O O2 . MAN H . ? 0.4183 0.5098 0.4160 0.0052 0.0177 -0.0138 507 MAN A O2 3157 O O3 . MAN H . ? 0.3703 0.4739 0.3754 0.0064 0.0199 -0.0124 507 MAN A O3 3158 O O4 . MAN H . ? 0.4315 0.5389 0.4352 0.0000 0.0203 -0.0092 507 MAN A O4 3159 O O5 . MAN H . ? 0.4087 0.4998 0.4062 -0.0005 0.0158 -0.0101 507 MAN A O5 3160 O O6 . MAN H . ? 0.3927 0.4893 0.3864 -0.0031 0.0190 -0.0089 507 MAN A O6 3161 C C1 . MAN I . ? 0.3743 0.4620 0.3714 0.0077 0.0173 -0.0156 508 MAN A C1 3162 C C2 . MAN I . ? 0.4092 0.4960 0.4027 0.0085 0.0186 -0.0173 508 MAN A C2 3163 C C3 . MAN I . ? 0.3843 0.4685 0.3742 0.0061 0.0178 -0.0167 508 MAN A C3 3164 C C4 . MAN I . ? 0.4030 0.4820 0.3923 0.0055 0.0156 -0.0166 508 MAN A C4 3165 C C5 . MAN I . ? 0.3492 0.4287 0.3420 0.0049 0.0145 -0.0151 508 MAN A C5 3166 C C6 . MAN I . ? 0.4102 0.4846 0.4026 0.0045 0.0124 -0.0151 508 MAN A C6 3167 O O2 . MAN I . ? 0.3668 0.4502 0.3597 0.0109 0.0186 -0.0193 508 MAN A O2 3168 O O3 . MAN I . ? 0.3615 0.4452 0.3478 0.0067 0.0189 -0.0182 508 MAN A O3 3169 O O4 . MAN I . ? 0.3144 0.3914 0.3006 0.0034 0.0148 -0.0159 508 MAN A O4 3170 O O5 . MAN I . ? 0.4386 0.5211 0.4348 0.0070 0.0153 -0.0155 508 MAN A O5 3171 O O6 . MAN I . ? 0.3855 0.4568 0.3774 0.0065 0.0123 -0.0169 508 MAN A O6 3172 C C1 . MAN J . ? 0.4385 0.5485 0.4555 -0.0138 0.0110 -0.0016 509 MAN A C1 3173 C C2 . MAN J . ? 0.3955 0.5096 0.4158 -0.0153 0.0100 -0.0010 509 MAN A C2 3174 C C3 . MAN J . ? 0.4182 0.5326 0.4378 -0.0195 0.0101 0.0000 509 MAN A C3 3175 C C4 . MAN J . ? 0.4054 0.5229 0.4244 -0.0206 0.0121 0.0005 509 MAN A C4 3176 C C5 . MAN J . ? 0.4121 0.5255 0.4278 -0.0187 0.0130 -0.0001 509 MAN A C5 3177 C C6 . MAN J . ? 0.4772 0.5934 0.4918 -0.0197 0.0150 0.0003 509 MAN A C6 3178 O O2 . MAN J . ? 0.3661 0.4873 0.3900 -0.0137 0.0108 -0.0011 509 MAN A O2 3179 O O3 . MAN J . ? 0.4624 0.5811 0.4850 -0.0210 0.0092 0.0005 509 MAN A O3 3180 O O4 . MAN J . ? 0.4313 0.5478 0.4490 -0.0246 0.0123 0.0015 509 MAN A O4 3181 O O5 . MAN J . ? 0.4037 0.5175 0.4205 -0.0149 0.0128 -0.0013 509 MAN A O5 3182 O O6 . MAN J . ? 0.5856 0.7095 0.6039 -0.0190 0.0162 0.0003 509 MAN A O6 3183 C C1 . MAN K . ? 0.6138 0.7411 0.6313 -0.0199 0.0183 0.0007 510 MAN A C1 3184 C C2 . MAN K . ? 0.7273 0.8629 0.7489 -0.0182 0.0195 0.0004 510 MAN A C2 3185 C C3 . MAN K . ? 0.7780 0.9182 0.8035 -0.0201 0.0185 0.0010 510 MAN A C3 3186 C C4 . MAN K . ? 0.6705 0.8105 0.6950 -0.0249 0.0187 0.0023 510 MAN A C4 3187 C C5 . MAN K . ? 0.7043 0.8353 0.7242 -0.0262 0.0178 0.0026 510 MAN A C5 3188 C C6 . MAN K . ? 0.7564 0.8861 0.7747 -0.0307 0.0182 0.0039 510 MAN A C6 3189 O O2 . MAN K . ? 0.6582 0.7978 0.6794 -0.0191 0.0217 0.0008 510 MAN A O2 3190 O O3 . MAN K . ? 0.7712 0.9197 0.8009 -0.0185 0.0195 0.0009 510 MAN A O3 3191 O O4 . MAN K . ? 0.7052 0.8486 0.7328 -0.0269 0.0175 0.0028 510 MAN A O4 3192 O O5 . MAN K . ? 0.6404 0.7679 0.6571 -0.0239 0.0187 0.0020 510 MAN A O5 3193 O O6 . MAN K . ? 0.8263 0.9478 0.8401 -0.0313 0.0177 0.0041 510 MAN A O6 3194 C C1 . MAN L . ? 0.5381 0.6521 0.5591 -0.0234 0.0078 0.0008 511 MAN A C1 3195 C C2 . MAN L . ? 0.6397 0.7587 0.6636 -0.0259 0.0070 0.0012 511 MAN A C2 3196 C C3 . MAN L . ? 0.6561 0.7793 0.6834 -0.0232 0.0060 0.0009 511 MAN A C3 3197 C C4 . MAN L . ? 0.6693 0.7866 0.6950 -0.0205 0.0047 0.0003 511 MAN A C4 3198 C C5 . MAN L . ? 0.5043 0.6165 0.5271 -0.0186 0.0056 -0.0002 511 MAN A C5 3199 C C6 . MAN L . ? 0.5018 0.6080 0.5229 -0.0163 0.0044 -0.0008 511 MAN A C6 3200 O O2 . MAN L . ? 0.5386 0.6529 0.5605 -0.0287 0.0059 0.0015 511 MAN A O2 3201 O O3 . MAN L . ? 0.5732 0.7008 0.6029 -0.0255 0.0050 0.0013 511 MAN A O3 3202 O O4 . MAN L . ? 0.5408 0.6619 0.5695 -0.0177 0.0040 0.0001 511 MAN A O4 3203 O O5 . MAN L . ? 0.5411 0.6500 0.5610 -0.0213 0.0064 0.0002 511 MAN A O5 3204 O O6 . MAN L . ? 0.4727 0.5754 0.4916 -0.0143 0.0053 -0.0014 511 MAN A O6 3205 CA CA . CA M . ? 0.5215 0.5702 0.5064 -0.0090 -0.0190 0.0061 512 CA A CA 3206 C C2 . BCZ N . ? 0.2444 0.2754 0.2429 -0.0051 -0.0117 0.0001 513 BCZ A C2 3207 N N25 . BCZ N . ? 0.1713 0.2016 0.1690 -0.0063 -0.0114 -0.0007 513 BCZ A N25 3208 C C26 . BCZ N . ? 0.2208 0.2502 0.2189 -0.0062 -0.0110 -0.0013 513 BCZ A C26 3209 N N30 . BCZ N . ? 0.2338 0.2629 0.2330 -0.0051 -0.0108 -0.0014 513 BCZ A N30 3210 N N27 . BCZ N . ? 0.2324 0.2612 0.2298 -0.0071 -0.0107 -0.0019 513 BCZ A N27 3211 C C3 . BCZ N . ? 0.2392 0.2726 0.2375 -0.0053 -0.0124 0.0007 513 BCZ A C3 3212 C C10 . BCZ N . ? 0.2414 0.2779 0.2409 -0.0054 -0.0126 0.0005 513 BCZ A C10 3213 C C24 . BCZ N . ? 0.2902 0.3304 0.2901 -0.0055 -0.0134 0.0012 513 BCZ A C24 3214 C C37 . BCZ N . ? 0.3048 0.3449 0.3029 -0.0070 -0.0139 0.0011 513 BCZ A C37 3215 C C38 . BCZ N . ? 0.2923 0.3315 0.2892 -0.0088 -0.0136 0.0000 513 BCZ A C38 3216 C C36 . BCZ N . ? 0.2431 0.2866 0.2445 -0.0057 -0.0136 0.0009 513 BCZ A C36 3217 C C39 . BCZ N . ? 0.2724 0.3202 0.2747 -0.0056 -0.0144 0.0016 513 BCZ A C39 3218 N N11 . BCZ N . ? 0.2385 0.2748 0.2377 -0.0067 -0.0122 -0.0005 513 BCZ A N11 3219 C C13 . BCZ N . ? 0.2607 0.2971 0.2610 -0.0062 -0.0117 -0.0009 513 BCZ A C13 3220 C C15 . BCZ N . ? 0.2269 0.2630 0.2266 -0.0075 -0.0114 -0.0016 513 BCZ A C15 3221 O O14 . BCZ N . ? 0.2576 0.2941 0.2590 -0.0048 -0.0116 -0.0007 513 BCZ A O14 3222 C C4 . BCZ N . ? 0.2914 0.3246 0.2900 -0.0040 -0.0125 0.0017 513 BCZ A C4 3223 O O9 . BCZ N . ? 0.2524 0.2869 0.2526 -0.0026 -0.0126 0.0021 513 BCZ A O9 3224 C C5 . BCZ N . ? 0.2629 0.2929 0.2610 -0.0038 -0.0120 0.0016 513 BCZ A C5 3225 C C6 . BCZ N . ? 0.2429 0.2722 0.2396 -0.0042 -0.0121 0.0023 513 BCZ A C6 3226 O O8 . BCZ N . ? 0.2630 0.2897 0.2592 -0.0041 -0.0115 0.0024 513 BCZ A O8 3227 O O7 . BCZ N . ? 0.2850 0.3163 0.2812 -0.0039 -0.0127 0.0032 513 BCZ A O7 3228 C C1 . BCZ N . ? 0.2514 0.2802 0.2492 -0.0047 -0.0115 0.0006 513 BCZ A C1 3229 O O . HOH O . ? 0.2105 0.2423 0.2059 -0.0091 -0.0118 -0.0014 601 HOH A O 3230 O O . HOH O . ? 0.1947 0.1983 0.1794 -0.0007 -0.0034 -0.0017 602 HOH A O 3231 O O . HOH O . ? 0.1734 0.1941 0.1713 -0.0058 -0.0078 -0.0022 603 HOH A O 3232 O O . HOH O . ? 0.1841 0.2090 0.1846 -0.0071 -0.0037 0.0003 604 HOH A O 3233 O O . HOH O . ? 0.1674 0.1935 0.1658 0.0032 0.0007 -0.0013 605 HOH A O 3234 O O . HOH O . ? 0.2180 0.2642 0.2363 -0.0206 -0.0118 -0.0080 606 HOH A O 3235 O O . HOH O . ? 0.2209 0.2558 0.2162 -0.0125 -0.0067 -0.0028 607 HOH A O 3236 O O . HOH O . ? 0.1799 0.2045 0.1846 -0.0100 -0.0049 0.0003 608 HOH A O 3237 O O . HOH O . ? 0.1805 0.2160 0.1889 -0.0045 -0.0053 -0.0010 609 HOH A O 3238 O O . HOH O . ? 0.2661 0.2564 0.2377 -0.0109 -0.0017 -0.0077 610 HOH A O 3239 O O . HOH O . ? 0.2193 0.2148 0.1895 -0.0124 -0.0025 -0.0095 611 HOH A O 3240 O O . HOH O . ? 0.1609 0.1799 0.1614 -0.0044 -0.0093 -0.0023 612 HOH A O 3241 O O . HOH O . ? 0.1723 0.1812 0.1542 -0.0091 -0.0053 -0.0053 613 HOH A O 3242 O O . HOH O . ? 0.1776 0.2016 0.1773 -0.0037 -0.0102 -0.0010 614 HOH A O 3243 O O . HOH O . ? 0.3306 0.3770 0.3139 -0.0061 -0.0186 0.0094 615 HOH A O 3244 O O . HOH O . ? 0.2144 0.2366 0.2046 -0.0100 0.0006 0.0073 616 HOH A O 3245 O O . HOH O . ? 0.2463 0.2397 0.2039 -0.0004 0.0109 -0.0146 617 HOH A O 3246 O O . HOH O . ? 0.1954 0.2163 0.1950 -0.0023 -0.0101 0.0012 618 HOH A O 3247 O O . HOH O . ? 0.3768 0.3794 0.3168 -0.0081 0.0106 -0.0164 619 HOH A O 3248 O O . HOH O . ? 0.2380 0.2580 0.2384 -0.0031 -0.0096 -0.0010 620 HOH A O 3249 O O . HOH O . ? 0.2917 0.3079 0.2924 -0.0020 -0.0082 -0.0087 621 HOH A O 3250 O O . HOH O . ? 0.2230 0.2101 0.1934 -0.0220 -0.0019 -0.0037 622 HOH A O 3251 O O . HOH O . ? 0.2565 0.2938 0.2720 -0.0170 -0.0080 -0.0042 623 HOH A O 3252 O O . HOH O . ? 0.1813 0.2404 0.1888 -0.0117 -0.0102 -0.0017 624 HOH A O 3253 O O . HOH O . ? 0.2460 0.2792 0.2386 -0.0073 -0.0133 0.0020 625 HOH A O 3254 O O . HOH O . ? 0.1737 0.1990 0.1525 -0.0101 -0.0101 0.0013 626 HOH A O 3255 O O . HOH O . ? 0.2461 0.2664 0.2107 -0.0046 0.0103 -0.0041 627 HOH A O 3256 O O . HOH O . ? 0.2622 0.2858 0.2292 -0.0151 -0.0097 -0.0040 628 HOH A O 3257 O O . HOH O . ? 0.2749 0.3241 0.2310 -0.0234 -0.0207 -0.0031 629 HOH A O 3258 O O . HOH O . ? 0.1422 0.1707 0.1349 -0.0120 -0.0071 -0.0025 630 HOH A O 3259 O O . HOH O . ? 