data_4LQY # _entry.id 4LQY # _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 4LQY RCSB RCSB080974 WWPDB D_1000080974 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4LR0 . unspecified PDB 4LR1 . unspecified PDB 4LR2 . unspecified PDB 4LR5 . unspecified # _pdbx_database_status.entry_id 4LQY _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2013-07-19 _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Albright, R.A.' 1 'Braddock, D.T.' 2 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary ;Molecular basis of purinergic signal metabolism by ectonucleotide pyrophosphatase/phosphodiesterases 4 and 1 and implications in stroke. ; J.Biol.Chem. 289 3294 3306 2014 JBCHA3 US 0021-9258 0071 ? 24338010 10.1074/jbc.M113.505867 1 'NPP4 is a procoagulant enzyme on the surface of vascular endothelium' Blood 120 4432 4440 2012 ? US 0006-4971 ? ? 22995898 ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Albright, R.A.' 1 primary 'Ornstein, D.L.' 2 primary 'Cao, W.' 3 primary 'Chang, W.C.' 4 primary 'Robert, D.' 5 primary 'Tehan, M.' 6 primary 'Hoyer, D.' 7 primary 'Liu, L.' 8 primary 'Stabach, P.' 9 primary 'Yang, G.' 10 primary 'De La Cruz, E.M.' 11 primary 'Braddock, D.T.' 12 1 'Albright, R.A.' 13 1 'Chang, W.C.' 14 1 'Robert, D.' 15 1 'Ornstein, D.L.' 16 1 'Cao, W.' 17 1 'Liu, L.' 18 1 'Redick, M.E.' 19 1 'Young, J.I.' 20 1 'De La Cruz, E.M.' 21 1 'Braddock, D.T.' 22 # _cell.length_a 181.533 _cell.length_b 51.143 _cell.length_c 52.741 _cell.angle_alpha 90.000 _cell.angle_beta 102.380 _cell.angle_gamma 90.000 _cell.entry_id 4LQY _cell.pdbx_unique_axis ? _cell.Z_PDB 4 _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.space_group_name_H-M 'C 1 2 1' _symmetry.entry_id 4LQY _symmetry.Int_Tables_number 5 _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _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 ;Bis(5'-adenosyl)-triphosphatase ENPP4 ; 46109.957 1 3.6.1.29 ? 'UNP residues 16-402' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer syn 'ADENOSINE MONOPHOSPHATE' 347.221 1 ? ? ? ? 4 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 5 water nat water 18.015 464 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'AP3A hydrolase, AP3Aase, Ectonucleotide pyrophosphatase/phosphodiesterase family member 4, E-NPP 4, NPP-4' # _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 ;FRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYD AVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSN PPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCI DHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADEGWTIVLNESSQKLGD HGYDNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILGLKPHPNNGTFGHTKCLLVDQWCINLPEALINENLYF Q ; _entity_poly.pdbx_seq_one_letter_code_can ;FRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYD AVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSN PPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCI DHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADEGWTIVLNESSQKLGD HGYDNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILGLKPHPNNGTFGHTKCLLVDQWCINLPEALINENLYF Q ; _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 PHE n 1 2 ARG n 1 3 SER n 1 4 ASP n 1 5 SER n 1 6 SER n 1 7 SER n 1 8 SER n 1 9 LEU n 1 10 PRO n 1 11 PRO n 1 12 LYS n 1 13 LEU n 1 14 LEU n 1 15 LEU n 1 16 VAL n 1 17 SER n 1 18 PHE n 1 19 ASP n 1 20 GLY n 1 21 PHE n 1 22 ARG n 1 23 ALA n 1 24 ASP n 1 25 TYR n 1 26 LEU n 1 27 LYS n 1 28 ASN n 1 29 TYR n 1 30 GLU n 1 31 PHE n 1 32 PRO n 1 33 HIS n 1 34 LEU n 1 35 GLN n 1 36 ASN n 1 37 PHE n 1 38 ILE n 1 39 LYS n 1 40 GLU n 1 41 GLY n 1 42 VAL n 1 43 LEU n 1 44 VAL n 1 45 GLU n 1 46 HIS n 1 47 VAL n 1 48 LYS n 1 49 ASN n 1 50 VAL n 1 51 PHE n 1 52 ILE n 1 53 THR n 1 54 LYS n 1 55 THR n 1 56 PHE n 1 57 PRO n 1 58 ASN n 1 59 HIS n 1 60 TYR n 1 61 SER n 1 62 ILE n 1 63 VAL n 1 64 THR n 1 65 GLY n 1 66 LEU n 1 67 TYR n 1 68 GLU n 1 69 GLU n 1 70 SER n 1 71 HIS n 1 72 GLY n 1 73 ILE n 1 74 VAL n 1 75 ALA n 1 76 ASN n 1 77 SER n 1 78 MET n 1 79 TYR n 1 80 ASP n 1 81 ALA n 1 82 VAL n 1 83 THR n 1 84 LYS n 1 85 LYS n 1 86 HIS n 1 87 PHE n 1 88 SER n 1 89 ASP n 1 90 SER n 1 91 ASN n 1 92 ASP n 1 93 LYS n 1 94 ASP n 1 95 PRO n 1 96 PHE n 1 97 TRP n 1 98 TRP n 1 99 ASN n 1 100 GLU n 1 101 ALA n 1 102 VAL n 1 103 PRO n 1 104 ILE n 1 105 TRP n 1 106 VAL n 1 107 THR n 1 108 ASN n 1 109 GLN n 1 110 LEU n 1 111 GLN n 1 112 GLU n 1 113 ASN n 1 114 ARG n 1 115 SER n 1 116 SER n 1 117 ALA n 1 118 ALA n 1 119 ALA n 1 120 MET n 1 121 TRP n 1 122 PRO n 1 123 GLY n 1 124 THR n 1 125 ASP n 1 126 VAL n 1 127 PRO n 1 128 ILE n 1 129 HIS n 1 130 ASP n 1 131 THR n 1 132 ILE n 1 133 SER n 1 134 SER n 1 135 TYR n 1 136 PHE n 1 137 MET n 1 138 ASN n 1 139 TYR n 1 140 ASN n 1 141 SER n 1 142 SER n 1 143 VAL n 1 144 SER n 1 145 PHE n 1 146 GLU n 1 147 GLU n 1 148 ARG n 1 149 LEU n 1 150 ASN n 1 151 ASN n 1 152 ILE n 1 153 THR n 1 154 MET n 1 155 TRP n 1 156 LEU n 1 157 ASN n 1 158 ASN n 1 159 SER n 1 160 ASN n 1 161 PRO n 1 162 PRO n 1 163 VAL n 1 164 THR n 1 165 PHE n 1 166 ALA n 1 167 THR n 1 168 LEU n 1 169 TYR n 1 170 TRP n 1 171 GLU n 1 172 GLU n 1 173 PRO n 1 174 ASP n 1 175 ALA n 1 176 SER n 1 177 GLY n 1 178 HIS n 1 179 LYS n 1 180 TYR n 1 181 GLY n 1 182 PRO n 1 183 GLU n 1 184 ASP n 1 185 LYS n 1 186 GLU n 1 187 ASN n 1 188 MET n 1 189 SER n 1 190 ARG n 1 191 VAL n 1 192 LEU n 1 193 LYS n 1 194 LYS n 1 195 ILE n 1 196 ASP n 1 197 ASP n 1 198 LEU n 1 199 ILE n 1 200 GLY n 1 201 ASP n 1 202 LEU n 1 203 VAL n 1 204 GLN n 1 205 ARG n 1 206 LEU n 1 207 LYS n 1 208 MET n 1 209 LEU n 1 210 GLY n 1 211 LEU n 1 212 TRP n 1 213 GLU n 1 214 ASN n 1 215 LEU n 1 216 ASN n 1 217 VAL n 1 218 ILE n 1 219 ILE n 1 220 THR n 1 221 SER n 1 222 ASP n 1 223 HIS n 1 224 GLY n 1 225 MET n 1 226 THR n 1 227 GLN n 1 228 CYS n 1 229 SER n 1 230 GLN n 1 231 ASP n 1 232 ARG n 1 233 LEU n 1 234 ILE n 1 235 ASN n 1 236 LEU n 1 237 ASP n 1 238 SER n 1 239 CYS n 1 240 ILE n 1 241 ASP n 1 242 HIS n 1 243 SER n 1 244 TYR n 1 245 TYR n 1 246 THR n 1 247 LEU n 1 248 ILE n 1 249 ASP n 1 250 LEU n 1 251 SER n 1 252 PRO n 1 253 VAL n 1 254 ALA n 1 255 ALA n 1 256 ILE n 1 257 LEU n 1 258 PRO n 1 259 LYS n 1 260 ILE n 1 261 ASN n 1 262 ARG n 1 263 THR n 1 264 GLU n 1 265 VAL n 1 266 TYR n 1 267 ASN n 1 268 LYS n 1 269 LEU n 1 270 LYS n 1 271 ASN n 1 272 CYS n 1 273 SER n 1 274 PRO n 1 275 HIS n 1 276 MET n 1 277 ASN n 1 278 VAL n 1 279 TYR n 1 280 LEU n 1 281 LYS n 1 282 GLU n 1 283 ASP n 1 284 ILE n 1 285 PRO n 1 286 ASN n 1 287 ARG n 1 288 PHE n 1 289 TYR n 1 290 TYR n 1 291 GLN n 1 292 HIS n 1 293 ASN n 1 294 ASP n 1 295 ARG n 1 296 ILE n 1 297 GLN n 1 298 PRO n 1 299 ILE n 1 300 ILE n 1 301 LEU n 1 302 VAL n 1 303 ALA n 1 304 ASP n 1 305 GLU n 1 306 GLY n 1 307 TRP n 1 308 THR n 1 309 ILE n 1 310 VAL n 1 311 LEU n 1 312 ASN n 1 313 GLU n 1 314 SER n 1 315 SER n 1 316 GLN n 1 317 LYS n 1 318 LEU n 1 319 GLY n 1 320 ASP n 1 321 HIS n 1 322 GLY n 1 323 TYR n 1 324 ASP n 1 325 ASN n 1 326 SER n 1 327 LEU n 1 328 PRO n 1 329 SER n 1 330 MET n 1 331 HIS n 1 332 PRO n 1 333 PHE n 1 334 LEU n 1 335 ALA n 1 336 ALA n 1 337 HIS n 1 338 GLY n 1 339 PRO n 1 340 ALA n 1 341 PHE n 1 342 HIS n 1 343 LYS n 1 344 GLY n 1 345 TYR n 1 346 LYS n 1 347 HIS n 1 348 SER n 1 349 THR n 1 350 ILE n 1 351 ASN n 1 352 ILE n 1 353 VAL n 1 354 ASP n 1 355 ILE n 1 356 TYR n 1 357 PRO n 1 358 MET n 1 359 MET n 1 360 CYS n 1 361 HIS n 1 362 ILE n 1 363 LEU n 1 364 GLY n 1 365 LEU n 1 366 LYS n 1 367 PRO n 1 368 HIS n 1 369 PRO n 1 370 ASN n 1 371 ASN n 1 372 GLY n 1 373 THR n 1 374 PHE n 1 375 GLY n 1 376 HIS n 1 377 THR n 1 378 LYS n 1 379 CYS n 1 380 LEU n 1 381 LEU n 1 382 VAL n 1 383 ASP n 1 384 GLN n 1 385 TRP n 1 386 CYS n 1 387 ILE n 1 388 ASN n 1 389 LEU n 1 390 PRO n 1 391 GLU n 1 392 ALA n 1 393 LEU n 1 394 ILE n 1 395 ASN n 1 396 GLU n 1 397 ASN n 1 398 LEU n 1 399 TYR n 1 400 PHE n 1 401 GLN 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 human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'ENPP4, KIAA0879, NPP4' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Trichoplusia ni' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7111 _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 HIGH5 _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pFASTBAC1 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code ENPP4_HUMAN _struct_ref.pdbx_db_accession Q9Y6X5 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;FRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYD AVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSN PPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCI DHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADEGWTIVLNESSQKLGD HGYDNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILGLKPHPNNGTFGHTKCLLVDQWCINLPEA ; _struct_ref.pdbx_align_begin 16 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4LQY _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 392 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9Y6X5 _struct_ref_seq.db_align_beg 16 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 407 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 16 _struct_ref_seq.pdbx_auth_seq_align_end 407 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4LQY LEU A 393 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 408 1 1 4LQY ILE A 394 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 409 2 1 4LQY ASN A 395 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 410 3 1 4LQY GLU A 396 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 411 4 1 4LQY ASN A 397 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 412 5 1 4LQY LEU A 398 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 413 6 1 4LQY TYR A 399 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 414 7 1 4LQY PHE A 400 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 415 8 1 4LQY GLN A 401 ? UNP Q9Y6X5 ? ? 'EXPRESSION TAG' 416 9 # 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 AMP non-polymer . 'ADENOSINE MONOPHOSPHATE' ? 'C10 H14 N5 O7 P' 347.221 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.crystals_number 1 _exptl.entry_id 4LQY _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.75 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 55.20 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'hanging drop' _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.temp 293 _exptl_crystal_grow.pdbx_details '200 mM ammonium citrate dibasic, 17.5% to 19.5% (w/v) PEG 3350, pH 6.5, hanging drop, temperature 293K' _exptl_crystal_grow.temp_details ? _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 2010-05-10 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.07500 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 24-ID-C' _diffrn_source.pdbx_wavelength_list 1.07500 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 24-ID-C # _reflns.entry_id 4LQY _reflns.d_resolution_high 1.500 _reflns.d_resolution_low 50.000 _reflns.number_obs 74645 _reflns.pdbx_Rmerge_I_obs 0.064 _reflns.pdbx_netI_over_sigmaI 14.700 _reflns.pdbx_chi_squared 1.872 _reflns.pdbx_redundancy 3.900 _reflns.percent_possible_obs 98.900 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.number_all ? _reflns.B_iso_Wilson_estimate ? _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_scaling_rejects ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # loop_ _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.number_measured_obs _reflns_shell.number_measured_all _reflns_shell.number_unique_obs _reflns_shell.Rmerge_I_obs _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.percent_possible_all _reflns_shell.pdbx_ordinal _reflns_shell.pdbx_diffrn_id 1.500 1.540 ? ? ? 0.662 ? ? 1.309 3.400 ? 4991 94.200 1 1 1.540 1.580 ? ? ? 0.534 ? ? 1.247 3.900 ? 5310 98.600 2 1 1.580 1.630 ? ? ? 0.423 ? ? 1.229 3.900 ? 5289 98.900 3 1 1.630 1.680 ? ? ? 0.339 ? ? 1.308 3.900 ? 5280 98.800 4 1 1.680 1.740 ? ? ? 0.248 ? ? 1.400 3.900 ? 5319 99.100 5 1 1.740 1.810 ? ? ? 0.198 ? ? 1.453 3.900 ? 5344 99.100 6 1 1.810 1.890 ? ? ? 0.154 ? ? 1.696 3.900 ? 5371 99.500 7 1 1.890 1.990 ? ? ? 0.120 ? ? 1.884 3.900 ? 5333 99.600 8 1 1.990 2.110 ? ? ? 0.093 ? ? 2.151 3.900 ? 5365 99.600 9 1 2.110 2.280 ? ? ? 0.077 ? ? 2.239 4.000 ? 5377 99.900 10 1 2.280 2.510 ? ? ? 0.066 ? ? 2.193 4.000 ? 5411 100.000 11 1 2.510 2.870 ? ? ? 0.063 ? ? 2.716 4.100 ? 5403 100.000 12 1 2.870 3.610 ? ? ? 0.047 ? ? 2.486 4.000 ? 5453 99.900 13 1 3.610 50.000 ? ? ? 0.040 ? ? 2.609 4.000 ? 5399 97.300 14 1 # _refine.entry_id 4LQY _refine.ls_d_res_high 1.5400 _refine.ls_d_res_low 37.8520 _refine.pdbx_ls_sigma_F 1.340 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 99.1400 _refine.ls_number_reflns_obs 69525 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method ? _refine.pdbx_R_Free_selection_details ? _refine.details ? _refine.ls_R_factor_obs 0.1424 _refine.ls_R_factor_R_work 0.1402 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.1844 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 5.0600 _refine.ls_number_reflns_R_free 3515 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 26.3885 _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.1500 _refine.overall_SU_B ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.pdbx_solvent_vdw_probe_radii 1.1100 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.9000 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model 'PDB ENTRY 2GSU' _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 0.8934 _refine.B_iso_max 75.610 _refine.B_iso_min 8.670 _refine.pdbx_overall_phase_error 18.0100 _refine.occupancy_max 1.000 _refine.occupancy_min 1.000 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.ls_R_factor_all ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3068 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 81 _refine_hist.number_atoms_solvent 464 _refine_hist.number_atoms_total 3613 _refine_hist.d_res_high 1.5400 _refine_hist.d_res_low 37.8520 # loop_ _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 _refine_ls_restr.pdbx_refine_id f_bond_d 3248 0.009 ? ? ? 'X-RAY DIFFRACTION' f_angle_d 4431 1.270 ? ? ? 'X-RAY DIFFRACTION' f_chiral_restr 484 0.088 ? ? ? 'X-RAY DIFFRACTION' f_plane_restr 561 0.007 ? ? ? 'X-RAY DIFFRACTION' f_dihedral_angle_d 1174 15.473 ? ? ? 'X-RAY DIFFRACTION' # 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.redundancy_reflns_obs _refine_ls_shell.pdbx_refine_id 1.54 1.5610 25 96.0000 2557 . 0.1810 0.2884 . 129 . 2686 . . 'X-RAY DIFFRACTION' 1.5610 1.5833 25 99.0000 2569 . 0.1710 0.2613 . 158 . 2727 . . 'X-RAY DIFFRACTION' 1.5833 1.6069 25 99.0000 2635 . 0.1639 0.2416 . 139 . 2774 . . 'X-RAY DIFFRACTION' 1.6069 1.6320 25 99.0000 2592 . 0.1604 0.2498 . 153 . 2745 . . 'X-RAY DIFFRACTION' 1.6320 1.6588 25 99.0000 2614 . 0.1546 0.2357 . 126 . 2740 . . 'X-RAY DIFFRACTION' 1.6588 1.6874 25 99.0000 2590 . 0.1419 0.2301 . 159 . 2749 . . 'X-RAY DIFFRACTION' 1.6874 1.7181 25 99.0000 2642 . 0.1403 0.2005 . 138 . 2780 . . 'X-RAY DIFFRACTION' 1.7181 1.7511 25 99.0000 2659 . 0.1373 0.2081 . 143 . 2802 . . 'X-RAY DIFFRACTION' 1.7511 1.7868 25 99.0000 2600 . 0.1398 0.2347 . 121 . 2721 . . 'X-RAY DIFFRACTION' 1.7868 1.8257 25 99.0000 2690 . 0.1335 0.1784 . 115 . 2805 . . 'X-RAY DIFFRACTION' 1.8257 1.8682 25 99.0000 2602 . 0.1270 0.1910 . 134 . 2736 . . 'X-RAY DIFFRACTION' 1.8682 1.9149 25 100.0000 2677 . 0.1271 0.1748 . 115 . 2792 . . 'X-RAY DIFFRACTION' 1.9149 1.9667 25 100.0000 2670 . 0.1274 0.1634 . 142 . 2812 . . 'X-RAY DIFFRACTION' 1.9667 2.0245 25 100.0000 2627 . 0.1288 0.1810 . 142 . 2769 . . 'X-RAY DIFFRACTION' 2.0245 2.0899 25 100.0000 2648 . 0.1294 0.1895 . 146 . 2794 . . 'X-RAY DIFFRACTION' 2.0899 2.1646 25 100.0000 2630 . 0.1280 0.1714 . 145 . 2775 . . 'X-RAY DIFFRACTION' 2.1646 2.2512 25 100.0000 2664 . 0.1285 0.1965 . 140 . 2804 . . 'X-RAY DIFFRACTION' 2.2512 2.3537 25 100.0000 2655 . 0.1316 0.1629 . 141 . 2796 . . 'X-RAY DIFFRACTION' 2.3537 2.4777 25 100.0000 2660 . 0.1381 0.1734 . 141 . 2801 . . 'X-RAY DIFFRACTION' 2.4777 2.6329 25 100.0000 2687 . 0.1406 0.1949 . 146 . 2833 . . 'X-RAY DIFFRACTION' 2.6329 2.8361 25 100.0000 2664 . 0.1412 0.1769 . 148 . 2812 . . 'X-RAY DIFFRACTION' 2.8361 3.1214 25 100.0000 2668 . 0.1436 0.1716 . 154 . 2822 . . 'X-RAY DIFFRACTION' 3.1214 3.5728 25 100.0000 2675 . 0.1315 0.1535 . 140 . 2815 . . 'X-RAY DIFFRACTION' 3.5728 4.5002 25 99.0000 2717 . 0.1330 0.1685 . 136 . 2853 . . 'X-RAY DIFFRACTION' 4.5002 37.852 25 95.0000 2618 . 0.1694 0.1970 . 164 . 2782 . . 'X-RAY DIFFRACTION' # _struct.entry_id 4LQY _struct.title 'Crystal Structure of Human ENPP4 with AMP' _struct.pdbx_descriptor ;Bis(5'-adenosyl)-triphosphatase ENPP4 (E.C.3.6.1.29) ; _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4LQY _struct_keywords.text 'NPP4, ENPP4, phosphodiesterase, hydrolase' _struct_keywords.pdbx_keywords HYDROLASE # 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 5 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 24 ? TYR A 29 ? ASP A 39 TYR A 44 1 ? 6 HELX_P HELX_P2 2 PHE A 31 ? GLU A 40 ? PHE A 46 GLU A 55 1 ? 10 HELX_P HELX_P3 3 LYS A 54 ? GLY A 65 ? LYS A 69 GLY A 80 1 ? 12 HELX_P HELX_P4 4 TYR A 67 ? GLY A 72 ? TYR A 82 GLY A 87 1 ? 6 HELX_P HELX_P5 5 ASP A 94 ? TRP A 98 ? ASP A 109 TRP A 113 5 ? 5 HELX_P HELX_P6 6 PRO A 103 ? LEU A 110 ? PRO A 118 LEU A 125 1 ? 8 HELX_P HELX_P7 7 SER A 144 ? ASN A 158 ? SER A 159 ASN A 173 1 ? 15 HELX_P HELX_P8 8 PRO A 173 ? GLY A 181 ? PRO A 188 GLY A 196 1 ? 9 HELX_P HELX_P9 9 ASP A 184 ? LEU A 209 ? ASP A 199 LEU A 224 1 ? 26 HELX_P HELX_P10 10 ASP A 237 ? CYS A 239 ? ASP A 252 CYS A 254 5 ? 3 HELX_P HELX_P11 11 ASP A 241 ? SER A 243 ? ASP A 256 SER A 258 5 ? 3 HELX_P HELX_P12 12 ASN A 261 ? LYS A 270 ? ASN A 276 LYS A 285 1 ? 10 HELX_P HELX_P13 13 GLU A 282 ? ILE A 284 ? GLU A 297 ILE A 299 5 ? 3 HELX_P HELX_P14 14 PRO A 285 ? TYR A 289 ? PRO A 300 TYR A 304 5 ? 5 HELX_P HELX_P15 15 LEU A 327 ? HIS A 331 ? LEU A 342 HIS A 346 5 ? 5 HELX_P HELX_P16 16 ASP A 354 ? GLY A 364 ? ASP A 369 GLY A 379 1 ? 11 HELX_P HELX_P17 17 THR A 373 ? LEU A 381 ? THR A 388 LEU A 396 5 ? 9 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 239 SG ? ? ? 1_555 A CYS 272 SG ? ? A CYS 254 A CYS 287 1_555 ? ? ? ? ? ? ? 2.028 ? disulf2 disulf ? ? A CYS 379 SG ? ? ? 1_555 A CYS 386 SG ? ? A CYS 394 A CYS 401 1_555 ? ? ? ? ? ? ? 2.046 ? covale1 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.435 ? covale2 covale ? ? A ASN 371 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 386 A NAG 501 1_555 ? ? ? ? ? ? ? 1.436 ? covale3 covale ? ? A ASN 151 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 166 A NAG 504 1_555 ? ? ? ? ? ? ? 1.441 ? covale4 covale ? ? A ASN 140 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 155 A NAG 503 1_555 ? ? ? ? ? ? ? 1.443 ? metalc1 metalc ? ? A HIS 223 NE2 ? ? ? 1_555 G ZN . ZN ? ? A HIS 238 A ZN 506 1_555 ? ? ? ? ? ? ? 1.970 ? metalc2 metalc ? ? F AMP . O2P ? ? ? 1_555 H ZN . ZN ? ? A AMP 505 A ZN 507 1_555 ? ? ? ? ? ? ? 1.974 ? metalc3 metalc ? ? A ASP 222 OD2 ? ? ? 1_555 G ZN . ZN ? ? A ASP 237 A ZN 506 1_555 ? ? ? ? ? ? ? 1.980 ? metalc4 metalc ? ? A ASP 19 OD1 ? ? ? 1_555 G ZN . ZN ? ? A ASP 34 A ZN 506 1_555 ? ? ? ? ? ? ? 1.987 ? metalc5 metalc ? ? A THR 55 OG1 ? ? ? 1_555 G ZN . ZN ? ? A THR 70 A ZN 506 1_555 ? ? ? ? ? ? ? 1.990 ? metalc6 metalc ? ? A HIS 178 NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS 193 A ZN 507 1_555 ? ? ? ? ? ? ? 1.993 ? metalc7 metalc ? ? A HIS 321 NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS 336 A ZN 507 1_555 ? ? ? ? ? ? ? 2.064 ? metalc8 metalc ? ? A ASP 174 OD1 ? ? ? 1_555 H ZN . ZN ? ? A ASP 189 A ZN 507 1_555 ? ? ? ? ? ? ? 2.065 ? metalc9 metalc ? ? H ZN . ZN ? ? ? 1_555 I HOH . O ? ? A ZN 507 A HOH 874 1_555 ? ? ? ? ? ? ? 2.343 ? metalc10 metalc ? ? A ASP 19 OD2 ? ? ? 1_555 G ZN . ZN ? ? A ASP 34 A ZN 506 1_555 ? ? ? ? ? ? ? 2.630 ? metalc11 metalc ? ? A ASP 174 OD2 ? ? ? 1_555 H ZN . ZN ? ? A ASP 189 A ZN 507 1_555 ? ? ? ? ? ? ? 2.636 ? # 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 PHE 51 A . ? PHE 66 A ILE 52 A ? ILE 67 A 1 -1.31 2 ASN 160 A . ? ASN 175 A PRO 161 A ? PRO 176 A 1 0.66 3 GLU 172 A . ? GLU 187 A PRO 173 A ? PRO 188 A 1 9.15 4 SER 251 A . ? SER 266 A PRO 252 A ? PRO 267 A 1 1.83 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 2 ? C ? 2 ? D ? 2 ? E ? 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 A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 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 SER A 115 ? ALA A 119 ? SER A 130 ALA A 134 A 2 VAL A 163 ? TRP A 170 ? VAL A 178 TRP A 185 A 3 LEU A 13 ? PHE A 18 ? LEU A 28 PHE A 33 A 4 ASN A 216 ? THR A 220 ? ASN A 231 THR A 235 A 5 LEU A 334 ? HIS A 337 ? LEU A 349 HIS A 352 A 6 VAL A 42 ? LYS A 48 ? VAL A 57 LYS A 63 A 7 TYR A 345 ? ASN A 351 ? TYR A 360 ASN A 366 B 1 MET A 78 ? TYR A 79 ? MET A 93 TYR A 94 B 2 HIS A 86 ? PHE A 87 ? HIS A 101 PHE A 102 C 1 THR A 226 ? GLN A 227 ? THR A 241 GLN A 242 C 2 GLY A 319 ? ASP A 320 ? GLY A 334 ASP A 335 D 1 LEU A 233 ? ASN A 235 ? LEU A 248 ASN A 250 D 2 THR A 308 ? VAL A 310 ? THR A 323 VAL A 325 E 1 TYR A 245 ? ASP A 249 ? TYR A 260 ASP A 264 E 2 VAL A 253 ? PRO A 258 ? VAL A 268 PRO A 273 E 3 ILE A 299 ? ALA A 303 ? ILE A 314 ALA A 318 E 4 MET A 276 ? LEU A 280 ? MET A 291 LEU A 295 # 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 SER A 115 ? N SER A 130 O THR A 164 ? O THR A 179 A 2 3 O ALA A 166 ? O ALA A 181 N LEU A 15 ? N LEU A 30 A 3 4 N VAL A 16 ? N VAL A 31 O ILE A 218 ? O ILE A 233 A 4 5 N VAL A 217 ? N VAL A 232 O HIS A 337 ? O HIS A 352 A 5 6 O LEU A 334 ? O LEU A 349 N VAL A 44 ? N VAL A 59 A 6 7 N LEU A 43 ? N LEU A 58 O HIS A 347 ? O HIS A 362 B 1 2 N MET A 78 ? N MET A 93 O PHE A 87 ? O PHE A 102 C 1 2 N THR A 226 ? N THR A 241 O ASP A 320 ? O ASP A 335 D 1 2 N ILE A 234 ? N ILE A 249 O VAL A 310 ? O VAL A 325 E 1 2 N ILE A 248 ? N ILE A 263 O ALA A 255 ? O ALA A 270 E 2 3 N ILE A 256 ? N ILE A 271 O ILE A 299 ? O ILE A 314 E 3 4 O ILE A 300 ? O ILE A 315 N TYR A 279 ? N TYR A 294 # 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 ? ? ? ? 19 'BINDING SITE FOR RESIDUE AMP A 505' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 506' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 507' AC4 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 503 BOUND TO ASN A 155' AC5 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A 504 BOUND TO ASN A 166' AC6 Software ? ? ? ? 7 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 386 RESIDUES 501 TO 502' # 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 19 ASP A 19 ? ASP A 34 . ? 1_555 ? 2 AC1 19 THR A 55 ? THR A 70 . ? 1_555 ? 3 AC1 19 PHE A 56 ? PHE A 71 . ? 1_555 ? 4 AC1 19 ASN A 76 ? ASN A 91 . ? 1_555 ? 5 AC1 19 ASP A 89 ? ASP A 104 . ? 1_555 ? 6 AC1 19 ASP A 92 ? ASP A 107 . ? 1_555 ? 7 AC1 19 TYR A 139 ? TYR A 154 . ? 1_555 ? 8 AC1 19 TYR A 169 ? TYR A 184 . ? 1_555 ? 9 AC1 19 ASP A 174 ? ASP A 189 . ? 1_555 ? 10 AC1 19 HIS A 178 ? HIS A 193 . ? 1_555 ? 11 AC1 19 HIS A 321 ? HIS A 336 . ? 1_555 ? 12 AC1 19 ZN H . ? ZN A 507 . ? 1_555 ? 13 AC1 19 HOH I . ? HOH A 654 . ? 1_555 ? 14 AC1 19 HOH I . ? HOH A 753 . ? 1_555 ? 15 AC1 19 HOH I . ? HOH A 788 . ? 1_555 ? 16 AC1 19 HOH I . ? HOH A 804 . ? 1_555 ? 17 AC1 19 HOH I . ? HOH A 860 . ? 1_555 ? 18 AC1 19 HOH I . ? HOH A 874 . ? 1_555 ? 19 AC1 19 HOH I . ? HOH A 983 . ? 1_555 ? 20 AC2 4 ASP A 19 ? ASP A 34 . ? 1_555 ? 21 AC2 4 THR A 55 ? THR A 70 . ? 1_555 ? 22 AC2 4 ASP A 222 ? ASP A 237 . ? 1_555 ? 23 AC2 4 HIS A 223 ? HIS A 238 . ? 1_555 ? 24 AC3 5 ASP A 174 ? ASP A 189 . ? 1_555 ? 25 AC3 5 HIS A 178 ? HIS A 193 . ? 1_555 ? 26 AC3 5 HIS A 321 ? HIS A 336 . ? 1_555 ? 27 AC3 5 AMP F . ? AMP A 505 . ? 1_555 ? 28 AC3 5 HOH I . ? HOH A 874 . ? 1_555 ? 29 AC4 2 ASN A 140 ? ASN A 155 . ? 1_555 ? 30 AC4 2 HOH I . ? HOH A 1035 . ? 1_555 ? 31 AC5 5 ASP A 130 ? ASP A 145 . ? 4_445 ? 32 AC5 5 GLU A 147 ? GLU A 162 . ? 1_555 ? 33 AC5 5 ASN A 151 ? ASN A 166 . ? 1_555 ? 34 AC5 5 HOH I . ? HOH A 845 . ? 1_555 ? 35 AC5 5 HOH I . ? HOH A 993 . ? 1_555 ? 36 AC6 7 TYR A 289 ? TYR A 304 . ? 1_555 ? 37 AC6 7 PRO A 369 ? PRO A 384 . ? 1_555 ? 38 AC6 7 ASN A 371 ? ASN A 386 . ? 1_555 ? 39 AC6 7 HOH I . ? HOH A 627 . ? 1_555 ? 40 AC6 7 HOH I . ? HOH A 673 . ? 1_555 ? 41 AC6 7 HOH I . ? HOH A 801 . ? 1_555 ? 42 AC6 7 HOH I . ? HOH A 819 . ? 1_555 ? # _atom_sites.entry_id 4LQY _atom_sites.fract_transf_matrix[1][1] 0.005509 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.001209 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.019553 _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] 0.019412 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol C N O P S ZN # 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 . LEU A 1 9 ? -37.094 137.586 -18.019 1.00 58.25 ? 24 LEU A N 1 ATOM 2 C CA . LEU A 1 9 ? -36.869 137.013 -16.694 1.00 55.92 ? 24 LEU A CA 1 ATOM 3 C C . LEU A 1 9 ? -35.683 137.664 -15.974 1.00 48.58 ? 24 LEU A C 1 ATOM 4 O O . LEU A 1 9 ? -34.531 137.288 -16.197 1.00 48.81 ? 24 LEU A O 1 ATOM 5 C CB . LEU A 1 9 ? -36.672 135.494 -16.792 1.00 56.95 ? 24 LEU A CB 1 ATOM 6 N N . PRO A 1 10 ? -35.966 138.641 -15.098 1.00 42.30 ? 25 PRO A N 1 ATOM 7 C CA . PRO A 1 10 ? -34.916 139.291 -14.305 1.00 37.27 ? 25 PRO A CA 1 ATOM 8 C C . PRO A 1 10 ? -34.342 138.364 -13.246 1.00 34.17 ? 25 PRO A C 1 ATOM 9 O O . PRO A 1 10 ? -35.058 137.498 -12.744 1.00 37.30 ? 25 PRO A O 1 ATOM 10 C CB . PRO A 1 10 ? -35.663 140.439 -13.625 1.00 37.66 ? 25 PRO A CB 1 ATOM 11 C CG . PRO A 1 10 ? -37.059 139.962 -13.531 1.00 45.71 ? 25 PRO A CG 1 ATOM 12 C CD . PRO A 1 10 ? -37.303 139.174 -14.781 1.00 43.95 ? 25 PRO A CD 1 ATOM 13 N N . PRO A 1 11 ? -33.060 138.552 -12.903 1.00 31.00 ? 26 PRO A N 1 ATOM 14 C CA . PRO A 1 11 ? -32.391 137.821 -11.817 1.00 30.67 ? 26 PRO A CA 1 ATOM 15 C C . PRO A 1 11 ? -33.154 138.010 -10.501 1.00 26.52 ? 26 PRO A C 1 ATOM 16 O O . PRO A 1 11 ? -33.679 139.102 -10.265 1.00 26.55 ? 26 PRO A O 1 ATOM 17 C CB . PRO A 1 11 ? -31.032 138.511 -11.714 1.00 30.04 ? 26 PRO A CB 1 ATOM 18 C CG . PRO A 1 11 ? -30.831 139.194 -13.003 1.00 35.18 ? 26 PRO A CG 1 ATOM 19 C CD . PRO A 1 11 ? -32.178 139.539 -13.548 1.00 33.20 ? 26 PRO A CD 1 ATOM 20 N N . LYS A 1 12 ? -33.219 136.973 -9.666 1.00 26.18 ? 27 LYS A N 1 ATOM 21 C CA . LYS A 1 12 ? -33.838 137.091 -8.351 1.00 25.42 ? 27 LYS A CA 1 ATOM 22 C C . LYS A 1 12 ? -32.864 136.630 -7.280 1.00 19.30 ? 27 LYS A C 1 ATOM 23 O O . LYS A 1 12 ? -32.060 135.721 -7.506 1.00 23.66 ? 27 LYS A O 1 ATOM 24 C CB . LYS A 1 12 ? -35.108 136.252 -8.263 1.00 26.43 ? 27 LYS A CB 1 ATOM 25 C CG . LYS A 1 12 ? -36.191 136.636 -9.236 1.00 25.85 ? 27 LYS A CG 1 ATOM 26 C CD . LYS A 1 12 ? -37.432 135.805 -8.991 1.00 33.81 ? 27 LYS A CD 1 ATOM 27 C CE . LYS A 1 12 ? -38.507 136.182 -9.984 1.00 38.57 ? 