0.5408 0.4879 0.4762 -0.0327 0.0044 -0.0249 631 HOH A O 3260 O O . HOH O . ? 0.2416 0.2490 0.2278 -0.0019 -0.0053 -0.0004 632 HOH A O 3261 O O . HOH O . ? 0.2672 0.2557 0.2438 0.0069 0.0038 -0.0037 633 HOH A O 3262 O O . HOH O . ? 0.1889 0.2096 0.1848 -0.0028 -0.0103 0.0049 634 HOH A O 3263 O O . HOH O . ? 0.2472 0.2954 0.2486 -0.0119 -0.0060 -0.0030 635 HOH A O 3264 O O . HOH O . ? 0.3096 0.3351 0.3042 -0.0131 0.0040 0.0095 636 HOH A O 3265 O O . HOH O . ? 0.3571 0.3867 0.3618 0.0031 -0.0102 0.0005 637 HOH A O 3266 O O . HOH O . ? 0.2280 0.2713 0.2072 -0.0146 -0.0175 0.0010 638 HOH A O 3267 O O . HOH O . ? 0.2494 0.2723 0.2312 -0.0280 -0.0001 0.0031 639 HOH A O 3268 O O . HOH O . ? 0.3062 0.3362 0.2956 -0.0035 -0.0132 0.0080 640 HOH A O 3269 O O . HOH O . ? 0.2046 0.2268 0.2044 -0.0060 -0.0071 -0.0018 641 HOH A O 3270 O O . HOH O . ? 0.1819 0.2020 0.1720 -0.0086 -0.0089 -0.0023 642 HOH A O 3271 O O . HOH O . ? 0.2132 0.2364 0.1967 -0.0090 -0.0093 0.0010 643 HOH A O 3272 O O . HOH O . ? 0.2722 0.3324 0.2512 -0.0081 -0.0232 0.0109 644 HOH A O 3273 O O . HOH O . ? 0.2401 0.2712 0.2549 -0.0198 -0.0064 -0.0033 645 HOH A O 3274 O O . HOH O . ? 0.2159 0.2441 0.1929 -0.0094 -0.0111 0.0042 646 HOH A O 3275 O O . HOH O . ? 0.2671 0.2940 0.2521 -0.0039 0.0073 0.0001 647 HOH A O 3276 O O . HOH O . ? 0.3140 0.3528 0.2760 -0.0099 -0.0146 0.0104 648 HOH A O 3277 O O . HOH O . ? 0.1893 0.2103 0.1820 -0.0087 -0.0091 -0.0030 649 HOH A O 3278 O O . HOH O . ? 0.1903 0.2149 0.1711 -0.0017 0.0093 -0.0022 650 HOH A O 3279 O O . HOH O . ? 0.2057 0.1991 0.1810 -0.0054 -0.0009 -0.0063 651 HOH A O 3280 O O . HOH O . ? 0.2979 0.3097 0.2666 -0.0174 -0.0075 -0.0092 652 HOH A O 3281 O O . HOH O . ? 0.2777 0.2349 0.2267 -0.0348 0.0020 -0.0154 653 HOH A O 3282 O O . HOH O . ? 0.2839 0.3049 0.2747 -0.0017 -0.0107 0.0105 654 HOH A O 3283 O O . HOH O . ? 0.2377 0.2651 0.2189 -0.0146 -0.0122 -0.0032 655 HOH A O 3284 O O . HOH O . ? 0.2958 0.3208 0.2927 -0.0052 -0.0097 -0.0057 656 HOH A O 3285 O O . HOH O . ? 0.2542 0.2756 0.2297 -0.0097 0.0003 0.0130 657 HOH A O 3286 O O . HOH O . ? 0.2141 0.2589 0.2203 -0.0025 -0.0091 -0.0026 658 HOH A O 3287 O O . HOH O . ? 0.2643 0.3045 0.2705 0.0005 -0.0085 -0.0034 659 HOH A O 3288 O O . HOH O . ? 0.2460 0.3317 0.2571 -0.0150 -0.0193 0.0019 660 HOH A O 3289 O O . HOH O . ? 0.2573 0.2823 0.2551 -0.0053 -0.0103 -0.0059 661 HOH A O 3290 O O . HOH O . ? 0.2511 0.2606 0.1921 -0.0267 -0.0073 -0.0184 662 HOH A O 3291 O O . HOH O . ? 0.4125 0.4863 0.3973 -0.0062 -0.0267 0.0131 663 HOH A O 3292 O O . HOH O . ? 0.2284 0.2514 0.2345 -0.0122 -0.0101 -0.0075 664 HOH A O 3293 O O . HOH O . ? 0.2633 0.2865 0.2381 -0.0120 -0.0093 -0.0015 665 HOH A O 3294 O O . HOH O . ? 0.2205 0.2554 0.2151 -0.0120 -0.0123 -0.0021 666 HOH A O 3295 O O . HOH O . ? 0.2655 0.2545 0.2209 -0.0060 0.0067 -0.0154 667 HOH A O 3296 O O . HOH O . ? 0.2708 0.2819 0.2677 -0.0055 -0.0070 0.0060 668 HOH A O 3297 O O . HOH O . ? 0.2983 0.3204 0.2996 -0.0067 -0.0081 -0.0025 669 HOH A O 3298 O O . HOH O . ? 0.2823 0.3491 0.2242 -0.0341 -0.0281 -0.0075 670 HOH A O 3299 O O . HOH O . ? 0.2580 0.2394 0.2252 -0.0123 -0.0002 -0.0082 671 HOH A O 3300 O O . HOH O . ? 0.2767 0.2950 0.2716 0.0057 -0.0033 0.0000 672 HOH A O 3301 O O . HOH O . ? 0.2245 0.2907 0.2355 -0.0044 -0.0036 -0.0039 673 HOH A O 3302 O O . HOH O . ? 0.2325 0.2705 0.2253 -0.0146 -0.0134 -0.0023 674 HOH A O 3303 O O . HOH O . ? 0.2547 0.2674 0.2517 -0.0032 -0.0083 0.0060 675 HOH A O 3304 O O . HOH O . ? 0.2989 0.2812 0.2636 0.0016 0.0076 -0.0115 676 HOH A O 3305 O O . HOH O . ? 0.2680 0.3163 0.2645 -0.0314 -0.0054 -0.0020 677 HOH A O 3306 O O . HOH O . ? 0.2122 0.2389 0.2060 0.0054 0.0072 -0.0025 678 HOH A O 3307 O O . HOH O . ? 0.2807 0.2995 0.2376 -0.0064 0.0096 -0.0051 679 HOH A O 3308 O O . HOH O . ? 0.2366 0.2656 0.2226 -0.0190 -0.0120 -0.0050 680 HOH A O 3309 O O . HOH O . ? 0.3024 0.3758 0.2595 -0.0352 -0.0295 -0.0069 681 HOH A O 3310 O O . HOH O . ? 0.2649 0.2914 0.2517 0.0006 0.0091 -0.0023 682 HOH A O 3311 O O . HOH O . ? 0.3959 0.3513 0.3486 -0.0049 0.0083 -0.0133 683 HOH A O 3312 O O . HOH O . ? 0.3591 0.3322 0.3008 0.0001 0.0161 -0.0225 684 HOH A O 3313 O O . HOH O . ? 0.2962 0.3133 0.2911 -0.0034 -0.0091 0.0064 685 HOH A O 3314 O O . HOH O . ? 0.3234 0.4186 0.3359 -0.0172 0.0067 -0.0010 686 HOH A O 3315 O O . HOH O . ? 0.3970 0.4207 0.3752 -0.0537 -0.0070 -0.0097 687 HOH A O 3316 O O . HOH O . ? 0.3327 0.3253 0.2639 -0.0076 0.0140 -0.0223 688 HOH A O 3317 O O . HOH O . ? 0.3927 0.3432 0.3273 -0.0078 0.0135 -0.0256 689 HOH A O 3318 O O . HOH O . ? 0.4764 0.5266 0.3939 -0.0406 -0.0231 -0.0182 690 HOH A O 3319 O O . HOH O . ? 0.3530 0.4058 0.2906 -0.0140 -0.0187 0.0127 691 HOH A O 3320 O O . HOH O . ? 0.2124 0.2401 0.2085 -0.0051 -0.0087 -0.0060 692 HOH A O 3321 O O . HOH O . ? 0.2094 0.2528 0.2092 -0.0092 -0.0060 -0.0037 693 HOH A O 3322 O O . HOH O . ? 0.2670 0.3277 0.2609 -0.0223 -0.0189 -0.0024 694 HOH A O 3323 O O . HOH O . ? 0.3503 0.3735 0.3462 -0.0004 -0.0114 0.0073 695 HOH A O 3324 O O . HOH O . ? 0.3069 0.3137 0.3081 -0.0146 -0.0024 0.0067 696 HOH A O 3325 O O . HOH O . ? 0.3655 0.4317 0.3635 -0.0379 -0.0150 -0.0058 697 HOH A O 3326 O O . HOH O . ? 0.3537 0.3537 0.2637 -0.0191 -0.0185 0.0185 698 HOH A O 3327 O O . HOH O . ? 0.4216 0.4465 0.4179 0.0019 -0.0087 0.0004 699 HOH A O 3328 O O . HOH O . ? 0.2956 0.3688 0.2911 -0.0245 -0.0218 -0.0017 700 HOH A O 3329 O O . HOH O . ? 0.5083 0.5527 0.4354 -0.0399 -0.0215 -0.0184 701 HOH A O 3330 O O . HOH O . ? 0.3999 0.4874 0.3721 -0.0420 -0.0316 -0.0084 702 HOH A O 3331 O O . HOH O . ? 0.2628 0.2841 0.2655 -0.0076 -0.0085 -0.0031 703 HOH A O 3332 O O . HOH O . ? 0.3249 0.3219 0.3239 -0.0061 -0.0065 -0.0131 704 HOH A O 3333 O O . HOH O . ? 0.4025 0.4351 0.4094 -0.0168 -0.0138 -0.0129 705 HOH A O 3334 O O . HOH O . ? 0.3512 0.3118 0.3082 -0.0173 0.0032 -0.0089 706 HOH A O 3335 O O . HOH O . ? 0.2334 0.2558 0.2340 -0.0028 -0.0089 -0.0066 707 HOH A O 3336 O O . HOH O . ? 0.2615 0.3183 0.2493 -0.0072 -0.0211 0.0084 708 HOH A O 3337 O O . HOH O . ? 0.2579 0.2754 0.2511 -0.0052 -0.0082 0.0061 709 HOH A O 3338 O O . HOH O . ? 0.3209 0.3826 0.3290 -0.0051 -0.0152 0.0023 710 HOH A O 3339 O O . HOH O . ? 0.3845 0.4503 0.3316 -0.0370 -0.0280 -0.0099 711 HOH A O 3340 O O . HOH O . ? 0.5242 0.5016 0.4841 0.0075 0.0134 -0.0141 712 HOH A O 3341 O O . HOH O . ? 0.3163 0.3076 0.2864 -0.0003 0.0048 -0.0095 713 HOH A O 3342 O O . HOH O . ? 0.3861 0.4010 0.3819 -0.0101 -0.0032 0.0074 714 HOH A O 3343 O O . HOH O . ? 0.3831 0.3586 0.3481 -0.0209 0.0001 -0.0043 715 HOH A O 3344 O O . HOH O . ? 0.3823 0.3557 0.3169 -0.0142 0.0083 -0.0252 716 HOH A O 3345 O O . HOH O . ? 0.3965 0.3937 0.3703 -0.0022 -0.0038 0.0080 717 HOH A O 3346 O O . HOH O . ? 0.3492 0.3501 0.3318 -0.0006 -0.0039 0.0006 718 HOH A O 3347 O O . HOH O . ? 0.3882 0.4860 0.4081 -0.0155 0.0005 -0.0011 719 HOH A O 3348 O O . HOH O . ? 0.3282 0.3945 0.3419 -0.0003 -0.0048 -0.0035 720 HOH A O 3349 O O . HOH O . ? 0.3175 0.3215 0.2916 -0.0029 -0.0049 0.0085 721 HOH A O 3350 O O . HOH O . ? 0.4938 0.4796 0.4615 0.0001 -0.0017 0.0117 722 HOH A O 3351 O O . HOH O . ? 0.3532 0.3139 0.3131 -0.0121 0.0034 0.0028 723 HOH A O 3352 O O . HOH O . ? 0.3672 0.3679 0.3032 -0.0300 -0.0059 -0.0229 724 HOH A O 3353 O O . HOH O . ? 0.2366 0.2546 0.2351 -0.0023 -0.0096 0.0033 725 HOH A O 3354 O O . HOH O . ? 0.2512 0.2746 0.2314 -0.0058 0.0048 0.0005 726 HOH A O 3355 O O . HOH O . ? 0.5328 0.5182 0.4790 -0.0415 -0.0058 -0.0233 727 HOH A O 3356 O O . HOH O . ? 0.2875 0.2778 0.2618 -0.0073 -0.0013 -0.0056 728 HOH A O 3357 O O . HOH O . ? 0.2758 0.3744 0.2601 -0.0276 -0.0327 0.0014 729 HOH A O 3358 O O . HOH O . ? 0.2785 0.3153 0.2361 -0.0201 -0.0156 -0.0036 730 HOH A O 3359 O O . HOH O . ? 0.3658 0.3181 0.3228 -0.0015 0.0073 -0.0057 731 HOH A O 3360 O O . HOH O . ? 0.2622 0.2911 0.2591 -0.0038 -0.0114 -0.0039 732 HOH A O 3361 O O . HOH O . ? 0.4546 0.4599 0.3906 -0.0181 0.0007 -0.0174 733 HOH A O 3362 O O . HOH O . ? 0.4048 0.4750 0.3875 -0.0428 -0.0235 -0.0099 734 HOH A O 3363 O O . HOH O . ? 