27 LYS A CE 1 ATOM 28 N NZ . LYS A 1 12 ? -39.795 135.547 -9.665 1.00 42.91 ? 27 LYS A NZ 1 ATOM 29 N N . LEU A 1 13 ? -32.949 137.249 -6.107 1.00 24.30 ? 28 LEU A N 1 ATOM 30 C CA . LEU A 1 13 ? -32.045 136.945 -5.020 1.00 19.74 ? 28 LEU A CA 1 ATOM 31 C C . LEU A 1 13 ? -32.785 136.919 -3.689 1.00 23.76 ? 28 LEU A C 1 ATOM 32 O O . LEU A 1 13 ? -33.523 137.852 -3.367 1.00 22.54 ? 28 LEU A O 1 ATOM 33 C CB . LEU A 1 13 ? -30.919 137.989 -4.967 1.00 20.37 ? 28 LEU A CB 1 ATOM 34 C CG . LEU A 1 13 ? -29.940 137.931 -3.783 1.00 26.64 ? 28 LEU A CG 1 ATOM 35 C CD1 . LEU A 1 13 ? -29.115 136.672 -3.806 1.00 26.98 ? 28 LEU A CD1 1 ATOM 36 C CD2 . LEU A 1 13 ? -29.054 139.146 -3.855 1.00 27.26 ? 28 LEU A CD2 1 ATOM 37 N N . LEU A 1 14 ? -32.590 135.830 -2.941 1.00 19.79 ? 29 LEU A N 1 ATOM 38 C CA . LEU A 1 14 ? -33.099 135.666 -1.587 1.00 19.34 ? 29 LEU A CA 1 ATOM 39 C C . LEU A 1 14 ? -31.915 135.711 -0.620 1.00 18.09 ? 29 LEU A C 1 ATOM 40 O O . LEU A 1 14 ? -30.997 134.884 -0.730 1.00 19.64 ? 29 LEU A O 1 ATOM 41 C CB . LEU A 1 14 ? -33.805 134.304 -1.488 1.00 21.94 ? 29 LEU A CB 1 ATOM 42 C CG . LEU A 1 14 ? -34.206 133.863 -0.066 1.00 21.44 ? 29 LEU A CG 1 ATOM 43 C CD1 . LEU A 1 14 ? -35.161 134.866 0.602 1.00 18.16 ? 29 LEU A CD1 1 ATOM 44 C CD2 . LEU A 1 14 ? -34.789 132.446 -0.033 1.00 24.26 ? 29 LEU A CD2 1 ATOM 45 N N . LEU A 1 15 ? -31.943 136.671 0.314 1.00 19.88 ? 30 LEU A N 1 ATOM 46 C CA . LEU A 1 15 ? -30.898 136.851 1.330 1.00 17.43 ? 30 LEU A CA 1 ATOM 47 C C . LEU A 1 15 ? -31.428 136.394 2.674 1.00 17.48 ? 30 LEU A C 1 ATOM 48 O O . LEU A 1 15 ? -32.408 136.962 3.188 1.00 18.22 ? 30 LEU A O 1 ATOM 49 C CB . LEU A 1 15 ? -30.474 138.324 1.385 1.00 17.72 ? 30 LEU A CB 1 ATOM 50 C CG . LEU A 1 15 ? -29.488 138.760 2.479 1.00 14.72 ? 30 LEU A CG 1 ATOM 51 C CD1 . LEU A 1 15 ? -28.171 137.993 2.333 1.00 18.76 ? 30 LEU A CD1 1 ATOM 52 C CD2 . LEU A 1 15 ? -29.299 140.308 2.416 1.00 17.14 ? 30 LEU A CD2 1 ATOM 53 N N . VAL A 1 16 ? -30.792 135.370 3.243 1.00 15.83 ? 31 VAL A N 1 ATOM 54 C CA . VAL A 1 16 ? -31.282 134.731 4.472 1.00 18.16 ? 31 VAL A CA 1 ATOM 55 C C . VAL A 1 16 ? -30.268 134.899 5.588 1.00 13.24 ? 31 VAL A C 1 ATOM 56 O O . VAL A 1 16 ? -29.075 134.660 5.383 1.00 15.30 ? 31 VAL A O 1 ATOM 57 C CB . VAL A 1 16 ? -31.526 133.225 4.255 1.00 15.53 ? 31 VAL A CB 1 ATOM 58 C CG1 . VAL A 1 16 ? -32.182 132.579 5.492 1.00 21.04 ? 31 VAL A CG1 1 ATOM 59 C CG2 . VAL A 1 16 ? -32.423 133.009 3.038 1.00 17.06 ? 31 VAL A CG2 1 ATOM 60 N N . SER A 1 17 ? -30.718 135.360 6.755 1.00 14.59 ? 32 SER A N 1 ATOM 61 C CA . SER A 1 17 ? -29.845 135.476 7.921 1.00 12.93 ? 32 SER A CA 1 ATOM 62 C C . SER A 1 17 ? -30.392 134.668 9.072 1.00 15.29 ? 32 SER A C 1 ATOM 63 O O . SER A 1 17 ? -31.559 134.834 9.468 1.00 16.42 ? 32 SER A O 1 ATOM 64 C CB . SER A 1 17 ? -29.701 136.930 8.369 1.00 12.89 ? 32 SER A CB 1 ATOM 65 O OG . SER A 1 17 ? -28.910 136.989 9.550 1.00 14.44 ? 32 SER A OG 1 ATOM 66 N N . PHE A 1 18 ? -29.553 133.780 9.602 1.00 14.86 ? 33 PHE A N 1 ATOM 67 C CA . PHE A 1 18 ? -29.813 133.120 10.868 1.00 16.71 ? 33 PHE A CA 1 ATOM 68 C C . PHE A 1 18 ? -28.964 133.829 11.877 1.00 12.36 ? 33 PHE A C 1 ATOM 69 O O . PHE A 1 18 ? -27.732 133.734 11.846 1.00 16.49 ? 33 PHE A O 1 ATOM 70 C CB . PHE A 1 18 ? -29.469 131.626 10.803 1.00 16.71 ? 33 PHE A CB 1 ATOM 71 C CG . PHE A 1 18 ? -30.390 130.838 9.923 1.00 15.65 ? 33 PHE A CG 1 ATOM 72 C CD1 . PHE A 1 18 ? -31.611 130.374 10.400 1.00 20.24 ? 33 PHE A CD1 1 ATOM 73 C CD2 . PHE A 1 18 ? -30.054 130.577 8.599 1.00 17.30 ? 33 PHE A CD2 1 ATOM 74 C CE1 . PHE A 1 18 ? -32.458 129.653 9.573 1.00 21.29 ? 33 PHE A CE1 1 ATOM 75 C CE2 . PHE A 1 18 ? -30.913 129.863 7.772 1.00 18.10 ? 33 PHE A CE2 1 ATOM 76 C CZ . PHE A 1 18 ? -32.107 129.402 8.271 1.00 18.29 ? 33 PHE A CZ 1 ATOM 77 N N . ASP A 1 19 ? -29.607 134.614 12.738 1.00 14.30 ? 34 ASP A N 1 ATOM 78 C CA . ASP A 1 19 ? -28.873 135.480 13.661 1.00 14.12 ? 34 ASP A CA 1 ATOM 79 C C . ASP A 1 19 ? -27.873 134.718 14.517 1.00 12.80 ? 34 ASP A C 1 ATOM 80 O O . ASP A 1 19 ? -28.174 133.633 15.045 1.00 15.15 ? 34 ASP A O 1 ATOM 81 C CB . ASP A 1 19 ? -29.849 136.257 14.558 1.00 13.43 ? 34 ASP A CB 1 ATOM 82 C CG . ASP A 1 19 ? -29.240 137.536 15.097 1.00 9.77 ? 34 ASP A CG 1 ATOM 83 O OD1 . ASP A 1 19 ? -28.224 137.440 15.815 1.00 15.09 ? 34 ASP A OD1 1 ATOM 84 O OD2 . ASP A 1 19 ? -29.753 138.635 14.819 1.00 19.84 ? 34 ASP A OD2 1 ATOM 85 N N . GLY A 1 20 ? -26.650 135.240 14.606 1.00 12.36 ? 35 GLY A N 1 ATOM 86 C CA . GLY A 1 20 ? -25.675 134.730 15.573 1.00 15.28 ? 35 GLY A CA 1 ATOM 87 C C . GLY A 1 20 ? -25.020 133.399 15.196 1.00 11.06 ? 35 GLY A C 1 ATOM 88 O O . GLY A 1 20 ? -24.673 132.592 16.084 1.00 13.97 ? 35 GLY A O 1 ATOM 89 N N . PHE A 1 21 ? -24.884 133.145 13.897 1.00 12.65 ? 36 PHE A N 1 ATOM 90 C CA . PHE A 1 21 ? -24.321 131.887 13.431 1.00 13.47 ? 36 PHE A CA 1 ATOM 91 C C . PHE A 1 21 ? -22.802 132.035 13.271 1.00 15.35 ? 36 PHE A C 1 ATOM 92 O O . PHE A 1 21 ? -22.293 132.493 12.233 1.00 16.11 ? 36 PHE A O 1 ATOM 93 C CB . PHE A 1 21 ? -25.012 131.475 12.127 1.00 13.04 ? 36 PHE A CB 1 ATOM 94 C CG . PHE A 1 21 ? -24.871 130.023 11.776 1.00 15.76 ? 36 PHE A CG 1 ATOM 95 C CD1 . PHE A 1 21 ? -23.635 129.403 11.752 1.00 17.50 ? 36 PHE A CD1 1 ATOM 96 C CD2 . PHE A 1 21 ? -25.988 129.304 11.401 1.00 18.35 ? 36 PHE A CD2 1 ATOM 97 C CE1 . PHE A 1 21 ? -23.512 128.072 11.394 1.00 19.29 ? 36 PHE A CE1 1 ATOM 98 C CE2 . PHE A 1 21 ? -25.888 127.950 11.043 1.00 19.91 ? 36 PHE A CE2 1 ATOM 99 C CZ . PHE A 1 21 ? -24.640 127.341 11.024 1.00 19.80 ? 36 PHE A CZ 1 ATOM 100 N N . ARG A 1 22 ? -22.099 131.734 14.360 1.00 12.71 ? 37 ARG A N 1 ATOM 101 C CA . ARG A 1 22 ? -20.635 131.729 14.439 1.00 12.76 ? 37 ARG A CA 1 ATOM 102 C C . ARG A 1 22 ? -20.077 130.797 13.385 1.00 12.32 ? 37 ARG A C 1 ATOM 103 O O . ARG A 1 22 ? -20.527 129.650 13.276 1.00 15.39 ? 37 ARG A O 1 ATOM 104 C CB . ARG A 1 22 ? -20.252 131.244 15.841 1.00 12.30 ? 37 ARG A CB 1 ATOM 105 C CG . ARG A 1 22 ? -18.763 131.188 16.119 1.00 15.23 ? 37 ARG A CG 1 ATOM 106 C CD . ARG A 1 22 ? -18.481 130.838 17.573 1.00 17.73 ? 37 ARG A CD 1 ATOM 107 N NE . ARG A 1 22 ? -17.136 130.301 17.702 1.00 17.78 ? 37 ARG A NE 1 ATOM 108 C CZ . ARG A 1 22 ? -16.395 130.358 18.800 1.00 21.31 ? 37 ARG A CZ 1 ATOM 109 N NH1 . ARG A 1 22 ? -16.856 130.977 19.886 1.00 19.02 ? 37 ARG A NH1 1 ATOM 110 N NH2 . ARG A 1 22 ? -15.175 129.823 18.796 1.00 24.06 ? 37 ARG A NH2 1 ATOM 111 N N . ALA A 1 23 ? -19.080 131.273 12.627 1.00 15.33 ? 38 ALA A N 1 ATOM 112 C CA . ALA A 1 23 ? -18.501 130.521 11.510 1.00 16.81 ? 38 ALA A CA 1 ATOM 113 C C . ALA A 1 23 ? -18.054 129.112 11.866 1.00 15.00 ? 38 ALA A C 1 ATOM 114 O O . ALA A 1 23 ? -18.329 128.168 11.119 1.00 19.54 ? 38 ALA A O 1 ATOM 115 C CB . ALA A 1 23 ? -17.325 131.290 10.900 1.00 16.41 ? 38 ALA A CB 1 ATOM 116 N N . ASP A 1 24 ? -17.341 128.962 12.983 1.00 15.54 ? 39 ASP A N 1 ATOM 117 C CA . ASP A 1 24 ? -16.798 127.645 13.314 1.00 16.26 ? 39 ASP A CA 1 ATOM 118 C C . ASP A 1 24 ? -17.808 126.648 13.851 1.00 20.80 ? 39 ASP A C 1 ATOM 119 O O . ASP A 1 24 ? -17.448 125.501 14.112 1.00 21.42 ? 39 ASP A O 1 ATOM 120 C CB . ASP A 1 24 ? -15.520 127.715 14.161 1.00 20.99 ? 39 ASP A CB 1 ATOM 121 C CG . ASP A 1 24 ? -15.773 128.108 15.585 1.00 18.05 ? 39 ASP A CG 1 ATOM 122 O OD1 . ASP A 1 24 ? -14.762 128.332 16.298 1.00 25.83 ? 39 ASP A OD1 1 ATOM 123 O OD2 . ASP A 1 24 ? -16.953 128.210 15.998 1.00 21.45 ? 39 ASP A OD2 1 ATOM 124 N N . TYR A 1 25 ? -19.065 127.080 14.011 1.00 19.17 ? 40 TYR A N 1 ATOM 125 C CA . TYR A 1 25 ? -20.133 126.113 14.267 1.00 19.53 ? 40 TYR A CA 1 ATOM 126 C C . TYR A 1 25 ? -20.090 125.053 13.169 1.00 19.04 ? 40 TYR A C 1 ATOM 127 O O . TYR A 1 25 ? -20.343 123.888 13.423 1.00 22.50 ? 40 TYR A O 1 ATOM 128 C CB . TYR A 1 25 ? -21.519 126.762 14.279 1.00 18.87 ? 40 TYR A CB 1 ATOM 129 C CG . TYR A 1 25 ? -21.881 127.560 15.527 1.00 17.35 ? 40 TYR A CG 1 ATOM 130 C CD1 . TYR A 1 25 ? -22.933 128.482 15.492 1.00 15.79 ? 40 TYR A CD1 1 ATOM 131 C CD2 . TYR A 1 25 ? -21.206 127.376 16.740 1.00 16.16 ? 40 TYR A CD2 1 ATOM 132 C CE1 . TYR A 1 25 ? -23.303 129.199 16.618 1.00 15.69 ? 40 TYR A CE1 1 ATOM 133 C CE2 . TYR A 1 25 ? -21.568 128.112 17.872 1.00 17.40 ? 40 TYR A CE2 1 ATOM 134 C CZ . TYR A 1 25 ? -22.629 129.008 17.792 1.00 15.74 ? 40 TYR A CZ 1 ATOM 135 O OH . TYR A 1 25 ? -23.020 129.741 18.888 1.00 14.37 ? 40 TYR A OH 1 ATOM 136 N N . LEU A 1 26 ? -19.777 125.460 11.935 1.00 17.83 ? 41 LEU A N 1 ATOM 137 C CA . LEU A 1 26 ? -19.755 124.502 10.815 1.00 19.89 ? 41 LEU A CA 1 ATOM 138 C C . LEU A 1 26 ? -18.733 123.373 11.000 1.00 24.26 ? 41 LEU A C 1 ATOM 139 O O . LEU A 1 26 ? -18.900 122.267 10.462 1.00 26.70 ? 41 LEU A O 1 ATOM 140 C CB . LEU A 1 26 ? -19.497 125.218 9.481 1.00 19.59 ? 41 LEU A CB 1 ATOM 141 C CG . LEU A 1 26 ? -20.496 126.289 9.054 1.00 21.44 ? 41 LEU A CG 1 ATOM 142 C CD1 . LEU A 1 26 ? -20.146 126.804 7.665 1.00 25.10 ? 41 LEU A CD1 1 ATOM 143 C CD2 . LEU A 1 26 ? -21.904 125.726 9.074 1.00 25.02 ? 41 LEU A CD2 1 ATOM 144 N N . LYS A 1 27 ? -17.674 123.653 11.765 1.00 22.05 ? 42 LYS A N 1 ATOM 145 C CA . LYS A 1 27 ? -16.598 122.686 11.957 1.00 29.28 ? 42 LYS A CA 1 ATOM 146 C C . LYS A 1 27 ? -16.826 121.790 13.165 1.00 29.77 ? 42 LYS A C 1 ATOM 147 O O . LYS A 1 27 ? -16.145 120.780 13.315 1.00 38.95 ? 42 LYS A O 1 ATOM 148 C CB . LYS A 1 27 ? -15.236 123.389 12.068 1.00 29.48 ? 42 LYS A CB 1 ATOM 149 C CG . LYS A 1 27 ? -14.938 124.358 10.913 1.00 41.61 ? 42 LYS A CG 1 ATOM 150 C CD . LYS A 1 27 ? -13.445 124.669 10.813 1.00 49.34 ? 42 LYS A CD 1 ATOM 151 C CE . LYS A 1 27 ? -13.176 125.998 10.113 1.00 52.63 ? 42 LYS A CE 1 ATOM 152 N NZ . LYS A 1 27 ? -13.395 125.940 8.637 1.00 57.49 ? 42 LYS A NZ 1 ATOM 153 N N . ASN A 1 28 ? -17.782 122.157 14.021 1.00 24.32 ? 43 ASN A N 1 ATOM 154 C CA . ASN A 1 28 ? -17.969 121.453 15.289 1.00 30.51 ? 43 ASN A CA 1 ATOM 155 C C . ASN A 1 28 ? -19.307 120.723 15.455 1.00 27.00 ? 43 ASN A C 1 ATOM 156 O O . ASN A 1 28 ? -19.552 120.063 16.466 1.00 26.05 ? 43 ASN A O 1 ATOM 157 C CB . ASN A 1 28 ? -17.732 122.427 16.446 1.00 27.24 ? 43 ASN A CB 1 ATOM 158 C CG . ASN A 1 28 ? -16.290 122.880 16.515 1.00 32.61 ? 43 ASN A CG 1 ATOM 159 O OD1 . ASN A 1 28 ? -15.382 122.056 16.472 1.00 39.85 ? 43 ASN A OD1 1 ATOM 160 N ND2 . ASN A 1 28 ? -16.068 124.187 16.573 1.00 29.01 ? 43 ASN A ND2 1 ATOM 161 N N . TYR A 1 29 ? -20.172 120.840 14.457 1.00 26.25 ? 44 TYR A N 1 ATOM 162 C CA . TYR A 1 29 ? -21.478 120.190 14.500 1.00 25.58 ? 44 TYR A CA 1 ATOM 163 C C . TYR A 1 29 ? -21.790 119.676 13.110 1.00 26.59 ? 44 TYR A C 1 ATOM 164 O O . TYR A 1 29 ? -21.156 120.087 12.145 1.00 28.78 ? 44 TYR A O 1 ATOM 165 C CB . TYR A 1 29 ? -22.562 121.168 14.974 1.00 24.16 ? 44 TYR A CB 1 ATOM 166 C CG . TYR A 1 29 ? -22.299 121.774 16.344 1.00 22.92 ? 44 TYR A CG 1 ATOM 167 C CD1 . TYR A 1 29 ? -22.703 121.119 17.507 1.00 27.24 ? 44 TYR A CD1 1 ATOM 168 C CD2 . TYR A 1 29 ? -21.638 122.988 16.471 1.00 21.85 ? 44 TYR A CD2 1 ATOM 169 C CE1 . TYR A 1 29 ? -22.464 121.668 18.757 1.00 26.11 ? 44 TYR A CE1 1 ATOM 170 C CE2 . TYR A 1 29 ? -21.382 123.539 17.707 1.00 21.09 ? 44 TYR A CE2 1 ATOM 171 C CZ . TYR A 1 29 ? -21.803 122.881 18.847 1.00 21.75 ? 44 TYR A CZ 1 ATOM 172 O OH . TYR A 1 29 ? -21.552 123.445 20.073 1.00 24.63 ? 44 TYR A OH 1 ATOM 173 N N . GLU A 1 30 ? -22.776 118.795 12.995 1.00 30.27 ? 45 GLU A N 1 ATOM 174 C CA . GLU A 1 30 ? -23.139 118.233 11.696 1.00 30.36 ? 45 GLU A CA 1 ATOM 175 C C . GLU A 1 30 ? -24.273 119.017 11.056 1.00 26.38 ? 45 GLU A C 1 ATOM 176 O O . GLU A 1 30 ? -25.337 119.177 11.658 1.00 27.53 ? 45 GLU A O 1 ATOM 177 C CB . GLU A 1 30 ? -23.552 116.765 11.866 1.00 33.75 ? 45 GLU A CB 1 ATOM 178 C CG . GLU A 1 30 ? -22.385 115.836 12.112 1.00 40.98 ? 45 GLU A CG 1 ATOM 179 C CD . GLU A 1 30 ? -21.389 115.877 10.966 1.00 50.01 ? 45 GLU A CD 1 ATOM 180 O OE1 . GLU A 1 30 ? -21.828 116.035 9.804 1.00 57.58 ? 45 GLU A OE1 1 ATOM 181 O OE2 . GLU A 1 30 ? -20.170 115.769 11.219 1.00 57.81 ? 45 GLU A OE2 1 ATOM 182 N N . PHE A 1 31 ? -24.047 119.508 9.844 1.00 25.55 ? 46 PHE A N 1 ATOM 183 C CA . PHE A 1 31 ? -25.092 120.191 9.091 1.00 24.79 ? 46 PHE A CA 1 ATOM 184 C C . PHE A 1 31 ? -25.375 119.523 7.745 1.00 28.04 ? 46 PHE A C 1 ATOM 185 O O . PHE A 1 31 ? -25.028 120.087 6.692 1.00 26.76 ? 46 PHE A O 1 ATOM 186 C CB . PHE A 1 31 ? -24.706 121.654 8.840 1.00 24.11 ? 46 PHE A CB 1 ATOM 187 C CG . PHE A 1 31 ? -24.632 122.493 10.088 1.00 22.03 ? 46 PHE A CG 1 ATOM 188 C CD1 . PHE A 1 31 ? -25.730 123.203 10.517 1.00 23.46 ? 46 PHE A CD1 1 ATOM 189 C CD2 . PHE A 1 31 ? -23.454 122.588 10.810 1.00 26.82 ? 46 PHE A CD2 1 ATOM 190 C CE1 . PHE A 1 31 ? -25.670 124.003 11.664 1.00 20.24 ? 46 PHE A CE1 1 ATOM 191 C CE2 . PHE A 1 31 ? -23.387 123.381 11.965 1.00 22.58 ? 46 PHE A CE2 1 ATOM 192 C CZ . PHE A 1 31 ? -24.501 124.074 12.390 1.00 21.67 ? 46 PHE A CZ 1 ATOM 193 N N . PRO A 1 32 ? -26.007 118.332 7.755 1.00 25.46 ? 47 PRO A N 1 ATOM 194 C CA . PRO A 1 32 ? -26.295 117.626 6.495 1.00 27.79 ? 47 PRO A CA 1 ATOM 195 C C . PRO A 1 32 ? -27.040 118.461 5.440 1.00 25.59 ? 47 PRO A C 1 ATOM 196 O O . PRO A 1 32 ? -26.647 118.420 4.284 1.00 29.02 ? 47 PRO A O 1 ATOM 197 C CB . PRO A 1 32 ? -27.141 116.420 6.942 1.00 31.53 ? 47 PRO A CB 1 ATOM 198 C CG . PRO A 1 32 ? -27.605 116.759 8.331 1.00 32.69 ? 47 PRO A CG 1 ATOM 199 C CD . PRO A 1 32 ? -26.507 117.581 8.922 1.00 29.47 ? 47 PRO A CD 1 ATOM 200 N N . HIS A 1 33 ? -28.078 119.204 5.821 1.00 24.67 ? 48 HIS A N 1 ATOM 201 C CA . HIS A 1 33 ? -28.792 120.049 4.862 1.00 23.55 ? 48 HIS A CA 1 ATOM 202 C C . HIS A 1 33 ? -27.961 121.225 4.347 1.00 27.76 ? 48 HIS A C 1 ATOM 203 O O . HIS A 1 33 ? -27.969 121.512 3.150 1.00 26.79 ? 48 HIS A O 1 ATOM 204 C CB . HIS A 1 33 ? -30.123 120.533 5.430 1.00 30.65 ? 48 HIS A CB 1 ATOM 205 C CG . HIS A 1 33 ? -31.069 119.423 5.765 1.00 25.12 ? 48 HIS A CG 1 ATOM 206 N ND1 . HIS A 1 33 ? -31.639 118.613 4.803 1.00 30.87 ? 48 HIS A ND1 1 ATOM 207 C CD2 . HIS A 1 33 ? -31.552 118.992 6.956 1.00 30.83 ? 48 HIS A CD2 1 ATOM 208 C CE1 . HIS A 1 33 ? -32.427 117.727 5.388 1.00 32.37 ? 48 HIS A CE1 1 ATOM 209 N NE2 . HIS A 1 33 ? -32.389 117.931 6.694 1.00 31.37 ? 48 HIS A NE2 1 ATOM 210 N N . LEU A 1 34 ? -27.233 121.895 5.233 1.00 21.60 ? 49 LEU A N 1 ATOM 211 C CA . LEU A 1 34 ? -26.354 122.987 4.807 1.00 25.96 ? 49 LEU A CA 1 ATOM 212 C C . LEU A 1 34 ? -25.258 122.452 3.898 1.00 25.81 ? 49 LEU A C 1 ATOM 213 O O . LEU A 1 34 ? -24.945 123.068 2.876 1.00 24.52 ? 49 LEU A O 1 ATOM 214 C CB . LEU A 1 34 ? -25.716 123.686 6.011 1.00 29.06 ? 49 LEU A CB 1 ATOM 215 C CG . LEU A 1 34 ? -25.754 125.216 6.070 1.00 38.07 ? 49 LEU A CG 1 ATOM 216 C CD1 . LEU A 1 34 ? -24.766 125.744 7.087 1.00 34.34 ? 49 LEU A CD1 1 ATOM 217 C CD2 . LEU A 1 34 ? -25.526 125.854 4.734 1.00 27.02 ? 49 LEU A CD2 1 ATOM 218 N N . GLN A 1 35 ? -24.687 121.306 4.278 1.00 26.51 ? 50 GLN A N 1 ATOM 219 C CA . GLN A 1 35 ? -23.648 120.631 3.498 1.00 28.79 ? 50 GLN A CA 1 ATOM 220 C C . GLN A 1 35 ? -24.158 120.419 2.075 1.00 36.49 ? 50 GLN A C 1 ATOM 221 O O . GLN A 1 35 ? -23.439 120.672 1.111 1.00 36.91 ? 50 GLN A O 1 ATOM 222 C CB . GLN A 1 35 ? -23.296 119.280 4.155 1.00 39.98 ? 50 GLN A CB 1 ATOM 223 C CG . GLN A 1 35 ? -21.938 118.658 3.793 1.00 58.55 ? 50 GLN A CG 1 ATOM 224 C CD . GLN A 1 35 ? -21.796 117.202 4.280 1.00 68.82 ? 50 GLN A CD 1 ATOM 225 O OE1 . GLN A 1 35 ? -22.569 116.733 5.128 1.00 72.69 ? 50 GLN A OE1 1 ATOM 226 N NE2 . GLN A 1 35 ? -20.814 116.485 3.732 1.00 68.13 ? 50 GLN A NE2 1 ATOM 227 N N . ASN A 1 36 ? -25.414 119.987 1.954 1.00 29.50 ? 51 ASN A N 1 ATOM 228 C CA . ASN A 1 36 ? -26.040 119.754 0.650 1.00 28.99 ? 51 ASN A CA 1 ATOM 229 C C . ASN A 1 36 ? -26.170 121.026 -0.179 1.00 32.05 ? 51 ASN A C 1 ATOM 230 O O . ASN A 1 36 ? -25.875 121.037 -1.374 1.00 34.11 ? 51 ASN A O 1 ATOM 231 C CB . ASN A 1 36 ? -27.427 119.152 0.837 1.00 32.52 ? 51 ASN A CB 1 ATOM 232 C CG . ASN A 1 36 ? -28.177 119.007 -0.470 1.00 46.70 ? 51 ASN A CG 1 ATOM 233 O OD1 . ASN A 1 36 ? -27.859 118.132 -1.276 1.00 53.51 ? 51 ASN A OD1 1 ATOM 234 N ND2 . ASN A 1 36 ? -29.187 119.851 -0.683 1.00 42.94 ? 51 ASN A ND2 1 ATOM 235 N N . PHE A 1 37 ? -26.638 122.085 0.470 1.00 29.28 ? 52 PHE A N 1 ATOM 236 C CA . PHE A 1 37 ? -26.775 123.406 -0.132 1.00 26.96 ? 52 PHE A CA 1 ATOM 237 C C . PHE A 1 37 ? -25.413 123.880 -0.644 1.00 32.68 ? 52 PHE A C 1 ATOM 238 O O . PHE A 1 37 ? -25.303 124.416 -1.747 1.00 32.47 ? 52 PHE A O 1 ATOM 239 C CB . PHE A 1 37 ? -27.327 124.349 0.941 1.00 24.84 ? 52 PHE A CB 1 ATOM 240 C CG . PHE A 1 37 ? -27.538 125.769 0.492 1.00 19.85 ? 52 PHE A CG 1 ATOM 241 C CD1 . PHE A 1 37 ? -26.483 126.679 0.498 1.00 23.09 ? 52 PHE A CD1 1 ATOM 242 C CD2 . PHE A 1 37 ? -28.804 126.217 0.120 1.00 22.41 ? 52 PHE A CD2 1 ATOM 243 C CE1 . PHE A 1 37 ? -26.678 127.989 0.128 1.00 18.61 ? 52 PHE A CE1 1 ATOM 244 C CE2 . PHE A 1 37 ? -29.007 127.535 -0.266 1.00 23.70 ? 52 PHE A CE2 1 ATOM 245 C CZ . PHE A 1 37 ? -27.942 128.421 -0.269 1.00 24.24 ? 52 PHE A CZ 1 ATOM 246 N N . ILE A 1 38 ? -24.376 123.656 0.160 1.00 31.08 ? 53 ILE A N 1 ATOM 247 C CA . ILE A 1 38 ? -22.994 124.066 -0.140 1.00 27.94 ? 53 ILE A CA 1 ATOM 248 C C . ILE A 1 38 ? -22.389 123.271 -1.292 1.00 34.29 ? 53 ILE A C 1 ATOM 249 O O . ILE A 1 38 ? -21.645 123.815 -2.109 1.00 31.02 ? 53 ILE A O 1 ATOM 250 C CB . ILE A 1 38 ? -22.128 123.902 1.143 1.00 31.49 ? 53 ILE A CB 1 ATOM 251 C CG1 . ILE A 1 38 ? -22.480 125.001 2.150 1.00 34.22 ? 53 ILE A CG1 1 ATOM 252 C CG2 . ILE A 1 38 ? -20.645 123.920 0.862 1.00 35.43 ? 53 ILE A CG2 1 ATOM 253 C CD1 . ILE A 1 38 ? -21.872 124.789 3.553 1.00 31.38 ? 53 ILE A CD1 1 ATOM 254 N N . LYS A 1 39 ? -22.734 121.986 -1.360 1.00 33.86 ? 54 LYS A N 1 ATOM 255 C CA . LYS A 1 39 ? -22.105 121.018 -2.274 1.00 37.03 ? 54 LYS A CA 1 ATOM 256 C C . LYS A 1 39 ? -22.228 121.421 -3.730 1.00 38.67 ? 54 LYS A C 1 ATOM 257 O O . LYS A 1 39 ? -21.346 121.168 -4.549 1.00 34.80 ? 54 LYS A O 1 ATOM 258 C CB . LYS A 1 39 ? -22.764 119.651 -2.066 1.00 49.21 ? 54 LYS A CB 1 ATOM 259 C CG . LYS A 1 39 ? -22.204 118.504 -2.901 1.00 51.26 ? 54 LYS A CG 1 ATOM 260 C CD . LYS A 1 39 ? -22.984 117.222 -2.615 1.00 57.26 ? 54 LYS A CD 1 ATOM 261 C CE . LYS A 1 39 ? -23.515 116.594 -3.896 1.00 61.10 ? 54 LYS A CE 1 ATOM 262 N NZ . LYS A 1 39 ? -24.675 115.693 -3.627 1.00 63.41 ? 54 LYS A NZ 1 ATOM 263 N N . GLU A 1 40 ? -23.345 122.058 -4.036 1.00 35.78 ? 55 GLU A N 1 ATOM 264 C CA . GLU A 1 40 ? -23.658 122.486 -5.381 1.00 42.80 ? 55 GLU A CA 1 ATOM 265 C C . GLU A 1 40 ? -23.656 124.002 -5.459 1.00 33.36 ? 55 GLU A C 1 ATOM 266 O O . GLU A 1 40 ? -24.226 124.591 -6.384 1.00 31.14 ? 55 GLU A O 1 ATOM 267 C CB . GLU A 1 40 ? -25.048 122.008 -5.732 1.00 57.73 ? 55 GLU A CB 1 ATOM 268 C CG . GLU A 1 40 ? -25.117 120.609 -6.253 1.00 61.39 ? 55 GLU A CG 1 ATOM 269 C CD . GLU A 1 40 ? -26.439 120.379 -6.920 1.00 70.86 ? 55 GLU A CD 1 ATOM 270 O OE1 . GLU A 1 40 ? -27.471 120.392 -6.202 1.00 68.49 ? 55 GLU A OE1 1 ATOM 271 O OE2 . GLU A 1 40 ? -26.449 120.241 -8.166 1.00 74.82 ? 55 GLU A OE2 1 ATOM 272 N N . GLY A 1 41 ? -23.027 124.632 -4.476 1.00 30.39 ? 56 GLY A N 1 ATOM 273 C CA . GLY A 1 41 ? -22.981 126.079 -4.413 1.00 25.07 ? 56 GLY A CA 1 ATOM 274 C C . GLY A 1 41 ? -21.629 126.532 -3.916 1.00 25.40 ? 56 GLY A C 1 ATOM 275 O O . GLY A 1 41 ? -20.617 125.897 -4.201 1.00 22.92 ? 56 GLY A O 1 ATOM 276 N N . VAL A 1 42 ? -21.599 127.639 -3.179 1.00 20.64 ? 57 VAL A N 1 ATOM 277 C CA . VAL A 1 42 ? -20.336 128.162 -2.689 1.00 21.56 ? 57 VAL A CA 1 ATOM 278 C C . VAL A 1 42 ? -20.381 128.355 -1.177 1.00 21.83 ? 57 VAL A C 1 ATOM 279 O O . VAL A 1 42 ? -21.450 128.575 -0.574 1.00 21.62 ? 57 VAL A O 1 ATOM 280 C CB . VAL A 1 42 ? -19.976 129.497 -3.356 1.00 23.25 ? 57 VAL A CB 1 ATOM 281 C CG1 . VAL A 1 42 ? -19.890 129.329 -4.868 1.00 22.48 ? 57 VAL A CG1 1 ATOM 282 C CG2 . VAL A 1 42 ? -21.001 130.558 -3.011 1.00 24.89 ? 57 VAL A CG2 1 ATOM 283 N N . LEU A 1 43 ? -19.215 128.249 -0.552 1.00 20.12 ? 58 LEU A N 1 ATOM 284 C CA . LEU A 1 43 ? -19.097 128.529 0.873 1.00 20.44 ? 58 LEU A CA 1 ATOM 285 C C . LEU A 1 43 ? -17.951 129.495 1.094 1.00 19.74 ? 58 LEU A C 1 ATOM 286 O O . LEU A 1 43 ? -16.852 129.279 0.585 1.00 22.69 ? 58 LEU A O 1 ATOM 287 C CB . LEU A 1 43 ? -18.829 127.236 1.644 1.00 20.94 ? 58 LEU A CB 1 ATOM 288 C CG . LEU A 1 43 ? -18.417 127.425 3.103 1.00 24.24 ? 58 LEU A CG 1 ATOM 289 C CD1 . LEU A 1 43 ? -19.589 127.947 3.943 1.00 21.68 ? 58 LEU A CD1 1 ATOM 290 C CD2 . LEU A 1 43 ? -17.870 126.127 3.694 1.00 24.67 ? 58 LEU A CD2 1 ATOM 291 N N . VAL A 1 44 ? -18.209 130.557 1.857 1.00 19.47 ? 59 VAL A N 1 ATOM 292 C CA . VAL A 1 44 ? -17.153 131.403 2.401 1.00 19.72 ? 59 VAL A CA 1 ATOM 293 C C . VAL A 1 44 ? -17.020 131.003 3.869 1.00 17.70 ? 59 VAL A C 1 ATOM 294 O O . VAL A 1 44 ? -17.965 131.169 4.653 1.00 16.74 ? 59 VAL A O 1 ATOM 295 C CB . VAL A 1 44 ? -17.482 132.910 2.255 1.00 19.10 ? 59 VAL A CB 1 ATOM 296 C CG1 . VAL A 1 44 ? -16.373 133.757 2.875 1.00 17.14 ? 59 VAL A CG1 1 ATOM 297 C CG2 . VAL A 1 44 ? -17.648 133.285 0.773 1.00 19.01 ? 59 VAL A CG2 1 ATOM 298 N N . GLU A 1 45 ? -15.865 130.462 4.257 1.00 17.89 ? 60 GLU A N 1 ATOM 299 C CA . GLU A 1 45 ? -15.770 129.792 5.558 1.00 17.79 ? 60 GLU A CA 1 ATOM 300 C C . GLU A 1 45 ? -15.932 130.719 6.748 1.00 17.29 ? 60 GLU A C 1 ATOM 301 O O . GLU A 1 45 ? -16.497 130.336 7.763 1.00 18.53 ? 60 GLU A O 1 ATOM 302 C CB . GLU A 1 45 ? -14.453 129.041 5.676 1.00 21.02 ? 60 GLU A CB 1 ATOM 303 C CG . GLU A 1 45 ? -14.303 127.962 4.626 1.00 26.92 ? 60 GLU A CG 1 ATOM 304 C CD . GLU A 1 45 ? -13.191 127.027 4.962 1.00 48.07 ? 60 GLU A CD 1 ATOM 305 O OE1 . GLU A 1 45 ? -12.108 127.199 4.379 1.00 46.81 ? 60 GLU A OE1 1 ATOM 306 O OE2 . GLU A 1 45 ? -13.399 126.135 5.819 1.00 49.94 ? 60 GLU A OE2 1 ATOM 307 N N . HIS A 1 46 ? -15.451 131.948 6.610 1.00 15.99 ? 61 HIS A N 1 ATOM 308 C CA . HIS A 1 46 ? -15.685 132.955 7.623 1.00 15.08 ? 61 HIS A CA 1 ATOM 309 C C . HIS A 1 46 ? -15.656 134.370 7.006 1.00 16.72 ? 61 HIS A C 1 ATOM 310 O O . HIS A 1 46 ? -14.842 134.679 6.126 1.00 22.25 ? 61 HIS A O 1 ATOM 311 C CB . HIS A 1 46 ? -14.675 132.840 8.782 1.00 22.01 ? 61 HIS A CB 1 ATOM 312 C CG . HIS A 1 46 ? -13.248 132.719 8.333 1.00 28.67 ? 61 HIS A CG 1 ATOM 313 N ND1 . HIS A 1 46 ? -12.642 131.500 8.098 1.00 36.51 ? 61 HIS A ND1 1 ATOM 314 C CD2 . HIS A 1 46 ? -12.310 133.662 8.071 1.00 28.44 ? 61 HIS A CD2 1 ATOM 315 C CE1 . HIS A 1 46 ? -11.396 131.699 7.703 1.00 37.61 ? 61 HIS A CE1 1 ATOM 316 N NE2 . HIS A 1 46 ? -11.167 133.001 7.684 1.00 36.13 ? 61 HIS A NE2 1 ATOM 317 N N . VAL A 1 47 ? -16.588 135.192 7.453 1.00 15.07 ? 62 VAL A N 1 ATOM 318 C CA . VAL A 1 47 ? -16.752 136.550 6.969 1.00 13.53 ? 62 VAL A CA 1 ATOM 319 C C . VAL A 1 47 ? -16.259 137.495 8.057 1.00 12.26 ? 62 VAL A C 1 ATOM 320 O O . VAL A 1 47 ? -16.663 137.393 9.238 1.00 14.62 ? 62 VAL A O 1 ATOM 321 C CB . VAL A 1 47 ? -18.255 136.831 6.659 1.00 11.67 ? 62 VAL A CB 1 ATOM 322 C CG1 . VAL A 1 47 ? -18.484 138.322 6.374 1.00 15.04 ? 62 VAL A CG1 1 ATOM 323 C CG2 . VAL A 1 47 ? -18.761 135.931 5.536 1.00 15.35 ? 62 VAL A CG2 1 ATOM 324 N N . LYS A 1 48 ? -15.382 138.428 7.700 1.00 14.20 ? 63 LYS A N 1 ATOM 325 C CA . LYS A 1 48 ? -14.952 139.443 8.679 1.00 12.30 ? 63 LYS A CA 1 ATOM 326 C C . LYS A 1 48 ? -16.023 140.512 8.754 1.00 12.06 ? 63 LYS A C 1 ATOM 327 O O . LYS A 1 48 ? -16.250 141.223 7.768 1.00 13.47 ? 63 LYS A O 1 ATOM 328 C CB . LYS A 1 48 ? -13.598 140.061 8.306 1.00 14.01 ? 63 LYS A CB 1 ATOM 329 C CG . LYS A 1 48 ? -13.138 141.111 9.333 1.00 15.68 ? 63 LYS A CG 1 ATOM 330 C CD . LYS A 1 48 ? -11.772 141.670 9.001 1.00 19.85 ? 63 LYS A CD 1 ATOM 331 C CE . LYS A 1 48 ? -11.340 142.702 10.046 1.00 19.55 ? 63 LYS A CE 1 ATOM 332 N NZ . LYS A 1 48 ? -9.943 143.117 9.790 1.00 33.52 ? 63 LYS A NZ 1 ATOM 333 N N . ASN A 1 49 ? -16.727 140.586 9.879 1.00 14.59 ? 64 ASN A N 1 ATOM 334 C CA . ASN A 1 49 ? -17.847 141.487 9.986 1.00 13.49 ? 64 ASN A CA 1 ATOM 335 C C . ASN A 1 49 ? -17.383 142.850 10.509 1.00 9.96 ? 64 ASN A C 1 ATOM 336 O O . ASN A 1 49 ? -16.189 143.124 10.439 1.00 13.64 ? 64 ASN A O 1 ATOM 337 C CB . ASN A 1 49 ? -18.963 140.846 10.800 1.00 10.56 ? 64 ASN A CB 1 ATOM 338 C CG . ASN A 1 49 ? -18.533 140.410 12.189 1.00 9.74 ? 64 ASN A CG 1 ATOM 339 O OD1 . ASN A 1 49 ? -17.341 140.280 12.493 1.00 13.63 ? 64 ASN A OD1 1 ATOM 340 N ND2 . ASN A 1 49 ? -19.526 140.161 13.062 1.00 12.08 ? 64 ASN A ND2 1 ATOM 341 N N . VAL A 1 50 ? -18.278 143.693 11.005 1.00 12.73 ? 65 VAL A N 1 ATOM 342 C CA . VAL A 1 50 ? -17.899 145.063 11.411 1.00 11.41 ? 65 VAL A CA 1 ATOM 343 C C . VAL A 1 50 ? -18.091 145.316 12.908 1.00 10.97 ? 65 VAL A C 1 ATOM 344 O O . VAL A 1 50 ? -18.994 144.768 13.556 1.00 12.23 ? 65 VAL A O 1 ATOM 345 C CB . VAL A 1 50 ? -18.625 146.173 10.590 1.00 14.89 ? 65 VAL A CB 1 ATOM 346 C CG1 . VAL A 1 50 ? -18.135 146.213 9.152 1.00 17.06 ? 65 VAL A CG1 1 ATOM 347 C CG2 . VAL A 1 50 ? -20.129 145.985 10.580 1.00 16.36 ? 65 VAL A CG2 1 ATOM 348 N N . PHE A 1 51 ? -17.215 146.142 13.460 1.00 13.72 ? 66 PHE A N 1 ATOM 349 C CA . PHE A 1 51 ? -17.314 146.596 14.848 1.00 12.38 ? 66 PHE A CA 1 ATOM 350 C C . PHE A 1 51 ? -18.329 147.741 14.956 1.00 10.31 ? 66 PHE A C 1 ATOM 351 O O . PHE A 1 51 ? -18.317 148.635 14.117 1.00 13.12 ? 66 PHE A O 1 ATOM 352 C CB . PHE A 1 51 ? -15.919 147.087 15.273 1.00 13.78 ? 66 PHE A CB 1 ATOM 353 C CG . PHE A 1 51 ? -15.795 147.461 16.730 1.00 12.94 ? 66 PHE A CG 1 ATOM 354 C CD1 . PHE A 1 51 ? -15.560 146.491 17.704 1.00 15.67 ? 66 PHE A CD1 1 ATOM 355 C CD2 . PHE A 1 51 ? -15.874 148.782 17.114 1.00 14.10 ? 66 PHE A CD2 1 ATOM 356 C CE1 . PHE A 1 51 ? -15.424 146.826 19.029 1.00 18.70 ? 66 PHE A CE1 1 ATOM 357 C CE2 . PHE A 1 51 ? -15.734 149.139 18.446 1.00 12.35 ? 66 PHE A CE2 1 ATOM 358 C CZ . PHE A 1 51 ? -15.505 148.152 19.410 1.00 15.39 ? 66 PHE A CZ 1 ATOM 359 N N . ILE A 1 52 ? -19.227 147.736 15.949 1.00 10.79 ? 67 ILE A N 1 ATOM 360 C CA . ILE A 1 52 ? -19.334 146.667 16.961 1.00 9.22 ? 67 ILE A CA 1 ATOM 361 C C . ILE A 1 52 ? -20.133 145.501 16.427 1.00 11.37 ? 67 ILE A C 1 ATOM 362 O O . ILE A 1 52 ? -21.004 145.662 15.567 1.00 10.92 ? 67 ILE A O 1 ATOM 363 C CB . ILE A 1 52 ? -19.997 147.180 18.253 1.00 11.76 ? 67 ILE A CB 1 ATOM 364 C CG1 . ILE A 1 52 ? -21.499 147.474 18.059 1.00 11.87 ? 67 ILE A CG1 1 ATOM 365 C CG2 . ILE A 1 52 ? -19.244 148.413 18.797 1.00 12.91 ? 67 ILE A CG2 1 ATOM 366 C CD1 . ILE A 1 52 ? -22.160 148.009 19.356 1.00 14.31 ? 67 ILE A CD1 1 ATOM 367 N N . THR A 1 53 ? -19.843 144.304 16.916 1.00 11.49 ? 68 THR A N 1 ATOM 368 C CA . THR A 1 53 ? -20.390 143.098 16.296 1.00 13.20 ? 68 THR A CA 1 ATOM 369 C C . THR A 1 53 ? -21.762 142.732 16.861 1.00 12.91 ? 68 THR A C 1 ATOM 370 O O . THR A 1 53 ? -21.978 141.633 17.412 1.00 13.71 ? 68 THR A O 1 ATOM 371 C CB . THR A 1 53 ? -19.376 141.916 16.369 1.00 10.54 ? 68 THR A CB 1 ATOM 372 O OG1 . THR A 1 53 ? -18.935 141.741 17.725 1.00 12.32 ? 68 THR A OG1 1 ATOM 373 C CG2 . THR A 1 53 ? -18.153 142.208 15.492 1.00 12.08 ? 68 THR A CG2 1 ATOM 374 N N . LYS A 1 54 ? -22.696 143.659 16.705 1.00 12.18 ? 69 LYS A N 1 ATOM 375 C CA . LYS A 1 54 ? -24.060 143.491 17.171 1.00 10.39 ? 69 LYS A CA 1 ATOM 376 C C . LYS A 1 54 ? -24.998 143.335 15.986 1.00 13.86 ? 69 LYS A C 1 ATOM 377 O O . LYS A 1 54 ? -24.613 143.565 14.830 1.00 14.22 ? 69 LYS A O 1 ATOM 378 C CB . LYS A 1 54 ? -24.487 144.704 18.022 1.00 11.16 ? 69 LYS A CB 1 ATOM 379 C CG . LYS A 1 54 ? -23.726 144.808 19.367 1.00 13.66 ? 69 LYS A CG 1 ATOM 380 C CD . LYS A 1 54 ? -24.118 143.727 20.330 1.00 12.59 ? 69 LYS A CD 1 ATOM 381 C CE . LYS A 1 54 ? -23.585 144.055 21.733 1.00 18.08 ? 69 LYS A CE 1 ATOM 382 N NZ . LYS A 1 54 ? -23.909 142.999 22.729 1.00 20.38 ? 69 LYS A NZ 1 ATOM 383 N N . THR A 1 55 ? -26.247 142.981 16.288 1.00 10.12 ? 70 THR A N 1 ATOM 384 C CA . THR A 1 55 ? -27.232 142.607 15.282 1.00 13.85 ? 70 THR A CA 1 ATOM 385 C C . THR A 1 55 ? -27.676 143.688 14.334 1.00 14.54 ? 70 THR A C 1 ATOM 386 O O . THR A 1 55 ? -27.599 143.522 13.109 1.00 13.43 ? 70 THR A O 1 ATOM 387 C CB . THR A 1 55 ? -28.474 142.008 15.997 1.00 13.80 ? 70 THR A CB 1 ATOM 388 O OG1 . THR A 1 55 ? -28.062 140.820 16.682 1.00 11.40 ? 70 THR A OG1 1 ATOM 389 C CG2 . THR A 1 55 ? -29.627 141.682 15.002 1.00 14.60 ? 70 THR A CG2 1 ATOM 390 N N . PHE A 1 56 ? -28.182 144.781 14.883 1.00 11.54 ? 71 PHE A N 1 ATOM 391 C CA . PHE A 1 56 ? -28.694 145.844 14.007 1.00 15.00 ? 71 PHE A CA 1 ATOM 392 C C . PHE A 1 56 ? -27.589 146.463 13.141 1.00 12.54 ? 71 PHE A C 1 ATOM 393 O O . PHE A 1 56 ? -27.770 146.605 11.926 1.00 13.69 ? 71 PHE A O 1 ATOM 394 C CB . PHE A 1 56 ? -29.539 146.861 14.793 1.00 15.55 ? 71 PHE A CB 1 ATOM 395 C CG . PHE A 1 56 ? -30.979 146.432 14.971 1.00 14.95 ? 71 PHE A CG 1 ATOM 396 C CD1 . PHE A 1 56 ? -31.315 145.409 15.847 1.00 22.89 ? 71 PHE A CD1 1 ATOM 397 C CD2 . PHE A 1 56 ? -31.981 147.015 14.225 1.00 15.55 ? 71 PHE A CD2 1 ATOM 398 C CE1 . PHE A 1 56 ? -32.653 145.013 15.998 1.00 24.61 ? 71 PHE A CE1 1 ATOM 399 C CE2 . PHE A 1 56 ? -33.289 146.631 14.370 1.00 19.94 ? 71 PHE A CE2 1 ATOM 400 C CZ . PHE A 1 56 ? -33.636 145.626 15.251 1.00 20.41 ? 71 PHE A CZ 1 ATOM 401 N N . PRO A 1 57 ? -26.416 146.762 13.731 1.00 11.10 ? 72 PRO A N 1 ATOM 402 C CA . PRO A 1 57 ? -25.361 147.356 12.900 1.00 12.41 ? 72 PRO A CA 1 ATOM 403 C C . PRO A 1 57 ? -24.882 146.422 11.798 1.00 14.50 ? 72 PRO A C 1 ATOM 404 O O . PRO A 1 57 ? -24.660 146.871 10.663 1.00 13.84 ? 72 PRO A O 1 ATOM 405 C CB . PRO A 1 57 ? -24.231 147.610 13.905 1.00 12.15 ? 72 PRO A CB 1 ATOM 406 C CG . PRO A 1 57 ? -24.950 147.848 15.208 1.00 13.80 ? 72 PRO A CG 1 ATOM 407 C CD . PRO A 1 57 ? -26.096 146.860 15.171 1.00 14.74 ? 72 PRO A CD 1 ATOM 408 N N . ASN A 1 58 ? -24.706 145.141 12.093 1.00 12.06 ? 73 ASN A N 1 ATOM 409 C CA . ASN A 1 58 ? -24.185 144.267 11.047 1.00 12.43 ? 73 ASN A CA 1 ATOM 410 C C . ASN A 1 58 ? -25.184 143.919 9.973 1.00 11.83 ? 73 ASN A C 1 ATOM 411 O O . ASN A 1 58 ? -24.797 143.754 8.809 1.00 13.47 ? 73 ASN A O 1 ATOM 412 C CB . ASN A 1 58 ? -23.509 143.012 11.611 1.00 12.49 ? 73 ASN A CB 1 ATOM 413 C CG . ASN A 1 58 ? -22.066 143.266 11.980 1.00 11.49 ? 73 ASN A CG 1 ATOM 414 O OD1 . ASN A 1 58 ? -21.167 143.026 11.166 1.00 13.66 ? 73 ASN A OD1 1 ATOM 415 N ND2 . ASN A 1 58 ? -21.818 143.771 13.206 1.00 13.37 ? 73 ASN A ND2 1 ATOM 416 N N . HIS A 1 59 ? -26.449 143.751 10.341 1.00 12.57 ? 74 HIS A N 1 ATOM 417 C CA . HIS A 1 59 ? -27.439 143.525 9.281 1.00 13.16 ? 74 HIS A CA 1 ATOM 418 C C . HIS A 1 59 ? -27.482 144.693 8.312 1.00 18.58 ? 74 HIS A C 1 ATOM 419 O O . HIS A 1 59 ? -27.639 144.511 7.095 1.00 14.15 ? 74 HIS A O 1 ATOM 420 C CB . HIS A 1 59 ? -28.858 143.204 9.828 1.00 14.17 ? 74 HIS A CB 1 ATOM 421 C CG . HIS A 1 59 ? -29.021 141.780 10.267 1.00 11.43 ? 74 HIS A CG 1 ATOM 422 N ND1 . HIS A 1 59 ? -28.723 141.374 11.546 1.00 12.90 ? 74 HIS A ND1 1 ATOM 423 C CD2 . HIS A 1 59 ? -29.421 140.665 9.598 1.00 14.44 ? 74 HIS A CD2 1 ATOM 424 C CE1 . HIS A 1 59 ? -28.956 140.070 11.661 1.00 12.65 ? 74 HIS A CE1 1 ATOM 425 N NE2 . HIS A 1 59 ? -29.374 139.615 10.489 1.00 12.66 ? 74 HIS A NE2 1 ATOM 426 N N . TYR A 1 60 ? -27.335 145.901 8.835 1.00 14.76 ? 75 TYR A N 1 ATOM 427 C CA . TYR A 1 60 ? -27.404 147.051 7.938 1.00 11.20 ? 75 TYR A CA 1 ATOM 428 C C . TYR A 1 60 ? -26.156 147.120 7.083 1.00 11.57 ? 75 TYR A C 1 ATOM 429 O O . TYR A 1 60 ? -26.208 147.582 5.931 1.00 15.47 ? 75 TYR A O 1 ATOM 430 C CB . TYR A 1 60 ? -27.624 148.364 8.698 1.00 14.28 ? 75 TYR A CB 1 ATOM 431 C CG . TYR A 1 60 ? -28.481 149.389 7.947 1.00 14.76 ? 75 TYR A CG 1 ATOM 432 C CD1 . TYR A 1 60 ? -29.591 148.994 7.182 1.00 13.37 ? 75 TYR A CD1 1 ATOM 433 C CD2 . TYR A 1 60 ? -28.207 150.757 8.051 1.00 19.32 ? 75 TYR A CD2 1 ATOM 434 C CE1 . TYR A 1 60 ? -30.379 149.934 6.546 1.00 19.68 ? 75 TYR A CE1 1 ATOM 435 C CE2 . TYR A 1 60 ? -28.994 151.708 7.402 1.00 17.96 ? 75 TYR A CE2 1 ATOM 436 C CZ . TYR A 1 60 ? -30.081 151.280 6.657 1.00 20.37 ? 75 TYR A CZ 1 ATOM 437 O OH . TYR A 1 60 ? -30.881 152.198 6.004 1.00 20.64 ? 75 TYR A OH 1 ATOM 438 N N . SER A 1 61 ? -25.021 146.711 7.644 1.00 12.98 ? 76 SER A N 1 ATOM 439 C CA . SER A 1 61 ? -23.827 146.667 6.818 1.00 13.38 ? 76 SER A CA 1 ATOM 440 C C . SER A 1 61 ? -23.964 145.691 5.651 1.00 13.07 ? 76 SER A C 1 ATOM 441 O O . SER A 1 61 ? -23.482 145.977 4.552 1.00 14.59 ? 76 SER A O 1 ATOM 442 C CB . SER A 1 61 ? -22.584 146.342 7.651 1.00 12.94 ? 76 SER A CB 1 ATOM 443 O OG . SER A 1 61 ? -22.235 147.500 8.432 1.00 13.01 ? 76 SER A OG 1 ATOM 444 N N . ILE A 1 62 ? -24.570 144.535 5.893 1.00 13.14 ? 77 ILE A N 1 ATOM 445 C CA . ILE A 1 62 ? -24.801 143.566 4.818 1.00 15.28 ? 77 ILE A CA 1 ATOM 446 C C . ILE A 1 62 ? -25.546 144.218 3.658 1.00 12.16 ? 77 ILE A C 1 ATOM 447 O O . ILE A 1 62 ? -25.137 144.053 2.503 1.00 15.85 ? 77 ILE A O 1 ATOM 448 C CB . ILE A 1 62 ? -25.608 142.309 5.297 1.00 14.77 ? 77 ILE A CB 1 ATOM 449 C CG1 . ILE A 1 62 ? -24.793 141.459 6.283 1.00 16.48 ? 77 ILE A CG1 1 ATOM 450 C CG2 . ILE A 1 62 ? -26.013 141.451 4.106 1.00 14.95 ? 77 ILE A CG2 1 ATOM 451 C CD1 . ILE A 1 62 ? -25.643 140.335 6.980 1.00 16.63 ? 77 ILE A CD1 1 ATOM 452 N N . VAL A 1 63 ? -26.606 144.977 3.947 1.00 14.56 ? 78 VAL A N 1 ATOM 453 C CA . VAL A 1 63 ? -27.456 145.537 2.884 1.00 14.59 ? 78 VAL A CA 1 ATOM 454 C C . VAL A 1 63 ? -27.078 146.934 2.397 1.00 14.59 ? 78 VAL A C 1 ATOM 455 O O . VAL A 1 63 ? -27.740 147.471 1.501 1.00 17.02 ? 78 VAL A O 1 ATOM 456 C CB . VAL A 1 63 ? -28.950 145.513 3.270 1.00 14.69 ? 78 VAL A CB 1 ATOM 457 C CG1 . VAL A 1 63 ? -29.409 144.084 3.391 1.00 16.72 ? 78 VAL A CG1 1 ATOM 458 C CG2 . VAL A 1 63 ? -29.197 146.281 4.579 1.00 18.39 ? 78 VAL A CG2 1 ATOM 459 N N . THR A 1 64 ? -26.000 147.498 2.939 1.00 14.73 ? 79 THR A N 1 ATOM 460 C CA . THR A 1 64 ? -25.512 148.805 2.474 1.00 16.56 ? 79 THR A CA 1 ATOM 461 C C . THR A 1 64 ? -24.062 148.806 2.015 1.00 15.59 ? 79 THR A C 1 ATOM 462 O O . THR A 1 64 ? -23.641 149.743 1.331 1.00 16.47 ? 79 THR A O 1 ATOM 463 C CB . THR A 1 64 ? -25.633 149.907 3.541 1.00 15.15 ? 79 THR A CB 1 ATOM 464 O OG1 . THR A 1 64 ? -24.816 149.566 4.671 1.00 15.49 ? 79 THR A OG1 1 ATOM 465 C CG2 . THR A 1 64 ? -27.078 150.129 3.965 1.00 16.79 ? 79 THR A CG2 1 ATOM 466 N N . GLY A 1 65 ? -23.305 147.783 2.408 1.00 14.21 ? 80 GLY A N 1 ATOM 467 C CA . GLY A 1 65 ? -21.872 147.756 2.144 1.00 18.26 ? 80 GLY A CA 1 ATOM 468 C C . GLY A 1 65 ? -21.061 148.793 2.904 1.00 16.56 ? 80 GLY A C 1 ATOM 469 O O . GLY A 1 65 ? -19.927 149.102 2.524 1.00 14.20 ? 80 GLY A O 1 ATOM 470 N N . LEU A 1 66 ? -21.622 149.340 3.972 1.00 13.57 ? 81 LEU A N 1 ATOM 471 C CA . LEU A 1 66 ? -20.962 150.409 4.716 1.00 13.69 ? 81 LEU A CA 1 ATOM 472 C C . LEU A 1 66 ? -20.552 149.993 6.100 1.00 16.49 ? 81 LEU A C 1 ATOM 473 O O . LEU A 1 66 ? -21.232 149.186 6.750 1.00 15.54 ? 81 LEU A O 1 ATOM 474 C CB . LEU A 1 66 ? -21.884 151.619 4.861 1.00 15.77 ? 81 LEU A CB 1 ATOM 475 C CG . LEU A 1 66 ? -22.253 152.321 3.547 1.00 14.60 ? 81 LEU A CG 1 ATOM 476 C CD1 . LEU A 1 66 ? -23.488 153.176 3.767 1.00 16.36 ? 81 LEU A CD1 1 ATOM 477 C CD2 . LEU A 1 66 ? -21.072 153.119 3.072 1.00 20.26 ? 81 LEU A CD2 1 ATOM 478 N N . TYR A 1 67 ? -19.444 150.580 6.537 1.00 13.65 ? 82 TYR A N 1 ATOM 479 C CA . TYR A 1 67 ? -19.048 150.572 7.941 1.00 12.56 ? 82 TYR A CA 1 ATOM 480 C C . TYR A 1 67 ? -20.080 151.295 8.819 1.00 13.28 ? 82 TYR A C 1 ATOM 481 O O . TYR A 1 67 ? -20.858 152.159 8.335 1.00 14.38 ? 82 TYR A O 1 ATOM 482 C CB . TYR A 1 67 ? -17.682 151.241 8.113 1.00 13.94 ? 82 TYR A CB 1 ATOM 483 C CG . TYR A 1 67 ? -16.565 150.551 7.371 1.00 14.75 ? 82 TYR A CG 1 ATOM 484 C CD1 . TYR A 1 67 ? -16.414 149.173 7.419 1.00 23.37 ? 82 TYR A CD1 1 ATOM 485 C CD2 . TYR A 1 67 ? -15.682 151.280 6.591 1.00 19.33 ? 82 TYR A CD2 1 ATOM 486 C CE1 . TYR A 1 67 ? -15.389 148.546 6.722 1.00 25.92 ? 82 TYR A CE1 1 ATOM 487 C CE2 . TYR A 1 67 ? -14.668 150.671 5.900 1.00 20.75 ? 82 TYR A CE2 1 ATOM 488 C CZ . TYR A 1 67 ? -14.522 149.314 5.969 1.00 25.53 ? 82 TYR A CZ 1 ATOM 489 O OH . TYR A 1 67 ? -13.504 148.744 5.254 1.00 29.49 ? 82 TYR A OH 1 ATOM 490 N N . GLU A 1 68 ? -20.075 150.976 10.108 1.00 14.18 ? 83 GLU A N 1 ATOM 491 C CA . GLU A 1 68 ? -21.124 151.479 10.997 1.00 13.34 ? 83 GLU A CA 1 ATOM 492 C C . GLU A 1 68 ? -21.075 152.992 11.175 1.00 14.80 ? 83 GLU A C 1 ATOM 493 O O . GLU A 1 68 ? -22.123 153.626 11.309 1.00 15.35 ? 83 GLU A O 1 ATOM 494 C CB . GLU A 1 68 ? -21.078 150.780 12.356 1.00 11.99 ? 83 GLU A CB 1 ATOM 495 C CG . GLU A 1 68 ? -21.129 149.265 12.212 1.00 13.33 ? 83 GLU A CG 1 ATOM 496 C CD . GLU A 1 68 ? -21.167 148.515 13.529 1.00 16.49 ? 83 GLU A CD 1 ATOM 497 O OE1 . GLU A 1 68 ? -21.375 149.126 14.597 1.00 13.80 ? 83 GLU A OE1 1 ATOM 498 O OE2 . GLU A 1 68 ? -21.060 147.279 13.476 1.00 13.57 ? 83 GLU A OE2 1 ATOM 499 N N . GLU A 1 69 ? -19.877 153.580 11.194 1.00 12.08 ? 84 GLU A N 1 ATOM 500 C CA . GLU A 1 69 ? -19.788 155.035 11.329 1.00 12.50 ? 84 GLU A CA 1 ATOM 501 C C . GLU A 1 69 ? -20.436 155.714 10.136 1.00 15.68 ? 84 GLU A C 1 ATOM 502 O O . GLU A 1 69 ? -20.839 156.867 10.227 1.00 17.45 ? 84 GLU A O 1 ATOM 503 C CB . GLU A 1 69 ? -18.325 155.511 11.468 1.00 15.83 ? 84 GLU A CB 1 ATOM 504 C CG . GLU A 1 69 ? -17.472 155.239 10.224 1.00 13.86 ? 84 GLU A CG 1 ATOM 505 C CD . GLU A 1 69 ? -15.995 155.572 10.401 1.00 16.74 ? 84 GLU A CD 1 ATOM 506 O OE1 . GLU A 1 69 ? -15.602 156.128 11.449 1.00 16.71 ? 84 GLU A OE1 1 ATOM 507 O OE2 . GLU A 1 69 ? -15.208 155.310 9.458 1.00 19.29 ? 84 GLU A OE2 1 ATOM 508 N N . SER A 1 70 ? -20.536 154.996 9.017 1.00 15.19 ? 85 SER A N 1 ATOM 509 C CA . SER A 1 70 ? -21.070 155.573 7.781 1.00 14.54 ? 85 SER A CA 1 ATOM 510 C C . SER A 1 70 ? -22.574 155.364 7.619 1.00 16.25 ? 85 SER A C 1 ATOM 511 O O . SER A 1 70 ? -23.280 156.276 7.185 1.00 23.60 ? 85 SER A O 1 ATOM 512 C CB . SER A 1 70 ? -20.332 155.030 6.544 1.00 15.93 ? 85 SER A CB 1 ATOM 513 O OG . SER A 1 70 ? -18.974 155.481 6.483 1.00 17.97 ? 85 SER A OG 1 ATOM 514 N N . HIS A 1 71 ? -23.079 154.163 7.928 1.00 13.25 ? 86 HIS A N 1 ATOM 515 C CA . HIS A 1 71 ? -24.519 153.934 7.805 1.00 12.39 ? 86 HIS A CA 1 ATOM 516 C C . HIS A 1 71 ? -25.324 154.380 9.023 1.00 16.50 ? 86 HIS A C 1 ATOM 517 O O . HIS A 1 71 ? -26.541 154.478 8.958 1.00 17.99 ? 86 HIS A O 1 ATOM 518 C CB . HIS A 1 71 ? -24.874 152.497 7.353 1.00 15.41 ? 86 HIS A CB 1 ATOM 519 C CG . HIS A 1 71 ? -24.564 151.418 8.344 1.00 13.07 ? 86 HIS A CG 1 ATOM 520 N ND1 . HIS A 1 71 ? -24.971 151.466 9.666 1.00 16.15 ? 86 HIS A ND1 1 ATOM 521 C CD2 . HIS A 1 71 ? -23.916 150.235 8.186 1.00 13.83 ? 86 HIS A CD2 1 ATOM 522 C CE1 . HIS A 1 71 ? -24.558 150.370 10.285 1.00 14.49 ? 86 HIS A CE1 1 ATOM 523 N NE2 . HIS A 1 71 ? -23.922 149.602 9.409 1.00 13.58 ? 86 HIS A NE2 1 ATOM 524 N N . GLY A 1 72 ? -24.636 154.623 10.139 1.00 16.45 ? 87 GLY A N 1 ATOM 525 C CA . GLY A 1 72 ? -25.236 155.299 11.283 1.00 14.74 ? 87 GLY A CA 1 ATOM 526 C C . GLY A 1 72 ? -25.948 154.413 12.290 1.00 18.09 ? 87 GLY A C 1 ATOM 527 O O . GLY A 1 72 ? -26.453 154.911 13.299 1.00 18.42 ? 87 GLY A O 1 ATOM 528 N N . ILE A 1 73 ? -26.000 153.108 12.051 1.00 16.42 ? 88 ILE A N 1 ATOM 529 C CA . ILE A 1 73 ? -26.571 152.222 13.054 1.00 18.01 ? 88 ILE A CA 1 ATOM 530 C C . ILE A 1 73 ? -25.387 151.627 13.798 1.00 16.98 ? 88 ILE A C 1 ATOM 531 O O . ILE A 1 73 ? -24.811 150.609 13.398 1.00 14.79 ? 88 ILE A O 1 ATOM 532 C CB . ILE A 1 73 ? -27.485 151.136 12.437 1.00 18.29 ? 88 ILE A CB 1 ATOM 533 C CG1 . ILE A 1 73 ? -28.627 151.789 11.653 1.00 14.08 ? 88 ILE A CG1 1 ATOM 534 C CG2 . ILE A 1 73 ? -28.055 150.193 13.513 1.00 16.63 ? 88 ILE A CG2 1 ATOM 535 C CD1 . ILE A 1 73 ? -29.635 150.819 11.212 1.00 22.14 ? 88 ILE A CD1 1 ATOM 536 N N . VAL A 1 74 ? -24.997 152.291 14.879 1.00 14.37 ? 89 VAL A N 1 ATOM 537 C CA . VAL A 1 74 ? -23.719 151.986 15.519 1.00 16.05 ? 89 VAL A CA 1 ATOM 538 C C . VAL A 1 74 ? -23.890 151.056 16.704 1.00 12.46 ? 89 VAL A C 1 ATOM 539 O O . VAL A 1 74 ? -22.910 150.617 17.289 1.00 14.47 ? 89 VAL A O 1 ATOM 540 C CB . VAL A 1 74 ? -22.949 153.264 15.944 1.00 14.52 ? 89 VAL A CB 1 ATOM 541 C CG1 . VAL A 1 74 ? -22.735 154.185 14.712 1.00 16.82 ? 89 VAL A CG1 1 ATOM 542 C CG2 . VAL A 1 74 ? -23.650 153.992 17.084 1.00 16.58 ? 89 VAL A CG2 1 ATOM 543 N N . ALA A 1 75 ? -25.137 150.770 17.068 1.00 13.84 ? 90 ALA A N 1 ATOM 544 C CA . ALA A 1 75 ? -25.390 149.827 18.153 1.00 13.55 ? 90 ALA A CA 1 ATOM 545 C C . ALA A 1 75 ? -26.862 149.420 18.136 1.00 11.97 ? 90 ALA A C 1 ATOM 546 O O . ALA A 1 75 ? -27.656 149.997 17.398 1.00 16.04 ? 90 ALA A O 1 ATOM 547 C CB . ALA A 1 75 ? -25.051 150.462 19.509 1.00 13.72 ? 90 ALA A CB 1 ATOM 548 N N . ASN A 1 76 ? -27.221 148.434 18.947 1.00 14.48 ? 91 ASN A N 1 ATOM 549 C CA . ASN A 1 76 ? -28.627 148.097 19.107 1.00 13.10 ? 91 ASN A CA 1 ATOM 550 C C . ASN A 1 76 ? -29.366 149.102 19.978 1.00 15.47 ? 91 ASN A C 1 ATOM 551 O O . ASN A 1 76 ? -30.591 149.176 19.926 1.00 19.72 ? 91 ASN A O 1 ATOM 552 C CB . ASN A 1 76 ? -28.815 146.702 19.723 1.00 13.15 ? 91 ASN A CB 1 ATOM 553 C CG . ASN A 1 76 ? -28.263 145.588 18.871 1.00 22.95 ? 91 ASN A CG 1 ATOM 554 O OD1 . ASN A 1 76 ? -28.257 145.652 17.627 1.00 18.12 ? 91 ASN A OD1 1 ATOM 555 N ND2 . ASN A 1 76 ? -27.803 144.522 19.546 1.00 26.93 ? 91 ASN A ND2 1 ATOM 556 N N . SER A 1 77 ? -28.627 149.834 20.812 1.00 14.13 ? 92 SER A N 1 ATOM 557 C CA . SER A 1 77 ? -29.186 150.913 21.629 1.00 18.65 ? 92 SER A CA 1 ATOM 558 C C . SER A 1 77 ? -28.385 152.171 21.377 1.00 13.56 ? 92 SER A C 1 ATOM 559 O O . SER A 1 77 ? -27.156 152.166 21.557 1.00 16.56 ? 92 SER A O 1 ATOM 560 C CB . SER A 1 77 ? -29.142 150.573 23.116 1.00 21.51 ? 92 SER A CB 1 ATOM 561 O OG . SER A 1 77 ? -29.965 149.441 23.400 1.00 22.29 ? 92 SER A OG 1 ATOM 562 N N . MET A 1 78 ? -29.058 153.233 20.923 1.00 15.35 ? 93 MET A N 1 ATOM 563 C CA . MET A 1 78 ? -28.386 154.497 20.617 1.00 16.13 ? 93 MET A CA 1 ATOM 564 C C . MET A 1 78 ? -29.136 155.679 21.209 1.00 19.41 ? 93 MET A C 1 ATOM 565 O O . MET A 1 78 ? -30.348 155.610 21.462 1.00 16.93 ? 93 MET A O 1 ATOM 566 C CB . MET A 1 78 ? -28.272 154.708 19.099 1.00 16.82 ? 93 MET A CB 1 ATOM 567 C CG . MET A 1 78 ? -27.471 153.629 18.367 1.00 15.06 ? 93 MET A CG 1 ATOM 568 S SD . MET A 1 78 ? -27.369 154.018 16.593 1.00 16.29 ? 93 MET A SD 1 ATOM 569 C CE . MET A 1 78 ? -28.940 153.414 16.057 1.00 17.44 ? 93 MET A CE 1 ATOM 570 N N . TYR A 1 79 ? -28.407 156.774 21.401 1.00 20.01 ? 94 TYR A N 1 ATOM 571 C CA . TYR A 1 79 ? -28.980 158.041 21.847 1.00 19.36 ? 94 TYR A CA 1 ATOM 572 C C . TYR A 1 79 ? -28.371 159.168 21.009 1.00 15.40 ? 94 TYR A C 1 ATOM 573 O O . TYR A 1 79 ? -27.134 159.276 20.904 1.00 18.37 ? 94 TYR A O 1 ATOM 574 C CB . TYR A 1 79 ? -28.708 158.284 23.331 1.00 18.26 ? 94 TYR A CB 1 ATOM 575 C CG . TYR A 1 79 ? -29.079 159.679 23.802 1.00 22.26 ? 94 TYR A CG 1 ATOM 576 C CD1 . TYR A 1 79 ? -28.101 160.565 24.222 1.00 21.03 ? 94 TYR A CD1 1 ATOM 577 C CD2 . TYR A 1 79 ? -30.405 160.091 23.838 1.00 19.26 ? 94 TYR A CD2 1 ATOM 578 C CE1 . TYR A 1 79 ? -28.422 161.834 24.651 1.00 22.37 ? 94 TYR A CE1 1 ATOM 579 C CE2 . TYR A 1 79 ? -30.745 161.375 24.272 1.00 23.66 ? 94 TYR A CE2 1 ATOM 580 C CZ . TYR A 1 79 ? -29.744 162.233 24.678 1.00 26.15 ? 94 TYR A CZ 1 ATOM 581 O OH . TYR A 1 79 ? -30.049 163.508 25.115 1.00 26.91 ? 94 TYR A OH 1 ATOM 582 N N . ASP A 1 80 ? -29.221 159.977 20.400 1.00 19.26 ? 95 ASP A N 1 ATOM 583 C CA . ASP A 1 80 ? -28.747 161.128 19.647 1.00 20.27 ? 95 ASP A CA 1 ATOM 584 C C . ASP A 1 80 ? -28.950 162.360 20.515 1.00 17.37 ? 95 ASP A C 1 ATOM 585 O O . ASP A 1 80 ? -30.086 162.753 20.761 1.00 23.71 ? 95 ASP A O 1 ATOM 586 C CB . ASP A 1 80 ? -29.540 161.289 18.351 1.00 20.81 ? 95 ASP A CB 1 ATOM 587 C CG . ASP A 1 80 ? -29.006 162.397 17.484 1.00 27.31 ? 95 ASP A CG 1 ATOM 588 O OD1 . ASP A 1 80 ? -27.833 162.290 17.052 1.00 28.64 ? 95 ASP A OD1 1 ATOM 589 O OD2 . ASP A 1 80 ? -29.755 163.367 17.216 1.00 25.53 ? 95 ASP A OD2 1 ATOM 590 N N . ALA A 1 81 ? -27.857 162.941 21.000 1.00 20.70 ? 96 ALA A N 1 ATOM 591 C CA . ALA A 1 81 ? -27.943 164.034 21.964 1.00 23.28 ? 96 ALA A CA 1 ATOM 592 C C . ALA A 1 81 ? -28.642 165.262 21.388 1.00 27.79 ? 96 ALA A C 1 ATOM 593 O O . ALA A 1 81 ? -29.356 165.964 22.100 1.00 31.49 ? 96 ALA A O 1 ATOM 594 C CB . ALA A 1 81 ? -26.578 164.383 22.504 1.00 34.13 ? 96 ALA A CB 1 ATOM 595 N N . VAL A 1 82 ? -28.461 165.509 20.096 1.00 26.32 ? 97 VAL A N 1 ATOM 596 C CA . VAL A 1 82 ? -29.013 166.713 19.486 1.00 21.57 ? 97 VAL A CA 1 ATOM 597 C C . VAL A 1 82 ? -30.547 166.675 19.401 1.00 24.32 ? 97 VAL A C 1 ATOM 598 O O . VAL A 1 82 ? -31.215 167.618 19.847 1.00 31.16 ? 97 VAL A O 1 ATOM 599 C CB . VAL A 1 82 ? -28.392 166.977 18.102 1.00 27.50 ? 97 VAL A CB 1 ATOM 600 C CG1 . VAL A 1 82 ? -29.037 168.193 17.463 1.00 29.17 ? 97 VAL A CG1 1 ATOM 601 C CG2 . VAL A 1 82 ? -26.887 167.198 18.232 1.00 32.70 ? 97 VAL A CG2 1 ATOM 602 N N . THR A 1 83 ? -31.099 165.591 18.850 1.00 26.83 ? 98 THR A N 1 ATOM 603 C CA . THR A 1 83 ? -32.552 165.475 18.695 1.00 25.53 ? 98 THR A CA 1 ATOM 604 C C . THR A 1 83 ? -33.206 164.897 19.956 1.00 23.91 ? 98 THR A C 1 ATOM 605 O O . THR A 1 83 ? -34.438 164.949 20.097 1.00 25.75 ? 98 THR A O 1 ATOM 606 C CB . THR A 1 83 ? -32.938 164.542 17.532 1.00 28.16 ? 98 THR A CB 1 ATOM 607 O OG1 . THR A 1 83 ? -32.309 163.275 17.730 1.00 26.36 ? 98 THR A OG1 1 ATOM 608 C CG2 . THR A 1 83 ? -32.510 165.110 16.191 1.00 28.78 ? 98 THR A CG2 1 ATOM 609 N N . LYS A 1 84 ? -32.373 164.355 20.852 1.00 26.31 ? 99 LYS A N 1 ATOM 610 C CA . LYS A 1 84 ? -32.804 163.634 22.069 1.00 22.36 ? 99 LYS A CA 1 ATOM 611 C C . LYS A 1 84 ? -33.490 162.311 21.781 1.00 23.65 ? 99 LYS A C 1 ATOM 612 O O . LYS A 1 84 ? -34.119 161.728 22.667 1.00 24.92 ? 99 LYS A O 1 ATOM 613 C CB . LYS A 1 84 ? -33.685 164.495 22.974 1.00 28.10 ? 99 LYS A CB 1 ATOM 614 C CG . LYS A 1 84 ? -33.025 165.767 23.427 1.00 30.67 ? 99 LYS A CG 1 ATOM 615 C CD . LYS A 1 84 ? -33.840 166.442 24.505 1.00 37.90 ? 99 LYS A CD 1 ATOM 616 C CE . LYS A 1 84 ? -32.922 167.010 25.568 1.00 49.10 ? 99 LYS A CE 1 ATOM 617 N NZ . LYS A 1 84 ? -33.698 167.719 26.624 1.00 54.79 ? 99 LYS A NZ 1 ATOM 618 N N . LYS A 1 85 ? -33.367 161.837 20.546 1.00 19.53 ? 100 LYS A N 1 ATOM 619 C CA . LYS A 1 85 ? -34.001 160.578 20.158 1.00 20.25 ? 100 LYS A CA 1 ATOM 620 C C . LYS A 1 85 ? -33.280 159.372 20.715 1.00 21.33 ? 100 LYS A C 1 ATOM 621 O O . LYS A 1 85 ? -32.034 159.358 20.862 1.00 20.52 ? 100 LYS A O 1 ATOM 622 C CB . LYS A 1 85 ? -34.112 160.452 18.639 1.00 21.41 ? 100 LYS A CB 1 ATOM 623 C CG . LYS A 1 85 ? -35.090 161.421 17.994 1.00 26.69 ? 100 LYS A CG 1 ATOM 624 C CD . LYS A 1 85 ? -35.029 161.276 16.467 1.00 25.78 ? 100 LYS A CD 1 ATOM 625 C CE . LYS A 1 85 ? -35.894 162.301 15.740 1.00 29.22 ? 100 LYS A CE 1 ATOM 626 N NZ . LYS A 1 85 ? -37.313 161.883 15.617 1.00 31.20 ? 100 LYS A NZ 1 ATOM 627 N N . HIS A 1 86 ? -34.078 158.358 21.020 1.00 20.00 ? 101 HIS A N 1 ATOM 628 C CA . HIS A 1 86 ? -33.564 157.050 21.452 1.00 18.17 ? 101 HIS A CA 1 ATOM 629 C C . HIS A 1 86 ? -33.913 155.951 20.437 1.00 25.56 ? 101 HIS A C 1 ATOM 630 O O . HIS A 1 86 ? -34.983 155.960 19.826 1.00 21.40 ? 101 HIS A O 1 ATOM 631 C CB . HIS A 1 86 ? -34.112 156.671 22.833 1.00 28.13 ? 101 HIS A CB 1 ATOM 632 C CG . HIS A 1 86 ? -33.664 157.575 23.943 1.00 24.70 ? 101 HIS A CG 1 ATOM 633 N ND1 . HIS A 1 86 ? -32.666 157.228 24.829 1.00 29.13 ? 101 HIS A ND1 1 ATOM 634 C CD2 . HIS A 1 86 ? -34.106 158.793 24.338 1.00 32.07 ? 101 HIS A CD2 1 ATOM 635 C CE1 . HIS A 1 86 ? -32.507 158.195 25.717 1.00 26.35 ? 101 HIS A CE1 1 ATOM 636 N NE2 . HIS A 1 86 ? -33.368 159.159 25.441 1.00 31.79 ? 101 HIS A NE2 1 ATOM 637 N N . PHE A 1 87 ? -32.987 155.016 20.256 1.00 17.73 ? 102 PHE A N 1 ATOM 638 C CA . PHE A 1 87 ? -33.191 153.839 19.415 1.00 17.58 ? 102 PHE A CA 1 ATOM 639 C C . PHE A 1 87 ? -32.928 152.619 20.267 1.00 17.51 ? 102 PHE A C 1 ATOM 640 O O . PHE A 1 87 ? -31.979 152.602 21.067 1.00 18.35 ? 102 PHE A O 1 ATOM 641 C CB . PHE A 1 87 ? -32.193 153.853 18.249 1.00 20.89 ? 102 PHE A CB 1 ATOM 642 C CG . PHE A 1 87 ? -32.276 152.650 17.320 1.00 19.97 ? 102 PHE A CG 1 ATOM 643 C CD1 . PHE A 1 87 ? -33.052 152.683 16.166 1.00 19.34 ? 102 PHE A CD1 1 ATOM 644 C CD2 . PHE A 1 87 ? -31.522 151.519 17.567 1.00 17.19 ? 102 PHE A CD2 1 ATOM 645 C CE1 . PHE A 1 87 ? -33.080 151.596 15.306 1.00 21.15 ? 102 PHE A CE1 1 ATOM 646 C CE2 . PHE A 1 87 ? -31.572 150.435 16.728 1.00 19.89 ? 102 PHE A CE2 1 ATOM 647 C CZ . PHE A 1 87 ? -32.350 150.475 15.585 1.00 18.92 ? 102 PHE A CZ 1 ATOM 648 N N . SER A 1 88 ? -33.777 151.605 20.111 1.00 20.94 ? 103 SER A N 1 ATOM 649 C CA . SER A 1 88 ? -33.492 150.287 20.653 1.00 17.74 ? 103 SER A CA 1 ATOM 650 C C . SER A 1 88 ? -34.118 149.249 19.744 1.00 29.96 ? 103 SER A C 1 ATOM 651 O O . SER A 1 88 ? -34.852 149.617 18.822 1.00 22.36 ? 103 SER A O 1 ATOM 652 C CB . SER A 1 88 ? -34.009 150.153 22.069 1.00 23.54 ? 103 SER A CB 1 ATOM 653 O OG . SER A 1 88 ? -35.427 150.135 22.095 1.00 28.95 ? 103 SER A OG 1 ATOM 654 N N . ASP A 1 89 ? -33.844 147.964 19.989 1.00 29.57 ? 104 ASP A N 1 ATOM 655 C CA . ASP A 1 89 ? -34.310 146.923 19.070 1.00 37.22 ? 104 ASP A CA 1 ATOM 656 C C . ASP A 1 89 ? -35.821 146.964 18.882 1.00 34.42 ? 104 ASP A C 1 ATOM 657 O O . ASP A 1 89 ? -36.308 146.868 17.756 1.00 42.98 ? 104 ASP A O 1 ATOM 658 C CB . ASP A 1 89 ? -33.870 145.528 19.518 1.00 36.97 ? 104 ASP A CB 1 ATOM 659 C CG . ASP A 1 89 ? -34.239 145.233 20.957 1.00 42.34 ? 104 ASP A CG 1 ATOM 660 O OD1 . ASP A 1 89 ? -35.236 145.780 21.459 1.00 51.34 ? 104 ASP A OD1 1 ATOM 661 O OD2 . ASP A 1 89 ? -33.515 144.452 21.602 1.00 59.47 ? 104 ASP A OD2 1 ATOM 662 N N . SER A 1 90 ? -36.544 147.140 19.986 1.00 31.67 ? 105 SER A N 1 ATOM 663 C CA . SER A 1 90 ? -37.992 147.311 19.938 1.00 36.72 ? 105 SER A CA 1 ATOM 664 C C . SER A 1 90 ? -38.377 148.682 19.374 1.00 40.13 ? 105 SER A C 1 ATOM 665 O O . SER A 1 90 ? -39.258 148.789 18.506 1.00 47.10 ? 105 SER A O 1 ATOM 666 C CB . SER A 1 90 ? -38.608 147.110 21.332 1.00 38.21 ? 105 SER A CB 1 ATOM 667 O OG . SER A 1 90 ? -38.080 148.024 22.280 1.00 45.49 ? 105 SER A OG 1 ATOM 668 N N . ASN A 1 91 ? -37.703 149.725 19.858 1.00 27.28 ? 106 ASN A N 1 ATOM 669 C CA . ASN A 1 91 ? -38.028 151.097 19.478 1.00 26.32 ? 106 ASN A CA 1 ATOM 670 C C . ASN A 1 91 ? -37.210 151.508 18.264 1.00 23.18 ? 106 ASN A C 1 ATOM 671 O O . ASN A 1 91 ? -36.349 152.401 18.340 1.00 21.27 ? 106 ASN A O 1 ATOM 672 C CB . ASN A 1 91 ? -37.736 152.018 20.656 1.00 25.99 ? 106 ASN A CB 1 ATOM 673 C CG . ASN A 1 91 ? -38.129 153.452 20.395 1.00 32.86 ? 106 ASN A CG 1 ATOM 674 O OD1 . ASN A 1 91 ? -39.013 153.731 19.583 1.00 36.95 ? 106 ASN A OD1 1 ATOM 675 N ND2 . ASN A 1 91 ? -37.471 154.381 21.091 1.00 35.30 ? 106 ASN A ND2 1 ATOM 676 N N . ASP A 1 92 ? -37.454 150.846 17.133 1.00 21.78 ? 107 ASP A N 1 ATOM 677 C CA . ASP A 1 92 ? -36.530 150.962 16.014 1.00 25.79 ? 107 ASP A CA 1 ATOM 678 C C . ASP A 1 92 ? -37.200 151.463 14.738 1.00 26.03 ? 107 ASP A C 1 ATOM 679 O O . ASP A 1 92 ? -36.664 151.279 13.640 1.00 28.16 ? 107 ASP A O 1 ATOM 680 C CB . ASP A 1 92 ? -35.866 149.602 15.757 1.00 25.57 ? 107 ASP A CB 1 ATOM 681 C CG . ASP A 1 92 ? -36.750 148.646 14.949 1.00 26.37 ? 107 ASP A CG 1 ATOM 682 O OD1 . ASP A 1 92 ? -37.995 148.660 15.103 1.00 27.51 ? 107 ASP A OD1 1 ATOM 683 O OD2 . ASP A 1 92 ? -36.196 147.900 14.114 1.00 32.48 ? 107 ASP A OD2 1 ATOM 684 N N . LYS A 1 93 ? -38.363 152.102 14.870 1.00 24.63 ? 108 LYS A N 1 ATOM 685 C CA . LYS A 1 93 ? -39.134 152.446 13.675 1.00 24.57 ? 108 LYS A CA 1 ATOM 686 C C . LYS A 1 93 ? -39.127 153.901 13.193 1.00 26.86 ? 108 LYS A C 1 ATOM 687 O O . LYS A 1 93 ? -39.777 154.224 12.201 1.00 30.09 ? 108 LYS A O 1 ATOM 688 C CB . LYS A 1 93 ? -40.555 151.897 13.794 1.00 29.43 ? 108 LYS A CB 1 ATOM 689 C CG . LYS A 1 93 ? -40.526 150.444 14.164 1.00 33.57 ? 108 LYS A CG 1 ATOM 690 C CD . LYS A 1 93 ? -41.788 149.751 13.823 1.00 43.38 ? 108 LYS A CD 1 ATOM 691 C CE . LYS A 1 93 ? -42.095 149.883 12.355 1.00 38.71 ? 108 LYS A CE 1 ATOM 692 N NZ . LYS A 1 93 ? -43.477 149.392 12.149 1.00 47.16 ? 108 LYS A NZ 1 ATOM 693 N N . ASP A 1 94 ? -38.378 154.765 13.865 1.00 18.50 ? 109 ASP A N 1 ATOM 694 C CA . ASP A 1 94 ? -38.196 156.137 13.393 1.00 23.37 ? 109 ASP A CA 1 ATOM 695 C C . ASP A 1 94 ? -37.167 156.119 12.261 1.00 22.62 ? 109 ASP A C 1 ATOM 696 O O . ASP A 1 94 ? -36.003 155.756 12.484 1.00 23.78 ? 109 ASP A O 1 ATOM 697 C CB . ASP A 1 94 ? -37.704 157.011 14.549 1.00 23.43 ? 109 ASP A CB 1 ATOM 698 C CG . ASP A 1 94 ? -37.681 158.493 14.211 1.00 29.26 ? 109 ASP A CG 1 ATOM 699 O OD1 . ASP A 1 94 ? -37.699 158.848 13.009 1.00 26.39 ? 109 ASP A OD1 1 ATOM 700 O OD2 . ASP A 1 94 ? -37.640 159.314 15.155 1.00 29.99 ? 109 ASP A OD2 1 ATOM 701 N N . PRO A 1 95 ? -37.580 156.523 11.051 1.00 21.69 ? 110 PRO A N 1 ATOM 702 C CA . PRO A 1 95 ? -36.696 156.546 9.879 1.00 23.85 ? 110 PRO A CA 1 ATOM 703 C C . PRO A 1 95 ? -35.404 157.343 10.100 1.00 24.53 ? 110 PRO A C 1 ATOM 704 O O . PRO A 1 95 ? -34.400 157.091 9.427 1.00 21.15 ? 110 PRO A O 1 ATOM 705 C CB . PRO A 1 95 ? -37.546 157.237 8.823 1.00 22.89 ? 110 PRO A CB 1 ATOM 706 C CG . PRO A 1 95 ? -38.932 156.913 9.202 1.00 27.24 ? 