0.4404 0.4330 0.4384 -0.0075 -0.0040 0.0075 735 HOH A O 3364 O O . HOH O . ? 0.2720 0.3023 0.2701 -0.0055 -0.0084 -0.0049 736 HOH A O 3365 O O . HOH O . ? 0.4176 0.4427 0.3896 -0.0041 -0.0098 0.0193 737 HOH A O 3366 O O . HOH O . ? 0.3206 0.3383 0.3074 -0.0060 -0.0076 0.0000 738 HOH A O 3367 O O . HOH O . ? 0.3540 0.3720 0.3538 -0.0123 -0.0019 0.0061 739 HOH A O 3368 O O . HOH O . ? 0.4794 0.5237 0.4348 -0.0481 -0.0218 -0.0189 740 HOH A O 3369 O O . HOH O . ? 0.2873 0.2959 0.2651 -0.0135 -0.0064 -0.0069 741 HOH A O 3370 O O . HOH O . ? 0.3885 0.3730 0.3547 0.0068 0.0106 -0.0113 742 HOH A O 3371 O O . HOH O . ? 0.4079 0.4738 0.4035 -0.0359 -0.0173 -0.0060 743 HOH A O 3372 O O . HOH O . ? 0.3498 0.4489 0.3449 -0.0266 -0.0297 0.0010 744 HOH A O 3373 O O . HOH O . ? 0.3839 0.4204 0.3892 0.0014 -0.0087 -0.0003 745 HOH A O 3374 O O . HOH O . ? 0.3029 0.3696 0.2964 -0.0322 -0.0194 -0.0053 746 HOH A O 3375 O O . HOH O . ? 0.6998 0.6558 0.6402 -0.0296 0.0030 -0.0228 747 HOH A O 3376 O O . HOH O . ? 0.2528 0.3261 0.2633 -0.0179 -0.0046 -0.0016 748 HOH A O 3377 O O . HOH O . ? 0.4621 0.4818 0.4636 -0.0008 -0.0083 -0.0068 749 HOH A O 3378 O O . HOH O . ? 0.4354 0.4745 0.4261 -0.0373 -0.0069 -0.0041 750 HOH A O 3379 O O . HOH O . ? 0.4443 0.5179 0.4374 -0.0304 -0.0221 -0.0041 751 HOH A O 3380 O O . HOH O . ? 0.2946 0.2922 0.2964 -0.0093 -0.0064 -0.0055 752 HOH A O 3381 O O . HOH O . ? 0.5525 0.6068 0.4752 -0.0163 -0.0171 0.0122 753 HOH A O 3382 O O . HOH O . ? 0.5599 0.6217 0.5004 -0.0441 -0.0278 -0.0159 754 HOH A O 3383 O O . HOH O . ? 0.4560 0.4738 0.4369 -0.0108 0.0010 0.0156 755 HOH A O 3384 O O . HOH O . ? 0.4407 0.4520 0.4314 0.0084 0.0002 -0.0008 756 HOH A O 3385 O O . HOH O . ? 0.3934 0.3949 0.3948 -0.0073 -0.0072 -0.0079 757 HOH A O 3386 O O . HOH O . ? 0.3837 0.4050 0.3669 -0.0301 -0.0018 0.0007 758 HOH A O 3387 O O . HOH O . ? 0.3734 0.3643 0.3493 -0.0027 -0.0024 0.0026 759 HOH A O 3388 O O . HOH O . ? 0.4426 0.4913 0.3929 -0.0489 -0.0237 -0.0196 760 HOH A O 3389 O O . HOH O . ? 0.3941 0.4635 0.3217 -0.0378 -0.0294 -0.0102 761 HOH A O 3390 O O . HOH O . ? 0.2471 0.2827 0.2116 -0.0179 -0.0151 -0.0022 762 HOH A O 3391 O O . HOH O . ? 0.4197 0.4675 0.3451 -0.0238 -0.0171 -0.0025 763 HOH A O 3392 O O . HOH O . ? 0.3755 0.3801 0.3494 -0.0211 -0.0067 -0.0089 764 HOH A O 3393 O O . HOH O . ? 0.4696 0.4648 0.4761 -0.0256 -0.0036 -0.0044 765 HOH A O 3394 O O . HOH O . ? 0.4757 0.5130 0.4722 -0.0038 -0.0143 0.0043 766 HOH A O 3395 O O . HOH O . ? 0.4095 0.4304 0.3735 -0.0547 -0.0132 -0.0189 767 HOH A O 3396 O O . HOH O . ? 0.4904 0.5756 0.5020 -0.0326 -0.0116 -0.0022 768 HOH A O 3397 O O . HOH O . ? 0.4377 0.4458 0.3705 -0.0105 0.0102 -0.0156 769 HOH A O 3398 O O . HOH O . ? 0.5219 0.5955 0.5150 0.0112 0.0151 -0.0198 770 HOH A O 3399 O O . HOH O . ? 0.3745 0.4270 0.3371 -0.0028 -0.0214 0.0225 771 HOH A O 3400 O O . HOH O . ? 0.5467 0.5571 0.5429 -0.0107 -0.0030 0.0090 772 HOH A O 3401 O O . HOH O . ? 0.5426 0.5603 0.5220 -0.0033 -0.0080 0.0189 773 HOH A O 3402 O O . HOH O . ? 0.3276 0.3247 0.2671 -0.0107 0.0079 -0.0185 774 HOH A O 3403 O O . HOH O . ? 0.2790 0.3063 0.2762 -0.0050 -0.0111 -0.0055 775 HOH A O 3404 O O . HOH O . ? 0.5729 0.6086 0.5729 0.0000 0.0000 0.0000 776 HOH A O 3405 O O . HOH O . ? 0.4015 0.4397 0.4089 0.0035 -0.0089 -0.0022 777 HOH A O 3406 O O . HOH O . ? 0.4186 0.3997 0.3898 0.0007 -0.0004 0.0052 778 HOH A O 3407 O O . HOH O . ? 0.3636 0.4084 0.3635 -0.0032 -0.0153 0.0043 779 HOH A O 3408 O O . HOH O . ? 0.4922 0.5641 0.4781 -0.0369 -0.0235 -0.0072 780 HOH A O 3409 O O . HOH O . ? 0.4146 0.3714 0.3758 0.0045 0.0069 -0.0018 781 HOH A O 3410 O O . HOH O . ? 0.3497 0.3783 0.3653 -0.0255 -0.0005 0.0027 782 HOH A O 3411 O O . HOH O . ? 0.3421 0.3947 0.3530 0.0020 -0.0081 -0.0024 783 HOH A O 3412 O O . HOH O . ? 0.4593 0.4578 0.4091 -0.0459 -0.0094 -0.0228 784 HOH A O 3413 O O . HOH O . ? 0.3865 0.4100 0.3834 0.0083 -0.0056 0.0024 785 HOH A O 3414 O O . HOH O . ? 0.4203 0.4178 0.3698 -0.0518 -0.0096 -0.0239 786 HOH A O 3415 O O . HOH O . ? 0.3455 0.3443 0.3219 0.0031 0.0051 -0.0073 787 HOH A O 3416 O O . HOH O . ? 0.5273 0.5417 0.5060 -0.0099 0.0000 0.0193 788 HOH A O 3417 O O . HOH O . ? 0.4414 0.4286 0.3921 -0.0260 -0.0030 -0.0190 789 HOH A O 3418 O O . HOH O . ? 0.4679 0.5021 0.4732 0.0014 -0.0099 -0.0013 790 HOH A O 3419 O O . HOH O . ? 0.5374 0.6357 0.5585 -0.0085 0.0019 -0.0022 791 HOH A O 3420 O O . HOH O . ? 0.3963 0.4163 0.3842 -0.0029 -0.0088 0.0006 792 HOH A O 3421 O O . HOH O . ? 0.3505 0.3463 0.3277 0.0069 0.0062 -0.0065 793 HOH A O 3422 O O . HOH O . ? 0.4788 0.5164 0.4835 0.0009 -0.0117 0.0015 794 HOH A O 3423 O O . HOH O . ? 0.6799 0.6928 0.6688 -0.0072 -0.0047 0.0121 795 HOH A O 3424 O O . HOH O . ? 0.3727 0.4591 0.3887 -0.0100 -0.0167 0.0025 796 HOH A O 3425 O O . HOH O . ? 0.3445 0.3167 0.2823 -0.0186 0.0050 -0.0243 797 HOH A O 3426 O O . HOH O . ? 0.4922 0.5302 0.4883 -0.0127 0.0107 0.0092 798 HOH A O 3427 O O . HOH O . ? 0.4394 0.5122 0.4555 -0.0028 -0.0116 0.0009 799 HOH A O 3428 O O . HOH O . ? 0.4379 0.4262 0.3830 -0.0628 -0.0081 -0.0269 800 HOH A O 3429 O O . HOH O . ? 0.2996 0.3854 0.2936 -0.0270 -0.0260 -0.0010 801 HOH A O 3430 O O . HOH O . ? 0.3660 0.3906 0.3577 -0.0023 -0.0102 -0.0010 802 HOH A O 3431 O O . HOH O . ? 0.5604 0.5244 0.5152 0.0047 0.0126 -0.0149 803 HOH A O 3432 O O . HOH O . ? 0.5345 0.5125 0.5331 0.0096 -0.0019 -0.0047 804 HOH A O 3433 O O . HOH O . ? 0.4468 0.4175 0.4079 -0.0124 0.0022 -0.0099 805 HOH A O 3434 O O . HOH O . ? 0.4211 0.4766 0.3530 -0.0431 -0.0259 -0.0174 806 HOH A O 3435 O O . HOH O . ? 0.4285 0.4293 0.4262 -0.0110 -0.0031 0.0092 807 HOH A O 3436 O O . HOH O . ? 0.4594 0.5564 0.4505 -0.0227 -0.0307 0.0034 808 HOH A O 3437 O O . HOH O . ? 0.3497 0.3755 0.3112 -0.0015 0.0183 -0.0048 809 HOH A O 3438 O O . HOH O . ? 0.5130 0.4729 0.4477 -0.0095 0.0121 -0.0259 810 HOH A O 3439 O O . HOH O . ? 0.4071 0.4631 0.4070 -0.0314 -0.0076 -0.0027 811 HOH A O 3440 O O . HOH O . ? 0.4512 0.4519 0.4574 -0.0228 -0.0062 -0.0087 812 HOH A O 3441 O O . HOH O . ? 0.3943 0.4516 0.4024 -0.0004 -0.0151 0.0040 813 HOH A O 3442 O O . HOH O . ? 0.4282 0.5259 0.3979 -0.0292 -0.0353 0.0013 814 HOH A O 3443 O O . HOH O . ? 0.4008 0.3996 0.4014 -0.0095 -0.0071 -0.0114 815 HOH A O 3444 O O . HOH O . ? 0.5784 0.5213 0.5207 -0.0380 0.0046 -0.0167 816 HOH A O 3445 O O . HOH O . ? 0.5455 0.5756 0.5163 -0.0089 0.0111 0.0067 817 HOH A O 3446 O O . HOH O . ? 0.4377 0.4790 0.4392 -0.0013 -0.0141 0.0039 818 HOH A O 3447 O O . HOH O . ? 0.5180 0.5572 0.5249 -0.0159 -0.0153 -0.0126 819 HOH A O 3448 O O . HOH O . ? 0.4498 0.5474 0.4630 -0.0128 -0.0227 0.0046 820 HOH A O 3449 O O . HOH O . ? 0.4330 0.4576 0.4470 -0.0263 -0.0086 -0.0090 821 HOH A O 3450 O O . HOH O . ? 0.5283 0.5176 0.4756 -0.0237 -0.0021 -0.0198 822 HOH A O 3451 O O . HOH O . ? 0.5340 0.4554 0.4683 -0.0260 0.0102 -0.0175 823 HOH A O 3452 O O . HOH O . ? 0.4736 0.4862 0.4572 -0.0051 -0.0067 0.0020 824 HOH A O 3453 O O . HOH O . ? 0.3882 0.4567 0.3977 -0.0017 -0.0176 0.0055 825 HOH A O 3454 O O . HOH O . ? 0.4859 0.5008 0.4699 -0.0020 -0.0077 0.0030 826 HOH A O 3455 O O . HOH O . ? 0.4921 0.5217 0.4751 -0.0095 0.0081 0.0073 827 HOH A O 3456 O O . HOH O . ? 0.5401 0.6001 0.4976 -0.0093 -0.0237 0.0159 828 HOH A O 3457 O O . HOH O . ? 0.4596 0.4492 0.4086 -0.0347 -0.0056 -0.0211 829 HOH A O 3458 O O . HOH O . ? 0.4727 0.5263 0.4697 -0.0375 -0.0083 -0.0039 830 HOH A O 3459 O O . HOH O . ? 0.5400 0.5851 0.4870 -0.0107 -0.0156 0.0150 831 HOH A O 3460 O O . HOH O . ? 0.6045 0.6673 0.5579 -0.0543 -0.0277 -0.0197 832 HOH A O 3461 O O . HOH O . ? 0.5142 0.4903 0.4456 -0.0121 0.0104 -0.0260 833 HOH A O 3462 O O . HOH O . ? 0.4316 0.4344 0.4046 -0.0152 -0.0016 0.0065 834 HOH A O 3463 O O . HOH O . ? 0.5296 0.5490 0.4505 -0.0280 -0.0074 -0.0191 835 HOH A O 3464 O O . HOH O . ? 0.5063 0.4774 0.4336 -0.0227 0.0053 -0.0291 836 HOH A O 3465 O O . HOH O . ? 0.4861 0.4721 0.4610 0.0023 -0.0008 0.0030 837 HOH A O 3466 O O . HOH O . ? 0.5222 0.5267 0.4508 -0.0340 -0.0076 -0.0253 838 HOH A O 3467 O O . HOH O . ? 