110 PRO A CG 1 ATOM 707 C CD . PRO A 1 95 ? -38.960 156.895 10.698 1.00 22.39 ? 110 PRO A CD 1 ATOM 708 N N . PHE A 1 96 ? -35.440 158.304 11.020 1.00 20.80 ? 111 PHE A N 1 ATOM 709 C CA . PHE A 1 96 ? -34.257 159.069 11.397 1.00 22.19 ? 111 PHE A CA 1 ATOM 710 C C . PHE A 1 96 ? -33.044 158.162 11.545 1.00 18.66 ? 111 PHE A C 1 ATOM 711 O O . PHE A 1 96 ? -31.935 158.485 11.094 1.00 19.43 ? 111 PHE A O 1 ATOM 712 C CB . PHE A 1 96 ? -34.532 159.819 12.711 1.00 25.86 ? 111 PHE A CB 1 ATOM 713 C CG . PHE A 1 96 ? -33.307 160.405 13.353 1.00 26.42 ? 111 PHE A CG 1 ATOM 714 C CD1 . PHE A 1 96 ? -32.690 159.765 14.421 1.00 26.30 ? 111 PHE A CD1 1 ATOM 715 C CD2 . PHE A 1 96 ? -32.785 161.612 12.910 1.00 25.59 ? 111 PHE A CD2 1 ATOM 716 C CE1 . PHE A 1 96 ? -31.564 160.315 15.020 1.00 23.24 ? 111 PHE A CE1 1 ATOM 717 C CE2 . PHE A 1 96 ? -31.663 162.157 13.504 1.00 26.57 ? 111 PHE A CE2 1 ATOM 718 C CZ . PHE A 1 96 ? -31.055 161.512 14.560 1.00 24.15 ? 111 PHE A CZ 1 ATOM 719 N N . TRP A 1 97 ? -33.265 157.007 12.165 1.00 19.27 ? 112 TRP A N 1 ATOM 720 C CA . TRP A 1 97 ? -32.153 156.119 12.492 1.00 20.39 ? 112 TRP A CA 1 ATOM 721 C C . TRP A 1 97 ? -31.622 155.326 11.322 1.00 19.46 ? 112 TRP A C 1 ATOM 722 O O . TRP A 1 97 ? -30.481 154.874 11.366 1.00 21.20 ? 112 TRP A O 1 ATOM 723 C CB . TRP A 1 97 ? -32.524 155.170 13.636 1.00 18.29 ? 112 TRP A CB 1 ATOM 724 C CG . TRP A 1 97 ? -32.803 155.892 14.927 1.00 17.50 ? 112 TRP A CG 1 ATOM 725 C CD1 . TRP A 1 97 ? -34.033 156.144 15.477 1.00 24.61 ? 112 TRP A CD1 1 ATOM 726 C CD2 . TRP A 1 97 ? -31.840 156.472 15.816 1.00 16.27 ? 112 TRP A CD2 1 ATOM 727 N NE1 . TRP A 1 97 ? -33.893 156.829 16.658 1.00 21.58 ? 112 TRP A NE1 1 ATOM 728 C CE2 . TRP A 1 97 ? -32.560 157.043 16.893 1.00 23.65 ? 112 TRP A CE2 1 ATOM 729 C CE3 . TRP A 1 97 ? -30.441 156.558 15.813 1.00 20.00 ? 112 TRP A CE3 1 ATOM 730 C CZ2 . TRP A 1 97 ? -31.933 157.686 17.958 1.00 18.14 ? 112 TRP A CZ2 1 ATOM 731 C CZ3 . TRP A 1 97 ? -29.808 157.193 16.886 1.00 22.92 ? 112 TRP A CZ3 1 ATOM 732 C CH2 . TRP A 1 97 ? -30.561 157.749 17.944 1.00 21.44 ? 112 TRP A CH2 1 ATOM 733 N N . TRP A 1 98 ? -32.418 155.205 10.263 1.00 19.16 ? 113 TRP A N 1 ATOM 734 C CA . TRP A 1 98 ? -32.083 154.382 9.096 1.00 16.99 ? 113 TRP A CA 1 ATOM 735 C C . TRP A 1 98 ? -31.614 155.214 7.894 1.00 20.88 ? 113 TRP A C 1 ATOM 736 O O . TRP A 1 98 ? -30.998 154.693 6.960 1.00 22.70 ? 113 TRP A O 1 ATOM 737 C CB . TRP A 1 98 ? -33.306 153.518 8.707 1.00 18.42 ? 113 TRP A CB 1 ATOM 738 C CG . TRP A 1 98 ? -33.734 152.618 9.814 1.00 16.93 ? 113 TRP A CG 1 ATOM 739 C CD1 . TRP A 1 98 ? -34.603 152.915 10.829 1.00 21.19 ? 113 TRP A CD1 1 ATOM 740 C CD2 . TRP A 1 98 ? -33.310 151.270 10.029 1.00 18.78 ? 113 TRP A CD2 1 ATOM 741 N NE1 . TRP A 1 98 ? -34.732 151.835 11.672 1.00 18.42 ? 113 TRP A NE1 1 ATOM 742 C CE2 . TRP A 1 98 ? -33.951 150.812 11.202 1.00 19.79 ? 113 TRP A CE2 1 ATOM 743 C CE3 . TRP A 1 98 ? -32.459 150.396 9.335 1.00 14.28 ? 113 TRP A CE3 1 ATOM 744 C CZ2 . TRP A 1 98 ? -33.761 149.516 11.704 1.00 14.83 ? 113 TRP A CZ2 1 ATOM 745 C CZ3 . TRP A 1 98 ? -32.268 149.108 9.839 1.00 13.45 ? 113 TRP A CZ3 1 ATOM 746 C CH2 . TRP A 1 98 ? -32.909 148.691 11.021 1.00 17.19 ? 113 TRP A CH2 1 ATOM 747 N N . ASN A 1 99 ? -31.885 156.515 7.933 1.00 20.04 ? 114 ASN A N 1 ATOM 748 C CA . ASN A 1 99 ? -31.777 157.339 6.741 1.00 18.81 ? 114 ASN A CA 1 ATOM 749 C C . ASN A 1 99 ? -30.386 157.853 6.389 1.00 20.61 ? 114 ASN A C 1 ATOM 750 O O . ASN A 1 99 ? -30.234 158.613 5.419 1.00 29.76 ? 114 ASN A O 1 ATOM 751 C CB . ASN A 1 99 ? -32.753 158.526 6.826 1.00 20.86 ? 114 ASN A CB 1 ATOM 752 C CG . ASN A 1 99 ? -34.161 158.164 6.392 1.00 19.12 ? 114 ASN A CG 1 ATOM 753 O OD1 . ASN A 1 99 ? -34.379 157.174 5.674 1.00 25.24 ? 114 ASN A OD1 1 ATOM 754 N ND2 . ASN A 1 99 ? -35.131 158.979 6.802 1.00 31.06 ? 114 ASN A ND2 1 ATOM 755 N N . GLU A 1 100 ? -29.372 157.463 7.146 1.00 20.13 ? 115 GLU A N 1 ATOM 756 C CA . GLU A 1 100 ? -28.006 157.857 6.765 1.00 17.62 ? 115 GLU A CA 1 ATOM 757 C C . GLU A 1 100 ? -27.457 156.998 5.633 1.00 19.27 ? 115 GLU A C 1 ATOM 758 O O . GLU A 1 100 ? -26.377 157.285 5.102 1.00 25.22 ? 115 GLU A O 1 ATOM 759 C CB . GLU A 1 100 ? -27.056 157.893 7.978 1.00 18.59 ? 115 GLU A CB 1 ATOM 760 C CG . GLU A 1 100 ? -27.445 158.996 8.937 1.00 21.65 ? 115 GLU A CG 1 ATOM 761 C CD . GLU A 1 100 ? -26.527 159.165 10.124 1.00 26.30 ? 115 GLU A CD 1 ATOM 762 O OE1 . GLU A 1 100 ? -26.759 160.120 10.895 1.00 27.29 ? 115 GLU A OE1 1 ATOM 763 O OE2 . GLU A 1 100 ? -25.574 158.374 10.290 1.00 23.52 ? 115 GLU A OE2 1 ATOM 764 N N . ALA A 1 101 ? -28.196 155.953 5.269 1.00 17.93 ? 116 ALA A N 1 ATOM 765 C CA . ALA A 1 101 ? -27.810 155.079 4.157 1.00 18.04 ? 116 ALA A CA 1 ATOM 766 C C . ALA A 1 101 ? -29.039 154.645 3.390 1.00 19.06 ? 116 ALA A C 1 ATOM 767 O O . ALA A 1 101 ? -30.164 154.923 3.804 1.00 22.25 ? 116 ALA A O 1 ATOM 768 C CB . ALA A 1 101 ? -27.043 153.846 4.659 1.00 19.03 ? 116 ALA A CB 1 ATOM 769 N N . VAL A 1 102 ? -28.820 153.954 2.269 1.00 18.23 ? 117 VAL A N 1 ATOM 770 C CA . VAL A 1 102 ? -29.907 153.429 1.447 1.00 15.55 ? 117 VAL A CA 1 ATOM 771 C C . VAL A 1 102 ? -29.692 151.936 1.255 1.00 17.53 ? 117 VAL A C 1 ATOM 772 O O . VAL A 1 102 ? -28.720 151.516 0.590 1.00 19.90 ? 117 VAL A O 1 ATOM 773 C CB . VAL A 1 102 ? -29.907 154.074 0.075 1.00 18.93 ? 117 VAL A CB 1 ATOM 774 C CG1 . VAL A 1 102 ? -31.054 153.452 -0.758 1.00 23.05 ? 117 VAL A CG1 1 ATOM 775 C CG2 . VAL A 1 102 ? -30.081 155.571 0.211 1.00 25.48 ? 117 VAL A CG2 1 ATOM 776 N N . PRO A 1 103 ? -30.530 151.114 1.887 1.00 18.03 ? 118 PRO A N 1 ATOM 777 C CA . PRO A 1 103 ? -30.302 149.667 1.806 1.00 18.41 ? 118 PRO A CA 1 ATOM 778 C C . PRO A 1 103 ? -30.742 149.100 0.456 1.00 16.98 ? 118 PRO A C 1 ATOM 779 O O . PRO A 1 103 ? -31.530 149.738 -0.264 1.00 20.32 ? 118 PRO A O 1 ATOM 780 C CB . PRO A 1 103 ? -31.166 149.119 2.952 1.00 19.80 ? 118 PRO A CB 1 ATOM 781 C CG . PRO A 1 103 ? -32.316 150.087 3.017 1.00 22.21 ? 118 PRO A CG 1 ATOM 782 C CD . PRO A 1 103 ? -31.697 151.448 2.728 1.00 19.37 ? 118 PRO A CD 1 ATOM 783 N N . ILE A 1 104 ? -30.236 147.916 0.120 1.00 21.55 ? 119 ILE A N 1 ATOM 784 C CA . ILE A 1 104 ? -30.419 147.363 -1.229 1.00 22.62 ? 119 ILE A CA 1 ATOM 785 C C . ILE A 1 104 ? -31.876 147.104 -1.566 1.00 17.55 ? 119 ILE A C 1 ATOM 786 O O . ILE A 1 104 ? -32.271 147.212 -2.727 1.00 21.83 ? 119 ILE A O 1 ATOM 787 C CB . ILE A 1 104 ? -29.575 146.079 -1.451 1.00 17.93 ? 119 ILE A CB 1 ATOM 788 C CG1 . ILE A 1 104 ? -29.476 145.722 -2.935 1.00 19.62 ? 119 ILE A CG1 1 ATOM 789 C CG2 . ILE A 1 104 ? -30.089 144.922 -0.637 1.00 17.60 ? 119 ILE A CG2 1 ATOM 790 C CD1 . ILE A 1 104 ? -28.552 144.524 -3.190 1.00 20.82 ? 119 ILE A CD1 1 ATOM 791 N N . TRP A 1 105 ? -32.699 146.778 -0.574 1.00 16.91 ? 120 TRP A N 1 ATOM 792 C CA . TRP A 1 105 ? -34.116 146.557 -0.890 1.00 18.22 ? 120 TRP A CA 1 ATOM 793 C C . TRP A 1 105 ? -34.792 147.812 -1.432 1.00 25.02 ? 120 TRP A C 1 ATOM 794 O O . TRP A 1 105 ? -35.743 147.734 -2.200 1.00 23.01 ? 120 TRP A O 1 ATOM 795 C CB . TRP A 1 105 ? -34.896 145.966 0.293 1.00 19.38 ? 120 TRP A CB 1 ATOM 796 C CG . TRP A 1 105 ? -34.971 146.802 1.544 1.00 18.52 ? 120 TRP A CG 1 ATOM 797 C CD1 . TRP A 1 105 ? -35.761 147.894 1.762 1.00 23.18 ? 120 TRP A CD1 1 ATOM 798 C CD2 . TRP A 1 105 ? -34.241 146.588 2.765 1.00 21.55 ? 120 TRP A CD2 1 ATOM 799 N NE1 . TRP A 1 105 ? -35.577 148.373 3.043 1.00 22.51 ? 120 TRP A NE1 1 ATOM 800 C CE2 . TRP A 1 105 ? -34.648 147.591 3.676 1.00 14.87 ? 120 TRP A CE2 1 ATOM 801 C CE3 . TRP A 1 105 ? -33.305 145.636 3.179 1.00 17.45 ? 120 TRP A CE3 1 ATOM 802 C CZ2 . TRP A 1 105 ? -34.146 147.679 4.968 1.00 20.69 ? 120 TRP A CZ2 1 ATOM 803 C CZ3 . TRP A 1 105 ? -32.796 145.720 4.473 1.00 18.13 ? 120 TRP A CZ3 1 ATOM 804 C CH2 . TRP A 1 105 ? -33.215 146.746 5.347 1.00 16.54 ? 120 TRP A CH2 1 ATOM 805 N N . VAL A 1 106 ? -34.286 148.974 -1.043 1.00 19.86 ? 121 VAL A N 1 ATOM 806 C CA . VAL A 1 106 ? -34.846 150.231 -1.503 1.00 26.38 ? 121 VAL A CA 1 ATOM 807 C C . VAL A 1 106 ? -34.430 150.451 -2.959 1.00 20.77 ? 121 VAL A C 1 ATOM 808 O O . VAL A 1 106 ? -35.280 150.619 -3.835 1.00 25.65 ? 121 VAL A O 1 ATOM 809 C CB . VAL A 1 106 ? -34.381 151.391 -0.601 1.00 18.92 ? 121 VAL A CB 1 ATOM 810 C CG1 . VAL A 1 106 ? -34.597 152.731 -1.288 1.00 26.14 ? 121 VAL A CG1 1 ATOM 811 C CG2 . VAL A 1 106 ? -35.096 151.339 0.751 1.00 27.51 ? 121 VAL A CG2 1 ATOM 812 N N . THR A 1 107 ? -33.130 150.419 -3.234 1.00 25.05 ? 122 THR A N 1 ATOM 813 C CA . THR A 1 107 ? -32.646 150.547 -4.608 1.00 24.47 ? 122 THR A CA 1 ATOM 814 C C . THR A 1 107 ? -33.358 149.568 -5.544 1.00 22.60 ? 122 THR A C 1 ATOM 815 O O . THR A 1 107 ? -33.731 149.917 -6.668 1.00 23.82 ? 122 THR A O 1 ATOM 816 C CB . THR A 1 107 ? -31.136 150.299 -4.641 1.00 22.57 ? 122 THR A CB 1 ATOM 817 O OG1 . THR A 1 107 ? -30.503 151.203 -3.730 1.00 24.58 ? 122 THR A OG1 1 ATOM 818 C CG2 . THR A 1 107 ? -30.572 150.519 -6.010 1.00 24.78 ? 122 THR A CG2 1 ATOM 819 N N . ASN A 1 108 ? -33.568 148.344 -5.075 1.00 24.22 ? 123 ASN A N 1 ATOM 820 C CA . ASN A 1 108 ? -34.297 147.362 -5.884 1.00 22.14 ? 123 ASN A CA 1 ATOM 821 C C . ASN A 1 108 ? -35.760 147.770 -6.082 1.00 20.82 ? 123 ASN A C 1 ATOM 822 O O . ASN A 1 108 ? -36.282 147.716 -7.207 1.00 26.38 ? 123 ASN A O 1 ATOM 823 C CB . ASN A 1 108 ? -34.182 145.949 -5.283 1.00 25.09 ? 123 ASN A CB 1 ATOM 824 C CG . ASN A 1 108 ? -34.818 144.890 -6.162 1.00 26.37 ? 123 ASN A CG 1 ATOM 825 O OD1 . ASN A 1 108 ? -34.211 144.436 -7.141 1.00 30.53 ? 123 ASN A OD1 1 ATOM 826 N ND2 . ASN A 1 108 ? -36.054 144.490 -5.821 1.00 25.53 ? 123 ASN A ND2 1 ATOM 827 N N . GLN A 1 109 ? -36.424 148.216 -5.016 1.00 25.18 ? 124 GLN A N 1 ATOM 828 C CA . GLN A 1 109 ? -37.838 148.623 -5.075 1.00 20.86 ? 124 GLN A CA 1 ATOM 829 C C . GLN A 1 109 ? -38.082 149.795 -6.043 1.00 25.93 ? 124 GLN A C 1 ATOM 830 O O . GLN A 1 109 ? -39.172 149.936 -6.632 1.00 31.83 ? 124 GLN A O 1 ATOM 831 C CB . GLN A 1 109 ? -38.313 148.985 -3.652 1.00 28.27 ? 124 GLN A CB 1 ATOM 832 C CG . GLN A 1 109 ? -39.799 149.309 -3.518 1.00 28.96 ? 124 GLN A CG 1 ATOM 833 C CD . GLN A 1 109 ? -40.689 148.128 -3.804 1.00 30.00 ? 124 GLN A CD 1 ATOM 834 O OE1 . GLN A 1 109 ? -40.465 147.011 -3.300 1.00 29.78 ? 124 GLN A OE1 1 ATOM 835 N NE2 . GLN A 1 109 ? -41.730 148.364 -4.608 1.00 34.63 ? 124 GLN A NE2 1 ATOM 836 N N . LEU A 1 110 ? -37.057 150.613 -6.236 1.00 29.06 ? 125 LEU A N 1 ATOM 837 C CA . LEU A 1 110 ? -37.163 151.848 -7.024 1.00 33.21 ? 125 LEU A CA 1 ATOM 838 C C . LEU A 1 110 ? -37.016 151.622 -8.534 1.00 26.32 ? 125 LEU A C 1 ATOM 839 O O . LEU A 1 110 ? -37.230 152.536 -9.321 1.00 38.92 ? 125 LEU A O 1 ATOM 840 C CB . LEU A 1 110 ? -36.131 152.883 -6.549 1.00 29.71 ? 125 LEU A CB 1 ATOM 841 C CG . LEU A 1 110 ? -36.410 153.789 -5.340 1.00 40.55 ? 125 LEU A CG 1 ATOM 842 C CD1 . LEU A 1 110 ? -37.489 154.832 -5.636 1.00 45.35 ? 125 LEU A CD1 1 ATOM 843 C CD2 . LEU A 1 110 ? -36.836 152.998 -4.174 1.00 52.72 ? 125 LEU A CD2 1 ATOM 844 N N . GLN A 1 111 ? -36.639 150.409 -8.936 1.00 28.99 ? 126 GLN A N 1 ATOM 845 C CA . GLN A 1 111 ? -36.568 150.092 -10.362 1.00 30.68 ? 126 GLN A CA 1 ATOM 846 C C . GLN A 1 111 ? -37.949 149.791 -10.914 1.00 34.90 ? 126 GLN A C 1 ATOM 847 O O . GLN A 1 111 ? -38.786 149.209 -10.226 1.00 33.84 ? 126 GLN A O 1 ATOM 848 C CB . GLN A 1 111 ? -35.680 148.878 -10.616 1.00 32.84 ? 126 GLN A CB 1 ATOM 849 C CG . GLN A 1 111 ? -34.317 148.944 -9.975 1.00 33.29 ? 126 GLN A CG 1 ATOM 850 C CD . GLN A 1 111 ? -33.508 150.121 -10.441 1.00 46.11 ? 126 GLN A CD 1 ATOM 851 O OE1 . GLN A 1 111 ? -33.169 150.227 -11.622 1.00 48.93 ? 126 GLN A OE1 1 ATOM 852 N NE2 . GLN A 1 111 ? -33.181 151.024 -9.508 1.00 39.61 ? 126 GLN A NE2 1 ATOM 853 N N . GLU A 1 112 ? -38.177 150.164 -12.168 1.00 36.32 ? 127 GLU A N 1 ATOM 854 C CA . GLU A 1 112 ? -39.462 149.895 -12.799 1.00 36.12 ? 127 GLU A CA 1 ATOM 855 C C . GLU A 1 112 ? -39.704 148.393 -12.940 1.00 39.10 ? 127 GLU A C 1 ATOM 856 O O . GLU A 1 112 ? -38.782 147.616 -13.219 1.00 41.21 ? 127 GLU A O 1 ATOM 857 C CB . GLU A 1 112 ? -39.564 150.611 -14.149 1.00 47.88 ? 127 GLU A CB 1 ATOM 858 C CG . GLU A 1 112 ? -39.476 152.132 -14.021 1.00 60.62 ? 127 GLU A CG 1 ATOM 859 C CD . GLU A 1 112 ? -39.975 152.874 -15.252 1.00 68.20 ? 127 GLU A CD 1 ATOM 860 O OE1 . GLU A 1 112 ? -39.924 152.301 -16.364 1.00 68.84 ? 127 GLU A OE1 1 ATOM 861 O OE2 . GLU A 1 112 ? -40.422 154.035 -15.102 1.00 72.21 ? 127 GLU A OE2 1 ATOM 862 N N . ASN A 1 113 ? -40.949 147.994 -12.717 1.00 39.35 ? 128 ASN A N 1 ATOM 863 C CA . ASN A 1 113 ? -41.353 146.603 -12.856 1.00 40.74 ? 128 ASN A CA 1 ATOM 864 C C . ASN A 1 113 ? -40.568 145.624 -11.989 1.00 32.75 ? 128 ASN A C 1 ATOM 865 O O . ASN A 1 113 ? -40.374 144.473 -12.386 1.00 33.92 ? 128 ASN A O 1 ATOM 866 C CB . ASN A 1 113 ? -41.294 146.153 -14.319 1.00 45.56 ? 128 ASN A CB 1 ATOM 867 C CG . ASN A 1 113 ? -42.220 146.950 -15.217 1.00 58.72 ? 128 ASN A CG 1 ATOM 868 O OD1 . ASN A 1 113 ? -43.166 147.595 -14.752 1.00 62.64 ? 128 ASN A OD1 1 ATOM 869 N ND2 . ASN A 1 113 ? -41.951 146.908 -16.519 1.00 62.63 ? 128 ASN A ND2 1 ATOM 870 N N . ARG A 1 114 ? -40.134 146.073 -10.814 1.00 38.15 ? 129 ARG A N 1 ATOM 871 C CA . ARG A 1 114 ? -39.478 145.197 -9.846 1.00 33.15 ? 129 ARG A CA 1 ATOM 872 C C . ARG A 1 114 ? -40.001 145.464 -8.442 1.00 26.12 ? 129 ARG A C 1 ATOM 873 O O . ARG A 1 114 ? -40.330 146.600 -8.117 1.00 35.12 ? 129 ARG A O 1 ATOM 874 C CB . ARG A 1 114 ? -37.967 145.438 -9.848 1.00 32.95 ? 129 ARG A CB 1 ATOM 875 C CG . ARG A 1 114 ? -37.263 145.045 -11.133 1.00 44.23 ? 129 ARG A CG 1 ATOM 876 C CD . ARG A 1 114 ? -35.868 145.612 -11.104 1.00 56.07 ? 129 ARG A CD 1 ATOM 877 N NE . ARG A 1 114 ? -34.884 144.845 -11.861 1.00 63.30 ? 129 ARG A NE 1 ATOM 878 C CZ . ARG A 1 114 ? -33.749 145.361 -12.332 1.00 63.41 ? 129 ARG A CZ 1 ATOM 879 N NH1 . ARG A 1 114 ? -32.895 144.595 -13.001 1.00 66.73 ? 129 ARG A NH1 1 ATOM 880 N NH2 . ARG A 1 114 ? -33.469 146.646 -12.132 1.00 59.82 ? 129 ARG A NH2 1 ATOM 881 N N . SER A 1 115 ? -40.049 144.432 -7.597 1.00 26.57 ? 130 SER A N 1 ATOM 882 C CA . SER A 1 115 ? -40.406 144.633 -6.197 1.00 28.59 ? 130 SER A CA 1 ATOM 883 C C . SER A 1 115 ? -39.400 143.990 -5.271 1.00 28.25 ? 130 SER A C 1 ATOM 884 O O . SER A 1 115 ? -38.681 143.054 -5.644 1.00 27.49 ? 130 SER A O 1 ATOM 885 C CB . SER A 1 115 ? -41.780 144.053 -5.862 1.00 23.14 ? 130 SER A CB 1 ATOM 886 O OG . SER A 1 115 ? -42.814 144.773 -6.513 1.00 37.77 ? 130 SER A OG 1 ATOM 887 N N . SER A 1 116 ? -39.392 144.485 -4.043 1.00 23.07 ? 131 SER A N 1 ATOM 888 C CA . SER A 1 116 ? -38.662 143.845 -2.947 1.00 22.87 ? 131 SER A CA 1 ATOM 889 C C . SER A 1 116 ? -39.663 143.188 -1.992 1.00 25.71 ? 131 SER A C 1 ATOM 890 O O . SER A 1 116 ? -40.814 143.626 -1.907 1.00 27.24 ? 131 SER A O 1 ATOM 891 C CB . SER A 1 116 ? -37.811 144.867 -2.187 1.00 21.41 ? 131 SER A CB 1 ATOM 892 O OG . SER A 1 116 ? -36.783 145.389 -3.014 1.00 27.15 ? 131 SER A OG 1 ATOM 893 N N . ALA A 1 117 ? -39.238 142.140 -1.290 1.00 21.95 ? 132 ALA A N 1 ATOM 894 C CA . ALA A 1 117 ? -40.079 141.487 -0.292 1.00 20.72 ? 132 ALA A CA 1 ATOM 895 C C . ALA A 1 117 ? -39.245 141.239 0.969 1.00 21.35 ? 132 ALA A C 1 ATOM 896 O O . ALA A 1 117 ? -38.009 141.166 0.907 1.00 20.27 ? 132 ALA A O 1 ATOM 897 C CB . ALA A 1 117 ? -40.624 140.187 -0.826 1.00 25.29 ? 132 ALA A CB 1 ATOM 898 N N . ALA A 1 118 ? -39.905 141.109 2.110 1.00 22.16 ? 133 ALA A N 1 ATOM 899 C CA . ALA A 1 118 ? -39.157 140.928 3.352 1.00 19.12 ? 133 ALA A CA 1 ATOM 900 C C . ALA A 1 118 ? -39.916 140.119 4.383 1.00 17.33 ? 133 ALA A C 1 ATOM 901 O O . ALA A 1 118 ? -41.135 140.250 4.527 1.00 23.10 ? 133 ALA A O 1 ATOM 902 C CB . ALA A 1 118 ? -38.805 142.261 3.942 1.00 18.06 ? 133 ALA A CB 1 ATOM 903 N N . ALA A 1 119 ? -39.184 139.302 5.122 1.00 22.04 ? 134 ALA A N 1 ATOM 904 C CA . ALA A 1 119 ? -39.771 138.526 6.206 1.00 21.24 ? 134 ALA A CA 1 ATOM 905 C C . ALA A 1 119 ? -38.896 138.670 7.448 1.00 24.51 ? 134 ALA A C 1 ATOM 906 O O . ALA A 1 119 ? -38.078 137.803 7.747 1.00 21.78 ? 134 ALA A O 1 ATOM 907 C CB . ALA A 1 119 ? -39.907 137.063 5.811 1.00 22.74 ? 134 ALA A CB 1 ATOM 908 N N . MET A 1 120 ? -39.062 139.802 8.131 1.00 19.63 ? 135 MET A N 1 ATOM 909 C CA . MET A 1 120 ? -38.552 140.044 9.491 1.00 21.46 ? 135 MET A CA 1 ATOM 910 C C . MET A 1 120 ? -37.133 140.592 9.573 1.00 19.99 ? 135 MET A C 1 ATOM 911 O O . MET A 1 120 ? -36.596 140.737 10.664 1.00 21.85 ? 135 MET A O 1 ATOM 912 C CB . MET A 1 120 ? -38.686 138.805 10.404 1.00 22.92 ? 135 MET A CB 1 ATOM 913 C CG . MET A 1 120 ? -40.092 138.230 10.479 1.00 28.19 ? 135 MET A CG 1 ATOM 914 S SD . MET A 1 120 ? -41.220 139.435 11.169 1.00 31.99 ? 135 MET A SD 1 ATOM 915 C CE . MET A 1 120 ? -42.765 138.508 11.315 1.00 22.73 ? 135 MET A CE 1 ATOM 916 N N . TRP A 1 121 ? -36.532 140.903 8.436 1.00 19.43 ? 136 TRP A N 1 ATOM 917 C CA . TRP A 1 121 ? -35.165 141.437 8.453 1.00 17.06 ? 136 TRP A CA 1 ATOM 918 C C . TRP A 1 121 ? -35.166 142.835 9.074 1.00 12.45 ? 136 TRP A C 1 ATOM 919 O O . TRP A 1 121 ? -36.045 143.652 8.791 1.00 17.91 ? 136 TRP A O 1 ATOM 920 C CB . TRP A 1 121 ? -34.629 141.501 7.024 1.00 17.84 ? 136 TRP A CB 1 ATOM 921 C CG . TRP A 1 121 ? -33.182 141.912 6.884 1.00 18.48 ? 136 TRP A CG 1 ATOM 922 C CD1 . TRP A 1 121 ? -32.660 143.178 7.035 1.00 15.88 ? 136 TRP A CD1 1 ATOM 923 C CD2 . TRP A 1 121 ? -32.087 141.062 6.524 1.00 17.60 ? 136 TRP A CD2 1 ATOM 924 N NE1 . TRP A 1 121 ? -31.296 143.152 6.788 1.00 13.73 ? 136 TRP A NE1 1 ATOM 925 C CE2 . TRP A 1 121 ? -30.927 141.866 6.488 1.00 15.22 ? 136 TRP A CE2 1 ATOM 926 C CE3 . TRP A 1 121 ? -31.979 139.703 6.218 1.00 17.27 ? 136 TRP A CE3 1 ATOM 927 C CZ2 . TRP A 1 121 ? -29.662 141.348 6.157 1.00 10.72 ? 136 TRP A CZ2 1 ATOM 928 C CZ3 . TRP A 1 121 ? -30.747 139.180 5.914 1.00 14.97 ? 136 TRP A CZ3 1 ATOM 929 C CH2 . TRP A 1 121 ? -29.585 140.009 5.892 1.00 12.78 ? 136 TRP A CH2 1 ATOM 930 N N . PRO A 1 122 ? -34.173 143.123 9.934 1.00 15.36 ? 137 PRO A N 1 ATOM 931 C CA . PRO A 1 122 ? -34.112 144.434 10.601 1.00 13.91 ? 137 PRO A CA 1 ATOM 932 C C . PRO A 1 122 ? -34.220 145.634 9.644 1.00 17.80 ? 137 PRO A C 1 ATOM 933 O O . PRO A 1 122 ? -33.477 145.743 8.646 1.00 17.02 ? 137 PRO A O 1 ATOM 934 C CB . PRO A 1 122 ? -32.747 144.394 11.320 1.00 16.21 ? 137 PRO A CB 1 ATOM 935 C CG . PRO A 1 122 ? -32.535 142.964 11.573 1.00 18.73 ? 137 PRO A CG 1 ATOM 936 C CD . PRO A 1 122 ? -33.098 142.226 10.395 1.00 17.72 ? 137 PRO A CD 1 ATOM 937 N N . GLY A 1 123 ? -35.202 146.503 9.923 1.00 17.09 ? 138 GLY A N 1 ATOM 938 C CA . GLY A 1 123 ? -35.421 147.707 9.127 1.00 14.46 ? 138 GLY A CA 1 ATOM 939 C C . GLY A 1 123 ? -36.402 147.560 7.982 1.00 16.93 ? 138 GLY A C 1 ATOM 940 O O . GLY A 1 123 ? -36.767 148.553 7.351 1.00 21.00 ? 138 GLY A O 1 ATOM 941 N N . THR A 1 124 ? -36.808 146.336 7.671 1.00 21.51 ? 139 THR A N 1 ATOM 942 C CA . THR A 1 124 ? -37.607 146.149 6.463 1.00 14.99 ? 139 THR A CA 1 ATOM 943 C C . THR A 1 124 ? -39.052 146.539 6.687 1.00 20.43 ? 139 THR A C 1 ATOM 944 O O . THR A 1 124 ? -39.812 146.644 5.718 1.00 24.02 ? 139 THR A O 1 ATOM 945 C CB . THR A 1 124 ? -37.555 144.721 5.907 1.00 17.11 ? 139 THR A CB 1 ATOM 946 O OG1 . THR A 1 124 ? -37.967 143.792 6.918 1.00 20.71 ? 139 THR A OG1 1 ATOM 947 C CG2 . THR A 1 124 ? -36.164 144.380 5.371 1.00 18.30 ? 139 THR A CG2 1 ATOM 948 N N . ASP A 1 125 ? -39.427 146.747 7.948 1.00 22.03 ? 140 ASP A N 1 ATOM 949 C CA . ASP A 1 125 ? -40.756 147.273 8.272 1.00 22.80 ? 140 ASP A CA 1 ATOM 950 C C . ASP A 1 125 ? -40.751 148.796 8.495 1.00 21.19 ? 140 ASP A C 1 ATOM 951 O O . ASP A 1 125 ? -41.704 149.372 9.036 1.00 26.84 ? 140 ASP A O 1 ATOM 952 C CB . ASP A 1 125 ? -41.372 146.540 9.477 1.00 25.30 ? 140 ASP A CB 1 ATOM 953 C CG . ASP A 1 125 ? -40.492 146.596 10.729 1.00 26.79 ? 140 ASP A CG 1 ATOM 954 O OD1 . ASP A 1 125 ? -39.314 147.029 10.634 1.00 24.76 ? 140 ASP A OD1 1 ATOM 955 O OD2 . ASP A 1 125 ? -40.972 146.162 11.806 1.00 28.98 ? 140 ASP A OD2 1 ATOM 956 N N . VAL A 1 126 ? -39.680 149.454 8.061 1.00 22.72 ? 141 VAL A N 1 ATOM 957 C CA . VAL A 1 126 ? -39.536 150.901 8.240 1.00 17.59 ? 141 VAL A CA 1 ATOM 958 C C . VAL A 1 126 ? -39.382 151.566 6.866 1.00 21.34 ? 141 VAL A C 1 ATOM 959 O O . VAL A 1 126 ? -38.583 151.110 6.063 1.00 24.55 ? 141 VAL A O 1 ATOM 960 C CB . VAL A 1 126 ? -38.277 151.220 9.052 1.00 19.78 ? 141 VAL A CB 1 ATOM 961 C CG1 . VAL A 1 126 ? -38.137 152.730 9.254 1.00 24.97 ? 141 VAL A CG1 1 ATOM 962 C CG2 . VAL A 1 126 ? -38.349 150.515 10.406 1.00 21.48 ? 141 VAL A CG2 1 ATOM 963 N N . PRO A 1 127 ? -40.128 152.653 6.594 1.00 27.61 ? 142 PRO A N 1 ATOM 964 C CA . PRO A 1 127 ? -39.845 153.363 5.342 1.00 23.75 ? 142 PRO A CA 1 ATOM 965 C C . PRO A 1 127 ? -38.512 154.122 5.424 1.00 25.81 ? 142 PRO A C 1 ATOM 966 O O . PRO A 1 127 ? -38.275 154.900 6.339 1.00 26.46 ? 142 PRO A O 1 ATOM 967 C CB . PRO A 1 127 ? -41.026 154.330 5.199 1.00 26.77 ? 142 PRO A CB 1 ATOM 968 C CG . PRO A 1 127 ? -41.519 154.542 6.578 1.00 35.08 ? 142 PRO A CG 1 ATOM 969 C CD . PRO A 1 127 ? -41.212 153.285 7.369 1.00 29.91 ? 142 PRO A CD 1 ATOM 970 N N . ILE A 1 128 ? -37.635 153.867 4.467 1.00 25.33 ? 143 ILE A N 1 ATOM 971 C CA . ILE A 1 128 ? -36.305 154.457 4.472 1.00 26.96 ? 143 ILE A CA 1 ATOM 972 C C . ILE A 1 128 ? -36.171 155.257 3.200 1.00 26.54 ? 143 ILE A C 1 ATOM 973 O O . ILE A 1 128 ? -36.394 154.725 2.116 1.00 22.94 ? 143 ILE A O 1 ATOM 974 C CB . ILE A 1 128 ? -35.253 153.365 4.530 1.00 21.75 ? 143 ILE A CB 1 ATOM 975 C CG1 . ILE A 1 128 ? -35.453 152.532 5.802 1.00 22.96 ? 143 ILE A CG1 1 ATOM 976 C CG2 . ILE A 1 128 ? -33.841 153.973 4.476 1.00 23.52 ? 143 ILE A CG2 1 ATOM 977 C CD1 . ILE A 1 128 ? -34.503 151.345 5.942 1.00 20.26 ? 143 ILE A CD1 1 ATOM 978 N N . HIS A 1 129 ? -35.825 156.539 3.336 1.00 26.68 ? 144 HIS A N 1 ATOM 979 C CA . HIS A 1 129 ? -35.942 157.492 2.229 1.00 29.07 ? 144 HIS A CA 1 ATOM 980 C C . HIS A 1 129 ? -37.308 157.374 1.555 1.00 26.71 ? 144 HIS A C 1 ATOM 981 O O . HIS A 1 129 ? -37.413 157.398 0.330 1.00 33.09 ? 144 HIS A O 1 ATOM 982 C CB . HIS A 1 129 ? -34.794 157.328 1.239 1.00 29.79 ? 144 HIS A CB 1 ATOM 983 C CG . HIS A 1 129 ? -33.471 157.739 1.802 1.00 30.56 ? 144 HIS A CG 1 ATOM 984 N ND1 . HIS A 1 129 ? -32.701 158.741 1.250 1.00 43.11 ? 144 HIS A ND1 1 ATOM 985 C CD2 . HIS A 1 129 ? -32.791 157.298 2.885 1.00 32.66 ? 144 HIS A CD2 1 ATOM 986 C CE1 . HIS A 1 129 ? -31.601 158.895 1.966 1.00 38.54 ? 144 HIS A CE1 1 ATOM 987 N NE2 . HIS A 1 129 ? -31.633 158.031 2.966 1.00 35.69 ? 144 HIS A NE2 1 ATOM 988 N N . ASP A 1 130 ? -38.339 157.233 2.387 1.00 34.52 ? 145 ASP A N 1 ATOM 989 C CA . ASP A 1 130 ? -39.740 157.217 1.948 1.00 26.48 ? 145 ASP A CA 1 ATOM 990 C C . ASP A 1 130 ? -40.117 155.987 1.129 1.00 31.36 ? 145 ASP A C 1 ATOM 991 O O . ASP A 1 130 ? -41.142 155.968 0.465 1.00 40.01 ? 145 ASP A O 1 ATOM 992 C CB . ASP A 1 130 ? -40.072 158.493 1.175 1.00 35.75 ? 145 ASP A CB 1 ATOM 993 C CG . ASP A 1 130 ? -39.886 159.728 2.019 1.00 40.67 ? 145 ASP A CG 1 ATOM 994 O OD1 . ASP A 1 130 ? -40.415 159.747 3.149 1.00 50.11 ? 145 ASP A OD1 1 ATOM 995 O OD2 . ASP A 1 130 ? -39.180 160.659 1.574 1.00 53.62 ? 145 ASP A OD2 1 ATOM 996 N N . THR A 1 131 ? -39.296 154.949 1.192 1.00 27.16 ? 146 THR A N 1 ATOM 997 C CA . THR A 1 131 ? -39.546 153.754 0.400 1.00 23.31 ? 146 THR A CA 1 ATOM 998 C C . THR A 1 131 ? -39.623 152.507 1.260 1.00 21.37 ? 146 THR A C 1 ATOM 999 O O . THR A 1 131 ? -38.740 152.234 2.109 1.00 27.34 ? 146 THR A O 1 ATOM 1000 C CB . THR A 1 131 ? -38.446 153.541 -0.655 1.00 27.58 ? 146 THR A CB 1 ATOM 1001 O OG1 . THR A 1 131 ? -38.386 154.680 -1.524 1.00 34.98 ? 146 THR A OG1 1 ATOM 1002 C CG2 . THR A 1 131 ? -38.716 152.282 -1.472 1.00 28.80 ? 146 THR A CG2 1 ATOM 1003 N N . ILE A 1 132 ? -40.688 151.746 1.068 1.00 29.58 ? 147 ILE A N 1 ATOM 1004 C CA . ILE A 1 132 ? -40.818 150.478 1.762 1.00 22.79 ? 147 ILE A CA 1 ATOM 1005 C C . ILE A 1 132 ? -41.032 149.381 0.729 1.00 28.60 ? 147 ILE A C 1 ATOM 1006 O O . ILE A 1 132 ? -41.541 149.647 -0.366 1.00 28.22 ? 147 ILE A O 1 ATOM 1007 C CB . ILE A 1 132 ? -41.948 150.544 2.818 1.00 26.48 ? 147 ILE A CB 1 ATOM 1008 C CG1 . ILE A 1 132 ? -41.809 149.413 3.833 1.00 29.58 ? 147 ILE A CG1 1 ATOM 1009 C CG2 . ILE A 1 132 ? -43.322 150.540 2.153 1.00 22.16 ? 147 ILE A CG2 1 ATOM 1010 C CD1 . ILE A 1 132 ? -42.433 149.739 5.153 1.00 31.57 ? 147 ILE A CD1 1 ATOM 1011 N N . SER A 1 133 ? -40.593 148.170 1.057 1.00 24.30 ? 148 SER A N 1 ATOM 1012 C CA . SER A 1 133 ? -40.766 147.012 0.192 1.00 23.72 ? 148 SER A CA 1 ATOM 1013 C C . SER A 1 133 ? -42.246 146.767 -0.060 1.00 25.69 ? 148 SER A C 1 ATOM 1014 O O . SER A 1 133 ? -43.082 147.014 0.813 1.00 30.08 ? 148 SER A O 1 ATOM 1015 C CB . SER A 1 133 ? -40.168 145.776 0.859 1.00 25.67 ? 148 SER A CB 1 ATOM 1016 O OG . SER A 1 133 ? -38.785 145.984 1.156 1.00 26.41 ? 148 SER A OG 1 ATOM 1017 N N . SER A 1 134 ? -42.562 146.274 -1.255 1.00 24.18 ? 149 SER A N 1 ATOM 1018 C CA . SER A 1 134 ? -43.939 145.950 -1.622 1.00 29.32 ? 149 SER A CA 1 ATOM 1019 C C . SER A 1 134 ? -44.580 144.994 -0.645 1.00 28.72 ? 149 SER A C 1 ATOM 1020 O O . SER A 1 134 ? -45.772 145.111 -0.343 1.00 34.72 ? 149 SER A O 1 ATOM 1021 C CB . SER A 1 134 ? -43.985 145.316 -3.011 1.00 36.80 ? 149 SER A CB 1 ATOM 1022 O OG . SER A 1 134 ? -43.694 146.277 -4.003 1.00 27.69 ? 149 SER A OG 1 ATOM 1023 N N . TYR A 1 135 ? -43.789 144.029 -0.187 1.00 28.28 ? 150 TYR A N 1 ATOM 1024 C CA . TYR A 1 135 ? -44.246 143.014 0.756 1.00 26.60 ? 150 TYR A CA 1 ATOM 1025 C C . TYR A 1 135 ? -43.288 143.013 1.922 1.00 23.45 ? 150 TYR A C 1 ATOM 1026 O O . TYR A 1 135 ? -42.070 142.990 1.738 1.00 24.81 ? 150 TYR A O 1 ATOM 1027 C CB . TYR A 1 135 ? -44.251 141.632 0.106 1.00 26.23 ? 150 TYR A CB 1 ATOM 1028 C CG . TYR A 1 135 ? -45.006 141.600 -1.202 1.00 33.35 ? 150 TYR A CG 1 ATOM 1029 C CD1 . TYR A 1 135 ? -46.383 141.747 -1.224 1.00 28.89 ? 150 TYR A CD1 1 ATOM 1030 C CD2 . TYR A 1 135 ? -44.344 141.428 -2.409 1.00 30.48 ? 150 TYR A CD2 1 ATOM 1031 C CE1 . TYR A 1 135 ? -47.082 141.729 -2.407 1.00 30.80 ? 150 TYR A CE1 1 ATOM 1032 C CE2 . TYR A 1 135 ? -45.045 141.404 -3.605 1.00 32.79 ? 150 TYR A CE2 1 ATOM 1033 C CZ . TYR A 1 135 ? -46.406 141.553 -3.592 1.00 40.42 ? 150 TYR A CZ 1 ATOM 1034 O OH . TYR A 1 135 ? -47.092 141.529 -4.779 1.00 48.70 ? 150 TYR A OH 1 ATOM 1035 N N . PHE A 1 136 ? -43.828 143.060 3.125 1.00 24.90 ? 151 PHE A N 1 ATOM 1036 C CA . PHE A 1 136 ? -42.977 142.983 4.301 1.00 21.84 ? 151 PHE A CA 1 ATOM 1037 C C . PHE A 1 136 ? -43.797 142.491 5.468 1.00 20.87 ? 