0.4504 0.4810 0.4360 0.0028 -0.0148 0.0184 839 HOH A O 3468 O O . HOH O . ? 0.4003 0.3942 0.3803 0.0060 -0.0014 0.0027 840 HOH A O 3469 O O . HOH O . ? 0.5506 0.5978 0.5388 0.0031 -0.0194 0.0175 841 HOH A O 3470 O O . HOH O . ? 0.5402 0.5097 0.5370 0.0048 -0.0014 -0.0044 842 HOH A O 3471 O O . HOH O . ? 0.6009 0.5576 0.5389 -0.0403 0.0010 -0.0250 843 HOH A O 3472 O O . HOH O . ? 0.4647 0.4673 0.4475 0.0064 0.0037 -0.0044 844 HOH A O 3473 O O . HOH O . ? 0.4153 0.4217 0.3988 -0.0067 -0.0056 -0.0001 845 HOH A O 3474 O O . HOH O . ? 0.4358 0.5103 0.4492 -0.0014 -0.0169 0.0050 846 HOH A O 3475 O O . HOH O . ? 0.4995 0.5544 0.4105 -0.0313 -0.0209 -0.0084 847 HOH A O 3476 O O . HOH O . ? 0.4163 0.4400 0.4059 -0.0092 -0.0071 -0.0018 848 HOH A O 3477 O O . HOH O . ? 0.5108 0.5172 0.5143 -0.0125 -0.0079 -0.0081 849 HOH A O 3478 O O . HOH O . ? 0.5096 0.5828 0.5105 0.0073 0.0100 -0.0141 850 HOH A O 3479 O O . HOH O . ? 0.5082 0.5568 0.5094 0.0005 -0.0165 0.0075 851 HOH A O 3480 O O . HOH O . ? 0.4504 0.4830 0.3813 -0.0444 -0.0191 -0.0234 852 HOH A O 3481 O O . HOH O . ? 0.4310 0.4574 0.4096 -0.0084 0.0060 0.0053 853 HOH A O 3482 O O . HOH O . ? 0.5924 0.5334 0.5171 -0.0096 0.0162 -0.0308 854 HOH A O 3483 O O . HOH O . ? 0.5269 0.5230 0.4733 -0.0286 -0.0054 -0.0203 855 HOH A O 3484 O O . HOH O . ? 0.4857 0.5601 0.4353 -0.0235 -0.0295 0.0035 856 HOH A O 3485 O O . HOH O . ? 0.5557 0.4802 0.4967 -0.0218 0.0098 -0.0080 857 HOH A O 3486 O O . HOH O . ? 0.4430 0.4788 0.4332 -0.0341 -0.0049 -0.0024 858 HOH A O 3487 O O . HOH O . ? 0.4947 0.4541 0.4505 0.0021 0.0102 -0.0124 859 HOH A O 3488 O O . HOH O . ? 0.4338 0.5279 0.4496 -0.0249 0.0011 0.0001 860 HOH A O 3489 O O . HOH O . ? 0.4346 0.4533 0.4286 -0.0013 -0.0102 0.0087 861 HOH A O 3490 O O . HOH O . ? 0.4955 0.4873 0.4263 -0.0117 0.0100 -0.0226 862 HOH A O 3491 O O . HOH O . ? 0.4381 0.4677 0.4509 -0.0209 -0.0001 0.0038 863 HOH A O 3492 O O . HOH O . ? 0.5556 0.6143 0.5460 0.0053 -0.0225 0.0197 864 HOH A O 3493 O O . HOH O . ? 0.3810 0.4175 0.3891 -0.0039 -0.0028 -0.0002 865 HOH A O 3494 O O . HOH O . ? 0.3516 0.3884 0.3413 -0.0193 -0.0133 -0.0042 866 HOH A O 3495 O O . HOH O . ? 0.5455 0.6246 0.5658 0.0033 -0.0041 -0.0025 867 HOH A O 3496 O O . HOH O . ? 0.5738 0.5550 0.5402 -0.0097 0.0001 0.0081 868 HOH A O 3497 O O . HOH O . ? 0.5421 0.5201 0.5418 -0.0148 -0.0032 -0.0055 869 HOH A O 3498 O O . HOH O . ? 0.5202 0.4678 0.4737 -0.0001 0.0095 -0.0087 870 HOH A O 3499 O O . HOH O . ? 0.4266 0.4468 0.4208 -0.0132 0.0019 0.0104 871 HOH A O 3500 O O . HOH O . ? 0.5646 0.6431 0.5732 -0.0355 -0.0095 -0.0025 872 HOH A O 3501 O O . HOH O . ? 0.4474 0.5496 0.4234 -0.0378 -0.0352 -0.0038 873 HOH A O 3502 O O . HOH O . ? 0.5476 0.5526 0.5513 -0.0152 -0.0080 -0.0102 874 HOH A O 3503 O O . HOH O . ? 0.5629 0.5811 0.4823 -0.0390 -0.0124 -0.0260 875 HOH A O 3504 O O . HOH O . ? 0.5283 0.5418 0.4846 0.0065 0.0234 -0.0131 876 HOH A O 3505 O O . HOH O . ? 0.4932 0.5171 0.4890 0.0054 -0.0076 0.0021 877 HOH A O 3506 O O . HOH O . ? 0.5331 0.4595 0.4770 -0.0131 0.0101 -0.0047 878 HOH A O 3507 O O . HOH O . ? 0.4569 0.4808 0.4648 -0.0184 0.0001 0.0053 879 HOH A O 3508 O O . HOH O . ? 0.3948 0.4892 0.3514 -0.0276 -0.0359 0.0031 880 HOH A O 3509 O O . HOH O . ? 0.5598 0.6507 0.5796 -0.0125 -0.0040 -0.0011 881 HOH A O 3510 O O . HOH O . ? 0.5568 0.6428 0.5626 0.0004 -0.0251 0.0128 882 HOH A O 3511 O O . HOH O . ? 0.5380 0.5276 0.5325 -0.0191 -0.0076 -0.0247 883 HOH A O 3512 O O . HOH O . ? 0.2122 0.2212 0.2141 0.0004 -0.0078 -0.0019 884 HOH A O 3513 O O . HOH O . ? 0.4053 0.4143 0.3831 -0.0045 -0.0057 0.0057 885 HOH A O 3514 O O . HOH O . ? 0.3659 0.4394 0.3547 -0.0167 -0.0250 0.0036 886 HOH A O 3515 O O . HOH O . ? 0.3256 0.3309 0.3276 0.0034 -0.0072 -0.0007 887 HOH A O 3516 O O . HOH O . ? 0.3760 0.3940 0.3715 -0.0091 -0.0037 0.0053 888 HOH A O 3517 O O . HOH O . ? 0.3938 0.4035 0.3776 -0.0072 -0.0061 0.0006 889 HOH A O 3518 O O . HOH O . ? 0.3978 0.4714 0.4027 -0.0064 0.0038 -0.0053 890 HOH A O 3519 O O . HOH O . ? 0.3635 0.3955 0.3784 -0.0255 -0.0107 -0.0105 891 HOH A O 3520 O O . HOH O . ? 0.4026 0.4046 0.4126 -0.0304 -0.0029 -0.0033 892 HOH A O 3521 O O . HOH O . ? 0.4137 0.4194 0.3897 -0.0357 -0.0012 -0.0010 893 HOH A O 3522 O O . HOH O . ? 0.4636 0.4832 0.4421 -0.0256 0.0008 0.0051 894 HOH A O 3523 O O . HOH O . ? 0.4046 0.3962 0.3737 -0.0158 -0.0003 0.0072 895 HOH A O 3524 O O . HOH O . ? 0.4941 0.4961 0.4976 -0.0131 -0.0068 -0.0062 896 HOH A O 3525 O O . HOH O . ? 0.4639 0.4819 0.4451 -0.0375 -0.0019 -0.0010 897 HOH A O 3526 O O . HOH O . ? 0.3904 0.4156 0.3922 -0.0017 -0.0092 -0.0042 898 HOH A O 3527 O O . HOH O . ? 0.6659 0.6284 0.6086 -0.0339 0.0007 -0.0224 899 HOH A O 3528 O O . HOH O . ? 0.5201 0.5941 0.5185 0.0097 0.0125 -0.0166 900 HOH A O 3529 O O . HOH O . ? 0.4542 0.5657 0.4576 -0.0245 -0.0305 0.0031 901 HOH A O 3530 O O . HOH O . ? 0.5371 0.5267 0.5052 -0.0223 0.0011 0.0063 902 HOH A O 3531 O O . HOH O . ? 0.6557 0.5563 0.5876 -0.0137 0.0153 -0.0076 903 HOH A O 3532 O O . HOH O . ? 0.4592 0.5907 0.4724 -0.0191 0.0232 0.0007 904 HOH A O 3533 O O . HOH O . ? 0.5849 0.6214 0.5907 0.0041 -0.0068 0.0006 905 HOH A O 3534 O O . HOH O . ? 0.5438 0.5584 0.5217 -0.0322 0.0010 0.0039 906 HOH A O 3535 O O . HOH O . ? 0.5113 0.4996 0.4811 -0.0139 -0.0008 0.0055 907 HOH A O 3536 O O . HOH O . ? 0.4096 0.4346 0.4101 -0.0010 -0.0108 0.0017 908 HOH A O 3537 O O . HOH O . ? 0.4557 0.5123 0.3709 -0.0155 -0.0164 0.0162 909 HOH A O 3538 O O . HOH O . ? 0.6174 0.6604 0.5571 -0.0148 -0.0136 0.0081 910 HOH A O 3539 O O . HOH O . ? 0.5166 0.5838 0.4901 -0.0542 -0.0247 -0.0156 911 HOH A O 3540 O O . HOH O . ? 0.5627 0.5620 0.5431 -0.0016 -0.0041 0.0022 912 HOH A O 3541 O O . HOH O . ? 0.6358 0.6547 0.6229 0.0001 -0.0089 0.0026 913 HOH A O 3542 O O . HOH O . ? 0.5137 0.5939 0.5170 0.0068 -0.0252 0.0177 914 HOH A O 3543 O O . HOH O . ? 0.6396 0.6572 0.6247 -0.0130 0.0033 0.0159 915 HOH A O 3544 O O . HOH O . ? 0.6238 0.6318 0.6122 -0.0069 -0.0040 0.0155 916 HOH A O 3545 O O . HOH O . ? 0.6150 0.6488 0.5800 -0.0030 -0.0135 0.0225 917 HOH A O 3546 O O . HOH O . ? 0.5004 0.5301 0.4517 -0.0454 -0.0178 -0.0204 918 HOH A O 3547 O O . HOH O . ? 0.5451 0.6035 0.5567 0.0031 -0.0043 -0.0050 919 HOH A O 3548 O O . HOH O . ? 0.5360 0.5664 0.5373 0.0085 -0.0058 0.0022 920 HOH A O 3549 O O . HOH O . ? 0.4713 0.5566 0.4234 -0.0368 -0.0338 -0.0058 921 HOH A O 3550 O O . HOH O . ? 0.5312 0.4688 0.4765 -0.0068 0.0107 -0.0136 922 HOH A O 3551 O O . HOH O . ? 0.5198 0.5430 0.4746 -0.0406 -0.0152 -0.0185 923 HOH A O 3552 O O . HOH O . ? 0.4586 0.4826 0.4259 -0.0096 -0.0003 0.0079 924 HOH A O 3553 O O . HOH O . ? 0.7064 0.7899 0.6550 -0.0269 -0.0328 0.0023 925 HOH A O 3554 O O . HOH O . ? 0.5184 0.5487 0.5039 -0.0432 -0.0052 -0.0046 926 HOH A O 3555 O O . HOH O . ? 0.5511 0.6260 0.5015 -0.0437 -0.0311 -0.0125 927 HOH A O 3556 O O . HOH O . ? 0.6076 0.5949 0.6037 -0.0036 -0.0039 0.0106 928 HOH A O 3557 O O . HOH O . ? 0.4522 0.5159 0.4655 0.0003 -0.0125 0.0018 929 HOH A O 3558 O O . HOH O . ? 0.5469 0.5719 0.5475 0.0029 -0.0057 -0.0110 930 HOH A O 3559 O O . HOH O . ? 0.4891 0.5979 0.5050 -0.0038 0.0132 -0.0052 931 HOH A O 3560 O O . HOH O . ? 0.5434 0.6324 0.5558 -0.0195 -0.0182 0.0005 932 HOH A O 3561 O O . HOH O . ? 0.6544 0.6249 0.5958 -0.0412 -0.0023 -0.0247 933 HOH A O 3562 O O . HOH O . ? 0.4776 0.5081 0.3917 -0.0306 -0.0116 -0.0173 934 HOH A O 3563 O O . HOH O . ? 0.5710 0.6246 0.4885 -0.0250 -0.0189 -0.0015 935 HOH A O 3564 O O . HOH O . ? 0.5319 0.6207 0.5530 -0.0058 -0.0125 0.0017 936 HOH A O 3565 O O . HOH O . ? 0.5557 0.5851 0.5324 -0.0584 -0.0100 -0.0130 937 HOH A O 3566 O O . HOH O . ? 0.5468 0.5487 0.5454 0.0051 -0.0076 0.0093 938 HOH A O 3567 O O . HOH O . ? 0.4846 0.5802 0.5005 0.0014 0.0086 -0.0067 939 HOH A O 3568 O O . HOH O . ? 0.4709 0.5166 0.4812 0.0053 -0.0099 0.0001 940 HOH A O 3569 O O . HOH O . ? 0.5844 0.5801 0.5237 -0.0317 -0.0057 -0.0233 941 HOH A O 3570 O O . HOH O . ? 0.6389 0.7339 0.6526 -0.0068 -0.0227 0.0069 942 HOH A O 3571 O O . HOH O . ? 0.7039 0.6014 0.6363 -0.0077 0.0162 -0.0035 943 HOH A O 3572 O O . HOH O . ? 