151 PHE A C 1 ATOM 1038 O O . PHE A 1 136 ? -45.046 142.452 5.397 1.00 28.13 ? 151 PHE A O 1 ATOM 1039 C CB . PHE A 1 136 ? -42.316 144.347 4.593 1.00 22.38 ? 151 PHE A CB 1 ATOM 1040 C CG . PHE A 1 136 ? -43.262 145.405 5.049 1.00 26.50 ? 151 PHE A CG 1 ATOM 1041 C CD1 . PHE A 1 136 ? -43.884 146.241 4.129 1.00 28.76 ? 151 PHE A CD1 1 ATOM 1042 C CD2 . PHE A 1 136 ? -43.534 145.580 6.397 1.00 25.45 ? 151 PHE A CD2 1 ATOM 1043 C CE1 . PHE A 1 136 ? -44.770 147.226 4.547 1.00 30.98 ? 151 PHE A CE1 1 ATOM 1044 C CE2 . PHE A 1 136 ? -44.426 146.560 6.817 1.00 32.46 ? 151 PHE A CE2 1 ATOM 1045 C CZ . PHE A 1 136 ? -45.038 147.383 5.894 1.00 35.43 ? 151 PHE A CZ 1 ATOM 1046 N N . MET A 1 137 ? -43.135 142.120 6.547 1.00 23.14 ? 152 MET A N 1 ATOM 1047 C CA . MET A 1 137 ? -43.845 141.715 7.750 1.00 25.63 ? 152 MET A CA 1 ATOM 1048 C C . MET A 1 137 ? -43.429 142.634 8.872 1.00 21.94 ? 152 MET A C 1 ATOM 1049 O O . MET A 1 137 ? -42.237 142.836 9.097 1.00 25.70 ? 152 MET A O 1 ATOM 1050 C CB . MET A 1 137 ? -43.499 140.265 8.117 1.00 25.96 ? 152 MET A CB 1 ATOM 1051 C CG . MET A 1 137 ? -43.588 139.281 6.967 1.00 29.23 ? 152 MET A CG 1 ATOM 1052 S SD . MET A 1 137 ? -43.202 137.614 7.533 1.00 27.60 ? 152 MET A SD 1 ATOM 1053 C CE . MET A 1 137 ? -43.651 136.653 6.091 1.00 31.61 ? 152 MET A CE 1 ATOM 1054 N N . ASN A 1 138 ? -44.405 143.187 9.583 1.00 24.75 ? 153 ASN A N 1 ATOM 1055 C CA . ASN A 1 138 ? -44.108 143.932 10.791 1.00 24.16 ? 153 ASN A CA 1 ATOM 1056 C C . ASN A 1 138 ? -43.421 143.006 11.777 1.00 24.01 ? 153 ASN A C 1 ATOM 1057 O O . ASN A 1 138 ? -43.868 141.876 11.979 1.00 25.12 ? 153 ASN A O 1 ATOM 1058 C CB . ASN A 1 138 ? -45.396 144.483 11.389 1.00 28.15 ? 153 ASN A CB 1 ATOM 1059 C CG . ASN A 1 138 ? -45.949 145.627 10.584 1.00 33.50 ? 153 ASN A CG 1 ATOM 1060 O OD1 . ASN A 1 138 ? -47.085 145.590 10.108 1.00 45.31 ? 153 ASN A OD1 1 ATOM 1061 N ND2 . ASN A 1 138 ? -45.132 146.651 10.400 1.00 28.73 ? 153 ASN A ND2 1 ATOM 1062 N N . TYR A 1 139 ? -42.322 143.455 12.375 1.00 26.61 ? 154 TYR A N 1 ATOM 1063 C CA . TYR A 1 139 ? -41.542 142.531 13.193 1.00 19.90 ? 154 TYR A CA 1 ATOM 1064 C C . TYR A 1 139 ? -42.334 141.900 14.324 1.00 22.79 ? 154 TYR A C 1 ATOM 1065 O O . TYR A 1 139 ? -42.987 142.592 15.111 1.00 27.72 ? 154 TYR A O 1 ATOM 1066 C CB . TYR A 1 139 ? -40.277 143.164 13.760 1.00 24.90 ? 154 TYR A CB 1 ATOM 1067 C CG . TYR A 1 139 ? -39.451 142.107 14.436 1.00 20.00 ? 154 TYR A CG 1 ATOM 1068 C CD1 . TYR A 1 139 ? -39.448 141.978 15.819 1.00 21.13 ? 154 TYR A CD1 1 ATOM 1069 C CD2 . TYR A 1 139 ? -38.732 141.180 13.682 1.00 21.39 ? 154 TYR A CD2 1 ATOM 1070 C CE1 . TYR A 1 139 ? -38.713 140.990 16.441 1.00 23.78 ? 154 TYR A CE1 1 ATOM 1071 C CE2 . TYR A 1 139 ? -38.008 140.180 14.292 1.00 21.84 ? 154 TYR A CE2 1 ATOM 1072 C CZ . TYR A 1 139 ? -37.994 140.096 15.675 1.00 23.52 ? 154 TYR A CZ 1 ATOM 1073 O OH . TYR A 1 139 ? -37.262 139.111 16.294 1.00 25.07 ? 154 TYR A OH 1 ATOM 1074 N N . ASN A 1 140 ? -42.275 140.569 14.386 1.00 21.28 ? 155 ASN A N 1 ATOM 1075 C CA . ASN A 1 140 ? -42.966 139.793 15.409 1.00 27.26 ? 155 ASN A CA 1 ATOM 1076 C C . ASN A 1 140 ? -42.219 138.471 15.558 1.00 21.95 ? 155 ASN A C 1 ATOM 1077 O O . ASN A 1 140 ? -42.333 137.570 14.724 1.00 24.52 ? 155 ASN A O 1 ATOM 1078 C CB . ASN A 1 140 ? -44.441 139.569 15.019 1.00 25.63 ? 155 ASN A CB 1 ATOM 1079 C CG . ASN A 1 140 ? -45.232 138.811 16.074 1.00 27.34 ? 155 ASN A CG 1 ATOM 1080 O OD1 . ASN A 1 140 ? -44.673 138.130 16.937 1.00 30.73 ? 155 ASN A OD1 1 ATOM 1081 N ND2 . ASN A 1 140 ? -46.566 138.917 15.993 1.00 37.10 ? 155 ASN A ND2 1 ATOM 1082 N N . SER A 1 141 ? -41.432 138.355 16.620 1.00 24.45 ? 156 SER A N 1 ATOM 1083 C CA . SER A 1 141 ? -40.577 137.178 16.773 1.00 27.39 ? 156 SER A CA 1 ATOM 1084 C C . SER A 1 141 ? -41.358 135.864 16.973 1.00 24.36 ? 156 SER A C 1 ATOM 1085 O O . SER A 1 141 ? -40.782 134.772 16.869 1.00 29.04 ? 156 SER A O 1 ATOM 1086 C CB . SER A 1 141 ? -39.579 137.390 17.905 1.00 28.07 ? 156 SER A CB 1 ATOM 1087 O OG . SER A 1 141 ? -40.254 137.471 19.146 1.00 29.87 ? 156 SER A OG 1 ATOM 1088 N N . SER A 1 142 ? -42.662 135.966 17.244 1.00 30.23 ? 157 SER A N 1 ATOM 1089 C CA . SER A 1 142 ? -43.484 134.771 17.453 1.00 28.57 ? 157 SER A CA 1 ATOM 1090 C C . SER A 1 142 ? -43.858 134.052 16.155 1.00 28.22 ? 157 SER A C 1 ATOM 1091 O O . SER A 1 142 ? -44.273 132.896 16.178 1.00 32.54 ? 157 SER A O 1 ATOM 1092 C CB . SER A 1 142 ? -44.760 135.117 18.209 1.00 31.56 ? 157 SER A CB 1 ATOM 1093 O OG . SER A 1 142 ? -44.469 135.654 19.486 1.00 38.61 ? 157 SER A OG 1 ATOM 1094 N N . VAL A 1 143 ? -43.737 134.746 15.031 1.00 27.12 ? 158 VAL A N 1 ATOM 1095 C CA . VAL A 1 143 ? -44.101 134.165 13.751 1.00 28.98 ? 158 VAL A CA 1 ATOM 1096 C C . VAL A 1 143 ? -43.132 133.043 13.426 1.00 21.98 ? 158 VAL A C 1 ATOM 1097 O O . VAL A 1 143 ? -41.904 133.235 13.465 1.00 23.68 ? 158 VAL A O 1 ATOM 1098 C CB . VAL A 1 143 ? -44.109 135.244 12.636 1.00 29.41 ? 158 VAL A CB 1 ATOM 1099 C CG1 . VAL A 1 143 ? -44.292 134.604 11.249 1.00 27.76 ? 158 VAL A CG1 1 ATOM 1100 C CG2 . VAL A 1 143 ? -45.208 136.268 12.910 1.00 30.98 ? 158 VAL A CG2 1 ATOM 1101 N N . SER A 1 144 ? -43.672 131.870 13.119 1.00 25.43 ? 159 SER A N 1 ATOM 1102 C CA . SER A 1 144 ? -42.853 130.687 12.899 1.00 27.11 ? 159 SER A CA 1 ATOM 1103 C C . SER A 1 144 ? -41.947 130.835 11.685 1.00 26.83 ? 159 SER A C 1 ATOM 1104 O O . SER A 1 144 ? -42.196 131.661 10.790 1.00 24.04 ? 159 SER A O 1 ATOM 1105 C CB . SER A 1 144 ? -43.734 129.459 12.719 1.00 29.00 ? 159 SER A CB 1 ATOM 1106 O OG . SER A 1 144 ? -44.409 129.513 11.470 1.00 34.78 ? 159 SER A OG 1 ATOM 1107 N N . PHE A 1 145 ? -40.895 130.026 11.646 1.00 28.72 ? 160 PHE A N 1 ATOM 1108 C CA . PHE A 1 145 ? -40.034 130.037 10.475 1.00 22.40 ? 160 PHE A CA 1 ATOM 1109 C C . PHE A 1 145 ? -40.814 129.597 9.247 1.00 25.07 ? 160 PHE A C 1 ATOM 1110 O O . PHE A 1 145 ? -40.640 130.168 8.171 1.00 28.39 ? 160 PHE A O 1 ATOM 1111 C CB . PHE A 1 145 ? -38.782 129.170 10.645 1.00 26.05 ? 160 PHE A CB 1 ATOM 1112 C CG . PHE A 1 145 ? -37.809 129.294 9.498 1.00 23.22 ? 160 PHE A CG 1 ATOM 1113 C CD1 . PHE A 1 145 ? -37.839 128.401 8.438 1.00 23.31 ? 160 PHE A CD1 1 ATOM 1114 C CD2 . PHE A 1 145 ? -36.876 130.324 9.473 1.00 25.15 ? 160 PHE A CD2 1 ATOM 1115 C CE1 . PHE A 1 145 ? -36.931 128.517 7.389 1.00 23.37 ? 160 PHE A CE1 1 ATOM 1116 C CE2 . PHE A 1 145 ? -35.980 130.452 8.428 1.00 21.56 ? 160 PHE A CE2 1 ATOM 1117 C CZ . PHE A 1 145 ? -36.004 129.560 7.388 1.00 24.15 ? 160 PHE A CZ 1 ATOM 1118 N N . GLU A 1 146 ? -41.670 128.595 9.412 1.00 28.75 ? 161 GLU A N 1 ATOM 1119 C CA . GLU A 1 146 ? -42.448 128.056 8.294 1.00 27.55 ? 161 GLU A CA 1 ATOM 1120 C C . GLU A 1 146 ? -43.250 129.151 7.613 1.00 30.04 ? 161 GLU A C 1 ATOM 1121 O O . GLU A 1 146 ? -43.321 129.232 6.380 1.00 31.17 ? 161 GLU A O 1 ATOM 1122 C CB . GLU A 1 146 ? -43.401 126.972 8.792 1.00 32.07 ? 161 GLU A CB 1 ATOM 1123 C CG . GLU A 1 146 ? -44.160 126.294 7.636 1.00 34.47 ? 161 GLU A CG 1 ATOM 1124 C CD . GLU A 1 146 ? -45.409 125.547 8.084 1.00 47.38 ? 161 GLU A CD 1 ATOM 1125 O OE1 . GLU A 1 146 ? -45.956 124.753 7.279 1.00 47.56 ? 161 GLU A OE1 1 ATOM 1126 O OE2 . GLU A 1 146 ? -45.859 125.766 9.234 1.00 52.38 ? 161 GLU A OE2 1 ATOM 1127 N N . GLU A 1 147 ? -43.868 129.995 8.423 1.00 28.66 ? 162 GLU A N 1 ATOM 1128 C CA . GLU A 1 147 ? -44.672 131.080 7.911 1.00 33.05 ? 162 GLU A CA 1 ATOM 1129 C C . GLU A 1 147 ? -43.822 132.127 7.205 1.00 25.56 ? 162 GLU A C 1 ATOM 1130 O O . GLU A 1 147 ? -44.181 132.624 6.142 1.00 29.74 ? 162 GLU A O 1 ATOM 1131 C CB . GLU A 1 147 ? -45.457 131.724 9.046 1.00 32.84 ? 162 GLU A CB 1 ATOM 1132 C CG . GLU A 1 147 ? -46.255 132.914 8.586 1.00 35.12 ? 162 GLU A CG 1 ATOM 1133 C CD . GLU A 1 147 ? -47.503 133.108 9.401 1.00 42.74 ? 162 GLU A CD 1 ATOM 1134 O OE1 . GLU A 1 147 ? -47.633 132.413 10.437 1.00 43.07 ? 162 GLU A OE1 1 ATOM 1135 O OE2 . GLU A 1 147 ? -48.348 133.948 9.002 1.00 51.02 ? 162 GLU A OE2 1 ATOM 1136 N N . ARG A 1 148 ? -42.681 132.467 7.807 1.00 24.41 ? 163 ARG A N 1 ATOM 1137 C CA . ARG A 1 148 ? -41.743 133.372 7.153 1.00 21.43 ? 163 ARG A CA 1 ATOM 1138 C C . ARG A 1 148 ? -41.292 132.794 5.823 1.00 19.34 ? 163 ARG A C 1 ATOM 1139 O O . ARG A 1 148 ? -41.284 133.506 4.816 1.00 23.68 ? 163 ARG A O 1 ATOM 1140 C CB . ARG A 1 148 ? -40.538 133.647 8.061 1.00 22.69 ? 163 ARG A CB 1 ATOM 1141 C CG . ARG A 1 148 ? -40.869 134.409 9.346 1.00 21.22 ? 163 ARG A CG 1 ATOM 1142 C CD . ARG A 1 148 ? -39.656 134.556 10.237 1.00 19.19 ? 163 ARG A CD 1 ATOM 1143 N NE . ARG A 1 148 ? -40.050 134.651 11.650 1.00 19.91 ? 163 ARG A NE 1 ATOM 1144 C CZ . ARG A 1 148 ? -39.322 135.234 12.606 1.00 17.69 ? 163 ARG A CZ 1 ATOM 1145 N NH1 . ARG A 1 148 ? -38.147 135.807 12.323 1.00 19.07 ? 163 ARG A NH1 1 ATOM 1146 N NH2 . ARG A 1 148 ? -39.751 135.242 13.857 1.00 23.16 ? 163 ARG A NH2 1 ATOM 1147 N N . LEU A 1 149 ? -40.950 131.506 5.827 1.00 21.19 ? 164 LEU A N 1 ATOM 1148 C CA . LEU A 1 149 ? -40.423 130.805 4.660 1.00 24.24 ? 164 LEU A CA 1 ATOM 1149 C C . LEU A 1 149 ? -41.467 130.674 3.573 1.00 26.04 ? 164 LEU A C 1 ATOM 1150 O O . LEU A 1 149 ? -41.226 130.984 2.409 1.00 28.15 ? 164 LEU A O 1 ATOM 1151 C CB . LEU A 1 149 ? -39.981 129.396 5.073 1.00 24.49 ? 164 LEU A CB 1 ATOM 1152 C CG . LEU A 1 149 ? -39.620 128.437 3.939 1.00 27.39 ? 164 LEU A CG 1 ATOM 1153 C CD1 . LEU A 1 149 ? -38.491 129.026 3.128 1.00 33.23 ? 164 LEU A CD1 1 ATOM 1154 C CD2 . LEU A 1 149 ? -39.233 127.053 4.482 1.00 26.59 ? 164 LEU A CD2 1 ATOM 1155 N N . ASN A 1 150 ? -42.637 130.196 3.957 1.00 27.49 ? 165 ASN A N 1 ATOM 1156 C CA . ASN A 1 150 ? -43.680 129.954 2.958 1.00 28.26 ? 165 ASN A CA 1 ATOM 1157 C C . ASN A 1 150 ? -44.117 131.244 2.282 1.00 30.89 ? 165 ASN A C 1 ATOM 1158 O O . ASN A 1 150 ? -44.307 131.276 1.062 1.00 37.80 ? 165 ASN A O 1 ATOM 1159 C CB . ASN A 1 150 ? -44.865 129.199 3.577 1.00 29.27 ? 165 ASN A CB 1 ATOM 1160 C CG . ASN A 1 150 ? -44.536 127.738 3.845 1.00 35.41 ? 165 ASN A CG 1 ATOM 1161 O OD1 . ASN A 1 150 ? -43.517 127.214 3.356 1.00 33.37 ? 165 ASN A OD1 1 ATOM 1162 N ND2 . ASN A 1 150 ? -45.396 127.066 4.602 1.00 32.39 ? 165 ASN A ND2 1 ATOM 1163 N N . ASN A 1 151 ? -44.255 132.314 3.062 1.00 28.83 ? 166 ASN A N 1 ATOM 1164 C CA . ASN A 1 151 ? -44.623 133.620 2.508 1.00 30.07 ? 166 ASN A CA 1 ATOM 1165 C C . ASN A 1 151 ? -43.559 134.275 1.633 1.00 29.75 ? 166 ASN A C 1 ATOM 1166 O O . ASN A 1 151 ? -43.869 134.866 0.606 1.00 35.45 ? 166 ASN A O 1 ATOM 1167 C CB . ASN A 1 151 ? -44.985 134.610 3.617 1.00 24.90 ? 166 ASN A CB 1 ATOM 1168 C CG . ASN A 1 151 ? -46.346 134.343 4.227 1.00 31.60 ? 166 ASN A CG 1 ATOM 1169 O OD1 . ASN A 1 151 ? -46.875 133.230 4.123 1.00 42.48 ? 166 ASN A OD1 1 ATOM 1170 N ND2 . ASN A 1 151 ? -46.918 135.362 4.886 1.00 34.87 ? 166 ASN A ND2 1 ATOM 1171 N N . ILE A 1 152 ? -42.304 134.249 2.071 1.00 25.66 ? 167 ILE A N 1 ATOM 1172 C CA . ILE A 1 152 ? -41.275 134.885 1.277 1.00 23.86 ? 167 ILE A CA 1 ATOM 1173 C C . ILE A 1 152 ? -41.074 134.154 -0.053 1.00 21.49 ? 167 ILE A C 1 ATOM 1174 O O . ILE A 1 152 ? -40.848 134.790 -1.085 1.00 29.85 ? 167 ILE A O 1 ATOM 1175 C CB . ILE A 1 152 ? -39.941 135.048 2.085 1.00 22.70 ? 167 ILE A CB 1 ATOM 1176 C CG1 . ILE A 1 152 ? -39.039 136.107 1.438 1.00 26.79 ? 167 ILE A CG1 1 ATOM 1177 C CG2 . ILE A 1 152 ? -39.219 133.726 2.262 1.00 24.48 ? 167 ILE A CG2 1 ATOM 1178 C CD1 . ILE A 1 152 ? -39.595 137.503 1.568 1.00 20.19 ? 167 ILE A CD1 1 ATOM 1179 N N . THR A 1 153 ? -41.194 132.826 -0.036 1.00 27.65 ? 168 THR A N 1 ATOM 1180 C CA . THR A 1 153 ? -41.028 132.036 -1.247 1.00 23.36 ? 168 THR A CA 1 ATOM 1181 C C . THR A 1 153 ? -42.252 132.140 -2.166 1.00 29.89 ? 168 THR A C 1 ATOM 1182 O O . THR A 1 153 ? -42.102 132.124 -3.391 1.00 28.65 ? 168 THR A O 1 ATOM 1183 C CB . THR A 1 153 ? -40.678 130.551 -0.947 1.00 24.00 ? 168 THR A CB 1 ATOM 1184 O OG1 . THR A 1 153 ? -41.697 129.970 -0.125 1.00 30.67 ? 168 THR A OG1 1 ATOM 1185 C CG2 . THR A 1 153 ? -39.351 130.463 -0.222 1.00 26.12 ? 168 THR A CG2 1 ATOM 1186 N N . MET A 1 154 ? -43.450 132.247 -1.590 1.00 28.60 ? 169 MET A N 1 ATOM 1187 C CA . MET A 1 154 ? -44.646 132.520 -2.394 1.00 29.62 ? 169 MET A CA 1 ATOM 1188 C C . MET A 1 154 ? -44.460 133.839 -3.118 1.00 33.25 ? 169 MET A C 1 ATOM 1189 O O . MET A 1 154 ? -44.735 133.944 -4.307 1.00 32.82 ? 169 MET A O 1 ATOM 1190 C CB . MET A 1 154 ? -45.895 132.663 -1.510 1.00 34.60 ? 169 MET A CB 1 ATOM 1191 C CG . MET A 1 154 ? -47.007 131.639 -1.693 1.00 43.39 ? 169 MET A CG 1 ATOM 1192 S SD . MET A 1 154 ? -47.204 130.829 -3.309 1.00 47.12 ? 169 MET A SD 1 ATOM 1193 C CE . MET A 1 154 ? -46.810 129.144 -2.870 1.00 45.47 ? 169 MET A CE 1 ATOM 1194 N N . TRP A 1 155 ? -44.017 134.860 -2.390 1.00 32.49 ? 170 TRP A N 1 ATOM 1195 C CA . TRP A 1 155 ? -43.810 136.191 -2.974 1.00 29.39 ? 170 TRP A CA 1 ATOM 1196 C C . TRP A 1 155 ? -42.782 136.135 -4.114 1.00 31.43 ? 170 TRP A C 1 ATOM 1197 O O . TRP A 1 155 ? -43.006 136.696 -5.190 1.00 31.96 ? 170 TRP A O 1 ATOM 1198 C CB . TRP A 1 155 ? -43.398 137.209 -1.892 1.00 28.05 ? 170 TRP A CB 1 ATOM 1199 C CG . TRP A 1 155 ? -44.523 137.652 -0.990 1.00 32.00 ? 170 TRP A CG 1 ATOM 1200 C CD1 . TRP A 1 155 ? -45.854 137.693 -1.297 1.00 35.48 ? 170 TRP A CD1 1 ATOM 1201 C CD2 . TRP A 1 155 ? -44.418 138.106 0.373 1.00 32.02 ? 170 TRP A CD2 1 ATOM 1202 N NE1 . TRP A 1 155 ? -46.579 138.154 -0.218 1.00 36.45 ? 170 TRP A NE1 1 ATOM 1203 C CE2 . TRP A 1 155 ? -45.722 138.410 0.819 1.00 32.68 ? 170 TRP A CE2 1 ATOM 1204 C CE3 . TRP A 1 155 ? -43.351 138.282 1.254 1.00 24.43 ? 170 TRP A CE3 1 ATOM 1205 C CZ2 . TRP A 1 155 ? -45.983 138.896 2.099 1.00 32.47 ? 170 TRP A CZ2 1 ATOM 1206 C CZ3 . TRP A 1 155 ? -43.613 138.759 2.525 1.00 30.50 ? 170 TRP A CZ3 1 ATOM 1207 C CH2 . TRP A 1 155 ? -44.913 139.050 2.942 1.00 33.03 ? 170 TRP A CH2 1 ATOM 1208 N N . LEU A 1 156 ? -41.665 135.446 -3.887 1.00 22.59 ? 171 LEU A N 1 ATOM 1209 C CA . LEU A 1 156 ? -40.660 135.265 -4.945 1.00 25.79 ? 171 LEU A CA 1 ATOM 1210 C C . LEU A 1 156 ? -41.221 134.524 -6.158 1.00 34.19 ? 171 LEU A C 1 ATOM 1211 O O . LEU A 1 156 ? -40.858 134.819 -7.295 1.00 35.82 ? 171 LEU A O 1 ATOM 1212 C CB . LEU A 1 156 ? -39.442 134.506 -4.409 1.00 27.58 ? 171 LEU A CB 1 ATOM 1213 C CG . LEU A 1 156 ? -38.460 135.338 -3.574 1.00 24.20 ? 171 LEU A CG 1 ATOM 1214 C CD1 . LEU A 1 156 ? -37.632 134.454 -2.635 1.00 26.50 ? 171 LEU A CD1 1 ATOM 1215 C CD2 . LEU A 1 156 ? -37.549 136.167 -4.483 1.00 30.81 ? 171 LEU A CD2 1 ATOM 1216 N N . ASN A 1 157 ? -42.108 133.564 -5.915 1.00 32.79 ? 172 ASN A N 1 ATOM 1217 C CA . ASN A 1 157 ? -42.615 132.695 -6.982 1.00 39.10 ? 172 ASN A CA 1 ATOM 1218 C C . ASN A 1 157 ? -43.723 133.352 -7.794 1.00 44.52 ? 172 ASN A C 1 ATOM 1219 O O . ASN A 1 157 ? -43.746 133.278 -9.025 1.00 45.34 ? 172 ASN A O 1 ATOM 1220 C CB . ASN A 1 157 ? -43.126 131.379 -6.391 1.00 38.25 ? 172 ASN A CB 1 ATOM 1221 C CG . ASN A 1 157 ? -43.849 130.523 -7.405 1.00 47.93 ? 172 ASN A CG 1 ATOM 1222 O OD1 . ASN A 1 157 ? -45.074 130.360 -7.343 1.00 51.15 ? 172 ASN A OD1 1 ATOM 1223 N ND2 . ASN A 1 157 ? -43.095 129.957 -8.342 1.00 49.63 ? 172 ASN A ND2 1 ATOM 1224 N N . ASN A 1 158 ? -44.643 133.989 -7.079 1.00 45.32 ? 173 ASN A N 1 ATOM 1225 C CA . ASN A 1 158 ? -45.766 134.679 -7.688 1.00 49.31 ? 173 ASN A CA 1 ATOM 1226 C C . ASN A 1 158 ? -45.394 136.140 -7.886 1.00 50.03 ? 173 ASN A C 1 ATOM 1227 O O . ASN A 1 158 ? -44.305 136.438 -8.375 1.00 65.30 ? 173 ASN A O 1 ATOM 1228 C CB . ASN A 1 158 ? -47.007 134.536 -6.804 1.00 50.53 ? 173 ASN A CB 1 ATOM 1229 C CG . ASN A 1 158 ? -47.581 133.124 -6.824 1.00 54.85 ? 173 ASN A CG 1 ATOM 1230 O OD1 . ASN A 1 158 ? -47.040 132.207 -6.199 1.00 62.48 ? 173 ASN A OD1 1 ATOM 1231 N ND2 . ASN A 1 158 ? -48.684 132.945 -7.548 1.00 49.00 ? 173 ASN A ND2 1 ATOM 1232 N N . SER A 1 159 ? -46.291 137.041 -7.505 1.00 51.31 ? 174 SER A N 1 ATOM 1233 C CA . SER A 1 159 ? -46.026 138.486 -7.523 1.00 32.57 ? 174 SER A CA 1 ATOM 1234 C C . SER A 1 159 ? -45.879 139.104 -8.918 1.00 41.68 ? 174 SER A C 1 ATOM 1235 O O . SER A 1 159 ? -45.120 138.619 -9.757 1.00 37.79 ? 174 SER A O 1 ATOM 1236 C CB . SER A 1 159 ? -44.839 138.847 -6.630 1.00 35.76 ? 174 SER A CB 1 ATOM 1237 O OG . SER A 1 159 ? -45.050 138.293 -5.346 1.00 43.89 ? 174 SER A OG 1 ATOM 1238 N N . ASN A 1 160 ? -46.651 140.166 -9.141 1.00 39.99 ? 175 ASN A N 1 ATOM 1239 C CA . ASN A 1 160 ? -46.567 141.009 -10.328 1.00 41.40 ? 175 ASN A CA 1 ATOM 1240 C C . ASN A 1 160 ? -46.697 142.481 -9.930 1.00 40.61 ? 175 ASN A C 1 ATOM 1241 O O . ASN A 1 160 ? -47.725 142.890 -9.380 1.00 46.64 ? 175 ASN A O 1 ATOM 1242 C CB . ASN A 1 160 ? -47.650 140.649 -11.342 1.00 49.19 ? 175 ASN A CB 1 ATOM 1243 C CG . ASN A 1 160 ? -47.136 139.754 -12.443 1.00 57.07 ? 175 ASN A CG 1 ATOM 1244 O OD1 . ASN A 1 160 ? -46.667 140.233 -13.481 1.00 61.02 ? 175 ASN A OD1 1 ATOM 1245 N ND2 . ASN A 1 160 ? -47.219 138.444 -12.228 1.00 60.37 ? 175 ASN A ND2 1 ATOM 1246 N N . PRO A 1 161 ? -45.656 143.286 -10.202 1.00 36.83 ? 176 PRO A N 1 ATOM 1247 C CA . PRO A 1 161 ? -44.393 142.911 -10.860 1.00 40.94 ? 176 PRO A CA 1 ATOM 1248 C C . PRO A 1 161 ? -43.544 141.898 -10.070 1.00 34.74 ? 176 PRO A C 1 ATOM 1249 O O . PRO A 1 161 ? -43.820 141.684 -8.879 1.00 36.06 ? 176 PRO A O 1 ATOM 1250 C CB . PRO A 1 161 ? -43.660 144.255 -10.983 1.00 41.96 ? 176 PRO A CB 1 ATOM 1251 C CG . PRO A 1 161 ? -44.262 145.127 -9.966 1.00 38.13 ? 176 PRO A CG 1 ATOM 1252 C CD . PRO A 1 161 ? -45.700 144.726 -9.891 1.00 38.30 ? 176 PRO A CD 1 ATOM 1253 N N . PRO A 1 162 ? -42.551 141.257 -10.727 1.00 31.33 ? 177 PRO A N 1 ATOM 1254 C CA . PRO A 1 162 ? -41.781 140.205 -10.048 1.00 30.53 ? 177 PRO A CA 1 ATOM 1255 C C . PRO A 1 162 ? -41.002 140.698 -8.833 1.00 30.83 ? 177 PRO A C 1 ATOM 1256 O O . PRO A 1 162 ? -40.463 141.813 -8.826 1.00 31.54 ? 177 PRO A O 1 ATOM 1257 C CB . PRO A 1 162 ? -40.808 139.727 -11.132 1.00 36.70 ? 177 PRO A CB 1 ATOM 1258 C CG . PRO A 1 162 ? -40.697 140.876 -12.063 1.00 34.29 ? 177 PRO A CG 1 ATOM 1259 C CD . PRO A 1 162 ? -42.074 141.459 -12.107 1.00 34.29 ? 177 PRO A CD 1 ATOM 1260 N N . VAL A 1 163 ? -40.967 139.863 -7.804 1.00 28.79 ? 178 VAL A N 1 ATOM 1261 C CA . VAL A 1 163 ? -40.100 140.114 -6.654 1.00 24.45 ? 178 VAL A CA 1 ATOM 1262 C C . VAL A 1 163 ? -38.719 139.625 -7.031 1.00 26.17 ? 178 VAL A C 1 ATOM 1263 O O . VAL A 1 163 ? -38.548 138.441 -7.350 1.00 27.82 ? 178 VAL A O 1 ATOM 1264 C CB . VAL A 1 163 ? -40.609 139.365 -5.398 1.00 22.21 ? 178 VAL A CB 1 ATOM 1265 C CG1 . VAL A 1 163 ? -39.558 139.361 -4.306 1.00 20.64 ? 178 VAL A CG1 1 ATOM 1266 C CG2 . VAL A 1 163 ? -41.895 139.995 -4.875 1.00 28.47 ? 178 VAL A CG2 1 ATOM 1267 N N . THR A 1 164 ? -37.737 140.524 -6.986 1.00 26.33 ? 179 THR A N 1 ATOM 1268 C CA . THR A 1 164 ? -36.389 140.214 -7.451 1.00 23.67 ? 179 THR A CA 1 ATOM 1269 C C . THR A 1 164 ? -35.386 140.215 -6.311 1.00 17.71 ? 179 THR A C 1 ATOM 1270 O O . THR A 1 164 ? -34.291 139.660 -6.440 1.00 27.64 ? 179 THR A O 1 ATOM 1271 C CB . THR A 1 164 ? -35.943 141.199 -8.545 1.00 24.84 ? 179 THR A CB 1 ATOM 1272 O OG1 . THR A 1 164 ? -36.121 142.537 -8.082 1.00 24.39 ? 179 THR A OG1 1 ATOM 1273 C CG2 . THR A 1 164 ? -36.796 141.002 -9.818 1.00 27.36 ? 179 THR A CG2 1 ATOM 1274 N N . PHE A 1 165 ? -35.766 140.841 -5.196 1.00 20.65 ? 180 PHE A N 1 ATOM 1275 C CA . PHE A 1 165 ? -34.932 140.819 -3.990 1.00 17.48 ? 180 PHE A CA 1 ATOM 1276 C C . PHE A 1 165 ? -35.808 140.550 -2.778 1.00 18.38 ? 180 PHE A C 1 ATOM 1277 O O . PHE A 1 165 ? -36.815 141.233 -2.579 1.00 23.04 ? 180 PHE A O 1 ATOM 1278 C CB . PHE A 1 165 ? -34.193 142.140 -3.756 1.00 20.47 ? 180 PHE A CB 1 ATOM 1279 C CG . PHE A 1 165 ? -33.335 142.111 -2.499 1.00 18.42 ? 180 PHE A CG 1 ATOM 1280 C CD1 . PHE A 1 165 ? -33.748 142.741 -1.320 1.00 21.44 ? 180 PHE A CD1 1 ATOM 1281 C CD2 . PHE A 1 165 ? -32.151 141.387 -2.489 1.00 20.13 ? 180 PHE A CD2 1 ATOM 1282 C CE1 . PHE A 1 165 ? -32.968 142.673 -0.161 1.00 17.39 ? 180 PHE A CE1 1 ATOM 1283 C CE2 . PHE A 1 165 ? -31.370 141.310 -1.342 1.00 17.48 ? 180 PHE A CE2 1 ATOM 1284 C CZ . PHE A 1 165 ? -31.789 141.961 -0.170 1.00 20.77 ? 180 PHE A CZ 1 ATOM 1285 N N . ALA A 1 166 ? -35.388 139.609 -1.930 1.00 21.49 ? 181 ALA A N 1 ATOM 1286 C CA . ALA A 1 166 ? -36.173 139.228 -0.770 1.00 19.57 ? 181 ALA A CA 1 ATOM 1287 C C . ALA A 1 166 ? -35.254 138.975 0.410 1.00 19.34 ? 181 ALA A C 1 ATOM 1288 O O . ALA A 1 166 ? -34.134 138.497 0.230 1.00 20.73 ? 181 ALA A O 1 ATOM 1289 C CB . ALA A 1 166 ? -36.999 137.984 -1.072 1.00 20.04 ? 181 ALA A CB 1 ATOM 1290 N N . THR A 1 167 ? -35.720 139.306 1.614 1.00 18.23 ? 182 THR A N 1 ATOM 1291 C CA . THR A 1 167 ? -34.953 139.004 2.815 1.00 18.89 ? 182 THR A CA 1 ATOM 1292 C C . THR A 1 167 ? -35.722 138.061 3.731 1.00 17.08 ? 182 THR A C 1 ATOM 1293 O O . THR A 1 167 ? -36.962 138.098 3.801 1.00 21.93 ? 182 THR A O 1 ATOM 1294 C CB . THR A 1 167 ? -34.573 140.272 3.635 1.00 22.96 ? 182 THR A CB 1 ATOM 1295 O OG1 . THR A 1 167 ? -35.717 141.131 3.773 1.00 23.02 ? 182 THR A OG1 1 ATOM 1296 C CG2 . THR A 1 167 ? -33.402 141.031 3.000 1.00 20.84 ? 182 THR A CG2 1 ATOM 1297 N N . LEU A 1 168 ? -34.992 137.221 4.456 1.00 19.61 ? 183 LEU A N 1 ATOM 1298 C CA . LEU A 1 168 ? -35.602 136.285 5.401 1.00 17.29 ? 183 LEU A CA 1 ATOM 1299 C C . LEU A 1 168 ? -34.715 136.236 6.635 1.00 17.25 ? 183 LEU A C 1 ATOM 1300 O O . LEU A 1 168 ? -33.492 136.086 6.528 1.00 21.37 ? 183 LEU A O 1 ATOM 1301 C CB . LEU A 1 168 ? -35.747 134.892 4.787 1.00 20.56 ? 183 LEU A CB 1 ATOM 1302 C CG . LEU A 1 168 ? -36.164 133.713 5.659 1.00 17.75 ? 183 LEU A CG 1 ATOM 1303 C CD1 . LEU A 1 168 ? -37.550 133.921 6.326 1.00 20.18 ? 183 LEU A CD1 1 ATOM 1304 C CD2 . LEU A 1 168 ? -36.180 132.444 4.804 1.00 25.40 ? 183 LEU A CD2 1 ATOM 1305 N N . TYR A 1 169 ? -35.320 136.365 7.810 1.00 18.19 ? 184 TYR A N 1 ATOM 1306 C CA . TYR A 1 169 ? -34.546 136.487 9.050 1.00 18.66 ? 184 TYR A CA 1 ATOM 1307 C C . TYR A 1 169 ? -35.071 135.558 10.126 1.00 16.64 ? 184 TYR A C 1 ATOM 1308 O O . TYR A 1 169 ? -36.286 135.378 10.262 1.00 18.81 ? 184 TYR A O 1 ATOM 1309 C CB . TYR A 1 169 ? -34.583 137.930 9.552 1.00 15.50 ? 184 TYR A CB 1 ATOM 1310 C CG . TYR A 1 169 ? -34.024 138.125 10.937 1.00 16.74 ? 184 TYR A CG 1 ATOM 1311 C CD1 . TYR A 1 169 ? -32.659 138.289 11.145 1.00 17.51 ? 184 TYR A CD1 1 ATOM 1312 C CD2 . TYR A 1 169 ? -34.871 138.150 12.039 1.00 14.03 ? 184 TYR A CD2 1 ATOM 1313 C CE1 . TYR A 1 169 ? -32.151 138.464 12.418 1.00 18.66 ? 184 TYR A CE1 1 ATOM 1314 C CE2 . TYR A 1 169 ? -34.366 138.332 13.305 1.00 16.09 ? 184 TYR A CE2 1 ATOM 1315 C CZ . TYR A 1 169 ? -33.014 138.480 13.483 1.00 17.69 ? 184 TYR A CZ 1 ATOM 1316 O OH . TYR A 1 169 ? -32.515 138.650 14.759 1.00 19.93 ? 184 TYR A OH 1 ATOM 1317 N N . TRP A 1 170 ? -34.163 134.993 10.914 1.00 14.52 ? 185 TRP A N 1 ATOM 1318 C CA . TRP A 1 170 ? -34.539 134.104 12.012 1.00 14.60 ? 185 TRP A CA 1 ATOM 1319 C C . TRP A 1 170 ? -33.672 134.455 13.214 1.00 14.33 ? 185 TRP A C 1 ATOM 1320 O O . TRP A 1 170 ? -32.486 134.819 13.046 1.00 15.85 ? 185 TRP A O 1 ATOM 1321 C CB . TRP A 1 170 ? -34.361 132.648 11.578 1.00 18.76 ? 185 TRP A CB 1 ATOM 1322 C CG . TRP A 1 170 ? -34.909 131.660 12.567 1.00 16.73 ? 185 TRP A CG 1 ATOM 1323 C CD1 . TRP A 1 170 ? -34.212 130.710 13.242 1.00 17.17 ? 185 TRP A CD1 1 ATOM 1324 C CD2 . TRP A 1 170 ? -36.282 131.531 12.988 1.00 18.61 ? 185 TRP A CD2 1 ATOM 1325 N NE1 . TRP A 1 170 ? -35.056 130.001 14.074 1.00 22.39 ? 185 TRP A NE1 1 ATOM 1326 C CE2 . TRP A 1 170 ? -36.330 130.485 13.926 1.00 18.38 ? 185 TRP A CE2 1 ATOM 1327 C CE3 . TRP A 1 170 ? -37.461 132.213 12.675 1.00 22.85 ? 185 TRP A CE3 1 ATOM 1328 C CZ2 . TRP A 1 170 ? -37.514 130.095 14.551 1.00 21.92 ? 185 TRP A CZ2 1 ATOM 1329 C CZ3 . TRP A 1 170 ? -38.640 131.824 13.286 1.00 22.85 ? 185 TRP A CZ3 1 ATOM 1330 C CH2 . TRP A 1 170 ? -38.660 130.766 14.208 1.00 21.08 ? 185 TRP A CH2 1 ATOM 1331 N N . GLU A 1 171 ? -34.242 134.344 14.418 1.00 16.70 ? 186 GLU A N 1 ATOM 1332 C CA . GLU A 1 171 ? -33.594 134.806 15.650 1.00 16.04 ? 186 GLU A CA 1 ATOM 1333 C C . GLU A 1 171 ? -32.587 133.834 16.235 1.00 13.79 ? 186 GLU A C 1 ATOM 1334 O O . GLU A 1 171 ? -31.822 134.203 17.134 1.00 15.69 ? 186 GLU A O 1 ATOM 1335 C CB . GLU A 1 171 ? -34.643 135.089 16.739 1.00 16.17 ? 186 GLU A CB 1 ATOM 1336 C CG . GLU A 1 171 ? -35.545 136.286 16.443 1.00 18.98 ? 186 GLU A CG 1 ATOM 1337 C CD . GLU A 1 171 ? -36.655 135.983 15.449 1.00 17.71 ? 186 GLU A CD 1 ATOM 1338 O OE1 . GLU A 1 171 ? -37.273 136.955 14.951 1.00 21.97 ? 186 GLU A OE1 1 ATOM 1339 O OE2 . GLU A 1 171 ? -36.910 134.792 15.165 1.00 20.44 ? 186 GLU A OE2 1 ATOM 1340 N N . GLU A 1 172 ? -32.600 132.591 15.761 1.00 15.17 ? 187 GLU A N 1 ATOM 1341 C CA . GLU A 1 172 ? -31.638 131.583 16.213 1.00 15.01 ? 187 GLU A CA 1 ATOM 1342 C C . GLU A 1 172 ? -30.586 131.381 15.153 1.00 15.98 ? 187 GLU A C 1 ATOM 1343 O O . GLU A 1 172 ? -30.881 131.582 13.968 1.00 16.26 ? 187 GLU A O 1 ATOM 1344 C CB . GLU A 1 172 ? -32.361 130.259 16.482 1.00 17.28 ? 187 GLU A CB 1 ATOM 1345 C CG . GLU A 1 172 ? -33.291 130.309 17.689 1.00 16.56 ? 187 GLU A CG 1 ATOM 1346 C CD . GLU A 1 172 ? -32.567 130.240 19.004 1.00 14.70 ? 187 GLU A CD 1 ATOM 1347 O OE1 . GLU A 1 172 ? -31.360 130.538 19.076 1.00 16.70 ? 187 GLU A OE1 1 ATOM 1348 O OE2 . GLU A 1 172 ? -33.217 129.852 20.009 1.00 25.90 ? 187 GLU A OE2 1 ATOM 1349 N N . PRO A 1 173 ? -29.361 130.942 15.544 1.00 14.49 ? 188 PRO A N 1 ATOM 1350 C CA . PRO A 1 173 ? -28.973 130.454 16.879 1.00 18.16 ? 188 PRO A CA 1 ATOM 1351 C C . PRO A 1 173 ? -28.512 131.518 17.881 1.00 12.61 ? 188 PRO A C 1 ATOM 1352 O O . PRO A 1 173 ? -28.007 131.156 18.934 1.00 14.63 ? 188 PRO A O 1 ATOM 1353 C CB . PRO A 1 173 ? -27.814 129.504 16.569 1.00 17.29 ? 188 PRO A CB 1 ATOM 1354 C CG . PRO A 1 173 ? -27.131 130.162 15.353 1.00 16.34 ? 188 PRO A CG 1 ATOM 1355 C CD . PRO A 1 173 ? -28.327 130.635 14.524 1.00 14.69 ? 188 PRO A CD 1 ATOM 1356 N N . ASP A 1 174 ? -28.703 132.796 17.577 1.00 14.13 ? 189 ASP A N 1 ATOM 1357 C CA . ASP A 1 174 ? -28.336 133.869 18.519 1.00 13.63 ? 189 ASP A CA 1 ATOM 1358 C C . ASP A 1 174 ? -29.014 133.733 19.881 1.00 12.50 ? 189 ASP A C 1 ATOM 1359 O O . ASP A 1 174 ? -28.351 133.755 20.910 1.00 14.21 ? 189 ASP A O 1 ATOM 1360 C CB . ASP A 1 174 ? -28.646 135.240 17.916 1.00 16.30 ? 189 ASP A CB 1 ATOM 1361 C CG . ASP A 1 174 ? -28.356 136.393 18.867 1.00 11.83 ? 189 ASP A CG 1 ATOM 1362 O OD1 . ASP A 1 174 ? -27.201 136.828 18.918 1.00 18.05 ? 189 ASP A OD1 1 ATOM 1363 O OD2 . ASP A 1 174 ? -29.297 136.851 19.560 1.00 18.99 ? 189 ASP A OD2 1 ATOM 1364 N N . ALA A 1 175 ? -30.340 133.606 19.891 1.00 12.95 ? 