0.5691 0.6382 0.5721 -0.0396 -0.0100 -0.0038 944 HOH A O 3573 O O . HOH O . ? 0.6301 0.7268 0.6056 -0.0229 -0.0342 0.0052 945 HOH A O 3574 O O . HOH O . ? 0.5910 0.6194 0.5865 -0.0005 -0.0128 0.0075 946 HOH A O 3575 O O . HOH O . ? 0.5198 0.6058 0.5101 -0.0371 -0.0263 -0.0055 947 HOH A O 3576 O O . HOH O . ? 0.5001 0.5928 0.5180 -0.0147 -0.0159 0.0014 948 HOH A O 3577 O O . HOH O . ? 0.6358 0.7462 0.6464 -0.0024 0.0175 -0.0068 949 HOH A O 3578 O O . HOH O . ? 0.5733 0.6049 0.5738 0.0073 -0.0080 0.0026 950 HOH A O 3579 O O . HOH O . ? 0.6215 0.7363 0.6283 -0.0190 -0.0308 0.0059 951 HOH A O 3580 O O . HOH O . ? 0.5238 0.5721 0.5338 0.0047 -0.0117 0.0023 952 HOH A O 3581 O O . HOH O . ? 0.5898 0.6684 0.5942 -0.0380 -0.0151 -0.0045 953 HOH A O 3582 O O . HOH O . ? 0.6310 0.5998 0.5990 0.0122 0.0078 -0.0024 954 HOH A O 3583 O O . HOH O . ? 0.6160 0.5590 0.5645 0.0087 0.0159 -0.0142 955 HOH A O 3584 O O . HOH O . ? 0.5639 0.5635 0.5361 -0.0265 0.0007 0.0047 956 HOH A O 3585 O O . HOH O . ? 0.5603 0.6088 0.5394 -0.0542 -0.0166 -0.0141 957 HOH A O 3586 O O . HOH O . ? 0.5925 0.5781 0.5962 -0.0273 -0.0042 -0.0103 958 HOH A O 3587 O O . HOH O . ? 0.5560 0.6211 0.5341 0.0037 -0.0258 0.0246 959 HOH A O 3588 O O . HOH O . ? 0.6254 0.6123 0.6294 -0.0247 -0.0014 0.0002 960 HOH A O 3589 O O . HOH O . ? 0.6896 0.6652 0.6913 -0.0283 -0.0026 -0.0101 961 HOH A O 3590 O O . HOH O . ? 0.5857 0.6218 0.5888 0.0036 -0.0096 0.0009 962 HOH A O 3591 O O . HOH O . ? 0.5888 0.5446 0.5231 -0.0539 -0.0006 -0.0283 963 HOH A O 3592 O O . HOH O . ? 0.6683 0.6987 0.6618 -0.0131 0.0072 0.0098 964 HOH A O 3593 O O . HOH O . ? 0.6454 0.5753 0.5809 -0.0044 0.0155 -0.0213 965 HOH A O 3594 O O . HOH O . ? 0.3160 0.3631 0.3128 -0.0079 -0.0161 0.0025 966 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 1 ARG ARG A . n A 1 2 ASN 2 84 2 ASN ASN A . n A 1 3 PHE 3 85 3 PHE PHE A . n A 1 4 ASN 4 86 4 ASN ASN A . n A 1 5 ASN 5 87 5 ASN ASN A . n A 1 6 LEU 6 88 6 LEU LEU A . n A 1 7 THR 7 89 7 THR THR A . n A 1 8 LYS 8 90 8 LYS LYS A . n A 1 9 GLY 9 91 9 GLY GLY A . n A 1 10 LEU 10 92 10 LEU LEU A . n A 1 11 CYS 11 93 11 CYS CYS A . n A 1 12 THR 12 94 12 THR THR A . n A 1 13 ILE 13 95 13 ILE ILE A . n A 1 14 ASN 14 96 14 ASN ASN A . n A 1 15 SER 15 97 15 SER SER A . n A 1 16 TRP 16 98 16 TRP TRP A . n A 1 17 HIS 17 99 17 HIS HIS A . n A 1 18 ILE 18 100 18 ILE ILE A . n A 1 19 TYR 19 101 19 TYR TYR A . n A 1 20 GLY 20 102 20 GLY GLY A . n A 1 21 LYS 21 103 21 LYS LYS A . n A 1 22 ASP 22 104 22 ASP ASP A . n A 1 23 ASN 23 105 23 ASN ASN A . n A 1 24 ALA 24 106 24 ALA ALA A . n A 1 25 VAL 25 107 25 VAL VAL A . n A 1 26 ARG 26 108 26 ARG ARG A . n A 1 27 ILE 27 109 27 ILE ILE A . n A 1 28 GLY 28 110 28 GLY GLY A . n A 1 29 GLU 29 111 29 GLU GLU A . n A 1 30 SER 30 112 30 SER SER A . n A 1 31 SER 31 113 31 SER SER A . n A 1 32 ASP 32 114 32 ASP ASP A . n A 1 33 VAL 33 115 33 VAL VAL A . n A 1 34 LEU 34 116 34 LEU LEU A . n A 1 35 VAL 35 117 35 VAL VAL A . n A 1 36 THR 36 118 36 THR THR A . n A 1 37 ARG 37 119 37 ARG ARG A . n A 1 38 GLU 38 120 38 GLU GLU A . n A 1 39 PRO 39 121 39 PRO PRO A . n A 1 40 TYR 40 122 40 TYR TYR A . n A 1 41 VAL 41 123 41 VAL VAL A . n A 1 42 SER 42 124 42 SER SER A . n A 1 43 CYS 43 125 43 CYS CYS A . n A 1 44 ASP 44 126 44 ASP ASP A . n A 1 45 PRO 45 127 45 PRO PRO A . n A 1 46 ASP 46 128 46 ASP ASP A . n A 1 47 GLU 47 129 47 GLU GLU A . n A 1 48 CYS 48 130 48 CYS CYS A . n A 1 49 ARG 49 131 49 ARG ARG A . n A 1 50 PHE 50 132 50 PHE PHE A . n A 1 51 TYR 51 133 51 TYR TYR A . n A 1 52 ALA 52 134 52 ALA ALA A . n A 1 53 LEU 53 135 53 LEU LEU A . n A 1 54 SER 54 136 54 SER SER A . n A 1 55 GLN 55 137 55 GLN GLN A . n A 1 56 GLY 56 138 56 GLY GLY A . n A 1 57 THR 57 139 57 THR THR A . n A 1 58 THR 58 140 58 THR THR A . n A 1 59 ILE 59 141 59 ILE ILE A . n A 1 60 ARG 60 142 60 ARG ARG A . n A 1 61 GLY 61 143 61 GLY GLY A . n A 1 62 LYS 62 144 62 LYS LYS A . n A 1 63 HIS 63 145 63 HIS HIS A . n A 1 64 SER 64 146 64 SER SER A . n A 1 65 ASN 65 147 65 ASN ASN A . n A 1 66 GLY 66 148 66 GLY GLY A . n A 1 67 THR 67 149 67 THR THR A . n A 1 68 ILE 68 150 68 ILE ILE A . n A 1 69 HIS 69 151 69 HIS HIS A . n A 1 70 ASP 70 152 70 ASP ASP A . n A 1 71 ARG 71 153 71 ARG ARG A . n A 1 72 SER 72 154 72 SER SER A . n A 1 73 GLN 73 155 73 GLN GLN A . n A 1 74 TYR 74 156 74 TYR TYR A . n A 1 75 ARG 75 157 75 ARG ARG A . n A 1 76 ALA 76 158 76 ALA ALA A . n A 1 77 LEU 77 159 77 LEU LEU A . n A 1 78 ILE 78 160 78 ILE ILE A . n A 1 79 SER 79 161 79 SER SER A . n A 1 80 TRP 80 162 80 TRP TRP A . n A 1 81 PRO 81 163 81 PRO PRO A . n A 1 82 LEU 82 164 82 LEU LEU A . n A 1 83 SER 83 165 83 SER SER A . n A 1 84 SER 84 166 84 SER SER A . n A 1 85 PRO 85 167 85 PRO PRO A . n A 1 86 PRO 86 168 86 PRO PRO A . n A 1 87 THR 87 169 87 THR THR A . n A 1 88 VAL 88 170 88 VAL VAL A . n A 1 89 TYR 89 171 89 TYR TYR A . n A 1 90 ASN 90 172 90 ASN ASN A . n A 1 91 SER 91 173 91 SER SER A . n A 1 92 ARG 92 174 92 ARG ARG A . n A 1 93 VAL 93 175 93 VAL VAL A . n A 1 94 GLU 94 176 94 GLU GLU A . n A 1 95 CYS 95 177 95 CYS CYS A . n A 1 96 ILE 96 178 96 ILE ILE A . n A 1 97 GLY 97 179 97 GLY GLY A . n A 1 98 TRP 98 180 98 TRP TRP A . n A 1 99 SER 99 181 99 SER SER A . n A 1 100 SER 100 182 100 SER SER A . n A 1 101 THR 101 183 101 THR THR A . n A 1 102 SER 102 184 102 SER SER A . n A 1 103 CYS 103 185 103 CYS CYS A . n A 1 104 HIS 104 186 104 HIS HIS A . n A 1 105 ASP 105 187 105 ASP ASP A . n A 1 106 GLY 106 188 106 GLY GLY A . n A 1 107 LYS 107 189 107 LYS LYS A . n A 1 108 SER 108 190 108 SER SER A . n A 1 109 ARG 109 191 109 ARG ARG A . n A 1 110 MET 110 192 110 MET MET A . n A 1 111 SER 111 193 111 SER SER A . n A 1 112 ILE 112 194 112 ILE ILE A . n A 1 113 CYS 113 195 113 CYS CYS A . n A 1 114 ILE 114 196 114 ILE ILE A . n A 1 115 SER 115 197 115 SER SER A . n A 1 116 GLY 116 198 116 GLY GLY A . n A 1 117 PRO 117 199 117 PRO PRO A . n A 1 118 ASN 118 200 118 ASN ASN A . n A 1 119 ASN 119 201 119 ASN ASN A . n A 1 120 ASN 120 202 120 ASN ASN A . n A 1 121 ALA 121 203 121 ALA ALA A . n A 1 122 SER 122 204 122 SER SER A . n A 1 123 ALA 123 205 123 ALA ALA A . n A 1 124 VAL 124 206 124 VAL VAL A . n A 1 125 VAL 125 207 125 VAL VAL A . n A 1 126 TRP 126 208 126 TRP TRP A . n A 1 127 TYR 127 209 127 TYR TYR A . n A 1 128 ASN 128 210 128 ASN ASN A . n A 1 129 ARG 129 211 129 ARG ARG A . n A 1 130 ARG 130 212 130 ARG ARG A . n A 1 131 PRO 131 213 131 PRO PRO A . n A 1 132 VAL 132 214 132 VAL VAL A . n A 1 133 ALA 133 215 133 ALA ALA A . n A 1 134 GLU 134 216 134 GLU GLU A . n A 1 135 ILE 135 217 135 ILE ILE A . n A 1 136 ASN 136 218 136 ASN ASN A . n A 1 137 THR 137 219 137 THR THR A . n A 1 138 TRP 138 220 138 TRP TRP A . n A 1 139 ALA 139 221 139 ALA ALA A . n A 1 140 ARG 140 222 140 ARG ARG A . n A 1 141 ASN 141 223 141 ASN ASN A . n A 1 142 ILE 142 224 142 ILE ILE A . n A 1 143 LEU 143 225 143 LEU LEU A . n A 1 144 ARG 144 226 144 ARG ARG A . n A 1 145 THR 145 227 145 THR THR A . n A 1 146 GLN 146 228 146 GLN GLN A . n A 1 147 GLU 147 229 147 GLU GLU A . n A 1 148 SER 148 230 148 SER SER A . n A 1 149 GLU 149 231 149 GLU GLU A . n A 1 150 CYS 150 232 150 CYS CYS A . n A 1 151 VAL 151 233 151 VAL VAL A . n A 1 152 CYS 152 234 152 CYS CYS A . n A 1 153 HIS 153 235 153 HIS HIS A . n A 1 154 ASN 154 236 154 ASN ASN A . n A 1 155 GLY 155 237 155 GLY GLY A . n A 1 156 VAL 156 238 156 VAL VAL A . n A 1 157 CYS 157 239 157 CYS CYS A . n A 1 158 PRO 158 240 158 PRO PRO A . n A 1 159 VAL 159 241 159 VAL VAL A . n A 1 160 VAL 160 242 160 VAL VAL A . n A 1 161 PHE 161 243 161 PHE PHE A . n A 1 162 THR 162 244 162 THR THR A . n A 1 163 ASP 163 245 163 ASP ASP A . n A 1 164 GLY 164 246 164 GLY GLY A . n A 1 165 SER 165 247 165 SER SER A . n A 1 166 ALA 166 248 166 ALA ALA A . n A 1 167 THR 167 249 167 THR THR A . n A 1 168 GLY 168 250 168 GLY GLY A . n A 1 169 PRO 169 251 169 PRO PRO A . n A 1 170 ALA 170 252 170 ALA ALA A . n A 1 171 ASP 171 253 171 ASP ASP A . n A 1 172 THR 172 254 172 THR THR A . n A 1 173 ARG 173 255 173 ARG ARG A . n A 1 174 ILE 174 256 174 ILE ILE A . n A 1 175 TYR 175 257 175 TYR TYR A . n A 1 176 TYR 176 258 176 TYR TYR A . n A 1 177 PHE 177 259 177 PHE PHE A . n A 1 178 LYS 178 260 178 LYS LYS A . n A 1 179 GLU 179 261 179 GLU GLU A . n A 1 180 GLY 180 262 180 GLY GLY A . n A 1 181 LYS 181 263 181 LYS LYS A . n A 1 182 ILE 182 264 182 ILE ILE A . n A 1 183 LEU 183 265 183 LEU LEU A . n A 1 184 LYS 184 266 184 LYS LYS A . n A 1 185 TRP 185 267 185 TRP TRP A . n A 1 186 GLU 186 268 186 GLU GLU A . n A 1 187 SER 187 269 187 SER SER A . n A 1 188 LEU 188 270 188 LEU LEU A . n A 1 189 THR 189 271 189 THR THR A . n A 1 190 GLY 190 272 190 GLY GLY A . n A 1 191 THR 191 273 191 THR THR A . n A 1 192 ALA 192 274 192 ALA ALA A . n A 1 193 LYS 193 275 193 LYS LYS A . n A 1 194 HIS 194 276 194 HIS HIS A . n A 1 195 ILE 195 277 195 ILE ILE A . n A 1 196 GLU 196 278 196 GLU GLU A . n A 1 197 GLU 197 279 197 GLU GLU A . n A 1 198 CYS 198 280 198 CYS CYS A . n A 1 199 SER 199 281 199 SER SER A . n A 1 200 CYS 200 282 200 CYS CYS A . n A 1 201 TYR 201 283 201 TYR TYR A . n A 1 202 GLY 202 284 202 GLY GLY A . n A 1 203 GLU 203 285 203 GLU GLU A . n A 1 204 ARG 204 286 204 ARG ARG A . n A 1 205 THR 205 287 205 THR THR A . n A 1 206 GLY 206 288 206 GLY GLY A . n A 1 207 ILE 207 289 207 ILE ILE A . n A 1 208 THR 208 290 208 THR THR A . n A 1 209 CYS 209 291 209 CYS CYS A . n A 1 210 THR 210 292 210 THR THR A . n A 1 211 CYS 211 293 211 CYS CYS A . n A 1 212 LYS 212 294 212 LYS LYS A . n A 1 213 ASP 213 295 213 ASP ASP A . n A 1 214 ASN 214 296 214 ASN ASN A . n A 1 215 TRP 215 297 215 TRP TRP A . n A 1 216 GLN 216 298 216 GLN GLN A . n A 1 217 GLY 217 299 217 GLY GLY A . n A 1 218 SER 218 300 218 SER SER A . n A 1 219 ASN 219 301 219 ASN ASN A . n A 1 220 ARG 220 302 220 ARG ARG A . n A 1 221 PRO 221 303 221 PRO PRO A . n A 1 222 VAL 222 304 222 VAL VAL A . n A 1 223 ILE 223 305 223 ILE ILE A . n A 1 224 GLN 224 306 224 GLN GLN A . n A 1 225 ILE 225 307 225 ILE ILE A . n A 1 226 ASP 226 308 226 ASP ASP A . n A 1 227 PRO 227 309 227 PRO PRO A . n A 1 228 VAL 228 310 228 VAL VAL A . n A 1 229 ALA 229 311 229 ALA ALA A . n A 1 230 MET 230 312 230 MET MET A . n A 1 231 THR 231 313 231 THR THR A . n A 1 232 HIS 232 314 232 HIS HIS A . n A 1 233 THR 233 315 233 THR THR A . n A 1 234 SER 234 316 234 SER SER A . n A 1 235 GLN 235 317 235 GLN GLN A . n A 1 236 TYR 236 318 236 TYR TYR A . n A 1 237 ILE 237 319 237 ILE ILE A . n A 1 238 CYS 238 320 238 CYS CYS A . n A 1 239 SER 239 321 239 SER SER A . n A 1 240 PRO 240 322 240 PRO PRO A . n A 1 241 VAL 241 323 241 VAL VAL A . n A 1 242 LEU 242 324 242 LEU LEU A . n A 1 243 THR 243 325 243 THR THR A . n A 1 244 ASP 244 326 244 ASP ASP A . n A 1 245 ASN 245 327 245 ASN ASN A . n A 1 246 PRO 246 328 246 PRO PRO A . n A 1 247 ARG 247 329 247 ARG ARG A . n A 1 248 PRO 248 330 248 PRO PRO A . n A 1 249 ASN 249 331 249 ASN ASN A . n A 1 250 ASP 250 332 250 ASP ASP A . n A 1 251 PRO 251 333 251 PRO PRO A . n A 1 252 ASN 252 334 252 ASN ASN A . n A 1 253 ILE 253 335 253 ILE ILE A . n A 1 254 GLY 254 336 254 GLY GLY A . n A 1 255 LYS 255 337 255 LYS LYS A . n A 1 256 CYS 256 338 256 CYS CYS A . n A 1 257 ASN 257 339 257 ASN ASN A . n A 1 258 ASP 258 340 258 ASP ASP A . n A 1 259 PRO 259 341 259 PRO PRO A . n A 1 260 TYR 260 342 260 TYR TYR A . n A 1 261 PRO 261 343 261 PRO PRO A . n A 1 262 GLY 262 344 262 GLY GLY A . n A 1 263 ASN 263 345 263 ASN ASN A . n A 1 264 ASN 264 346 264 ASN ASN A . n A 1 265 ASN 265 347 265 ASN ASN A . n A 1 266 ASN 266 348 266 ASN ASN A . n A 1 267 GLY 267 349 267 GLY GLY A . n A 1 268 VAL 268 350 268 VAL VAL A . n A 1 269 LYS 269 351 269 LYS LYS A . n A 1 270 GLY 270 352 270 GLY GLY A . n A 1 271 PHE 271 353 271 PHE PHE A . n A 1 272 SER 272 354 272 SER SER A . n A 1 273 TYR 273 355 273 TYR TYR A . n A 1 274 LEU 274 356 274 LEU LEU A . n A 1 275 ASP 275 357 275 ASP ASP A . n A 1 276 GLY 276 358 276 GLY GLY A . n A 1 277 ALA 277 359 277 ALA ALA A . n A 1 278 ASN 278 360 278 ASN ASN A . n A 1 279 THR 279 361 279 THR THR A . n A 1 280 TRP 280 362 280 TRP TRP A . n A 1 281 LEU 281 363 281 LEU LEU A . n A 1 282 GLY 282 364 282 GLY GLY A . n A 1 283 ARG 283 365 283 ARG ARG A . n A 1 284 THR 284 366 284 THR THR A . n A 1 285 ILE 285 367 285 ILE ILE A . n A 1 286 SER 286 368 286 SER SER A . n A 1 287 THR 287 369 287 THR THR A . n A 1 288 ALA 288 370 288 ALA ALA A . n A 1 289 SER 289 371 289 SER SER A . n A 1 290 ARG 290 372 290 ARG ARG A . n A 1 291 SER 291 373 291 SER SER A . n A 1 292 GLY 292 374 292 GLY GLY A . n A 1 293 TYR 293 375 293 TYR TYR A . n A 1 294 GLU 294 376 294 GLU GLU A . n A 1 295 MET 295 377 295 MET MET A . n A 1 296 LEU 296 378 296 LEU LEU A . n A 1 297 LYS 297 379 297 LYS LYS A . n A 1 298 VAL 298 380 298 VAL VAL A . n A 1 299 PRO 299 381 299 PRO PRO A . n A 1 300 ASN 300 382 300 ASN ASN A . n A 1 301 ALA 301 383 301 ALA ALA A . n A 1 302 LEU 302 384 302 LEU LEU A . n A 1 303 THR 303 385 303 THR THR A . n A 1 304 ASP 304 386 304 ASP ASP A . n A 1 305 ASP 305 387 305 ASP ASP A . n A 1 306 ARG 306 388 306 ARG ARG A . n A 1 307 SER 307 389 307 SER SER A . n A 1 308 LYS 308 390 308 LYS LYS A . n A 1 309 PRO 309 391 309 PRO PRO A . n A 1 310 ILE 310 392 310 ILE ILE A . n A 1 311 GLN 311 393 311 GLN GLN A . n A 1 312 GLY 312 394 312 GLY GLY A . n A 1 313 GLN 313 395 313 GLN GLN A . n A 1 314 THR 314 396 314 THR THR A . n A 1 315 ILE 315 397 315 ILE ILE A . n A 1 316 VAL 316 398 316 VAL VAL A . n A 1 317 LEU 317 399 317 LEU LEU A . n A 1 318 ASN 318 400 318 ASN ASN A . n A 1 319 ALA 319 401 319 ALA ALA A . n A 1 320 ASP 320 402 320 ASP ASP A . n A 1 321 TRP 321 403 321 TRP TRP A . n A 1 322 SER 322 404 322 SER SER A . n A 1 323 GLY 323 405 323 GLY GLY A . n A 1 324 TYR 324 406 324 TYR TYR A . n A 1 325 SER 325 407 325 SER SER A . n A 1 326 GLY 326 408 326 GLY GLY A . n A 1 327 SER 327 409 327 SER SER A . n A 1 328 PHE 328 410 328 PHE PHE A . n A 1 329 MET 329 411 329 MET MET A . n A 1 330 ASP 330 412 330 ASP ASP A . n A 1 331 TYR 331 413 331 TYR TYR A . n A 1 332 TRP 332 414 332 TRP TRP A . n A 1 333 ALA 333 415 333 ALA ALA A . n A 1 334 GLU 334 416 334 GLU GLU A . n A 1 335 GLY 335 417 335 GLY GLY A . n A 1 336 ASP 336 418 336 ASP ASP A . n A 1 337 CYS 337 419 337 CYS CYS A . n A 1 338 TYR 338 420 338 TYR TYR A . n A 1 339 ARG 339 421 339 ARG ARG A . n A 1 340 ALA 340 422 340 ALA ALA A . n A 1 341 CYS 341 423 341 CYS CYS A . n A 1 342 PHE 342 424 342 PHE PHE A . n A 1 343 TYR 343 425 343 TYR TYR A . n A 1 344 VAL 344 426 344 VAL VAL A . n A 1 345 GLU 345 427 345 GLU GLU A . n A 1 346 LEU 346 428 346 LEU LEU A . n A 1 347 ILE 347 429 347 ILE ILE A . n A 1 348 ARG 348 430 348 ARG ARG A . n A 1 349 GLY 349 431 349 GLY GLY A . n A 1 350 ARG 350 432 350 ARG ARG A . n A 1 351 PRO 351 433 351 PRO PRO A . n A 1 352 LYS 352 434 352 LYS LYS A . n A 1 353 GLU 353 435 353 GLU GLU A . n A 1 354 ASP 354 436 354 ASP ASP A . n A 1 355 LYS 355 437 355 LYS LYS A . n A 1 356 VAL 356 438 356 VAL VAL A . n A 1 357 TRP 357 439 357 TRP TRP A . n A 1 358 TRP 358 440 358 TRP TRP A . n A 1 359 THR 359 441 359 THR THR A . n A 1 360 SER 360 442 360 SER SER A . n A 1 361 ASN 361 443 361 ASN ASN A . n A 1 362 SER 362 444 362 SER SER A . n A 1 363 ILE 363 445 363 ILE ILE A . n A 1 364 VAL 364 446 364 VAL VAL A . n A 1 365 SER 365 447 365 SER SER A . n A 1 366 MET 366 448 366 MET MET A . n A 1 367 CYS 367 449 367 CYS CYS A . n A 1 368 SER 368 450 368 SER SER A . n A 1 369 SER 369 451 369 SER SER A . n A 1 370 THR 370 452 370 THR THR A . n A 1 371 GLU 371 453 371 GLU GLU A . n A 1 372 PHE 372 454 372 PHE PHE A . n A 1 373 LEU 373 455 373 LEU LEU A . n A 1 374 GLY 374 456 374 GLY GLY A . n A 1 375 GLN 375 457 375 GLN GLN A . n A 1 376 TRP 376 458 376 TRP TRP A . n A 1 377 ASN 377 459 377 ASN ASN A . n A 1 378 TRP 378 460 378 TRP TRP A . n A 1 379 PRO 379 461 379 PRO PRO A . n A 1 380 ASP 380 462 380 ASP ASP A . n A 1 381 GLY 381 463 381 GLY GLY A . n A 1 382 ALA 382 464 382 ALA ALA A . n A 1 383 LYS 383 465 383 LYS LYS A . n A 1 384 ILE 384 466 384 ILE ILE A . n A 1 385 GLU 385 467 385 GLU GLU A . n A 1 386 TYR 386 468 386 TYR TYR A . n A 1 387 PHE 387 469 387 PHE PHE A . n A 1 388 LEU 388 470 388 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 BCZ 1 513 801 BCZ BCZ A . O 7 HOH 1 601 1 HOH HOH A . O 7 HOH 2 602 2 HOH HOH A . O 7 HOH 3 603 3 HOH HOH A . O 7 HOH 4 604 4 HOH HOH A . O 7 HOH 5 605 5 HOH HOH A . O 7 HOH 6 606 6 HOH HOH A . O 7 HOH 7 607 7 HOH HOH A . O 7 HOH 8 608 8 HOH HOH A . O 7 HOH 9 609 9 HOH HOH A . O 7 HOH 10 610 10 HOH HOH A . O 7 HOH 11 611 11 HOH HOH A . O 7 HOH 12 612 12 HOH HOH A . O 7 HOH 13 613 13 HOH HOH A . O 7 HOH 14 614 14 HOH HOH A . O 7 HOH 15 615 15 HOH HOH A . O 7 HOH 16 616 16 HOH HOH A . O 7 HOH 17 617 17 HOH HOH A . O 7 HOH 18 618 18 HOH HOH A . O 7 HOH 19 619 19 HOH HOH A . O 7 HOH 20 620 20 HOH HOH A . O 7 HOH 21 621 21 HOH HOH A . O 7 HOH 22 622 22 HOH HOH A . O 7 HOH 23 623 23 HOH HOH A . O 7 HOH 24 624 24 HOH HOH A . O 7 HOH 25 625 25 HOH HOH A . O 7 HOH 26 626 26 HOH HOH A . O 7 HOH 27 627 27 HOH HOH A . O 7 HOH 28 628 28 HOH HOH A . O 7 HOH 29 629 29 HOH HOH A . O 7 HOH 30 630 30 HOH HOH A . O 7 HOH 31 631 31 HOH HOH A . O 7 HOH 32 632 32 HOH HOH A . O 7 HOH 33 633 33 HOH HOH A . O 7 HOH 34 634 34 HOH HOH A . O 7 HOH 35 635 35 HOH HOH A . O 7 HOH 36 636 36 HOH HOH A . O 7 HOH 37 637 37 HOH HOH A . O 7 HOH 38 638 38 HOH HOH A . O 7 HOH 39 639 39 HOH HOH A . O 7 HOH 40 640 40 HOH HOH A . O 7 HOH 41 641 41 HOH HOH A . O 7 HOH 42 642 42 HOH HOH A . O 7 HOH 43 643 43 HOH HOH A . O 7 HOH 44 644 44 HOH HOH A . O 7 HOH 45 645 45 HOH HOH A . O 7 HOH 46 646 46 HOH HOH A . O 7 HOH 47 647 47 HOH HOH A . O 7 HOH 48 648 48 HOH HOH A . O 7 HOH 49 649 49 HOH HOH A . O 7 HOH 50 650 50 HOH HOH A . O 7 HOH 51 651 51 HOH HOH A . O 7 HOH 52 652 52 HOH HOH A . O 7 HOH 53 653 53 HOH HOH A . O 7 HOH 54 654 54 HOH HOH A . O 7 HOH 55 655 55 HOH HOH A . O 7 HOH 56 656 56 HOH HOH A . O 7 HOH 57 657 57 HOH HOH A . O 7 HOH 58 658 58 HOH HOH A . O 7 HOH 59 659 59 HOH HOH A . O 7 HOH 60 660 60 HOH HOH A . O 7 HOH 61 661 61 HOH HOH A . O 7 HOH 62 662 62 HOH HOH A . O 7 HOH 63 663 63 HOH HOH A . O 7 HOH 64 664 64 HOH HOH A . O 7 HOH 65 665 65 HOH HOH A . O 7 HOH 66 666 66 HOH HOH A . O 7 HOH 67 667 67 HOH HOH A . O 7 HOH 68 668 68 HOH HOH A . O 7 HOH 69 669 69 HOH HOH A . O 7 HOH 70 670 70 HOH HOH A . O 7 HOH 71 671 71 HOH HOH A . O 7 HOH 72 672 72 HOH HOH A . O 7 HOH 73 673 73 HOH HOH A . O 7 HOH 74 674 74 HOH HOH A . O 7 HOH 75 675 75 HOH HOH A . O 7 HOH 76 676 76 HOH HOH A . O 7 HOH 77 677 77 HOH HOH A . O 7 HOH 78 678 78 HOH HOH A . O 7 HOH 79 679 79 HOH HOH A . O 7 HOH 80 680 80 HOH HOH A . O 7 HOH 81 681 81 HOH HOH A . O 7 HOH 82 682 82 HOH HOH A . O 7 HOH 83 683 83 HOH HOH A . O 7 HOH 84 684 84 HOH HOH A . O 7 HOH 85 685 85 HOH HOH A . O 7 HOH 86 686 86 HOH HOH A . O 7 HOH 87 687 87 HOH HOH A . O 7 HOH 88 688 88 HOH HOH A . O 7 HOH 89 689 89 HOH HOH A . O 7 HOH 90 690 90 HOH HOH A . O 7 HOH 91 691 91 HOH HOH A . O 7 HOH 92 692 92 HOH HOH A . O 7 HOH 93 693 93 HOH HOH A . O 7 HOH 94 694 94 HOH HOH A . O 7 HOH 95 695 95 HOH HOH A . O 7 HOH 96 696 96 HOH HOH A . O 7 HOH 97 697 97 HOH HOH A . O 7 HOH 98 698 98 HOH HOH A . O 7 HOH 99 699 99 HOH HOH A . O 7 HOH 100 700 100 HOH HOH A . O 7 HOH 101 701 101 HOH HOH A . O 7 HOH 102 702 102 HOH HOH A . O 7 HOH 103 703 103 HOH HOH A . O 7 HOH 104 704 104 HOH HOH A . O 7 HOH 105 705 105 HOH HOH A . O 7 HOH 106 706 106 HOH HOH A . O 7 HOH 107 707 107 HOH HOH A . O 7 HOH 108 708 108 HOH HOH A . O 7 HOH 109 709 109 HOH HOH A . O 7 HOH 110 710 110 HOH HOH A . O 7 HOH 111 711 111 HOH HOH A . O 7 HOH 112 712 112 HOH HOH A . O 7 HOH 113 713 113 HOH HOH A . O 7 HOH 114 714 114 HOH HOH A . O 7 HOH 115 715 115 HOH HOH A . O 7 HOH 116 716 116 HOH HOH A . O 7 HOH 117 717 117 HOH HOH A . O 7 HOH 118 718 118 HOH HOH A . O 7 HOH 119 719 119 HOH HOH A . O 7 HOH 120 720 120 HOH HOH A . O 7 HOH 121 721 121 HOH HOH A . O 7 HOH 122 722 122 HOH HOH A . O 7 HOH 123 723 123 HOH HOH A . O 7 HOH 124 724 124 HOH HOH A . O 7 HOH 125 725 125 HOH HOH A . O 7 HOH 126 726 126 HOH HOH A . O 7 HOH 127 727 127 HOH HOH A . O 7 HOH 128 728 128 HOH HOH A . O 7 HOH 129 729 129 HOH HOH A . O 7 HOH 130 730 130 HOH HOH A . O 7 HOH 131 731 131 HOH HOH A . O 7 HOH 132 732 132 HOH HOH A . O 7 HOH 133 733 133 HOH HOH A . O 7 HOH 134 734 134 HOH HOH A . O 7 HOH 135 735 135 HOH HOH A . O 7 HOH 136 736 136 HOH HOH A . O 7 HOH 137 737 137 HOH HOH A . O 7 HOH 138 738 138 HOH HOH A . O 7 HOH 139 739 139 HOH HOH A . O 7 HOH 140 740 140 HOH HOH A . O 7 HOH 141 741 141 HOH HOH A . O 7 HOH 142 742 142 HOH HOH A . O 7 HOH 143 743 143 HOH HOH A . O 7 HOH 144 744 144 HOH HOH A . O 7 HOH 145 745 145 HOH HOH A . O 7 HOH 146 746 146 HOH HOH A . O 7 HOH 147 747 147 HOH HOH A . O 7 HOH 148 748 148 HOH HOH A . O 7 HOH 149 749 149 HOH HOH A . O 7 HOH 150 750 150 HOH HOH A . O 7 HOH 151 751 151 HOH HOH A . O 7 HOH 152 752 152 HOH HOH A . O 7 HOH 153 753 153 HOH HOH A . O 7 HOH 154 754 154 HOH HOH A . O 7 HOH 155 755 155 HOH HOH A . O 7 HOH 156 756 156 HOH HOH A . O 7 HOH 157 757 157 HOH HOH A . O 7 HOH 158 758 158 HOH HOH A . O 7 HOH 159 759 159 HOH HOH A . O 7 HOH 160 760 160 HOH HOH A . O 7 HOH 161 761 161 HOH HOH A . O 7 HOH 162 762 162 HOH HOH A . O 7 HOH 163 763 163 HOH HOH A . O 7 HOH 164 764 164 HOH HOH A . O 7 HOH 165 765 165 HOH HOH A . O 7 HOH 166 766 166 HOH HOH A . O 7 HOH 167 767 167 HOH HOH A . O 7 HOH 168 768 168 HOH HOH A . O 7 HOH 169 769 169 HOH HOH A . O 7 HOH 170 770 170 HOH HOH A . O 7 HOH 171 771 171 HOH HOH A . O 7 HOH 172 772 172 HOH HOH A . O 7 HOH 173 773 173 HOH HOH A . O 7 HOH 174 774 174 HOH HOH A . O 7 HOH 175 775 175 HOH HOH A . O 7 HOH 176 776 176 HOH HOH A . O 7 HOH 177 777 177 HOH HOH A . O 7 HOH 178 778 178 HOH HOH A . O 7 HOH 179 779 179 HOH HOH A . O 7 HOH 180 780 180 HOH HOH A . O 7 HOH 181 781 181 HOH HOH A . O 7 HOH 182 782 182 HOH HOH A . O 7 HOH 183 783 183 HOH HOH A . O 7 HOH 184 784 184 HOH HOH A . O 7 HOH 185 785 185 HOH HOH A . O 7 HOH 186 786 186 HOH HOH A . O 7 HOH 187 787 187 HOH HOH A . O 7 HOH 188 788 188 HOH HOH A . O 7 HOH 189 789 189 HOH HOH A . O 7 HOH 190 790 190 HOH HOH A . O 7 HOH 191 791 191 HOH HOH A . O 7 HOH 192 792 192 HOH HOH A . O 7 HOH 193 793 193 HOH HOH A . O 7 HOH 194 794 194 HOH HOH A . O 7 HOH 195 795 195 HOH HOH A . O 7 HOH 196 796 196 HOH HOH A . O 7 HOH 197 797 197 HOH HOH A . O 7 HOH 198 798 198 HOH HOH A . O 7 HOH 199 799 199 HOH HOH A . O 7 HOH 200 800 200 HOH HOH A . O 7 HOH 201 801 201 HOH HOH A . O 7 HOH 202 802 202 HOH HOH A . O 7 HOH 203 803 203 HOH HOH A . O 7 HOH 204 804 204 HOH HOH A . O 7 HOH 205 805 205 HOH HOH A . O 7 HOH 206 806 206 HOH HOH A . O 7 HOH 207 807 207 HOH HOH A . O 7 HOH 208 808 208 HOH HOH A . O 7 HOH 209 809 209 HOH HOH A . O 7 HOH 210 810 210 HOH HOH A . O 7 HOH 211 811 211 HOH HOH A . O 7 HOH 212 812 212 HOH HOH A . O 7 HOH 213 813 213 HOH HOH A . O 7 HOH 214 814 214 HOH HOH A . O 7 HOH 215 815 215 HOH HOH A . O 7 HOH 216 816 216 HOH HOH A . O 7 HOH 217 817 217 HOH HOH A . O 7 HOH 218 818 218 HOH HOH A . O 7 HOH 219 819 219 HOH HOH A . O 7 HOH 220 820 220 HOH HOH A . O 7 HOH 221 821 221 HOH HOH A . O 7 HOH 222 822 222 HOH HOH A . O 7 HOH 223 823 223 HOH HOH A . O 7 HOH 224 824 224 HOH HOH A . O 7 HOH 225 825 225 HOH HOH A . O 7 HOH 226 826 226 HOH HOH A . O 7 HOH 227 827 227 HOH HOH A . O 7 HOH 228 828 228 HOH HOH A . O 7 HOH 229 829 229 HOH HOH A . O 7 HOH 230 830 230 HOH HOH A . O 7 HOH 231 831 231 HOH HOH A . O 7 HOH 232 832 232 HOH HOH A . O 7 HOH 233 833 233 HOH HOH A . O 7 HOH 234 834 234 HOH HOH A . O 7 HOH 235 835 235 HOH HOH A . O 7 HOH 236 836 236 HOH HOH A . O 7 HOH 237 837 237 HOH HOH A . O 7 HOH 238 838 238 HOH HOH A . O 7 HOH 239 839 239 HOH HOH A . O 7 HOH 240 840 240 HOH HOH A . O 7 HOH 241 841 241 HOH HOH A . O 7 HOH 242 842 242 HOH HOH A . O 7 HOH 243 843 243 HOH HOH A . O 7 HOH 244 844 244 HOH HOH A . O 7 HOH 245 845 245 HOH HOH A . O 7 HOH 246 846 246 HOH HOH A . O 7 HOH 247 847 247 HOH HOH A . O 7 HOH 248 848 248 HOH HOH A . O 7 HOH 249 849 249 HOH HOH A . O 7 HOH 250 850 250 HOH HOH A . O 7 HOH 251 851 251 HOH HOH A . O 7 HOH 252 852 252 HOH HOH A . O 7 HOH 253 853 253 HOH HOH A . O 7 HOH 254 854 254 HOH HOH A . O 7 HOH 255 855 255 HOH HOH A . O 7 HOH 256 856 256 HOH HOH A . O 