190 ALA A N 1 ATOM 1365 C CA . ALA A 1 175 ? -31.057 133.637 21.146 1.00 14.82 ? 190 ALA A CA 1 ATOM 1366 C C . ALA A 1 175 ? -30.584 132.559 22.112 1.00 14.10 ? 190 ALA A C 1 ATOM 1367 O O . ALA A 1 175 ? -30.354 132.833 23.300 1.00 15.88 ? 190 ALA A O 1 ATOM 1368 C CB . ALA A 1 175 ? -32.568 133.500 20.886 1.00 16.24 ? 190 ALA A CB 1 ATOM 1369 N N . SER A 1 176 ? -30.457 131.332 21.622 1.00 13.52 ? 191 SER A N 1 ATOM 1370 C CA . SER A 1 176 ? -30.014 130.250 22.493 1.00 16.39 ? 191 SER A CA 1 ATOM 1371 C C . SER A 1 176 ? -28.510 130.271 22.756 1.00 13.18 ? 191 SER A C 1 ATOM 1372 O O . SER A 1 176 ? -28.057 129.785 23.791 1.00 17.48 ? 191 SER A O 1 ATOM 1373 C CB . SER A 1 176 ? -30.424 128.886 21.935 1.00 16.56 ? 191 SER A CB 1 ATOM 1374 O OG . SER A 1 176 ? -31.844 128.717 21.974 1.00 19.73 ? 191 SER A OG 1 ATOM 1375 N N . GLY A 1 177 ? -27.734 130.780 21.796 1.00 13.87 ? 192 GLY A N 1 ATOM 1376 C CA . GLY A 1 177 ? -26.320 131.009 22.041 1.00 12.63 ? 192 GLY A CA 1 ATOM 1377 C C . GLY A 1 177 ? -26.086 131.919 23.228 1.00 12.73 ? 192 GLY A C 1 ATOM 1378 O O . GLY A 1 177 ? -25.132 131.702 23.994 1.00 14.60 ? 192 GLY A O 1 ATOM 1379 N N . HIS A 1 178 ? -26.937 132.937 23.390 1.00 13.27 ? 193 HIS A N 1 ATOM 1380 C CA . HIS A 1 178 ? -26.894 133.798 24.585 1.00 11.84 ? 193 HIS A CA 1 ATOM 1381 C C . HIS A 1 178 ? -27.230 133.010 25.847 1.00 14.45 ? 193 HIS A C 1 ATOM 1382 O O . HIS A 1 178 ? -26.569 133.156 26.876 1.00 15.95 ? 193 HIS A O 1 ATOM 1383 C CB . HIS A 1 178 ? -27.862 134.976 24.461 1.00 14.06 ? 193 HIS A CB 1 ATOM 1384 C CG . HIS A 1 178 ? -27.386 136.079 23.562 1.00 12.73 ? 193 HIS A CG 1 ATOM 1385 N ND1 . HIS A 1 178 ? -26.247 136.806 23.829 1.00 12.32 ? 193 HIS A ND1 1 ATOM 1386 C CD2 . HIS A 1 178 ? -27.897 136.585 22.413 1.00 16.54 ? 193 HIS A CD2 1 ATOM 1387 C CE1 . HIS A 1 178 ? -26.062 137.700 22.875 1.00 14.80 ? 193 HIS A CE1 1 ATOM 1388 N NE2 . HIS A 1 178 ? -27.066 137.608 22.016 1.00 11.89 ? 193 HIS A NE2 1 ATOM 1389 N N . LYS A 1 179 ? -28.269 132.179 25.762 1.00 13.29 ? 194 LYS A N 1 ATOM 1390 C CA . LYS A 1 179 ? -28.758 131.447 26.925 1.00 14.67 ? 194 LYS A CA 1 ATOM 1391 C C . LYS A 1 179 ? -27.764 130.398 27.448 1.00 15.84 ? 194 LYS A C 1 ATOM 1392 O O . LYS A 1 179 ? -27.478 130.332 28.645 1.00 19.76 ? 194 LYS A O 1 ATOM 1393 C CB . LYS A 1 179 ? -30.093 130.775 26.568 1.00 18.41 ? 194 LYS A CB 1 ATOM 1394 C CG . LYS A 1 179 ? -30.664 129.928 27.712 1.00 20.42 ? 194 LYS A CG 1 ATOM 1395 C CD . LYS A 1 179 ? -32.098 129.486 27.427 1.00 22.22 ? 194 LYS A CD 1 ATOM 1396 C CE . LYS A 1 179 ? -32.665 128.759 28.636 1.00 30.76 ? 194 LYS A CE 1 ATOM 1397 N NZ . LYS A 1 179 ? -34.056 128.318 28.385 1.00 40.00 ? 194 LYS A NZ 1 ATOM 1398 N N . TYR A 1 180 ? -27.229 129.588 26.541 1.00 17.80 ? 195 TYR A N 1 ATOM 1399 C CA . TYR A 1 180 ? -26.342 128.486 26.929 1.00 18.83 ? 195 TYR A CA 1 ATOM 1400 C C . TYR A 1 180 ? -24.851 128.818 26.865 1.00 16.52 ? 195 TYR A C 1 ATOM 1401 O O . TYR A 1 180 ? -24.069 128.275 27.649 1.00 23.61 ? 195 TYR A O 1 ATOM 1402 C CB . TYR A 1 180 ? -26.629 127.242 26.070 1.00 18.53 ? 195 TYR A CB 1 ATOM 1403 C CG . TYR A 1 180 ? -28.054 126.779 26.141 1.00 22.61 ? 195 TYR A CG 1 ATOM 1404 C CD1 . TYR A 1 180 ? -28.901 126.907 25.044 1.00 20.81 ? 195 TYR A CD1 1 ATOM 1405 C CD2 . TYR A 1 180 ? -28.553 126.191 27.299 1.00 22.32 ? 195 TYR A CD2 1 ATOM 1406 C CE1 . TYR A 1 180 ? -30.225 126.471 25.110 1.00 24.37 ? 195 TYR A CE1 1 ATOM 1407 C CE2 . TYR A 1 180 ? -29.862 125.764 27.374 1.00 23.87 ? 195 TYR A CE2 1 ATOM 1408 C CZ . TYR A 1 180 ? -30.692 125.898 26.280 1.00 26.69 ? 195 TYR A CZ 1 ATOM 1409 O OH . TYR A 1 180 ? -31.997 125.467 26.373 1.00 34.74 ? 195 TYR A OH 1 ATOM 1410 N N . GLY A 1 181 ? -24.467 129.718 25.959 1.00 17.49 ? 196 GLY A N 1 ATOM 1411 C CA . GLY A 1 181 ? -23.057 129.943 25.663 1.00 20.06 ? 196 GLY A CA 1 ATOM 1412 C C . GLY A 1 181 ? -22.595 128.951 24.610 1.00 15.04 ? 196 GLY A C 1 ATOM 1413 O O . GLY A 1 181 ? -23.027 127.793 24.600 1.00 18.13 ? 196 GLY A O 1 ATOM 1414 N N . PRO A 1 182 ? -21.710 129.386 23.708 1.00 18.98 ? 197 PRO A N 1 ATOM 1415 C CA . PRO A 1 182 ? -21.365 128.521 22.571 1.00 19.09 ? 197 PRO A CA 1 ATOM 1416 C C . PRO A 1 182 ? -20.564 127.307 23.001 1.00 23.91 ? 197 PRO A C 1 ATOM 1417 O O . PRO A 1 182 ? -20.442 126.357 22.232 1.00 26.69 ? 197 PRO A O 1 ATOM 1418 C CB . PRO A 1 182 ? -20.531 129.446 21.666 1.00 20.93 ? 197 PRO A CB 1 ATOM 1419 C CG . PRO A 1 182 ? -20.001 130.519 22.608 1.00 23.96 ? 197 PRO A CG 1 ATOM 1420 C CD . PRO A 1 182 ? -21.106 130.725 23.609 1.00 21.42 ? 197 PRO A CD 1 ATOM 1421 N N . GLU A 1 183 ? -20.053 127.309 24.226 1.00 24.03 ? 198 GLU A N 1 ATOM 1422 C CA . GLU A 1 183 ? -19.263 126.166 24.677 1.00 20.76 ? 198 GLU A CA 1 ATOM 1423 C C . GLU A 1 183 ? -20.102 125.030 25.237 1.00 22.88 ? 198 GLU A C 1 ATOM 1424 O O . GLU A 1 183 ? -19.596 123.932 25.463 1.00 27.76 ? 198 GLU A O 1 ATOM 1425 C CB . GLU A 1 183 ? -18.186 126.619 25.657 1.00 27.05 ? 198 GLU A CB 1 ATOM 1426 C CG . GLU A 1 183 ? -17.285 127.656 25.014 1.00 28.68 ? 198 GLU A CG 1 ATOM 1427 C CD . GLU A 1 183 ? -16.078 128.001 25.850 1.00 40.18 ? 198 GLU A CD 1 ATOM 1428 O OE1 . GLU A 1 183 ? -16.045 127.608 27.039 1.00 44.06 ? 198 GLU A OE1 1 ATOM 1429 O OE2 . GLU A 1 183 ? -15.162 128.668 25.315 1.00 42.21 ? 198 GLU A OE2 1 ATOM 1430 N N . ASP A 1 184 ? -21.389 125.283 25.434 1.00 19.86 ? 199 ASP A N 1 ATOM 1431 C CA . ASP A 1 184 ? -22.305 124.232 25.871 1.00 18.04 ? 199 ASP A CA 1 ATOM 1432 C C . ASP A 1 184 ? -22.699 123.396 24.667 1.00 24.64 ? 199 ASP A C 1 ATOM 1433 O O . ASP A 1 184 ? -23.730 123.653 24.023 1.00 18.91 ? 199 ASP A O 1 ATOM 1434 C CB . ASP A 1 184 ? -23.551 124.851 26.491 1.00 20.36 ? 199 ASP A CB 1 ATOM 1435 C CG . ASP A 1 184 ? -24.498 123.818 27.070 1.00 20.97 ? 199 ASP A CG 1 ATOM 1436 O OD1 . ASP A 1 184 ? -24.411 122.614 26.740 1.00 28.65 ? 199 ASP A OD1 1 ATOM 1437 O OD2 . ASP A 1 184 ? -25.376 124.220 27.857 1.00 24.12 ? 199 ASP A OD2 1 ATOM 1438 N N . LYS A 1 185 ? -21.878 122.406 24.350 1.00 25.94 ? 200 LYS A N 1 ATOM 1439 C CA . LYS A 1 185 ? -22.090 121.652 23.126 1.00 20.85 ? 200 LYS A CA 1 ATOM 1440 C C . LYS A 1 185 ? -23.347 120.785 23.145 1.00 22.44 ? 200 LYS A C 1 ATOM 1441 O O . LYS A 1 185 ? -23.978 120.599 22.097 1.00 21.86 ? 200 LYS A O 1 ATOM 1442 C CB . LYS A 1 185 ? -20.865 120.800 22.782 1.00 29.09 ? 200 LYS A CB 1 ATOM 1443 C CG . LYS A 1 185 ? -19.755 121.613 22.149 1.00 40.70 ? 200 LYS A CG 1 ATOM 1444 C CD . LYS A 1 185 ? -18.641 120.755 21.599 1.00 45.40 ? 200 LYS A CD 1 ATOM 1445 C CE . LYS A 1 185 ? -17.351 121.568 21.556 1.00 52.82 ? 200 LYS A CE 1 ATOM 1446 N NZ . LYS A 1 185 ? -16.192 120.810 21.007 1.00 60.40 ? 200 LYS A NZ 1 ATOM 1447 N N . GLU A 1 186 ? -23.711 120.238 24.304 1.00 23.49 ? 201 GLU A N 1 ATOM 1448 C CA . GLU A 1 186 ? -24.940 119.457 24.358 1.00 27.95 ? 201 GLU A CA 1 ATOM 1449 C C . GLU A 1 186 ? -26.150 120.272 23.939 1.00 26.87 ? 201 GLU A C 1 ATOM 1450 O O . GLU A 1 186 ? -26.950 119.837 23.097 1.00 28.25 ? 201 GLU A O 1 ATOM 1451 C CB . GLU A 1 186 ? -25.202 118.856 25.740 1.00 29.09 ? 201 GLU A CB 1 ATOM 1452 C CG . GLU A 1 186 ? -26.549 118.135 25.757 1.00 41.98 ? 201 GLU A CG 1 ATOM 1453 C CD . GLU A 1 186 ? -26.919 117.542 27.092 1.00 46.54 ? 201 GLU A CD 1 ATOM 1454 O OE1 . GLU A 1 186 ? -26.272 117.879 28.108 1.00 55.62 ? 201 GLU A OE1 1 ATOM 1455 O OE2 . GLU A 1 186 ? -27.874 116.736 27.120 1.00 46.96 ? 201 GLU A OE2 1 ATOM 1456 N N . ASN A 1 187 ? -26.297 121.451 24.528 1.00 24.60 ? 202 ASN A N 1 ATOM 1457 C CA . ASN A 1 187 ? -27.456 122.270 24.209 1.00 21.17 ? 202 ASN A CA 1 ATOM 1458 C C . ASN A 1 187 ? -27.346 122.970 22.874 1.00 21.12 ? 202 ASN A C 1 ATOM 1459 O O . ASN A 1 187 ? -28.331 123.049 22.159 1.00 21.81 ? 202 ASN A O 1 ATOM 1460 C CB . ASN A 1 187 ? -27.781 123.243 25.339 1.00 22.26 ? 202 ASN A CB 1 ATOM 1461 C CG . ASN A 1 187 ? -28.396 122.541 26.530 1.00 27.23 ? 202 ASN A CG 1 ATOM 1462 O OD1 . ASN A 1 187 ? -29.466 121.933 26.426 1.00 27.09 ? 202 ASN A OD1 1 ATOM 1463 N ND2 . ASN A 1 187 ? -27.721 122.598 27.667 1.00 23.12 ? 202 ASN A ND2 1 ATOM 1464 N N . MET A 1 188 ? -26.155 123.460 22.519 1.00 18.65 ? 203 MET A N 1 ATOM 1465 C CA . MET A 1 188 ? -26.023 124.144 21.234 1.00 20.34 ? 203 MET A CA 1 ATOM 1466 C C . MET A 1 188 ? -26.219 123.184 20.073 1.00 25.00 ? 203 MET A C 1 ATOM 1467 O O . MET A 1 188 ? -26.694 123.570 19.001 1.00 20.44 ? 203 MET A O 1 ATOM 1468 C CB . MET A 1 188 ? -24.675 124.876 21.109 1.00 19.14 ? 203 MET A CB 1 ATOM 1469 C CG . MET A 1 188 ? -24.534 126.156 21.933 1.00 19.42 ? 203 MET A CG 1 ATOM 1470 S SD . MET A 1 188 ? -25.920 127.284 21.696 1.00 20.99 ? 203 MET A SD 1 ATOM 1471 C CE . MET A 1 188 ? -25.727 127.723 19.953 1.00 22.40 ? 203 MET A CE 1 ATOM 1472 N N . SER A 1 189 ? -25.881 121.920 20.278 1.00 17.89 ? 204 SER A N 1 ATOM 1473 C CA . SER A 1 189 ? -26.063 120.956 19.182 1.00 18.37 ? 204 SER A CA 1 ATOM 1474 C C . SER A 1 189 ? -27.527 120.796 18.777 1.00 20.73 ? 204 SER A C 1 ATOM 1475 O O . SER A 1 189 ? -27.834 120.590 17.587 1.00 23.32 ? 204 SER A O 1 ATOM 1476 C CB . SER A 1 189 ? -25.435 119.588 19.495 1.00 19.51 ? 204 SER A CB 1 ATOM 1477 O OG . SER A 1 189 ? -26.141 118.930 20.546 1.00 25.05 ? 204 SER A OG 1 ATOM 1478 N N . ARG A 1 190 ? -28.423 120.871 19.756 1.00 20.48 ? 205 ARG A N 1 ATOM 1479 C CA . ARG A 1 190 ? -29.855 120.764 19.477 1.00 18.74 ? 205 ARG A CA 1 ATOM 1480 C C . ARG A 1 190 ? -30.357 122.042 18.819 1.00 23.47 ? 205 ARG A C 1 ATOM 1481 O O . ARG A 1 190 ? -31.172 121.990 17.911 1.00 21.73 ? 205 ARG A O 1 ATOM 1482 C CB . ARG A 1 190 ? -30.625 120.460 20.766 1.00 24.44 ? 205 ARG A CB 1 ATOM 1483 C CG . ARG A 1 190 ? -30.085 119.222 21.439 1.00 24.79 ? 205 ARG A CG 1 ATOM 1484 C CD . ARG A 1 190 ? -31.078 118.586 22.368 1.00 30.14 ? 205 ARG A CD 1 ATOM 1485 N NE . ARG A 1 190 ? -30.526 117.351 22.914 1.00 31.49 ? 205 ARG A NE 1 ATOM 1486 C CZ . ARG A 1 190 ? -30.050 117.226 24.146 1.00 30.80 ? 205 ARG A CZ 1 ATOM 1487 N NH1 . ARG A 1 190 ? -29.559 116.058 24.554 1.00 30.03 ? 205 ARG A NH1 1 ATOM 1488 N NH2 . ARG A 1 190 ? -30.078 118.263 24.975 1.00 35.50 ? 205 ARG A NH2 1 ATOM 1489 N N . VAL A 1 191 ? -29.856 123.186 19.275 1.00 20.60 ? 206 VAL A N 1 ATOM 1490 C CA . VAL A 1 191 ? -30.162 124.461 18.645 1.00 18.79 ? 206 VAL A CA 1 ATOM 1491 C C . VAL A 1 191 ? -29.760 124.447 17.176 1.00 19.26 ? 206 VAL A C 1 ATOM 1492 O O . VAL A 1 191 ? -30.528 124.828 16.297 1.00 19.83 ? 206 VAL A O 1 ATOM 1493 C CB . VAL A 1 191 ? -29.386 125.584 19.351 1.00 17.72 ? 206 VAL A CB 1 ATOM 1494 C CG1 . VAL A 1 191 ? -29.604 126.938 18.650 1.00 20.82 ? 206 VAL A CG1 1 ATOM 1495 C CG2 . VAL A 1 191 ? -29.804 125.679 20.807 1.00 19.44 ? 206 VAL A CG2 1 ATOM 1496 N N . LEU A 1 192 ? -28.526 124.037 16.908 1.00 17.01 ? 207 LEU A N 1 ATOM 1497 C CA . LEU A 1 192 ? -28.003 124.102 15.559 1.00 18.57 ? 207 LEU A CA 1 ATOM 1498 C C . LEU A 1 192 ? -28.568 123.029 14.645 1.00 20.60 ? 207 LEU A C 1 ATOM 1499 O O . LEU A 1 192 ? -28.617 123.205 13.434 1.00 20.75 ? 207 LEU A O 1 ATOM 1500 C CB . LEU A 1 192 ? -26.470 124.038 15.586 1.00 19.83 ? 207 LEU A CB 1 ATOM 1501 C CG . LEU A 1 192 ? -25.880 125.263 16.254 1.00 16.37 ? 207 LEU A CG 1 ATOM 1502 C CD1 . LEU A 1 192 ? -24.409 125.046 16.546 1.00 18.98 ? 207 LEU A CD1 1 ATOM 1503 C CD2 . LEU A 1 192 ? -26.081 126.474 15.349 1.00 19.86 ? 207 LEU A CD2 1 ATOM 1504 N N . LYS A 1 193 ? -28.971 121.904 15.216 1.00 22.22 ? 208 LYS A N 1 ATOM 1505 C CA . LYS A 1 193 ? -29.625 120.880 14.415 1.00 21.91 ? 208 LYS A CA 1 ATOM 1506 C C . LYS A 1 193 ? -30.940 121.436 13.892 1.00 24.79 ? 208 LYS A C 1 ATOM 1507 O O . LYS A 1 193 ? -31.322 121.198 12.736 1.00 26.03 ? 208 LYS A O 1 ATOM 1508 C CB . LYS A 1 193 ? -29.921 119.662 15.287 1.00 28.81 ? 208 LYS A CB 1 ATOM 1509 C CG . LYS A 1 193 ? -30.692 118.574 14.586 1.00 38.02 ? 208 LYS A CG 1 ATOM 1510 C CD . LYS A 1 193 ? -29.764 117.850 13.657 1.00 42.86 ? 208 LYS A CD 1 ATOM 1511 C CE . LYS A 1 193 ? -30.421 116.658 12.998 1.00 44.38 ? 208 LYS A CE 1 ATOM 1512 N NZ . LYS A 1 193 ? -29.394 115.981 12.143 1.00 44.68 ? 208 LYS A NZ 1 ATOM 1513 N N . LYS A 1 194 ? -31.647 122.163 14.756 1.00 21.26 ? 209 LYS A N 1 ATOM 1514 C CA . LYS A 1 194 ? -32.891 122.805 14.350 1.00 22.84 ? 209 LYS A CA 1 ATOM 1515 C C . LYS A 1 194 ? -32.644 123.798 13.213 1.00 19.83 ? 209 LYS A C 1 ATOM 1516 O O . LYS A 1 194 ? -33.445 123.874 12.280 1.00 23.13 ? 209 LYS A O 1 ATOM 1517 C CB . LYS A 1 194 ? -33.562 123.520 15.521 1.00 22.34 ? 209 LYS A CB 1 ATOM 1518 C CG . LYS A 1 194 ? -34.114 122.610 16.573 1.00 30.17 ? 209 LYS A CG 1 ATOM 1519 C CD . LYS A 1 194 ? -34.692 123.431 17.716 1.00 29.39 ? 209 LYS A CD 1 ATOM 1520 C CE . LYS A 1 194 ? -34.925 122.569 18.940 1.00 40.63 ? 209 LYS A CE 1 ATOM 1521 N NZ . LYS A 1 194 ? -35.621 123.347 20.013 1.00 45.04 ? 209 LYS A NZ 1 ATOM 1522 N N . ILE A 1 195 ? -31.553 124.565 13.287 1.00 19.21 ? 210 ILE A N 1 ATOM 1523 C CA . ILE A 1 195 ? -31.190 125.448 12.193 1.00 19.62 ? 210 ILE A CA 1 ATOM 1524 C C . ILE A 1 195 ? -30.938 124.679 10.898 1.00 23.96 ? 210 ILE A C 1 ATOM 1525 O O . ILE A 1 195 ? -31.414 125.080 9.828 1.00 22.51 ? 210 ILE A O 1 ATOM 1526 C CB . ILE A 1 195 ? -29.939 126.285 12.535 1.00 18.20 ? 210 ILE A CB 1 ATOM 1527 C CG1 . ILE A 1 195 ? -30.182 127.094 13.806 1.00 19.51 ? 210 ILE A CG1 1 ATOM 1528 C CG2 . ILE A 1 195 ? -29.538 127.157 11.335 1.00 20.78 ? 210 ILE A CG2 1 ATOM 1529 C CD1 . ILE A 1 195 ? -31.336 128.136 13.712 1.00 20.20 ? 210 ILE A CD1 1 ATOM 1530 N N . ASP A 1 196 ? -30.200 123.572 10.983 1.00 22.45 ? 211 ASP A N 1 ATOM 1531 C CA . ASP A 1 196 ? -29.968 122.769 9.785 1.00 25.29 ? 211 ASP A CA 1 ATOM 1532 C C . ASP A 1 196 ? -31.275 122.241 9.199 1.00 22.60 ? 211 ASP A C 1 ATOM 1533 O O . ASP A 1 196 ? -31.474 122.255 7.988 1.00 25.74 ? 211 ASP A O 1 ATOM 1534 C CB . ASP A 1 196 ? -29.013 121.612 10.060 1.00 22.16 ? 211 ASP A CB 1 ATOM 1535 C CG . ASP A 1 196 ? -28.532 120.966 8.790 1.00 29.02 ? 211 ASP A CG 1 ATOM 1536 O OD1 . ASP A 1 196 ? -27.846 121.649 8.003 1.00 22.65 ? 211 ASP A OD1 1 ATOM 1537 O OD2 . ASP A 1 196 ? -28.846 119.788 8.556 1.00 27.03 ? 211 ASP A OD2 1 ATOM 1538 N N . ASP A 1 197 ? -32.165 121.763 10.060 1.00 20.64 ? 212 ASP A N 1 ATOM 1539 C CA . ASP A 1 197 ? -33.505 121.369 9.611 1.00 25.07 ? 212 ASP A CA 1 ATOM 1540 C C . ASP A 1 197 ? -34.257 122.495 8.894 1.00 24.93 ? 212 ASP A C 1 ATOM 1541 O O . ASP A 1 197 ? -34.943 122.261 7.893 1.00 29.64 ? 212 ASP A O 1 ATOM 1542 C CB . ASP A 1 197 ? -34.351 120.836 10.775 1.00 29.78 ? 212 ASP A CB 1 ATOM 1543 C CG . ASP A 1 197 ? -33.800 119.550 11.359 1.00 36.35 ? 212 ASP A CG 1 ATOM 1544 O OD1 . ASP A 1 197 ? -32.956 118.911 10.691 1.00 30.08 ? 212 ASP A OD1 1 ATOM 1545 O OD2 . ASP A 1 197 ? -34.224 119.171 12.480 1.00 36.29 ? 212 ASP A OD2 1 ATOM 1546 N N . LEU A 1 198 ? -34.155 123.712 9.414 1.00 22.14 ? 213 LEU A N 1 ATOM 1547 C CA . LEU A 1 198 ? -34.809 124.842 8.773 1.00 19.79 ? 213 LEU A CA 1 ATOM 1548 C C . LEU A 1 198 ? -34.203 125.108 7.410 1.00 26.72 ? 213 LEU A C 1 ATOM 1549 O O . LEU A 1 198 ? -34.900 125.512 6.489 1.00 23.95 ? 213 LEU A O 1 ATOM 1550 C CB . LEU A 1 198 ? -34.678 126.096 9.628 1.00 19.80 ? 213 LEU A CB 1 ATOM 1551 C CG . LEU A 1 198 ? -35.420 126.046 10.968 1.00 23.68 ? 213 LEU A CG 1 ATOM 1552 C CD1 . LEU A 1 198 ? -35.325 127.389 11.741 1.00 19.70 ? 213 LEU A CD1 1 ATOM 1553 C CD2 . LEU A 1 198 ? -36.878 125.617 10.788 1.00 26.16 ? 213 LEU A CD2 1 ATOM 1554 N N . ILE A 1 199 ? -32.896 124.906 7.277 1.00 20.66 ? 214 ILE A N 1 ATOM 1555 C CA . ILE A 1 199 ? -32.251 125.099 5.980 1.00 23.22 ? 214 ILE A CA 1 ATOM 1556 C C . ILE A 1 199 ? -32.752 124.022 5.028 1.00 23.99 ? 214 ILE A C 1 ATOM 1557 O O . ILE A 1 199 ? -32.972 124.265 3.833 1.00 29.19 ? 214 ILE A O 1 ATOM 1558 C CB . ILE A 1 199 ? -30.718 125.050 6.107 1.00 21.58 ? 214 ILE A CB 1 ATOM 1559 C CG1 . ILE A 1 199 ? -30.235 126.289 6.846 1.00 23.51 ? 214 ILE A CG1 1 ATOM 1560 C CG2 . ILE A 1 199 ? -30.061 125.004 4.743 1.00 23.85 ? 214 ILE A CG2 1 ATOM 1561 C CD1 . ILE A 1 199 ? -28.820 126.199 7.367 1.00 26.24 ? 214 ILE A CD1 1 ATOM 1562 N N . GLY A 1 200 ? -32.970 122.834 5.578 1.00 29.49 ? 215 GLY A N 1 ATOM 1563 C CA . GLY A 1 200 ? -33.556 121.757 4.800 1.00 28.63 ? 215 GLY A CA 1 ATOM 1564 C C . GLY A 1 200 ? -34.944 122.133 4.329 1.00 28.86 ? 215 GLY A C 1 ATOM 1565 O O . GLY A 1 200 ? -35.302 121.877 3.169 1.00 31.73 ? 215 GLY A O 1 ATOM 1566 N N . ASP A 1 201 ? -35.730 122.737 5.221 1.00 29.86 ? 216 ASP A N 1 ATOM 1567 C CA . ASP A 1 201 ? -37.094 123.170 4.890 1.00 27.36 ? 216 ASP A CA 1 ATOM 1568 C C . ASP A 1 201 ? -37.065 124.219 3.792 1.00 29.05 ? 216 ASP A C 1 ATOM 1569 O O . ASP A 1 201 ? -37.929 124.241 2.904 1.00 27.63 ? 216 ASP A O 1 ATOM 1570 C CB . ASP A 1 201 ? -37.795 123.767 6.119 1.00 25.69 ? 216 ASP A CB 1 ATOM 1571 C CG . ASP A 1 201 ? -38.038 122.754 7.217 1.00 31.44 ? 216 ASP A CG 1 ATOM 1572 O OD1 . ASP A 1 201 ? -38.022 121.532 6.936 1.00 31.87 ? 216 ASP A OD1 1 ATOM 1573 O OD2 . ASP A 1 201 ? -38.265 123.192 8.367 1.00 32.00 ? 216 ASP A OD2 1 ATOM 1574 N N . LEU A 1 202 ? -36.068 125.090 3.859 1.00 30.04 ? 217 LEU A N 1 ATOM 1575 C CA . LEU A 1 202 ? -35.882 126.122 2.858 1.00 25.64 ? 217 LEU A CA 1 ATOM 1576 C C . LEU A 1 202 ? -35.617 125.492 1.499 1.00 28.36 ? 217 LEU A C 1 ATOM 1577 O O . LEU A 1 202 ? -36.277 125.832 0.524 1.00 29.32 ? 217 LEU A O 1 ATOM 1578 C CB . LEU A 1 202 ? -34.717 127.027 3.287 1.00 23.88 ? 217 LEU A CB 1 ATOM 1579 C CG . LEU A 1 202 ? -34.135 128.002 2.256 1.00 26.13 ? 217 LEU A CG 1 ATOM 1580 C CD1 . LEU A 1 202 ? -35.190 129.010 1.832 1.00 24.53 ? 217 LEU A CD1 1 ATOM 1581 C CD2 . LEU A 1 202 ? -32.895 128.692 2.838 1.00 27.95 ? 217 LEU A CD2 1 ATOM 1582 N N . VAL A 1 203 ? -34.670 124.558 1.438 1.00 22.30 ? 218 VAL A N 1 ATOM 1583 C CA . VAL A 1 203 ? -34.319 123.919 0.169 1.00 24.08 ? 218 VAL A CA 1 ATOM 1584 C C . VAL A 1 203 ? -35.490 123.094 -0.369 1.00 27.70 ? 218 VAL A C 1 ATOM 1585 O O . VAL A 1 203 ? -35.800 123.172 -1.558 1.00 30.37 ? 218 VAL A O 1 ATOM 1586 C CB . VAL A 1 203 ? -33.053 123.058 0.297 1.00 28.50 ? 218 VAL A CB 1 ATOM 1587 C CG1 . VAL A 1 203 ? -32.800 122.267 -0.984 1.00 27.43 ? 218 VAL A CG1 1 ATOM 1588 C CG2 . VAL A 1 203 ? -31.854 123.934 0.624 1.00 26.71 ? 218 VAL A CG2 1 ATOM 1589 N N . GLN A 1 204 ? -36.136 122.310 0.503 1.00 24.48 ? 219 GLN A N 1 ATOM 1590 C CA . GLN A 1 204 ? -37.313 121.506 0.119 1.00 27.27 ? 219 GLN A CA 1 ATOM 1591 C C . GLN A 1 204 ? -38.362 122.396 -0.520 1.00 25.07 ? 219 GLN A C 1 ATOM 1592 O O . GLN A 1 204 ? -38.971 122.056 -1.547 1.00 30.35 ? 219 GLN A O 1 ATOM 1593 C CB . GLN A 1 204 ? -37.936 120.835 1.359 1.00 36.28 ? 219 GLN A CB 1 ATOM 1594 C CG . GLN A 1 204 ? -37.155 119.667 1.981 1.00 50.78 ? 219 GLN A CG 1 ATOM 1595 C CD . GLN A 1 204 ? -37.711 119.235 3.358 1.00 63.15 ? 219 GLN A CD 1 ATOM 1596 O OE1 . GLN A 1 204 ? -38.907 119.385 3.639 1.00 69.51 ? 219 GLN A OE1 1 ATOM 1597 N NE2 . GLN A 1 204 ? -36.831 118.708 4.218 1.00 60.25 ? 219 GLN A NE2 1 ATOM 1598 N N . ARG A 1 205 ? -38.575 123.549 0.102 1.00 24.96 ? 220 ARG A N 1 ATOM 1599 C CA . ARG A 1 205 ? -39.590 124.496 -0.326 1.00 26.86 ? 220 ARG A CA 1 ATOM 1600 C C . ARG A 1 205 ? -39.250 125.094 -1.674 1.00 30.95 ? 220 ARG A C 1 ATOM 1601 O O . ARG A 1 205 ? -40.124 125.271 -2.515 1.00 29.96 ? 220 ARG A O 1 ATOM 1602 C CB . ARG A 1 205 ? -39.715 125.605 0.723 1.00 23.98 ? 220 ARG A CB 1 ATOM 1603 C CG . ARG A 1 205 ? -40.670 126.725 0.382 1.00 26.65 ? 220 ARG A CG 1 ATOM 1604 C CD . ARG A 1 205 ? -42.093 126.242 0.222 1.00 29.43 ? 220 ARG A CD 1 ATOM 1605 N NE . ARG A 1 205 ? -42.970 127.399 0.098 1.00 25.59 ? 220 ARG A NE 1 ATOM 1606 C CZ . ARG A 1 205 ? -44.297 127.351 0.098 1.00 28.52 ? 220 ARG A CZ 1 ATOM 1607 N NH1 . ARG A 1 205 ? -44.939 126.190 0.248 1.00 41.77 ? 220 ARG A NH1 1 ATOM 1608 N NH2 . ARG A 1 205 ? -44.977 128.479 -0.013 1.00 29.74 ? 220 ARG A NH2 1 ATOM 1609 N N . LEU A 1 206 ? -37.977 125.412 -1.879 1.00 25.82 ? 221 LEU A N 1 ATOM 1610 C CA . LEU A 1 206 ? -37.532 125.953 -3.159 1.00 25.48 ? 221 LEU A CA 1 ATOM 1611 C C . LEU A 1 206 ? -37.706 124.919 -4.256 1.00 23.51 ? 221 LEU A C 1 ATOM 1612 O O . LEU A 1 206 ? -38.134 125.252 -5.368 1.00 31.74 ? 221 LEU A O 1 ATOM 1613 C CB . LEU A 1 206 ? -36.078 126.417 -3.080 1.00 26.67 ? 221 LEU A CB 1 ATOM 1614 C CG . LEU A 1 206 ? -35.897 127.592 -2.109 1.00 25.97 ? 221 LEU A CG 1 ATOM 1615 C CD1 . LEU A 1 206 ? -34.449 128.003 -2.033 1.00 28.53 ? 221 LEU A CD1 1 ATOM 1616 C CD2 . LEU A 1 206 ? -36.781 128.787 -2.497 1.00 23.93 ? 221 LEU A CD2 1 ATOM 1617 N N . LYS A 1 207 ? -37.383 123.664 -3.942 1.00 27.18 ? 222 LYS A N 1 ATOM 1618 C CA . LYS A 1 207 ? -37.532 122.588 -4.921 1.00 21.07 ? 222 LYS A CA 1 ATOM 1619 C C . LYS A 1 207 ? -39.000 122.351 -5.253 1.00 26.87 ? 222 LYS A C 1 ATOM 1620 O O . LYS A 1 207 ? -39.349 122.163 -6.423 1.00 32.50 ? 222 LYS A O 1 ATOM 1621 C CB . LYS A 1 207 ? -36.876 121.290 -4.421 1.00 27.94 ? 222 LYS A CB 1 ATOM 1622 C CG . LYS A 1 207 ? -35.345 121.327 -4.458 1.00 27.90 ? 222 LYS A CG 1 ATOM 1623 C CD . LYS A 1 207 ? -34.754 120.073 -3.853 1.00 33.71 ? 222 LYS A CD 1 ATOM 1624 C CE . LYS A 1 207 ? -33.244 120.031 -3.998 1.00 32.45 ? 222 LYS A CE 1 ATOM 1625 N NZ . LYS A 1 207 ? -32.682 118.923 -3.167 1.00 42.90 ? 222 LYS A NZ 1 ATOM 1626 N N . MET A 1 208 ? -39.854 122.367 -4.228 1.00 29.37 ? 223 MET A N 1 ATOM 1627 C CA . MET A 1 208 ? -41.304 122.169 -4.415 1.00 35.72 ? 223 MET A CA 1 ATOM 1628 C C . MET A 1 208 ? -41.885 123.189 -5.380 1.00 30.63 ? 223 MET A C 1 ATOM 1629 O O . MET A 1 208 ? -42.642 122.841 -6.300 1.00 34.70 ? 223 MET A O 1 ATOM 1630 C CB . MET A 1 208 ? -42.032 122.320 -3.077 1.00 39.02 ? 223 MET A CB 1 ATOM 1631 C CG . MET A 1 208 ? -42.673 121.079 -2.537 1.00 52.42 ? 223 MET A CG 1 ATOM 1632 S SD . MET A 1 208 ? -42.444 121.080 -0.741 1.00 74.18 ? 223 MET A SD 1 ATOM 1633 C CE . MET A 1 208 ? -42.963 122.744 -0.303 1.00 56.03 ? 223 MET A CE 1 ATOM 1634 N N . LEU A 1 209 ? -41.541 124.455 -5.152 1.00 34.92 ? 224 LEU A N 1 ATOM 1635 C CA . LEU A 1 209 ? -42.049 125.557 -5.967 1.00 27.56 ? 224 LEU A CA 1 ATOM 1636 C C . LEU A 1 209 ? -41.316 125.760 -7.293 1.00 32.82 ? 224 LEU A C 1 ATOM 1637 O O . LEU A 1 209 ? -41.665 126.660 -8.055 1.00 38.94 ? 224 LEU A O 1 ATOM 1638 C CB . LEU A 1 209 ? -42.013 126.868 -5.188 1.00 33.24 ? 224 LEU A CB 1 ATOM 1639 C CG . LEU A 1 209 ? -42.757 126.960 -3.863 1.00 36.58 ? 224 LEU A CG 1 ATOM 1640 C CD1 . LEU A 1 209 ? -42.661 128.395 -3.343 1.00 37.22 ? 224 LEU A CD1 1 ATOM 1641 C CD2 . LEU A 1 209 ? -44.189 126.534 -4.017 1.00 37.58 ? 224 LEU A CD2 1 ATOM 1642 N N . GLY A 1 210 ? -40.291 124.952 -7.557 1.00 32.66 ? 225 GLY A N 1 ATOM 1643 C CA . GLY A 1 210 ? -39.522 125.077 -8.792 1.00 36.42 ? 225 GLY A CA 1 ATOM 1644 C C . GLY A 1 210 ? -38.617 126.299 -8.832 1.00 31.38 ? 225 GLY A C 1 ATOM 1645 O O . GLY A 1 210 ? -38.357 126.869 -9.899 1.00 36.31 ? 225 GLY A O 1 ATOM 1646 N N . LEU A 1 211 ? -38.141 126.713 -7.663 1.00 31.89 ? 226 LEU A N 1 ATOM 1647 C CA . LEU A 1 211 ? -37.290 127.894 -7.558 1.00 30.50 ? 226 LEU A CA 1 ATOM 1648 C C . LEU A 1 211 ? -35.845 127.501 -7.411 1.00 25.27 ? 226 LEU A C 1 ATOM 1649 O O . LEU A 1 211 ? -34.945 128.317 -7.634 1.00 31.09 ? 226 LEU A O 1 ATOM 1650 C CB . LEU A 1 211 ? -37.687 128.717 -6.336 1.00 32.86 ? 226 LEU A CB 1 ATOM 1651 C CG . LEU A 1 211 ? -38.869 129.658 -6.543 1.00 30.19 ? 226 LEU A CG 1 ATOM 1652 C CD1 . LEU A 1 211 ? -39.395 130.159 -5.191 1.00 32.12 ? 226 LEU A CD1 1 ATOM 1653 C CD2 . LEU A 1 211 ? -38.472 130.817 -7.450 1.00 38.84 ? 226 LEU A CD2 1 ATOM 1654 N N . TRP A 1 212 ? -35.621 126.247 -7.033 1.00 28.44 ? 227 TRP A N 1 ATOM 1655 C CA . TRP A 1 212 ? -34.297 125.821 -6.582 1.00 26.86 ? 227 TRP A CA 1 ATOM 1656 C C . TRP A 1 212 ? -33.213 126.065 -7.630 1.00 29.49 ? 227 TRP A C 1 ATOM 1657 O O . TRP A 1 212 ? -32.108 126.502 -7.301 1.00 32.78 ? 227 TRP A O 1 ATOM 1658 C CB . TRP A 1 212 ? -34.327 124.352 -6.171 1.00 24.77 ? 227 TRP A CB 1 ATOM 1659 C CG . TRP A 1 212 ? -32.990 123.820 -5.809 1.00 29.61 ? 227 TRP A CG 1 ATOM 1660 C CD1 . TRP A 1 212 ? -32.314 122.818 -6.435 1.00 29.23 ? 227 TRP A CD1 1 ATOM 1661 C CD2 . TRP A 1 212 ? -32.147 124.276 -4.749 1.00 26.10 ? 227 TRP A CD2 1 ATOM 1662 N NE1 . TRP A 1 212 ? -31.108 122.605 -5.823 1.00 31.09 ? 227 TRP A NE1 1 ATOM 1663 C CE2 . TRP A 1 212 ? -30.979 123.487 -4.783 1.00 27.43 ? 227 TRP A CE2 1 ATOM 1664 C CE3 . TRP A 1 212 ? -32.269 125.269 -3.761 1.00 24.35 ? 227 TRP A CE3 1 ATOM 1665 C CZ2 . TRP A 1 212 ? -29.939 123.656 -3.877 1.00 32.88 ? 227 TRP A CZ2 1 ATOM 1666 C CZ3 . TRP A 1 212 ? -31.228 125.436 -2.865 1.00 25.32 ? 227 TRP A CZ3 1 ATOM 1667 C CH2 . TRP A 1 212 ? -30.080 124.636 -2.930 1.00 29.30 ? 227 TRP A CH2 1 ATOM 1668 N N . GLU A 1 213 ? -33.521 125.806 -8.898 1.00 34.86 ? 228 GLU A N 1 ATOM 1669 C CA . GLU A 1 213 ? -32.503 125.972 -9.940 1.00 33.45 ? 228 GLU A CA 1 ATOM 1670 C C . GLU A 1 213 ? -32.290 127.405 -10.455 1.00 35.38 ? 228 GLU A C 1 ATOM 1671 O O . GLU A 1 213 ? -31.202 127.718 -10.950 1.00 41.89 ? 228 GLU A O 1 ATOM 1672 C CB . GLU A 1 213 ? -32.765 124.997 -11.088 1.00 36.79 ? 228 GLU A CB 1 ATOM 1673 C CG . GLU A 1 213 ? -32.204 123.600 -10.825 1.00 52.10 ? 228 GLU A CG 1 ATOM 1674 C CD . GLU A 1 213 ? -32.883 122.522 -11.657 1.00 68.21 ? 228 GLU A CD 1 ATOM 1675 O OE1 . GLU A 1 213 ? -33.607 122.872 -12.618 1.00 72.84 ? 228 GLU A OE1 1 ATOM 1676 O OE2 . GLU A 1 213 ? -32.700 121.322 -11.342 1.00 73.06 ? 228 GLU A OE2 1 ATOM 1677 N N . ASN A 1 214 ? -33.297 128.275 -10.335 1.00 30.56 ? 229 ASN A N 1 ATOM 1678 C CA . ASN A 1 214 ? -33.204 129.626 -10.917 1.00 28.58 ? 229 ASN A CA 1 ATOM 1679 C C . ASN A 1 214 ? -33.069 130.781 -9.933 1.00 30.13 ? 229 ASN A C 1 ATOM 1680 O O . ASN A 1 214 ? -32.709 131.892 -10.323 1.00 33.26 ? 229 ASN A O 1 ATOM 1681 C CB . ASN A 1 214 ? -34.389 129.917 -11.847 1.00 39.49 ? 229 ASN A CB 1 ATOM 1682 C CG . ASN A 1 214 ? -34.433 128.993 -13.041 1.00 50.38 ? 229 ASN A CG 1 ATOM 1683 O OD1 . ASN A 1 214 ? -35.510 128.586 -13.490 1.00 56.96 ? 229 ASN A OD1 1 ATOM 1684 N ND2 . ASN A 1 214 ? -33.260 128.641 -13.559 1.00 52.54 ? 229 ASN A ND2 1 ATOM 1685 N N . LEU A 1 215 ? -33.369 130.527 -8.668 1.00 29.94 ? 230 LEU A N 1 ATOM 1686 C CA . LEU A 1 215 ? -33.252 131.548 -7.631 1.00 26.80 ? 230 LEU A CA 1 ATOM 1687 C C . LEU A 1 215 ? -31.843 131.567 -7.026 1.00 23.46 ? 230 LEU A C 1 ATOM 1688 O O . LEU A 1 215 ? -31.291 130.516 -6.680 1.00 28.11 ? 230 LEU A O 1 ATOM 1689 C CB . LEU A 1 215 ? -34.292 131.299 -6.526 1.00 22.61 ? 230 LEU A CB 1 ATOM 1690 C CG . LEU A 1 215 ? -34.216 132.243 -5.316 1.00 23.23 ? 230 LEU A CG 1 ATOM 1691 C CD1 . LEU A 1 215 ? -34.617 133.650 -5.705 1.00 24.46 ? 