7 HOH 257 857 257 HOH HOH A . O 7 HOH 258 858 258 HOH HOH A . O 7 HOH 259 859 259 HOH HOH A . O 7 HOH 260 860 260 HOH HOH A . O 7 HOH 261 861 261 HOH HOH A . O 7 HOH 262 862 262 HOH HOH A . O 7 HOH 263 863 263 HOH HOH A . O 7 HOH 264 864 264 HOH HOH A . O 7 HOH 265 865 265 HOH HOH A . O 7 HOH 266 866 266 HOH HOH A . O 7 HOH 267 867 267 HOH HOH A . O 7 HOH 268 868 268 HOH HOH A . O 7 HOH 269 869 269 HOH HOH A . O 7 HOH 270 870 270 HOH HOH A . O 7 HOH 271 871 271 HOH HOH A . O 7 HOH 272 872 272 HOH HOH A . O 7 HOH 273 873 273 HOH HOH A . O 7 HOH 274 874 274 HOH HOH A . O 7 HOH 275 875 275 HOH HOH A . O 7 HOH 276 876 276 HOH HOH A . O 7 HOH 277 877 277 HOH HOH A . O 7 HOH 278 878 278 HOH HOH A . O 7 HOH 279 879 279 HOH HOH A . O 7 HOH 280 880 280 HOH HOH A . O 7 HOH 281 881 281 HOH HOH A . O 7 HOH 282 882 282 HOH HOH A . O 7 HOH 283 883 283 HOH HOH A . O 7 HOH 284 884 284 HOH HOH A . O 7 HOH 285 885 285 HOH HOH A . O 7 HOH 286 886 286 HOH HOH A . O 7 HOH 287 887 287 HOH HOH A . O 7 HOH 288 888 288 HOH HOH A . O 7 HOH 289 889 289 HOH HOH A . O 7 HOH 290 890 290 HOH HOH A . O 7 HOH 291 891 291 HOH HOH A . O 7 HOH 292 892 292 HOH HOH A . O 7 HOH 293 893 293 HOH HOH A . O 7 HOH 294 894 294 HOH HOH A . O 7 HOH 295 895 295 HOH HOH A . O 7 HOH 296 896 296 HOH HOH A . O 7 HOH 297 897 297 HOH HOH A . O 7 HOH 298 898 298 HOH HOH A . O 7 HOH 299 899 299 HOH HOH A . O 7 HOH 300 900 300 HOH HOH A . O 7 HOH 301 901 301 HOH HOH A . O 7 HOH 302 902 302 HOH HOH A . O 7 HOH 303 903 303 HOH HOH A . O 7 HOH 304 904 304 HOH HOH A . O 7 HOH 305 905 305 HOH HOH A . O 7 HOH 306 906 306 HOH HOH A . O 7 HOH 307 907 307 HOH HOH A . O 7 HOH 308 908 308 HOH HOH A . O 7 HOH 309 909 309 HOH HOH A . O 7 HOH 310 910 310 HOH HOH A . O 7 HOH 311 911 311 HOH HOH A . O 7 HOH 312 912 312 HOH HOH A . O 7 HOH 313 913 313 HOH HOH A . O 7 HOH 314 914 314 HOH HOH A . O 7 HOH 315 915 315 HOH HOH A . O 7 HOH 316 916 316 HOH HOH A . O 7 HOH 317 917 317 HOH HOH A . O 7 HOH 318 918 318 HOH HOH A . O 7 HOH 319 919 319 HOH HOH A . O 7 HOH 320 920 320 HOH HOH A . O 7 HOH 321 921 321 HOH HOH A . O 7 HOH 322 922 322 HOH HOH A . O 7 HOH 323 923 323 HOH HOH A . O 7 HOH 324 924 324 HOH HOH A . O 7 HOH 325 925 325 HOH HOH A . O 7 HOH 326 926 326 HOH HOH A . O 7 HOH 327 927 327 HOH HOH A . O 7 HOH 328 928 328 HOH HOH A . O 7 HOH 329 929 329 HOH HOH A . O 7 HOH 330 930 330 HOH HOH A . O 7 HOH 331 931 331 HOH HOH A . O 7 HOH 332 932 332 HOH HOH A . O 7 HOH 333 933 333 HOH HOH A . O 7 HOH 334 934 334 HOH HOH A . O 7 HOH 335 935 335 HOH HOH A . O 7 HOH 336 936 336 HOH HOH A . O 7 HOH 337 937 337 HOH HOH A . O 7 HOH 338 938 338 HOH HOH A . O 7 HOH 339 939 339 HOH HOH A . O 7 HOH 340 940 340 HOH HOH A . O 7 HOH 341 941 341 HOH HOH A . O 7 HOH 342 942 342 HOH HOH A . O 7 HOH 343 943 343 HOH HOH A . O 7 HOH 344 944 344 HOH HOH A . O 7 HOH 345 945 345 HOH HOH A . O 7 HOH 346 946 346 HOH HOH A . O 7 HOH 347 947 347 HOH HOH A . O 7 HOH 348 948 348 HOH HOH A . O 7 HOH 349 949 349 HOH HOH A . O 7 HOH 350 950 350 HOH HOH A . O 7 HOH 351 951 351 HOH HOH A . O 7 HOH 352 952 352 HOH HOH A . O 7 HOH 353 953 353 HOH HOH A . O 7 HOH 354 954 354 HOH HOH A . O 7 HOH 355 955 355 HOH HOH A . O 7 HOH 356 956 356 HOH HOH A . O 7 HOH 357 957 357 HOH HOH A . O 7 HOH 358 958 358 HOH HOH A . O 7 HOH 359 959 359 HOH HOH A . O 7 HOH 360 960 360 HOH HOH A . O 7 HOH 361 961 361 HOH HOH A . O 7 HOH 362 962 362 HOH HOH A . O 7 HOH 363 963 363 HOH HOH A . O 7 HOH 364 964 364 HOH HOH A . O 7 HOH 365 965 365 HOH HOH A . O 7 HOH 366 966 366 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 120 A ASN 202 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 65 A ASN 147 ? 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,O # 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)' 28810 ? 1 MORE 100 ? 1 'SSA (A^2)' 45980 ? # 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' 3_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' 21_555 z,y,-x 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 4 'crystal symmetry operation' 23_555 -z,y,x 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 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 698 ? O HOH . 2 1 A HOH 776 ? O 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 ? O HOH . ? A HOH 615 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 98.9 ? 2 O ? O HOH . ? A HOH 615 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? O HOH . ? A HOH 708 ? 1_555 89.6 ? 3 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? O HOH . ? A HOH 708 ? 1_555 171.3 ? 4 O ? O HOH . ? A HOH 615 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASP 213 ? A ASP 295 ? 1_555 175.4 ? 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 85.1 ? 6 O ? O HOH . ? A HOH 708 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASP 213 ? A ASP 295 ? 1_555 86.3 ? 7 O ? O HOH . ? A HOH 615 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASN 266 ? A ASN 348 ? 1_555 88.4 ? 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_555 103.7 ? 9 O ? O HOH . ? A HOH 708 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A ASN 266 ? A ASN 348 ? 1_555 78.4 ? 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 93.1 ? 11 O ? O HOH . ? A HOH 615 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A GLY 217 ? A GLY 299 ? 1_555 107.5 ? 12 OD2 ? A ASP 244 ? A ASP 326 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A GLY 217 ? A GLY 299 ? 1_555 83.4 ? 13 O ? O HOH . ? A HOH 708 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A GLY 217 ? A GLY 299 ? 1_555 92.2 ? 14 O ? A ASP 213 ? A ASP 295 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A GLY 217 ? A GLY 299 ? 1_555 70.4 ? 15 O ? A ASN 266 ? A ASN 348 ? 1_555 CA ? M CA . ? A CA 512 ? 1_555 O ? A GLY 217 ? A GLY 299 ? 1_555 161.6 ? # 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 19.7834 _pdbx_refine_tls.origin_y -54.8071 _pdbx_refine_tls.origin_z 19.8063 _pdbx_refine_tls.T[1][1] 0.1205 _pdbx_refine_tls.T[2][2] 0.1396 _pdbx_refine_tls.T[3][3] 0.1067 _pdbx_refine_tls.T[1][2] -0.0112 _pdbx_refine_tls.T[1][3] -0.0090 _pdbx_refine_tls.T[2][3] -0.0037 _pdbx_refine_tls.L[1][1] 0.1948 _pdbx_refine_tls.L[2][2] 0.1338 _pdbx_refine_tls.L[3][3] 0.2914 _pdbx_refine_tls.L[1][2] 0.0107 _pdbx_refine_tls.L[1][3] -0.0518 _pdbx_refine_tls.L[2][3] -0.0206 _pdbx_refine_tls.S[1][1] 0.0111 _pdbx_refine_tls.S[2][2] -0.0052 _pdbx_refine_tls.S[3][3] 0.0000 _pdbx_refine_tls.S[1][2] -0.0319 _pdbx_refine_tls.S[1][3] 0.0030 _pdbx_refine_tls.S[2][3] -0.0028 _pdbx_refine_tls.S[2][1] 0.0294 _pdbx_refine_tls.S[3][1] -0.0372 _pdbx_refine_tls.S[3][2] 0.0353 # _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.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _pdbx_refine_tls_group.selection_details ALL _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal HKL-2000 'data collection' . ? 1 PHENIX refinement '(phenix.refine: 1.7.3_928)' ? 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 O4 A NAG 501 ? ? O A HOH 903 ? ? 1.86 2 1 O A HOH 901 ? ? O A HOH 951 ? ? 1.96 3 1 O A HOH 631 ? ? O A HOH 747 ? ? 1.97 4 1 O5 A NAG 501 ? ? O A HOH 823 ? ? 2.11 5 1 O A HOH 747 ? ? O A HOH 899 ? ? 2.14 6 1 O A HOH 779 ? ? O A HOH 818 ? ? 2.18 7 1 O A HOH 734 ? ? O A HOH 780 ? ? 2.19 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 925 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 925 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 37_545 _pdbx_validate_symm_contact.dist 1.54 # 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 112 ? ? -151.93 59.67 2 1 SER A 112 ? ? -151.93 59.32 3 1 SER A 165 ? ? 70.09 -5.02 4 1 SER A 165 ? ? 70.09 -5.56 5 1 ASN A 202 ? ? -149.74 37.59 6 1 ASN A 223 ? ? -150.63 78.30 7 1 ILE A 224 ? ? 54.87 70.15 8 1 THR A 227 ? ? -139.10 -157.93 9 1 LYS A 266 ? ? -176.31 148.90 10 1 CYS A 293 ? ? -117.22 -156.98 11 1 GLN A 317 ? ? -161.52 -160.47 12 1 ASP A 357 ? ? -151.45 61.02 13 1 SER A 404 ? ? -116.07 -134.71 14 1 SER A 442 ? ? -147.53 -159.49 # 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 '3-(1-ACETYLAMINO-2-ETHYL-BUTYL)-4-GUANIDINO-2-HYDROXY-CYCLOPENTANECARBOXYLIC ACID' BCZ 7 water HOH #