230 LEU A CD1 1 ATOM 1692 C CD2 . LEU A 1 215 ? -35.111 131.736 -4.180 1.00 26.19 ? 230 LEU A CD2 1 ATOM 1693 N N . ASN A 1 216 ? -31.263 132.763 -6.927 1.00 21.67 ? 231 ASN A N 1 ATOM 1694 C CA . ASN A 1 216 ? -30.019 132.943 -6.170 1.00 20.15 ? 231 ASN A CA 1 ATOM 1695 C C . ASN A 1 216 ? -30.355 133.069 -4.697 1.00 24.39 ? 231 ASN A C 1 ATOM 1696 O O . ASN A 1 216 ? -31.217 133.873 -4.327 1.00 21.83 ? 231 ASN A O 1 ATOM 1697 C CB . ASN A 1 216 ? -29.275 134.173 -6.667 1.00 21.77 ? 231 ASN A CB 1 ATOM 1698 C CG . ASN A 1 216 ? -28.838 134.022 -8.100 1.00 18.77 ? 231 ASN A CG 1 ATOM 1699 O OD1 . ASN A 1 216 ? -27.979 133.194 -8.397 1.00 23.67 ? 231 ASN A OD1 1 ATOM 1700 N ND2 . ASN A 1 216 ? -29.446 134.786 -9.010 1.00 28.93 ? 231 ASN A ND2 1 ATOM 1701 N N . VAL A 1 217 ? -29.713 132.242 -3.870 1.00 20.78 ? 232 VAL A N 1 ATOM 1702 C CA . VAL A 1 217 ? -29.957 132.248 -2.425 1.00 18.83 ? 232 VAL A CA 1 ATOM 1703 C C . VAL A 1 217 ? -28.654 132.410 -1.667 1.00 17.82 ? 232 VAL A C 1 ATOM 1704 O O . VAL A 1 217 ? -27.720 131.650 -1.878 1.00 21.30 ? 232 VAL A O 1 ATOM 1705 C CB . VAL A 1 217 ? -30.599 130.931 -1.977 1.00 18.87 ? 232 VAL A CB 1 ATOM 1706 C CG1 . VAL A 1 217 ? -30.894 130.971 -0.489 1.00 22.22 ? 232 VAL A CG1 1 ATOM 1707 C CG2 . VAL A 1 217 ? -31.889 130.685 -2.747 1.00 23.41 ? 232 VAL A CG2 1 ATOM 1708 N N . ILE A 1 218 ? -28.604 133.391 -0.765 1.00 17.65 ? 233 ILE A N 1 ATOM 1709 C CA . ILE A 1 218 ? -27.458 133.572 0.129 1.00 16.20 ? 233 ILE A CA 1 ATOM 1710 C C . ILE A 1 218 ? -27.942 133.272 1.522 1.00 21.89 ? 233 ILE A C 1 ATOM 1711 O O . ILE A 1 218 ? -28.966 133.810 1.950 1.00 19.90 ? 233 ILE A O 1 ATOM 1712 C CB . ILE A 1 218 ? -26.938 135.020 0.090 1.00 16.85 ? 233 ILE A CB 1 ATOM 1713 C CG1 . ILE A 1 218 ? -26.341 135.329 -1.287 1.00 16.87 ? 233 ILE A CG1 1 ATOM 1714 C CG2 . ILE A 1 218 ? -25.889 135.238 1.190 1.00 16.91 ? 233 ILE A CG2 1 ATOM 1715 C CD1 . ILE A 1 218 ? -26.121 136.814 -1.533 1.00 19.01 ? 233 ILE A CD1 1 ATOM 1716 N N . ILE A 1 219 ? -27.244 132.366 2.203 1.00 18.68 ? 234 ILE A N 1 ATOM 1717 C CA . ILE A 1 219 ? -27.497 132.077 3.609 1.00 15.52 ? 234 ILE A CA 1 ATOM 1718 C C . ILE A 1 219 ? -26.292 132.610 4.357 1.00 15.92 ? 234 ILE A C 1 ATOM 1719 O O . ILE A 1 219 ? -25.150 132.215 4.087 1.00 16.82 ? 234 ILE A O 1 ATOM 1720 C CB . ILE A 1 219 ? -27.633 130.544 3.877 1.00 15.21 ? 234 ILE A CB 1 ATOM 1721 C CG1 . ILE A 1 219 ? -28.825 129.964 3.100 1.00 16.36 ? 234 ILE A CG1 1 ATOM 1722 C CG2 . ILE A 1 219 ? -27.845 130.267 5.376 1.00 18.97 ? 234 ILE A CG2 1 ATOM 1723 C CD1 . ILE A 1 219 ? -28.964 128.434 3.229 1.00 20.17 ? 234 ILE A CD1 1 ATOM 1724 N N . THR A 1 220 ? -26.522 133.509 5.309 1.00 13.95 ? 235 THR A N 1 ATOM 1725 C CA . THR A 1 220 ? -25.402 134.115 6.021 1.00 15.94 ? 235 THR A CA 1 ATOM 1726 C C . THR A 1 220 ? -25.864 134.502 7.434 1.00 15.73 ? 235 THR A C 1 ATOM 1727 O O . THR A 1 220 ? -26.911 134.015 7.925 1.00 15.23 ? 235 THR A O 1 ATOM 1728 C CB . THR A 1 220 ? -24.811 135.300 5.212 1.00 15.88 ? 235 THR A CB 1 ATOM 1729 O OG1 . THR A 1 220 ? -23.554 135.721 5.772 1.00 15.38 ? 235 THR A OG1 1 ATOM 1730 C CG2 . THR A 1 220 ? -25.750 136.474 5.145 1.00 16.06 ? 235 THR A CG2 1 ATOM 1731 N N . SER A 1 221 ? -25.082 135.333 8.113 1.00 14.22 ? 236 SER A N 1 ATOM 1732 C CA . SER A 1 221 ? -25.444 135.780 9.458 1.00 11.52 ? 236 SER A CA 1 ATOM 1733 C C . SER A 1 221 ? -24.731 137.098 9.758 1.00 16.02 ? 236 SER A C 1 ATOM 1734 O O . SER A 1 221 ? -23.972 137.611 8.918 1.00 14.76 ? 236 SER A O 1 ATOM 1735 C CB . SER A 1 221 ? -25.093 134.692 10.478 1.00 12.05 ? 236 SER A CB 1 ATOM 1736 O OG . SER A 1 221 ? -25.515 135.051 11.790 1.00 13.78 ? 236 SER A OG 1 ATOM 1737 N N . ASP A 1 222 ? -24.949 137.639 10.944 1.00 16.12 ? 237 ASP A N 1 ATOM 1738 C CA . ASP A 1 222 ? -24.430 138.958 11.293 1.00 12.04 ? 237 ASP A CA 1 ATOM 1739 C C . ASP A 1 222 ? -23.172 138.918 12.167 1.00 12.98 ? 237 ASP A C 1 ATOM 1740 O O . ASP A 1 222 ? -22.351 139.826 12.106 1.00 14.63 ? 237 ASP A O 1 ATOM 1741 C CB . ASP A 1 222 ? -25.529 139.803 11.950 1.00 14.27 ? 237 ASP A CB 1 ATOM 1742 C CG . ASP A 1 222 ? -26.206 139.106 13.127 1.00 19.19 ? 237 ASP A CG 1 ATOM 1743 O OD1 . ASP A 1 222 ? -26.050 137.871 13.297 1.00 14.09 ? 237 ASP A OD1 1 ATOM 1744 O OD2 . ASP A 1 222 ? -26.906 139.823 13.892 1.00 11.78 ? 237 ASP A OD2 1 ATOM 1745 N N . HIS A 1 223 ? -23.024 137.867 12.966 1.00 11.35 ? 238 HIS A N 1 ATOM 1746 C CA . HIS A 1 223 ? -21.920 137.786 13.926 1.00 11.28 ? 238 HIS A CA 1 ATOM 1747 C C . HIS A 1 223 ? -21.961 136.406 14.569 1.00 13.39 ? 238 HIS A C 1 ATOM 1748 O O . HIS A 1 223 ? -22.882 135.626 14.338 1.00 13.14 ? 238 HIS A O 1 ATOM 1749 C CB . HIS A 1 223 ? -22.055 138.820 15.061 1.00 11.38 ? 238 HIS A CB 1 ATOM 1750 C CG . HIS A 1 223 ? -23.402 138.765 15.721 1.00 13.64 ? 238 HIS A CG 1 ATOM 1751 N ND1 . HIS A 1 223 ? -23.757 137.747 16.590 1.00 10.66 ? 238 HIS A ND1 1 ATOM 1752 C CD2 . HIS A 1 223 ? -24.495 139.552 15.582 1.00 18.36 ? 238 HIS A CD2 1 ATOM 1753 C CE1 . HIS A 1 223 ? -25.028 137.893 16.928 1.00 11.56 ? 238 HIS A CE1 1 ATOM 1754 N NE2 . HIS A 1 223 ? -25.500 138.987 16.341 1.00 11.05 ? 238 HIS A NE2 1 ATOM 1755 N N . GLY A 1 224 ? -20.949 136.116 15.373 1.00 15.37 ? 239 GLY A N 1 ATOM 1756 C CA . GLY A 1 224 ? -20.879 134.874 16.127 1.00 13.37 ? 239 GLY A CA 1 ATOM 1757 C C . GLY A 1 224 ? -21.264 135.046 17.587 1.00 10.76 ? 239 GLY A C 1 ATOM 1758 O O . GLY A 1 224 ? -22.244 135.745 17.908 1.00 12.86 ? 239 GLY A O 1 ATOM 1759 N N . MET A 1 225 ? -20.542 134.350 18.461 1.00 11.43 ? 240 MET A N 1 ATOM 1760 C CA . MET A 1 225 ? -20.896 134.300 19.875 1.00 14.03 ? 240 MET A CA 1 ATOM 1761 C C . MET A 1 225 ? -19.671 133.784 20.607 1.00 13.92 ? 240 MET A C 1 ATOM 1762 O O . MET A 1 225 ? -18.931 132.997 20.056 1.00 14.54 ? 240 MET A O 1 ATOM 1763 C CB . MET A 1 225 ? -22.067 133.335 20.085 1.00 16.15 ? 240 MET A CB 1 ATOM 1764 C CG . MET A 1 225 ? -22.759 133.379 21.453 1.00 13.41 ? 240 MET A CG 1 ATOM 1765 S SD . MET A 1 225 ? -23.726 134.862 21.773 1.00 12.86 ? 240 MET A SD 1 ATOM 1766 C CE . MET A 1 225 ? -25.011 134.677 20.526 1.00 13.27 ? 240 MET A CE 1 ATOM 1767 N N . THR A 1 226 ? -19.431 134.244 21.823 1.00 12.15 ? 241 THR A N 1 ATOM 1768 C CA . THR A 1 226 ? -18.310 133.753 22.612 1.00 14.96 ? 241 THR A CA 1 ATOM 1769 C C . THR A 1 226 ? -18.762 133.547 24.047 1.00 14.75 ? 241 THR A C 1 ATOM 1770 O O . THR A 1 226 ? -19.711 134.188 24.500 1.00 14.61 ? 241 THR A O 1 ATOM 1771 C CB . THR A 1 226 ? -17.079 134.666 22.483 1.00 17.24 ? 241 THR A CB 1 ATOM 1772 O OG1 . THR A 1 226 ? -15.884 133.967 22.878 1.00 16.44 ? 241 THR A OG1 1 ATOM 1773 C CG2 . THR A 1 226 ? -17.235 135.973 23.277 1.00 13.91 ? 241 THR A CG2 1 ATOM 1774 N N . GLN A 1 227 ? -18.082 132.658 24.761 1.00 13.85 ? 242 GLN A N 1 ATOM 1775 C CA . GLN A 1 227 ? -18.513 132.298 26.108 1.00 15.20 ? 242 GLN A CA 1 ATOM 1776 C C . GLN A 1 227 ? -18.186 133.395 27.122 1.00 13.94 ? 242 GLN A C 1 ATOM 1777 O O . GLN A 1 227 ? -17.078 133.947 27.132 1.00 14.34 ? 242 GLN A O 1 ATOM 1778 C CB . GLN A 1 227 ? -17.839 130.997 26.540 1.00 17.68 ? 242 GLN A CB 1 ATOM 1779 C CG . GLN A 1 227 ? -18.434 130.365 27.800 1.00 18.84 ? 242 GLN A CG 1 ATOM 1780 C CD . GLN A 1 227 ? -19.730 129.626 27.537 1.00 20.28 ? 242 GLN A CD 1 ATOM 1781 O OE1 . GLN A 1 227 ? -20.060 129.309 26.396 1.00 19.28 ? 242 GLN A OE1 1 ATOM 1782 N NE2 . GLN A 1 227 ? -20.472 129.337 28.599 1.00 23.11 ? 242 GLN A NE2 1 ATOM 1783 N N . CYS A 1 228 ? -19.128 133.646 28.020 1.00 14.71 ? 243 CYS A N 1 ATOM 1784 C CA . CYS A 1 228 ? -18.929 134.588 29.123 1.00 14.14 ? 243 CYS A CA 1 ATOM 1785 C C . CYS A 1 228 ? -18.949 133.821 30.428 1.00 15.38 ? 243 CYS A C 1 ATOM 1786 O O . CYS A 1 228 ? -19.280 132.621 30.452 1.00 19.16 ? 243 CYS A O 1 ATOM 1787 C CB . CYS A 1 228 ? -20.023 135.658 29.099 1.00 15.03 ? 243 CYS A CB 1 ATOM 1788 S SG . CYS A 1 228 ? -19.864 136.745 27.672 1.00 15.72 ? 243 CYS A SG 1 ATOM 1789 N N . SER A 1 229 ? -18.540 134.473 31.522 1.00 14.36 ? 244 SER A N 1 ATOM 1790 C CA . SER A 1 229 ? -18.315 133.750 32.773 1.00 14.40 ? 244 SER A CA 1 ATOM 1791 C C . SER A 1 229 ? -18.352 134.681 33.958 1.00 17.50 ? 244 SER A C 1 ATOM 1792 O O . SER A 1 229 ? -17.976 135.844 33.847 1.00 15.71 ? 244 SER A O 1 ATOM 1793 C CB . SER A 1 229 ? -16.928 133.110 32.725 1.00 18.74 ? 244 SER A CB 1 ATOM 1794 O OG . SER A 1 229 ? -16.595 132.515 33.968 1.00 21.65 ? 244 SER A OG 1 ATOM 1795 N N . GLN A 1 230 ? -18.771 134.156 35.105 1.00 16.77 ? 245 GLN A N 1 ATOM 1796 C CA . GLN A 1 230 ? -18.742 134.893 36.360 1.00 19.27 ? 245 GLN A CA 1 ATOM 1797 C C . GLN A 1 230 ? -17.332 135.283 36.787 1.00 17.82 ? 245 GLN A C 1 ATOM 1798 O O . GLN A 1 230 ? -17.162 136.198 37.600 1.00 20.26 ? 245 GLN A O 1 ATOM 1799 C CB . GLN A 1 230 ? -19.435 134.105 37.482 1.00 20.21 ? 245 GLN A CB 1 ATOM 1800 C CG . GLN A 1 230 ? -18.757 132.795 37.909 1.00 21.35 ? 245 GLN A CG 1 ATOM 1801 C CD . GLN A 1 230 ? -18.891 131.673 36.879 1.00 37.64 ? 245 GLN A CD 1 ATOM 1802 O OE1 . GLN A 1 230 ? -19.654 131.776 35.913 1.00 37.69 ? 245 GLN A OE1 1 ATOM 1803 N NE2 . GLN A 1 230 ? -18.142 130.591 37.088 1.00 43.68 ? 245 GLN A NE2 1 ATOM 1804 N N . ASP A 1 231 ? -16.328 134.619 36.208 1.00 18.42 ? 246 ASP A N 1 ATOM 1805 C CA . ASP A 1 231 ? -14.929 134.919 36.486 1.00 19.54 ? 246 ASP A CA 1 ATOM 1806 C C . ASP A 1 231 ? -14.387 136.031 35.616 1.00 17.37 ? 246 ASP A C 1 ATOM 1807 O O . ASP A 1 231 ? -13.210 136.425 35.760 1.00 20.83 ? 246 ASP A O 1 ATOM 1808 C CB . ASP A 1 231 ? -14.067 133.676 36.272 1.00 25.07 ? 246 ASP A CB 1 ATOM 1809 C CG . ASP A 1 231 ? -14.425 132.543 37.207 1.00 33.46 ? 246 ASP A CG 1 ATOM 1810 O OD1 . ASP A 1 231 ? -14.947 132.807 38.319 1.00 34.84 ? 246 ASP A OD1 1 ATOM 1811 O OD2 . ASP A 1 231 ? -14.172 131.379 36.828 1.00 39.67 ? 246 ASP A OD2 1 ATOM 1812 N N . ARG A 1 232 ? -15.229 136.517 34.704 1.00 16.97 ? 247 ARG A N 1 ATOM 1813 C CA . ARG A 1 232 ? -14.810 137.525 33.726 1.00 15.55 ? 247 ARG A CA 1 ATOM 1814 C C . ARG A 1 232 ? -15.788 138.684 33.662 1.00 17.46 ? 247 ARG A C 1 ATOM 1815 O O . ARG A 1 232 ? -16.388 138.965 32.604 1.00 13.71 ? 247 ARG A O 1 ATOM 1816 C CB . ARG A 1 232 ? -14.605 136.888 32.349 1.00 15.28 ? 247 ARG A CB 1 ATOM 1817 C CG . ARG A 1 232 ? -13.508 135.826 32.372 1.00 16.98 ? 247 ARG A CG 1 ATOM 1818 C CD . ARG A 1 232 ? -13.099 135.376 30.998 1.00 18.91 ? 247 ARG A CD 1 ATOM 1819 N NE . ARG A 1 232 ? -14.213 134.791 30.251 1.00 15.31 ? 247 ARG A NE 1 ATOM 1820 C CZ . ARG A 1 232 ? -14.516 133.494 30.228 1.00 18.04 ? 247 ARG A CZ 1 ATOM 1821 N NH1 . ARG A 1 232 ? -13.823 132.625 30.965 1.00 19.90 ? 247 ARG A NH1 1 ATOM 1822 N NH2 . ARG A 1 232 ? -15.544 133.075 29.481 1.00 16.75 ? 247 ARG A NH2 1 ATOM 1823 N N . LEU A 1 233 ? -15.962 139.353 34.796 1.00 17.34 ? 248 LEU A N 1 ATOM 1824 C CA . LEU A 1 233 ? -16.890 140.485 34.885 1.00 16.50 ? 248 LEU A CA 1 ATOM 1825 C C . LEU A 1 233 ? -16.159 141.755 35.264 1.00 16.52 ? 248 LEU A C 1 ATOM 1826 O O . LEU A 1 233 ? -15.215 141.730 36.076 1.00 19.43 ? 248 LEU A O 1 ATOM 1827 C CB . LEU A 1 233 ? -17.969 140.232 35.954 1.00 14.77 ? 248 LEU A CB 1 ATOM 1828 C CG . LEU A 1 233 ? -18.716 138.907 35.857 1.00 17.25 ? 248 LEU A CG 1 ATOM 1829 C CD1 . LEU A 1 233 ? -19.686 138.821 37.023 1.00 15.10 ? 248 LEU A CD1 1 ATOM 1830 C CD2 . LEU A 1 233 ? -19.462 138.796 34.508 1.00 14.43 ? 248 LEU A CD2 1 ATOM 1831 N N . ILE A 1 234 ? -16.603 142.851 34.666 1.00 13.85 ? 249 ILE A N 1 ATOM 1832 C CA . ILE A 1 234 ? -16.139 144.197 34.982 1.00 15.34 ? 249 ILE A CA 1 ATOM 1833 C C . ILE A 1 234 ? -17.352 144.977 35.465 1.00 18.37 ? 249 ILE A C 1 ATOM 1834 O O . ILE A 1 234 ? -18.242 145.294 34.666 1.00 16.86 ? 249 ILE A O 1 ATOM 1835 C CB . ILE A 1 234 ? -15.551 144.884 33.720 1.00 19.94 ? 249 ILE A CB 1 ATOM 1836 C CG1 . ILE A 1 234 ? -14.417 144.024 33.131 1.00 18.92 ? 249 ILE A CG1 1 ATOM 1837 C CG2 . ILE A 1 234 ? -15.101 146.327 34.033 1.00 22.96 ? 249 ILE A CG2 1 ATOM 1838 C CD1 . ILE A 1 234 ? -13.984 144.421 31.709 1.00 19.22 ? 249 ILE A CD1 1 ATOM 1839 N N . ASN A 1 235 ? -17.418 145.263 36.766 1.00 17.25 ? 250 ASN A N 1 ATOM 1840 C CA . ASN A 1 235 ? -18.586 145.959 37.326 1.00 17.21 ? 250 ASN A CA 1 ATOM 1841 C C . ASN A 1 235 ? -18.345 147.461 37.365 1.00 17.01 ? 250 ASN A C 1 ATOM 1842 O O . ASN A 1 235 ? -17.527 147.946 38.161 1.00 20.68 ? 250 ASN A O 1 ATOM 1843 C CB . ASN A 1 235 ? -18.884 145.423 38.732 1.00 22.61 ? 250 ASN A CB 1 ATOM 1844 C CG . ASN A 1 235 ? -20.226 145.898 39.274 1.00 20.80 ? 250 ASN A CG 1 ATOM 1845 O OD1 . ASN A 1 235 ? -20.733 146.943 38.872 1.00 24.84 ? 250 ASN A OD1 1 ATOM 1846 N ND2 . ASN A 1 235 ? -20.810 145.123 40.199 1.00 25.41 ? 250 ASN A ND2 1 ATOM 1847 N N . LEU A 1 236 ? -19.045 148.201 36.506 1.00 18.78 ? 251 LEU A N 1 ATOM 1848 C CA . LEU A 1 236 ? -18.873 149.660 36.441 1.00 20.12 ? 251 LEU A CA 1 ATOM 1849 C C . LEU A 1 236 ? -19.243 150.341 37.754 1.00 23.06 ? 251 LEU A C 1 ATOM 1850 O O . LEU A 1 236 ? -18.658 151.346 38.108 1.00 23.96 ? 251 LEU A O 1 ATOM 1851 C CB . LEU A 1 236 ? -19.689 150.272 35.306 1.00 21.22 ? 251 LEU A CB 1 ATOM 1852 C CG . LEU A 1 236 ? -19.314 149.889 33.886 1.00 23.04 ? 251 LEU A CG 1 ATOM 1853 C CD1 . LEU A 1 236 ? -20.173 150.700 32.923 1.00 24.60 ? 251 LEU A CD1 1 ATOM 1854 C CD2 . LEU A 1 236 ? -17.824 150.109 33.635 1.00 25.65 ? 251 LEU A CD2 1 ATOM 1855 N N . ASP A 1 237 ? -20.223 149.795 38.469 1.00 24.28 ? 252 ASP A N 1 ATOM 1856 C CA . ASP A 1 237 ? -20.607 150.332 39.777 1.00 25.17 ? 252 ASP A CA 1 ATOM 1857 C C . ASP A 1 237 ? -19.493 150.239 40.828 1.00 25.97 ? 252 ASP A C 1 ATOM 1858 O O . ASP A 1 237 ? -19.512 150.959 41.821 1.00 32.75 ? 252 ASP A O 1 ATOM 1859 C CB . ASP A 1 237 ? -21.881 149.650 40.288 1.00 26.59 ? 252 ASP A CB 1 ATOM 1860 C CG . ASP A 1 237 ? -23.134 150.069 39.511 1.00 28.91 ? 252 ASP A CG 1 ATOM 1861 O OD1 . ASP A 1 237 ? -23.193 151.212 39.020 1.00 27.84 ? 252 ASP A OD1 1 ATOM 1862 O OD2 . ASP A 1 237 ? -24.066 149.249 39.385 1.00 29.60 ? 252 ASP A OD2 1 ATOM 1863 N N . SER A 1 238 ? -18.517 149.368 40.608 1.00 24.20 ? 253 SER A N 1 ATOM 1864 C CA . SER A 1 238 ? -17.375 149.276 41.522 1.00 28.22 ? 253 SER A CA 1 ATOM 1865 C C . SER A 1 238 ? -16.259 150.240 41.132 1.00 29.54 ? 253 SER A C 1 ATOM 1866 O O . SER A 1 238 ? -15.252 150.339 41.828 1.00 32.07 ? 253 SER A O 1 ATOM 1867 C CB . SER A 1 238 ? -16.808 147.855 41.560 1.00 26.22 ? 253 SER A CB 1 ATOM 1868 O OG . SER A 1 238 ? -17.799 146.904 41.886 1.00 38.31 ? 253 SER A OG 1 ATOM 1869 N N . CYS A 1 239 ? -16.450 150.942 40.018 1.00 30.63 ? 254 CYS A N 1 ATOM 1870 C CA . CYS A 1 239 ? -15.417 151.791 39.439 1.00 26.51 ? 254 CYS A CA 1 ATOM 1871 C C . CYS A 1 239 ? -15.811 153.252 39.351 1.00 30.73 ? 254 CYS A C 1 ATOM 1872 O O . CYS A 1 239 ? -14.947 154.131 39.360 1.00 30.09 ? 254 CYS A O 1 ATOM 1873 C CB . CYS A 1 239 ? -15.090 151.304 38.031 1.00 32.28 ? 254 CYS A CB 1 ATOM 1874 S SG . CYS A 1 239 ? -14.066 149.830 37.992 1.00 29.23 ? 254 CYS A SG 1 ATOM 1875 N N . ILE A 1 240 ? -17.106 153.523 39.231 1.00 24.35 ? 255 ILE A N 1 ATOM 1876 C CA . ILE A 1 240 ? -17.552 154.901 39.028 1.00 26.25 ? 255 ILE A CA 1 ATOM 1877 C C . ILE A 1 240 ? -19.007 155.093 39.470 1.00 24.51 ? 255 ILE A C 1 ATOM 1878 O O . ILE A 1 240 ? -19.879 154.252 39.187 1.00 28.44 ? 255 ILE A O 1 ATOM 1879 C CB . ILE A 1 240 ? -17.365 155.328 37.533 1.00 25.28 ? 255 ILE A CB 1 ATOM 1880 C CG1 . ILE A 1 240 ? -17.772 156.790 37.318 1.00 32.74 ? 255 ILE A CG1 1 ATOM 1881 C CG2 . ILE A 1 240 ? -18.131 154.397 36.595 1.00 25.07 ? 255 ILE A CG2 1 ATOM 1882 C CD1 . ILE A 1 240 ? -17.363 157.335 35.951 1.00 32.35 ? 255 ILE A CD1 1 ATOM 1883 N N . ASP A 1 241 ? -19.280 156.188 40.158 1.00 30.58 ? 256 ASP A N 1 ATOM 1884 C CA . ASP A 1 241 ? -20.644 156.427 40.597 1.00 32.16 ? 256 ASP A CA 1 ATOM 1885 C C . ASP A 1 241 ? -21.534 156.803 39.418 1.00 31.92 ? 256 ASP A C 1 ATOM 1886 O O . ASP A 1 241 ? -21.075 157.409 38.450 1.00 32.04 ? 256 ASP A O 1 ATOM 1887 C CB . ASP A 1 241 ? -20.698 157.512 41.670 1.00 33.24 ? 256 ASP A CB 1 ATOM 1888 C CG . ASP A 1 241 ? -21.979 157.458 42.466 1.00 44.50 ? 256 ASP A CG 1 ATOM 1889 O OD1 . ASP A 1 241 ? -22.044 156.690 43.455 1.00 45.95 ? 256 ASP A OD1 1 ATOM 1890 O OD2 . ASP A 1 241 ? -22.937 158.165 42.083 1.00 42.19 ? 256 ASP A OD2 1 ATOM 1891 N N . HIS A 1 242 ? -22.809 156.447 39.527 1.00 35.12 ? 257 HIS A N 1 ATOM 1892 C CA . HIS A 1 242 ? -23.826 156.743 38.516 1.00 38.86 ? 257 HIS A CA 1 ATOM 1893 C C . HIS A 1 242 ? -23.972 158.211 38.169 1.00 41.80 ? 257 HIS A C 1 ATOM 1894 O O . HIS A 1 242 ? -24.378 158.553 37.060 1.00 39.31 ? 257 HIS A O 1 ATOM 1895 C CB . HIS A 1 242 ? -25.187 156.259 39.005 1.00 51.63 ? 257 HIS A CB 1 ATOM 1896 C CG . HIS A 1 242 ? -25.455 154.822 38.713 1.00 55.88 ? 257 HIS A CG 1 ATOM 1897 N ND1 . HIS A 1 242 ? -26.691 154.245 38.910 1.00 60.44 ? 257 HIS A ND1 1 ATOM 1898 C CD2 . HIS A 1 242 ? -24.654 153.843 38.229 1.00 57.26 ? 257 HIS A CD2 1 ATOM 1899 C CE1 . HIS A 1 242 ? -26.641 152.971 38.563 1.00 57.19 ? 257 HIS A CE1 1 ATOM 1900 N NE2 . HIS A 1 242 ? -25.416 152.701 38.145 1.00 56.48 ? 257 HIS A NE2 1 ATOM 1901 N N . SER A 1 243 ? -23.684 159.076 39.130 1.00 39.25 ? 258 SER A N 1 ATOM 1902 C CA . SER A 1 243 ? -23.889 160.503 38.952 1.00 44.89 ? 258 SER A CA 1 ATOM 1903 C C . SER A 1 243 ? -22.954 161.103 37.901 1.00 41.30 ? 258 SER A C 1 ATOM 1904 O O . SER A 1 243 ? -23.178 162.221 37.434 1.00 45.63 ? 258 SER A O 1 ATOM 1905 C CB . SER A 1 243 ? -23.690 161.214 40.289 1.00 47.54 ? 258 SER A CB 1 ATOM 1906 O OG . SER A 1 243 ? -22.346 161.078 40.722 1.00 45.88 ? 258 SER A OG 1 ATOM 1907 N N . TYR A 1 244 ? -21.913 160.357 37.536 1.00 30.05 ? 259 TYR A N 1 ATOM 1908 C CA . TYR A 1 244 ? -20.864 160.866 36.658 1.00 29.74 ? 259 TYR A CA 1 ATOM 1909 C C . TYR A 1 244 ? -21.259 160.745 35.190 1.00 27.59 ? 259 TYR A C 1 ATOM 1910 O O . TYR A 1 244 ? -20.698 161.429 34.351 1.00 27.78 ? 259 TYR A O 1 ATOM 1911 C CB . TYR A 1 244 ? -19.570 160.065 36.849 1.00 35.98 ? 259 TYR A CB 1 ATOM 1912 C CG . TYR A 1 244 ? -18.547 160.604 37.835 1.00 43.81 ? 259 TYR A CG 1 ATOM 1913 C CD1 . TYR A 1 244 ? -17.191 160.579 37.529 1.00 43.23 ? 259 TYR A CD1 1 ATOM 1914 C CD2 . TYR A 1 244 ? -18.923 161.097 39.074 1.00 47.80 ? 259 TYR A CD2 1 ATOM 1915 C CE1 . TYR A 1 244 ? -16.234 161.041 38.415 1.00 50.91 ? 259 TYR A CE1 1 ATOM 1916 C CE2 . TYR A 1 244 ? -17.968 161.571 39.978 1.00 48.91 ? 259 TYR A CE2 1 ATOM 1917 C CZ . TYR A 1 244 ? -16.628 161.541 39.637 1.00 52.46 ? 259 TYR A CZ 1 ATOM 1918 O OH . TYR A 1 244 ? -15.673 162.003 40.515 1.00 52.37 ? 259 TYR A OH 1 ATOM 1919 N N . TYR A 1 245 ? -22.204 159.863 34.876 1.00 26.69 ? 260 TYR A N 1 ATOM 1920 C CA . TYR A 1 245 ? -22.426 159.506 33.471 1.00 23.44 ? 260 TYR A CA 1 ATOM 1921 C C . TYR A 1 245 ? -23.787 158.891 33.198 1.00 27.07 ? 260 TYR A C 1 ATOM 1922 O O . TYR A 1 245 ? -24.480 158.428 34.111 1.00 29.55 ? 260 TYR A O 1 ATOM 1923 C CB . TYR A 1 245 ? -21.348 158.520 32.997 1.00 24.54 ? 260 TYR A CB 1 ATOM 1924 C CG . TYR A 1 245 ? -21.540 157.118 33.542 1.00 20.62 ? 260 TYR A CG 1 ATOM 1925 C CD1 . TYR A 1 245 ? -21.232 156.822 34.878 1.00 19.16 ? 260 TYR A CD1 1 ATOM 1926 C CD2 . TYR A 1 245 ? -22.030 156.092 32.728 1.00 18.38 ? 260 TYR A CD2 1 ATOM 1927 C CE1 . TYR A 1 245 ? -21.414 155.537 35.385 1.00 21.87 ? 260 TYR A CE1 1 ATOM 1928 C CE2 . TYR A 1 245 ? -22.218 154.816 33.225 1.00 23.11 ? 260 TYR A CE2 1 ATOM 1929 C CZ . TYR A 1 245 ? -21.902 154.545 34.549 1.00 24.55 ? 260 TYR A CZ 1 ATOM 1930 O OH . TYR A 1 245 ? -22.095 153.272 35.026 1.00 23.27 ? 260 TYR A OH 1 ATOM 1931 N N . THR A 1 246 ? -24.163 158.876 31.924 1.00 21.50 ? 261 THR A N 1 ATOM 1932 C CA . THR A 1 246 ? -25.349 158.163 31.489 1.00 24.18 ? 261 THR A CA 1 ATOM 1933 C C . THR A 1 246 ? -24.899 156.998 30.625 1.00 20.31 ? 261 THR A C 1 ATOM 1934 O O . THR A 1 246 ? -24.063 157.153 29.727 1.00 20.65 ? 261 THR A O 1 ATOM 1935 C CB . THR A 1 246 ? -26.278 159.088 30.700 1.00 22.47 ? 261 THR A CB 1 ATOM 1936 O OG1 . THR A 1 246 ? -26.657 160.187 31.540 1.00 25.40 ? 261 THR A OG1 1 ATOM 1937 C CG2 . THR A 1 246 ? -27.530 158.361 30.239 1.00 26.61 ? 261 THR A CG2 1 ATOM 1938 N N . LEU A 1 247 ? -25.430 155.816 30.921 1.00 20.40 ? 262 LEU A N 1 ATOM 1939 C CA . LEU A 1 247 ? -25.110 154.605 30.165 1.00 18.19 ? 262 LEU A CA 1 ATOM 1940 C C . LEU A 1 247 ? -26.057 154.465 28.983 1.00 16.96 ? 262 LEU A C 1 ATOM 1941 O O . LEU A 1 247 ? -27.260 154.327 29.165 1.00 20.44 ? 262 LEU A O 1 ATOM 1942 C CB . LEU A 1 247 ? -25.222 153.388 31.090 1.00 21.10 ? 262 LEU A CB 1 ATOM 1943 C CG . LEU A 1 247 ? -24.882 152.043 30.466 1.00 22.08 ? 262 LEU A CG 1 ATOM 1944 C CD1 . LEU A 1 247 ? -23.382 151.994 30.214 1.00 22.19 ? 262 LEU A CD1 1 ATOM 1945 C CD2 . LEU A 1 247 ? -25.307 150.909 31.372 1.00 21.32 ? 262 LEU A CD2 1 ATOM 1946 N N . ILE A 1 248 ? -25.511 154.516 27.771 1.00 17.06 ? 263 ILE A N 1 ATOM 1947 C CA . ILE A 1 248 ? -26.322 154.431 26.559 1.00 17.27 ? 263 ILE A CA 1 ATOM 1948 C C . ILE A 1 248 ? -26.417 152.971 26.070 1.00 14.91 ? 263 ILE A C 1 ATOM 1949 O O . ILE A 1 248 ? -27.451 152.547 25.551 1.00 19.59 ? 263 ILE A O 1 ATOM 1950 C CB . ILE A 1 248 ? -25.761 155.379 25.445 1.00 15.78 ? 263 ILE A CB 1 ATOM 1951 C CG1 . ILE A 1 248 ? -25.693 156.828 25.943 1.00 20.50 ? 263 ILE A CG1 1 ATOM 1952 C CG2 . ILE A 1 248 ? -26.606 155.306 24.157 1.00 19.91 ? 263 ILE A CG2 1 ATOM 1953 C CD1 . ILE A 1 248 ? -27.008 157.368 26.481 1.00 19.67 ? 263 ILE A CD1 1 ATOM 1954 N N . ASP A 1 249 ? -25.354 152.203 26.266 1.00 17.10 ? 264 ASP A N 1 ATOM 1955 C CA . ASP A 1 249 ? -25.321 150.785 25.871 1.00 18.56 ? 264 ASP A CA 1 ATOM 1956 C C . ASP A 1 249 ? -24.334 150.124 26.808 1.00 15.73 ? 264 ASP A C 1 ATOM 1957 O O . ASP A 1 249 ? -23.371 150.777 27.217 1.00 15.62 ? 264 ASP A O 1 ATOM 1958 C CB . ASP A 1 249 ? -24.852 150.649 24.413 1.00 16.79 ? 264 ASP A CB 1 ATOM 1959 C CG . ASP A 1 249 ? -25.108 149.273 23.840 1.00 18.60 ? 264 ASP A CG 1 ATOM 1960 O OD1 . ASP A 1 249 ? -25.886 148.497 24.449 1.00 19.77 ? 264 ASP A OD1 1 ATOM 1961 O OD2 . ASP A 1 249 ? -24.528 148.959 22.769 1.00 17.06 ? 264 ASP A OD2 1 ATOM 1962 N N . LEU A 1 250 ? -24.524 148.841 27.130 1.00 15.10 ? 265 LEU A N 1 ATOM 1963 C CA . LEU A 1 250 ? -23.761 148.226 28.235 1.00 14.96 ? 265 LEU A CA 1 ATOM 1964 C C . LEU A 1 250 ? -22.587 147.319 27.859 1.00 14.31 ? 265 LEU A C 1 ATOM 1965 O O . LEU A 1 250 ? -21.437 147.650 28.153 1.00 16.34 ? 265 LEU A O 1 ATOM 1966 C CB . LEU A 1 250 ? -24.696 147.500 29.210 1.00 16.69 ? 265 LEU A CB 1 ATOM 1967 C CG . LEU A 1 250 ? -24.019 146.799 30.402 1.00 18.21 ? 265 LEU A CG 1 ATOM 1968 C CD1 . LEU A 1 250 ? -23.183 147.774 31.222 1.00 19.82 ? 265 LEU A CD1 1 ATOM 1969 C CD2 . LEU A 1 250 ? -25.059 146.113 31.300 1.00 19.63 ? 265 LEU A CD2 1 ATOM 1970 N N . SER A 1 251 ? -22.851 146.160 27.260 1.00 15.14 ? 266 SER A N 1 ATOM 1971 C CA . SER A 1 251 ? -21.785 145.177 27.102 1.00 12.27 ? 266 SER A CA 1 ATOM 1972 C C . SER A 1 251 ? -21.852 144.467 25.766 1.00 12.45 ? 266 SER A C 1 ATOM 1973 O O . SER A 1 251 ? -22.930 144.221 25.255 1.00 14.44 ? 266 SER A O 1 ATOM 1974 C CB . SER A 1 251 ? -21.871 144.138 28.250 1.00 14.25 ? 266 SER A CB 1 ATOM 1975 O OG . SER A 1 251 ? -20.705 143.316 28.272 1.00 14.14 ? 266 SER A OG 1 ATOM 1976 N N . PRO A 1 252 ? -20.693 144.134 25.185 1.00 11.05 ? 267 PRO A N 1 ATOM 1977 C CA . PRO A 1 252 ? -19.347 144.350 25.722 1.00 11.20 ? 267 PRO A CA 1 ATOM 1978 C C . PRO A 1 252 ? -18.695 145.637 25.240 1.00 12.57 ? 267 PRO A C 1 ATOM 1979 O O . PRO A 1 252 ? -17.487 145.851 25.451 1.00 12.24 ? 267 PRO A O 1 ATOM 1980 C CB . PRO A 1 252 ? -18.592 143.142 25.182 1.00 12.18 ? 267 PRO A CB 1 ATOM 1981 C CG . PRO A 1 252 ? -19.241 142.920 23.786 1.00 11.59 ? 267 PRO A CG 1 ATOM 1982 C CD . PRO A 1 252 ? -20.701 143.161 24.070 1.00 12.49 ? 267 PRO A CD 1 ATOM 1983 N N . VAL A 1 253 ? -19.453 146.468 24.545 1.00 13.62 ? 268 VAL A N 1 ATOM 1984 C CA . VAL A 1 253 ? -18.988 147.810 24.194 1.00 14.65 ? 268 VAL A CA 1 ATOM 1985 C C . VAL A 1 253 ? -19.929 148.783 24.882 1.00 11.87 ? 268 VAL A C 1 ATOM 1986 O O . VAL A 1 253 ? -21.097 148.937 24.475 1.00 13.52 ? 268 VAL A O 1 ATOM 1987 C CB . VAL A 1 253 ? -18.918 148.054 22.672 1.00 13.71 ? 268 VAL A CB 1 ATOM 1988 C CG1 . VAL A 1 253 ? -18.407 149.497 22.377 1.00 13.89 ? 268 VAL A CG1 1 ATOM 1989 C CG2 . VAL A 1 253 ? -18.000 147.016 22.008 1.00 13.41 ? 268 VAL A CG2 1 ATOM 1990 N N . ALA A 1 254 ? -19.454 149.382 25.973 1.00 14.29 ? 269 ALA A N 1 ATOM 1991 C CA . ALA A 1 254 ? -20.257 150.328 26.733 1.00 15.62 ? 269 ALA A CA 1 ATOM 1992 C C . ALA A 1 254 ? -20.142 151.702 26.095 1.00 13.02 ? 269 ALA A C 1 ATOM 1993 O O . ALA A 1 254 ? -19.039 152.160 25.758 1.00 16.32 ? 269 ALA A O 1 ATOM 1994 C CB . ALA A 1 254 ? -19.784 150.403 28.161 1.00 15.24 ? 269 ALA A CB 1 ATOM 1995 N N . ALA A 1 255 ? -21.285 152.348 25.915 1.00 14.31 ? 270 ALA A N 1 ATOM 1996 C CA . ALA A 1 255 ? -21.335 153.705 25.362 1.00 14.27 ? 270 ALA A CA 1 ATOM 1997 C C . ALA A 1 255 ? -21.627 154.663 26.506 1.00 20.41 ? 270 ALA A C 1 ATOM 1998 O O . ALA A 1 255 ? -22.707 154.607 27.110 1.00 17.39 ? 270 ALA A O 1 ATOM 1999 C CB . ALA A 1 255 ? -22.421 153.800 24.278 1.00 12.97 ? 270 ALA A CB 1 ATOM 2000 N N . ILE A 1 256 ? -20.639 155.503 26.820 1.00 16.34 ? 271 ILE A N 1 ATOM 2001 C CA . ILE A 1 256 ? -20.650 156.330 28.022 1.00 17.08 ? 271 ILE A CA 1 ATOM 2002 C C . ILE A 1 256 ? -20.819 157.804 27.657 1.00 18.29 ? 271 ILE A C 1 ATOM 2003 O O . ILE A 1 256 ? -19.999 158.366 26.931 1.00 19.41 ? 271 ILE A O 1 ATOM 2004 C CB . ILE A 1 256 ? -19.310 156.167 28.797 1.00 19.44 ? 271 ILE A CB 1 ATOM 2005 C CG1 . ILE A 1 256 ? -19.025 154.690 29.127 1.00 18.48 ? 271 ILE A CG1 1 ATOM 2006 C CG2 . ILE A 1 256 ? -19.255 157.073 30.070 1.00 18.80 ? 271 ILE A CG2 1 ATOM 2007 C CD1 . ILE A 1 256 ? -20.030 154.022 30.004 1.00 20.78 ? 271 ILE A CD1 1 ATOM 2008 N N . LEU A 1 257 ? -21.883 158.414 28.161 1.00 17.84 ? 272 LEU A N 1 ATOM 2009 C CA . LEU A 1 257 ? -22.114 159.846 28.014 1.00 17.67 ? 272 LEU A CA 1 ATOM 2010 C C . LEU A 1 257 ? -21.868 160.568 29.346 1.00 21.53 ? 272 LEU A C 1 ATOM 2011 O O . LEU A 1 257 ? -22.706 160.538 30.241 1.00 24.15 ? 272 LEU A O 1 ATOM 2012 C CB . LEU A 1 257 ? -23.558 160.078 27.581 1.00 18.07 ? 272 LEU A CB 1 ATOM 2013 C CG . LEU A 1 257 ? -24.011 161.527 27.385 1.00 23.94 ? 272 LEU A CG 1 ATOM 2014 C CD1 . LEU A 1 257 ? -23.086 162.318 26.456 1.00 26.28 ? 272 LEU A CD1 1 ATOM 2015 C CD2 . LEU A 1 257 ? -25.432 161.555 26.860 1.00 25.85 ? 272 LEU A CD2 1 ATOM 2016 N N . PRO A 1 258 ? -20.711 161.216 29.482 1.00 18.58 ? 273 PRO A N 1 ATOM 2017 C CA . PRO A 1 258 ? -20.409 161.885 30.751 1.00 26.15 ? 273 PRO A CA 1 ATOM 2018 C C . PRO A 1 258 ? -21.444 162.940 31.132 1.00 31.57 ? 273 PRO A C 1 ATOM 2019 O O . PRO A 1 258 ? -21.949 163.635 30.247 1.00 27.93 ? 273 PRO A O 1 ATOM 2020 C CB . PRO A 1 258 ? -19.059 162.553 30.485 1.00 26.98 ? 273 PRO A CB 1 ATOM 2021 C CG . PRO A 1 258 ? -18.428 161.717 29.380 1.00 25.23 ? 273 PRO A CG 1 ATOM 2022 C CD . PRO A 1 258 ? -19.596 161.299 28.516 1.00 22.59 ? 273 PRO A CD 1 ATOM 2023 N N . LYS A 1 259 ? -21.756 163.031 32.428 1.00 25.83 ? 274 LYS A N 1 ATOM 2024 C CA . LYS A 1 259 ? -22.596 164.094 32.984 1.00 29.94 ? 274 LYS A CA 1 ATOM 2025 C C . LYS A 1 259 ? -21.715 165.217 33.521 1.00 32.50 ? 274 LYS A C 1 ATOM 2026 O O . LYS A 1 259 ? -22.168 166.333 33.691 1.00 37.68 ? 274 LYS A O 1 ATOM 2027 C CB . LYS A 1 259 ? -23.489 163.552 34.108 1.00 31.02 ? 274 LYS A CB 1 ATOM 2028 C CG . LYS A 1 259 ? -24.594 162.596 33.650 1.00 34.57 ? 274 LYS A CG 1 ATOM 2029 C CD . LYS A 1 259 ? -25.373 162.007 34.836 1.00 39.92 ? 274 LYS A CD 1 ATOM 2030 C CE . LYS A 1 259 ? -26.427 162.968 35.381 1.00 43.26 ? 274 LYS A CE 1 ATOM 2031 N NZ . LYS A 1 259 ? -27.221 162.354 36.495 1.00 54.99 ? 274 LYS A NZ 1 ATOM 2032 N N . ILE A 1 260 ? -20.450 164.904 33.793 1.00 41.70 ? 275 ILE A N 1 ATOM 2033 C CA . ILE A 1 260 ? -19.490 165.898 34.272 1.00 38.07 ? 275 ILE A CA 1 ATOM 2034 C C . ILE A 1 260 ? -18.273 165.934 33.348 1.00 37.87 ? 275 ILE A C 1 ATOM 2035 O O . ILE A 1 260 ? -18.307 165.342 32.269 1.00 39.37 ? 275 ILE A O 1 ATOM 2036 C CB . ILE A 1 260 ? -19.035 165.604 35.722 1.00 42.28 ? 275 ILE A CB 1 ATOM 2037 C CG1 . ILE A 1 260 ? -18.182 164.337 35.771 1.00 43.37 ? 275 ILE A CG1 1 ATOM 2038 C CG2 . ILE A 1 260 ? -20.234 165.478 36.651 1.00 36.91 ? 275 ILE A CG2 1 ATOM 2039 C CD1 . ILE A 1 260 ? -17.191 164.321 36.900 1.00 50.56 ? 275 ILE A CD1 1 ATOM 2040 N N . ASN A 1 261 ? -17.214 166.632 33.762 1.00 36.74 ? 276 ASN A N 1 ATOM 2041 C CA . ASN A 1 261 ? -15.954 166.672 33.017 1.00 40.53 ? 276 ASN A CA 1 ATOM 2042 C C . ASN A 1 261 ? -15.610 165.318 32.434 1.00 30.95 ? 276 ASN A C 1 ATOM 2043 O O . ASN A 1 261 ? -15.429 164.357 33.184 1.00 31.61 ? 276 ASN A O 1 ATOM 2044 C CB . ASN A 1 261 ? -14.797 167.105 33.927 1.00 42.24 ? 276 ASN A CB 1 ATOM 2045 C CG . ASN A 1 261 ? -14.657 168.607 34.027 1.00 63.48 ? 276 ASN A CG 1 ATOM 2046 O OD1 . ASN A 1 261 ? -13.831 169.210 33.334 1.00 68.20 ? 276 ASN A OD1 1 ATOM 2047 N ND2 . ASN A 1 261 ? -15.454 169.222 34.902 1.00 69.77 ? 276 ASN A ND2 1 ATOM 2048 N N . ARG A 1 262 ? -15.547 165.230 31.107 1.00 32.67 ? 277 ARG A N 1 ATOM 2049 C CA . ARG A 1 262 ? -15.220 163.966 30.459 1.00 29.31 ? 277 ARG A CA 1 ATOM 2050 C C . ARG A 1 262 ? -13.891 163.435 30.972 1.00 30.56 ? 277 ARG A C 1 ATOM 2051 O O . ARG A 1 262 ? -13.719 162.229 31.144 1.00 30.40 ? 277 ARG A O 1 ATOM 2052 C CB . ARG A 1 262 ? -15.164 164.104 28.936 1.00 28.50 ? 277 ARG A CB 1 ATOM 2053 C CG . ARG A 1 262 ? -14.715 162.808 28.255 1.00 26.59 ? 277 ARG A CG 1 ATOM 2054 C CD . ARG A 1 262 ? -14.838 162.862 26.750 1.00 28.54 ? 277 ARG A CD 1 ATOM 2055 N NE . ARG A 1 262 ? -13.788 163.681 26.159 1.00 36.97 ? 277 ARG A NE 1 ATOM 2056 C CZ . ARG A 1 262 ? -13.346 163.530 24.916 1.00 37.41 ? 277 ARG A CZ 1 ATOM 2057 N NH1 . ARG A 1 262 ? -12.388 164.320 24.457 1.00 39.14 ? 277 ARG A NH1 1 ATOM 2058 N NH2 . ARG A 1 262 ? -13.857 162.577 24.135 1.00 33.23 ? 277 ARG A NH2 1 ATOM 2059 N N . THR A 1 263 ? -12.959 164.346 31.225 1.00 27.84 ? 278 THR A N 1 ATOM 2060 C CA . THR A 1 263 ? -11.654 163.984 31.765 1.00 30.54 ? 278 THR A CA 1 ATOM 2061 C C . THR A 1 263 ? -11.757 163.232 33.088 1.00 34.43 ? 278 THR A C 1 ATOM 2062 O O . THR A 1 263 ? -11.073 162.224 33.281 1.00 29.61 ? 278 THR A O 1 ATOM 2063 C CB . THR A 1 263 ? -10.773 165.230 31.897 1.00 36.47 ? 278 THR A CB 1 ATOM 2064 O OG1 . THR A 1 263 ? -10.456 165.703 30.581 1.00 42.19 ? 278 THR A OG1 1 ATOM 2065 C CG2 . THR A 1 263 ? -9.487 164.927 32.636 1.00 39.66 ? 278 THR A CG2 1 ATOM 2066 N N . GLU A 1 264 ? -12.614 163.704 33.988 1.00 37.69 ? 279 GLU A N 1 ATOM 2067 C CA . GLU A 1 264 ? -12.824 163.029 35.271 1.00 32.00 ? 279 GLU A CA 1 ATOM 2068 C C . GLU A 1 264 ? -13.418 161.635 35.073 1.00 27.81 ? 279 GLU A C 1 ATOM 2069 O O . GLU A 1 264 ? -12.997 160.679 35.716 1.00 26.43 ? 279 GLU A O 1 ATOM 2070 C CB . GLU A 1 264 ? -13.732 163.855 36.194 1.00 37.57 ? 279 GLU A CB 1 ATOM 2071 C CG . GLU A 1 264 ? -13.125 165.151 36.714 1.00 46.75 ? 279 GLU A CG 1 ATOM 2072 C CD . GLU A 1 264 ? -14.089 165.929 37.611 1.00 57.34 ? 279 GLU A CD 1 ATOM 2073 O OE1 . GLU A 1 264 ? -13.993 165.808 38.853 1.00 60.58 ? 279 GLU A OE1 1 ATOM 2074 O OE2 . GLU A 1 264 ? -14.951 166.662 37.073 1.00 62.55 ? 279 GLU A OE2 1 ATOM 2075 N N . VAL A 1 265 ? -14.392 161.513 34.175 1.00 23.86 ? 280 VAL A N 1 ATOM 2076 C CA . VAL A 1 265 ? -14.992 160.207 33.886 1.00 28.66 ? 280 VAL A CA 1 ATOM 2077 C C . VAL A 1 265 ? -13.973 159.247 33.280 1.00 27.52 ? 280 VAL A C 1 ATOM 2078 O O . VAL A 1 265 ? -13.890 158.080 33.660 1.00 22.46 ? 280 VAL A O 1 ATOM 2079 C CB . VAL A 1 265 ? -16.190 160.345 32.923 1.00 25.06 ? 280 VAL A CB 1 ATOM 2080 C CG1 . VAL A 1 265 ? -16.826 158.981 32.643 1.00 25.27 ? 280 VAL A CG1 1 ATOM 2081 C CG2 . VAL A 1 265 ? -17.215 161.338 33.474 1.00 30.13 ? 280 VAL A CG2 1 ATOM 2082 N N . TYR A 1 266 ? -13.195 159.750 32.330 1.00 22.13 ? 281 TYR A N 1 ATOM 2083 C CA . TYR A 1 266 ? -12.151 158.964 31.674 1.00 22.51 ? 281 TYR A CA 1 ATOM 2084 C C . TYR A 1 266 ? -11.104 158.491 32.689 1.00 25.74 ? 281 TYR A C 1 ATOM 2085 O O . TYR A 1 266 ? -10.685 157.332 32.662 1.00 22.53 ? 281 TYR A O 1 ATOM 2086 C CB . TYR A 1 266 ? -11.510 159.809 30.576 1.00 22.53 ? 281 TYR A CB 1 ATOM 2087 C CG . TYR A 1 266 ? -10.381 159.165 29.809 1.00 21.87 ? 281 TYR A CG 1 ATOM 2088 C CD1 . TYR A 1 266 ? -9.102 159.712 29.831 1.00 21.90 ? 281 TYR A CD1 1 ATOM 2089 C CD2 . TYR A 1 266 ? -10.598 158.035 29.021 1.00 23.28 ? 281 TYR A CD2 1 ATOM 2090 C CE1 . TYR A 1 266 ? -8.066 159.140 29.105 1.00 28.59 ? 281 TYR A CE1 1 ATOM 2091 C CE2 . TYR A 1 266 ? -9.559 157.448 28.303 1.00 23.44 ? 281 TYR A CE2 1 ATOM 2092 C CZ . TYR A 1 266 ? -8.302 158.016 28.340 1.00 27.04 ? 281 TYR A CZ 1 ATOM 2093 O OH . TYR A 1 266 ? -7.272 157.447 27.620 1.00 26.74 ? 281 TYR A OH 1 ATOM 2094 N N . ASN A 1 267 ? -10.691 159.370 33.594 1.00 23.22 ? 282 ASN A N 1 ATOM 2095 C CA . ASN A 1 267 ? -9.659 158.988 34.560 1.00 25.99 ? 282 ASN A CA 1 ATOM 2096 C C . ASN A 1 267 ? -10.092 157.844 35.483 1.00 23.38 ? 282 ASN A C 1 ATOM 2097 O O . ASN A 1 267 ? -9.294 156.966 35.829 1.00 27.29 ? 282 ASN A O 1 ATOM 2098 C CB . ASN A 1 267 ? -9.180 160.202 35.369 1.00 28.92 ? 282 ASN A CB 1 ATOM 2099 C CG . ASN A 1 267 ? -8.377 161.200 34.524 1.00 32.02 ? 282 ASN A CG 1 ATOM 2100 O OD1 . ASN A 1 267 ? -7.896 160.879 33.427 1.00 29.04 ? 282 ASN A OD1 1 ATOM 2101 N ND2 . ASN A 1 267 ? -8.214 162.414 35.048 1.00 31.16 ? 282 ASN A ND2 1 ATOM 2102 N N . LYS A 1 268 ? -11.359 157.863 35.889 1.00 24.37 ? 283 LYS A N 1 ATOM 2103 C CA . LYS A 1 268 ? -11.932 156.755 36.657 1.00 22.35 ? 283 LYS A CA 1 ATOM 2104 C C . LYS A 1 268 ? -12.003 155.481 35.820 1.00 24.56 ? 283 LYS A C 1 ATOM 2105 O O . LYS A 1 268 ? -11.548 154.416 36.242 1.00 24.71 ? 283 LYS A O 1 ATOM 2106 C CB . LYS A 1 268 ? -13.333 157.111 37.161 1.00 25.85 ? 283 LYS A CB 1 ATOM 2107 C CG . LYS A 1 268 ? -13.363 158.041 38.356 1.00 33.33 ? 283 LYS A CG 1 ATOM 2108 C CD . LYS A 1 268 ? -12.610 157.429 39.526 1.00 35.46 ? 283 LYS A CD 1 ATOM 2109 C CE . LYS A 1 268 ? -13.185 157.881 40.858 1.00 52.15 ? 283 LYS A CE 1 ATOM 2110 N NZ . LYS A 1 268 ? -12.547 157.138 41.985 1.00 58.28 ? 283 LYS A NZ 1 ATOM 2111 N N . LEU A 1 269 ? -12.577 155.589 34.628 1.00 20.48 ? 284 LEU A N 1 ATOM 2112 C CA . LEU A 1 269 ? -12.841 154.405 33.820 1.00 21.73 ? 284 LEU A CA 1 ATOM 2113 C C . LEU A 1 269 ? -11.575 153.734 33.307 1.00 21.80 ? 284 LEU A C 1 ATOM 2114 O O . LEU A 1 269 ? -11.546 152.505 33.166 1.00 20.18 ? 284 LEU A O 1 ATOM 2115 C CB . LEU A 1 269 ? -13.777 154.754 32.666 1.00 20.66 ? 284 LEU A CB 1 ATOM 2116 C CG . LEU A 1 269 ? -15.223 154.959 33.125 1.00 18.76 ? 284 LEU A CG 1 ATOM 2117 C CD1 . LEU A 1 269 ? -16.088 155.515 31.996 1.00 21.83 ? 284 LEU A CD1 1 ATOM 2118 C CD2 . LEU A 1 269 ? -15.801 153.627 33.633 1.00 21.67 ? 284 LEU A CD2 1 ATOM 2119 N N . LYS A 1 270 ? -10.523 154.518 33.054 1.00 20.67 ? 285 LYS A N 1 ATOM 2120 C CA . LYS A 1 270 ? -9.292 153.958 32.499 1.00 17.75 ? 285 LYS A CA 1 ATOM 2121 C C . LYS A 1 270 ? -8.533 153.183 33.566 1.00 21.94 ? 285 LYS A C 1 ATOM 2122 O O . LYS A 1 270 ? -7.594 152.444 33.260 1.00 19.81 ? 285 LYS A O 1 ATOM 2123 C CB . LYS A 1 270 ? -8.404 155.050 31.872 1.00 21.59 ? 285 LYS A CB 1 ATOM 2124 C CG . LYS A 1 270 ? -7.534 155.830 32.873 1.00 24.92 ? 285 LYS A CG 1 ATOM 2125 C CD . LYS A 1 270 ? -6.928 157.069 32.236 1.00 25.09 ? 285 LYS A CD 1 ATOM 2126 C CE . LYS A 1 270 ? -5.909 157.738 33.166 1.00 28.52 ? 285 LYS A CE 1 ATOM 2127 N NZ . LYS A 1 270 ? -5.680 159.181 32.779 1.00 23.26 ? 285 LYS A NZ 1 ATOM 2128 N N . ASN A 1 271 ? -8.943 153.347 34.820 1.00 18.98 ? 286 ASN A N 1 ATOM 2129 C CA . ASN A 1 271 ? -8.339 152.608 35.927 1.00 21.45 ? 286 ASN A CA 1 ATOM 2130 C C . ASN A 1 271 ? -9.275 151.589 36.592 1.00 20.38 ? 286 ASN A C 1 ATOM 2131 O O . ASN A 1 271 ? -9.147 151.306 37.776 1.00 27.29 ? 286 ASN A O 1 ATOM 2132 C CB . ASN A 1 271 ? -7.803 153.577 36.985 1.00 18.11 ? 286 ASN A CB 1 ATOM 2133 C CG . ASN A 1 271 ? -6.480 154.222 36.577 1.00 23.92 ? 286 ASN A CG 1 ATOM 2134 O OD1 . ASN A 1 271 ? -5.465 153.538 36.461 1.00 24.40 ? 286 ASN A OD1 1 ATOM 2135 N ND2 . ASN A 1 271 ? -6.484 155.544 36.364 1.00 24.68 ? 286 ASN A ND2 1 ATOM 2136 N N . CYS A 1 272 ? -10.181 151.018 35.815 1.00 22.24 ? 287 CYS A N 1 ATOM 2137 C CA . CYS A 1 272 ? -11.203 150.117 36.329 1.00 23.17 ? 287 CYS A CA 1 ATOM 2138 C C . CYS A 1 272 ? -10.834 148.627 36.174 1.00 19.51 ? 287 CYS A C 1 ATOM 2139 O O . CYS A 1 272 ? -10.928 147.843 37.131 1.00 21.94 ? 287 CYS A O 1 ATOM 2140 C CB . CYS A 1 272 ? -12.519 150.436 35.613 1.00 22.93 ? 287 CYS A CB 1 ATOM 2141 S SG . CYS A 1 272 ? -13.889 149.370 36.025 1.00 24.54 ? 287 CYS A SG 1 ATOM 2142 N N . SER A 1 273 ? -10.395 148.232 34.986 1.00 18.43 ? 288 SER A N 1 ATOM 2143 C CA . SER A 1 273 ? -10.060 146.830 34.741 1.00 19.47 ? 288 SER A CA 1 ATOM 2144 C C . SER A 1 273 ? -9.058 146.733 33.622 1.00 20.22 ? 288 SER A C 1 ATOM 2145 O O . SER A 1 273 ? -9.207 147.411 32.614 1.00 22.76 ? 288 SER A O 1 ATOM 2146 C CB . SER A 1 273 ? -11.308 146.043 34.342 1.00 18.71 ? 288 SER A CB 1 ATOM 2147 O OG . SER A 1 273 ? -10.967 144.714 33.974 1.00 19.75 ? 288 SER A OG 1 ATOM 2148 N N . PRO A 1 274 ? -8.038 145.874 33.773 1.00 20.99 ? 289 PRO A N 1 ATOM 2149 C CA . PRO A 1 274 ? -7.137 145.653 32.644 1.00 19.24 ? 289 PRO A CA 1 ATOM 2150 C C . PRO A 1 274 ? -7.770 144.828 31.531 1.00 16.79 ? 289 PRO A C 1 ATOM 2151 O O . PRO A 1 274 ? -7.161 144.648 30.467 1.00 19.40 ? 289 PRO A O 1 ATOM 2152 C CB . PRO A 1 274 ? -5.958 144.902 33.279 1.00 25.12 ? 289 PRO A CB 1 ATOM 2153 C CG . PRO A 1 274 ? -6.537 144.240 34.465 1.00 27.80 ? 289 PRO A CG 1 ATOM 2154 C CD . PRO A 1 274 ? -7.587 145.175 34.990 1.00 24.18 ? 289 PRO A CD 1 ATOM 2155 N N . HIS A 1 275 ? -9.000 144.356 31.738 1.00 16.14 ? 290 HIS A N 1 ATOM 2156 C CA . HIS A 1 275 ? -9.643 143.487 30.755 1.00 16.76 ? 290 HIS A CA 1 ATOM 2157 C C . HIS A 1 275 ? -10.604 144.233 29.850 1.00 17.78 ? 290 HIS A C 1 ATOM 2158 O O . HIS A 1 275 ? -11.441 143.625 29.192 1.00 14.74 ? 290 HIS A O 1 ATOM 2159 C CB . HIS A 1 275 ? -10.329 142.292 31.426 1.00 17.77 ? 290 HIS A CB 1 ATOM 2160 C CG . HIS A 1 275 ? -9.399 141.480 32.267 1.00 20.76 ? 290 HIS A CG 1 ATOM 2161 N ND1 . HIS A 1 275 ? -8.557 140.527 31.735 1.00 29.43 ? 290 HIS A ND1 1 ATOM 2162 C CD2 . HIS A 1 275 ? -9.173 141.480 33.603 1.00 23.06 ? 290 HIS A CD2 1 ATOM 2163 C CE1 . HIS A 1 275 ? -7.851 139.974 32.708 1.00 26.92 ? 290 HIS A CE1 1 ATOM 2164 N NE2 . HIS A 1 275 ? -8.198 140.541 33.851 1.00 27.79 ? 290 HIS A NE2 1 ATOM 2165 N N . MET A 1 276 ? -10.478 145.549 29.809 1.00 16.57 ? 291 MET A N 1 ATOM 2166 C CA . MET A 1 276 ? -11.120 146.317 28.754 1.00 17.01 ? 291 MET A CA 1 ATOM 2167 C C . MET A 1 276 ? -10.186 147.408 28.298 1.00 17.38 ? 291 MET A C 1 ATOM 2168 O O . MET A 1 276 ? -9.204 147.727 28.978 1.00 21.40 ? 291 MET A O 1 ATOM 2169 C CB . MET A 1 276 ? -12.451 146.900 29.230 1.00 18.07 ? 291 MET A CB 1 ATOM 2170 C CG . MET A 1 276 ? -12.328 147.843 30.416 1.00 18.27 ? 291 MET A CG 1 ATOM 2171 S SD . MET A 1 276 ? -14.003 148.413 30.836 1.00 19.90 ? 291 MET A SD 1 ATOM 2172 C CE . MET A 1 276 ? -13.671 149.479 32.263 1.00 16.80 ? 291 MET A CE 1 ATOM 2173 N N . ASN A 1 277 ? -10.446 147.950 27.129 1.00 16.73 ? 292 ASN A N 1 ATOM 2174 C CA . ASN A 1 277 ? -9.779 149.155 26.670 1.00 17.03 ? 292 ASN A CA 1 ATOM 2175 C C . ASN A 1 277 ? -10.760 150.290 26.807 1.00 14.90 ? 292 ASN A C 1 ATOM 2176 O O . ASN A 1 277 ? -11.923 150.171 26.424 1.00 20.93 ? 292 ASN A O 1 ATOM 2177 C CB . ASN A 1 277 ? -9.386 149.029 25.195 1.00 19.03 ? 292 ASN A CB 1 ATOM 2178 C CG . ASN A 1 277 ? -8.144 148.194 24.980 1.00 21.58 ? 292 ASN A CG 1 ATOM 2179 O OD1 . ASN A 1 277 ? -7.023 148.684 25.145 1.00 25.54 ? 292 ASN A OD1 1 ATOM 2180 N ND2 . ASN A 1 277 ? -8.332 146.941 24.565 1.00 21.28 ? 292 ASN A ND2 1 ATOM 2181 N N . VAL A 1 278 ? -10.297 151.417 27.314 1.00 18.15 ? 293 VAL A N 1 ATOM 2182 C CA . VAL A 1 278 ? -11.142 152.585 27.492 1.00 14.80 ? 293 VAL A CA 1 ATOM 2183 C C . VAL A 1 278 ? -10.685 153.646 26.476 1.00 17.00 ? 293 VAL A C 1 ATOM 2184 O O . VAL A 1 278 ? -9.528 154.056 26.477 1.00 19.57 ? 293 VAL A O 1 ATOM 2185 C CB . VAL A 1 278 ? -10.986 153.085 28.925 1.00 17.34 ? 293 VAL A CB 1 ATOM 2186 C CG1 . VAL A 1 278 ? -11.718 154.378 29.137 1.00 16.36 ? 293 VAL A CG1 1 ATOM 2187 C CG2 . VAL A 1 278 ? -11.455 152.018 29.915 1.00 19.26 ? 293 VAL A CG2 1 ATOM 2188 N N . TYR A 1 279 ? -11.579 154.053 25.581 1.00 16.46 ? 294 TYR A N 1 ATOM 2189 C CA . TYR A 1 279 ? -11.229 155.001 24.527 1.00 16.09 ? 294 TYR A CA 1 ATOM 2190 C C . TYR A 1 279 ? -12.020 156.306 24.615 1.00 15.43 ? 294 TYR A C 1 ATOM 2191 O O . TYR A 1 279 ? -13.256 156.298 24.636 1.00 16.37 ? 294 TYR A O 1 ATOM 2192 C CB . TYR A 1 279 ? -11.516 154.386 23.151 1.00 15.48 ? 294 TYR A CB 1 ATOM 2193 C CG . TYR A 1 279 ? -10.792 153.108 22.833 1.00 15.65 ? 294 TYR A CG 1 ATOM 2194 C CD1 . TYR A 1 279 ? -9.408 153.082 22.687 1.00 16.83 ? 294 TYR A CD1 1 ATOM 2195 C CD2 . TYR A 1 279 ? -11.493 151.929 22.610 1.00 18.33 ? 294 TYR A CD2 1 ATOM 2196 C CE1 . TYR A 1 279 ? -8.743 151.908 22.375 1.00 17.83 ? 294 TYR A CE1 1 ATOM 2197 C CE2 . TYR A 1 279 ? -10.841 150.752 22.300 1.00 18.38 ? 294 TYR A CE2 1 ATOM 2198 C CZ . TYR A 1 279 ? -9.470 150.745 22.185 1.00 14.86 ? 294 TYR A CZ 1 ATOM 2199 O OH . TYR A 1 279 ? -8.817 149.578 21.871 1.00 16.96 ? 294 TYR A OH 1 ATOM 2200 N N . LEU A 1 280 ? -11.330 157.435 24.637 1.00 18.10 ? 295 LEU A N 1 ATOM 2201 C CA . LEU A 1 280 ? -11.988 158.666 24.215 1.00 18.80 ? 295 LEU A CA 1 ATOM 2202 C C . LEU A 1 280 ? -12.371 158.444 22.754 1.00 18.16 ? 295 LEU A C 1 ATOM 2203 O O . LEU A 1 280 ? -11.649 157.773 22.012 1.00 18.94 ? 295 LEU A O 1 ATOM 2204 C CB . LEU A 1 280 ? -11.033 159.848 24.318 1.00 19.89 ? 295 LEU A CB 1 ATOM 2205 C CG . LEU A 1 280 ? -10.522 160.145 25.725 1.00 22.77 ? 295 LEU A CG 1 ATOM 2206 C CD1 . LEU A 1 280 ? -9.393 161.168 25.697 1.00 27.39 ? 295 LEU A CD1 1 ATOM 2207 C CD2 . LEU A 1 280 ? -11.660 160.624 26.588 1.00 23.93 ? 295 LEU A CD2 1 ATOM 2208 N N . LYS A 1 281 ? -13.516 158.980 22.350 1.00 14.59 ? 296 LYS A N 1 ATOM 2209 C CA . LYS A 1 281 ? -14.021 158.818 20.981 1.00 19.52 ? 296 LYS A CA 1 ATOM 2210 C C . LYS A 1 281 ? -12.949 159.060 19.910 1.00 20.64 ? 296 LYS A C 1 ATOM 2211 O O . LYS A 1 281 ? -12.785 158.275 18.962 1.00 19.52 ? 296 LYS A O 1 ATOM 2212 C CB . LYS A 1 281 ? -15.231 159.738 20.761 1.00 19.59 ? 296 LYS A CB 1 ATOM 2213 C CG . LYS A 1 281 ? -15.790 159.758 19.348 1.00 20.22 ? 296 LYS A CG 1 ATOM 2214 C CD . LYS A 1 281 ? -17.129 160.502 19.335 1.00 20.77 ? 296 LYS A CD 1 ATOM 2215 C CE . LYS A 1 281 ? -17.803 160.513 17.953 1.00 24.69 ? 296 LYS A CE 1 ATOM 2216 N NZ . LYS A 1 281 ? -16.969 161.356 17.030 1.00 30.89 ? 296 LYS A NZ 1 ATOM 2217 N N . GLU A 1 282 ? -12.192 160.126 20.080 1.00 21.53 ? 297 GLU A N 1 ATOM 2218 C CA . GLU A 1 282 ? -11.152 160.448 19.117 1.00 21.44 ? 297 GLU A CA 1 ATOM 2219 C C . GLU A 1 282 ? -9.950 159.482 19.126 1.00 21.50 ? 297 GLU A C 1 ATOM 2220 O O . GLU A 1 282 ? -9.082 159.555 18.242 1.00 20.44 ? 297 GLU A O 1 ATOM 2221 C CB . GLU A 1 282 ? -10.695 161.893 19.322 1.00 24.90 ? 297 GLU A CB 1 ATOM 2222 C CG . GLU A 1 282 ? -10.014 162.146 20.653 1.00 30.09 ? 297 GLU A CG 1 ATOM 2223 C CD . GLU A 1 282 ? -10.959 162.652 21.745 1.00 33.88 ? 297 GLU A CD 1 ATOM 2224 O OE1 . GLU A 1 282 ? -12.197 162.417 21.674 1.00 28.67 ? 297 GLU A OE1 1 ATOM 2225 O OE2 . GLU A 1 282 ? -10.441 163.294 22.691 1.00 38.77 ? 297 GLU A OE2 1 ATOM 2226 N N . ASP A 1 283 ? -9.896 158.587 20.111 1.00 19.57 ? 298 ASP A N 1 ATOM 2227 C CA . ASP A 1 283 ? -8.817 157.597 20.194 1.00 20.08 ? 298 ASP A CA 1 ATOM 2228 C C . ASP A 1 283 ? -9.271 156.183 19.813 1.00 21.00 ? 298 ASP A C 1 ATOM 2229 O O . ASP A 1 283 ? -8.476 155.232 19.889 1.00 20.24 ? 298 ASP A O 1 ATOM 2230 C CB . ASP A 1 283 ? -8.232 157.547 21.610 1.00 18.36 ? 298 ASP A CB 1 ATOM 2231 C CG . ASP A 1 283 ? -7.476 158.788 21.977 1.00 20.05 ? 298 ASP A CG 1 ATOM 2232 O OD1 . ASP A 1 283 ? -6.883 159.429 21.068 1.00 22.23 ? 298 ASP A OD1 1 ATOM 2233 O OD2 . ASP A 1 283 ? -7.463 159.134 23.174 1.00 27.47 ? 298 ASP A OD2 1 ATOM 2234 N N . ILE A 1 284 ? -10.530 156.035 19.404 1.00 17.68 ? 299 ILE A N 1 ATOM 2235 C CA . ILE A 1 284 ? -11.011 154.732 18.992 1.00 17.04 ? 299 ILE A CA 1 ATOM 2236 C C . ILE A 1 284 ? -10.187 154.281 17.791 1.00 17.60 ? 299 ILE A C 1 ATOM 2237 O O . ILE A 1 284 ? -9.999 155.037 16.842 1.00 16.94 ? 299 ILE A O 1 ATOM 2238 C CB . ILE A 1 284 ? -12.522 154.773 18.630 1.00 13.10 ? 299 ILE A CB 1 ATOM 2239 C CG1 . ILE A 1 284 ? -13.361 155.030 19.882 1.00 16.76 ? 299 ILE A CG1 1 ATOM 2240 C CG2 . ILE A 1 284 ? -12.957 153.471 18.013 1.00 16.57 ? 299 ILE A CG2 1 ATOM 2241 C CD1 . ILE A 1 284 ? -14.783 155.489 19.552 1.00 15.70 ? 299 ILE A CD1 1 ATOM 2242 N N . PRO A 1 285 ? -9.659 153.054 17.839 1.00 14.36 ? 300 PRO A N 1 ATOM 2243 C CA . PRO A 1 285 ? -8.731 152.597 16.791 1.00 15.97 ? 300 PRO A CA 1 ATOM 2244 C C . PRO A 1 285 ? -9.330 152.729 15.400 1.00 13.03 ? 300 PRO A C 1 ATOM 2245 O O . PRO A 1 285 ? -10.507 152.384 15.193 1.00 14.71 ? 300 PRO A O 1 ATOM 2246 C CB . PRO A 1 285 ? -8.515 151.129 17.147 1.00 20.34 ? 300 PRO A CB 1 ATOM 2247 C CG . PRO A 1 285 ? -8.603 151.153 18.697 1.00 20.40 ? 300 PRO A CG 1 ATOM 2248 C CD . PRO A 1 285 ? -9.694 152.141 18.998 1.00 17.69 ? 300 PRO A CD 1 ATOM 2249 N N . ASN A 1 286 ? -8.539 153.227 14.455 1.00 15.16 ? 301 ASN A N 1 ATOM 2250 C CA . ASN A 1 286 ? -8.985 153.401 13.084 1.00 16.14 ? 301 ASN A CA 1 ATOM 2251 C C . ASN A 1 286 ? -9.450 152.109 12.450 1.00 15.08 ? 301 ASN A C 1 ATOM 2252 O O . ASN A 1 286 ? -10.327 152.128 11.591 1.00 17.21 ? 301 ASN A O 1 ATOM 2253 C CB . ASN A 1 286 ? -7.855 153.972 12.236 1.00 20.35 ? 301 ASN A CB 1 ATOM 2254 C CG . ASN A 1 286 ? -7.565 155.407 12.556 1.00 23.11 ? 301 ASN A CG 1 ATOM 2255 O OD1 . ASN A 1 286 ? -8.450 156.149 12.996 1.00 29.30 ? 301 ASN A OD1 1 ATOM 2256 N ND2 . ASN A 1 286 ? -6.314 155.817 12.353 1.00 27.18 ? 301 ASN A ND2 1 ATOM 2257 N N . ARG A 1 287 ? -8.896 150.981 12.882 1.00 14.97 ? 302 ARG A N 1 ATOM 2258 C CA . ARG A 1 287 ? -9.237 149.698 12.261 1.00 15.18 ? 302 ARG A CA 1 ATOM 2259 C C . ARG A 1 287 ? -10.707 149.320 12.449 1.00 15.39 ? 302 ARG A C 1 ATOM 2260 O O . ARG A 1 287 ? -11.211 148.398 11.804 1.00 17.10 ? 302 ARG A O 1 ATOM 2261 C CB . ARG A 1 287 ? -8.347 148.581 12.811 1.00 17.25 ? 302 ARG A CB 1 ATOM 2262 C CG . ARG A 1 287 ? -8.587 148.246 14.287 1.00 15.83 ? 302 ARG A CG 1 ATOM 2263 C CD . ARG A 1 287 ? -7.590 147.220 14.785 1.00 20.88 ? 302 ARG A CD 1 ATOM 2264 N NE . ARG A 1 287 ? -7.812 146.864 16.189 1.00 23.43 ? 302 ARG A NE 1 ATOM 2265 C CZ . ARG A 1 287 ? -8.491 145.796 16.588 1.00 20.23 ? 302 ARG A CZ 1 ATOM 2266 N NH1 . ARG A 1 287 ? -9.018 144.967 15.691 1.00 17.41 ? 302 ARG A NH1 1 ATOM 2267 N NH2 . ARG A 1 287 ? -8.630 145.539 17.882 1.00 19.94 ? 302 ARG A NH2 1 ATOM 2268 N N . PHE A 1 288 ? -11.377 149.995 13.379 1.00 13.99 ? 303 PHE A N 1 ATOM 2269 C CA . PHE A 1 288 ? -12.772 149.672 13.691 1.00 14.49 ? 303 PHE A CA 1 ATOM 2270 C C . PHE A 1 288 ? -13.765 150.454 12.821 1.00 16.56 ? 303 PHE A C 1 ATOM 2271 O O . PHE A 1 288 ? -14.959 150.122 12.783 1.00 14.47 ? 303 PHE A O 1 ATOM 2272 C CB . PHE A 1 288 ? -13.066 149.991 15.154 1.00 15.41 ? 303 PHE A CB 1 ATOM 2273 C CG . PHE A 1 288 ? -12.489 149.006 16.147 1.00 14.44 ? 303 PHE A CG 1 ATOM 2274 C CD1 . PHE A 1 288 ? -12.053 149.441 17.384 1.00 18.74 ? 303 PHE A CD1 1 ATOM 2275 C CD2 . PHE A 1 288 ? -12.412 147.659 15.854 1.00 14.79 ? 303 PHE A CD2 1 ATOM 2276 C CE1 . PHE A 1 288 ? -11.533 148.539 18.316 1.00 19.79 ? 303 PHE A CE1 1 ATOM 2277 C CE2 . PHE A 1 288 ? -11.914 146.762 16.770 1.00 16.85 ? 303 PHE A CE2 1 ATOM 2278 C CZ . PHE A 1 288 ? -11.471 147.197 18.007 1.00 17.16 ? 303 PHE A CZ 1 ATOM 2279 N N . TYR A 1 289 ? -13.295 151.507 12.156 1.00 15.04 ? 304 TYR A N 1 ATOM 2280 C CA . TYR A 1 289 ? -14.201 152.373 11.385 1.00 13.23 ? 304 TYR A CA 1 ATOM 2281 C C . TYR A 1 289 ? -15.425 152.756 12.211 1.00 15.76 ? 304 TYR A C 1 ATOM 2282 O O . TYR A 1 289 ? -16.585 152.563 11.797 1.00 13.83 ? 304 TYR A O 1 ATOM 2283 C CB . TYR A 1 289 ? -14.577 151.724 10.035 1.00 14.89 ? 304 TYR A CB 1 ATOM 2284 C CG . TYR A 1 289 ? -13.359 151.284 9.248 1.00 16.88 ? 304 TYR A CG 1 ATOM 2285 C CD1 . TYR A 1 289 ? -12.481 152.221 8.712 1.00 17.97 ? 304 TYR A CD1 1 ATOM 2286 C CD2 . TYR A 1 289 ? -13.072 149.934 9.065 1.00 19.00 ? 304 TYR A CD2 1 ATOM 2287 C CE1 . TYR A 1 289 ? -11.359 151.824 8.014 1.00 20.35 ? 304 TYR A CE1 1 ATOM 2288 C CE2 . TYR A 1 289 ? -11.948 149.535 8.370 1.00 21.94 ? 304 TYR A CE2 1 ATOM 2289 C CZ . TYR A 1 289 ? -11.106 150.480 7.847 1.00 20.53 ? 304 TYR A CZ 1 ATOM 2290 O OH . TYR A 1 289 ? -9.989 150.081 7.145 1.00 27.51 ? 304 TYR A OH 1 ATOM 2291 N N . TYR A 1 290 ? -15.143 153.286 13.395 1.00 15.38 ? 305 TYR A N 1 ATOM 2292 C CA . TYR A 1 290 ? -16.151 153.494 14.427 1.00 18.16 ? 305 TYR A CA 1 ATOM 2293 C C . TYR A 1 290 ? -15.873 154.786 15.178 1.00 18.02 ? 305 TYR A C 1 ATOM 2294 O O . TYR A 1 290 ? -15.766 154.793 16.422 1.00 19.52 ? 305 TYR A O 1 ATOM 2295 C CB . TYR A 1 290 ? -16.133 152.309 15.403 1.00 14.50 ? 305 TYR A CB 1 ATOM 2296 C CG . TYR A 1 290 ? -17.394 152.159 16.231 1.00 15.35 ? 305 TYR A CG 1 ATOM 2297 C CD1 . TYR A 1 290 ? -17.441 152.595 17.554 1.00 15.17 ? 305 TYR A CD1 1 ATOM 2298 C CD2 . TYR A 1 290 ? -18.536 151.576 15.687 1.00 14.72 ? 305 TYR A CD2 1 ATOM 2299 C CE1 . TYR A 1 290 ? -18.592 152.459 18.308 1.00 16.36 ? 305 TYR A CE1 1 ATOM 2300 C CE2 . TYR A 1 290 ? -19.695 151.424 16.415 1.00 13.17 ? 305 TYR A CE2 1 ATOM 2301 C CZ . TYR A 1 290 ? -19.727 151.867 17.733 1.00 16.44 ? 305 TYR A CZ 1 ATOM 2302 O OH . TYR A 1 290 ? -20.890 151.732 18.463 1.00 13.89 ? 305 TYR A OH 1 ATOM 2303 N N . GLN A 1 291 ? -15.725 155.873 14.433 1.00 16.08 ? 306 GLN A N 1 ATOM 2304 C CA . GLN A 1 291 ? -15.447 157.177 15.027 1.00 21.26 ? 306 GLN A CA 1 ATOM 2305 C C . GLN A 1 291 ? -16.330 158.257 14.456 1.00 21.65 ? 306 GLN A C 1 ATOM 2306 O O . GLN A 1 291 ? -16.830 159.095 15.190 1.00 19.97 ? 306 GLN A O 1 ATOM 2307 C CB . GLN A 1 291 ? -13.993 157.598 14.769 1.00 28.65 ? 306 GLN A CB 1 ATOM 2308 C CG . GLN A 1 291 ? -13.092 157.423 15.936 1.00 34.14 ? 306 GLN A CG 1 ATOM 2309 C CD . GLN A 1 291 ? -11.865 158.294 15.852 1.00 27.13 ? 306 GLN A CD 1 ATOM 2310 O OE1 . GLN A 1 291 ? -11.948 159.488 15.544 1.00 30.04 ? 306 GLN A OE1 1 ATOM 2311 N NE2 . GLN A 1 291 ? -10.707 157.702 16.111 1.00 30.51 ? 306 GLN A NE2 1 ATOM 2312 N N . HIS A 1 292 ? -16.499 158.256 13.134 1.00 19.13 ? 307 HIS A N 1 ATOM 2313 C CA . HIS A 1 292 ? -17.026 159.447 12.485 1.00 21.40 ? 307 HIS A CA 1 ATOM 2314 C C . HIS A 1 292 ? -18.551 159.493 12.363 1.00 20.99 ? 307 HIS A C 1 ATOM 2315 O O . HIS A 1 292 ? -19.117 159.488 11.267 1.00 22.29 ? 307 HIS A O 1 ATOM 2316 C CB . HIS A 1 292 ? -16.311 159.682 11.157 1.00 24.54 ? 307 HIS A CB 1 ATOM 2317 C CG . HIS A 1 292 ? -14.819 159.725 11.296 1.00 31.47 ? 307 HIS A CG 1 ATOM 2318 N ND1 . HIS A 1 292 ? -14.159 160.767 11.917 1.00 38.18 ? 307 HIS A ND1 1 ATOM 2319 C CD2 . HIS A 1 292 ? -13.861 158.839 10.932 1.00 35.88 ? 307 HIS A CD2 1 ATOM 2320 C CE1 . HIS A 1 292 ? -12.857 160.533 11.906 1.00 30.24 ? 307 HIS A CE1 1 ATOM 2321 N NE2 . HIS A 1 292 ? -12.650 159.369 11.316 1.00 42.30 ? 307 HIS A NE2 1 ATOM 2322 N N . ASN A 1 293 ? -19.200 159.559 13.516 1.00 17.91 ? 308 ASN A N 1 ATOM 2323 C CA . ASN A 1 293 ? -20.646 159.655 13.580 1.00 18.78 ? 308 ASN A CA 1 ATOM 2324 C C . ASN A 1 293 ? -21.045 160.204 14.940 1.00 20.85 ? 308 ASN A C 1 ATOM 2325 O O . ASN A 1 293 ? -20.480 159.786 15.964 1.00 17.36 ? 308 ASN A O 1 ATOM 2326 C CB . ASN A 1 293 ? -21.255 158.282 13.377 1.00 17.82 ? 308 ASN A CB 1 ATOM 2327 C CG . ASN A 1 293 ? -22.701 158.352 12.989 1.00 16.22 ? 308 ASN A CG 1 ATOM 2328 O OD1 . ASN A 1 293 ? -23.571 158.674 13.817 1.00 18.12 ? 308 ASN A OD1 1 ATOM 2329 N ND2 . ASN A 1 293 ? -22.979 158.093 11.717 1.00 18.87 ? 308 ASN A ND2 1 ATOM 2330 N N . ASP A 1 294 ? -21.985 161.154 14.955 1.00 19.24 ? 309 ASP A N 1 ATOM 2331 C CA . ASP A 1 294 ? -22.413 161.814 16.198 1.00 20.35 ? 309 ASP A CA 1 ATOM 2332 C C . ASP A 1 294 ? -23.140 160.873 17.145 1.00 21.19 ? 309 ASP A C 1 ATOM 2333 O O . ASP A 1 294 ? -23.336 161.200 18.326 1.00 22.62 ? 309 ASP A O 1 ATOM 2334 C CB . ASP A 1 294 ? -23.286 163.046 15.911 1.00 30.50 ? 309 ASP A CB 1 ATOM 2335 C CG . ASP A 1 294 ? -22.499 164.178 15.278 1.00 42.04 ? 309 ASP A CG 1 ATOM 2336 O OD1 . ASP A 1 294 ? -21.255 164.196 15.432 1.00 40.71 ? 309 ASP A OD1 1 ATOM 2337 O OD2 . ASP A 1 294 ? -23.124 165.049 14.629 1.00 53.25 ? 309 ASP A OD2 1 ATOM 2338 N N . ARG A 1 295 ? -23.510 159.701 16.642 1.00 21.27 ? 310 ARG A N 1 ATOM 2339 C CA . ARG A 1 295 ? -24.212 158.707 17.461 1.00 19.13 ? 310 ARG A CA 1 ATOM 2340 C C . ARG A 1 295 ? -23.268 157.880 18.324 1.00 21.98 ? 310 ARG A C 1 ATOM 2341 O O . ARG A 1 295 ? -23.708 157.126 19.198 1.00 20.45 ? 310 ARG A O 1 ATOM 2342 C CB . ARG A 1 295 ? -25.084 157.813 16.564 1.00 18.12 ? 310 ARG A CB 1 ATOM 2343 C CG . ARG A 1 295 ? -26.167 158.600 15.855 1.00 18.20 ? 310 ARG A CG 1 ATOM 2344 C CD . ARG A 1 295 ? -26.799 157.805 14.722 1.00 21.14 ? 310 ARG A CD 1 ATOM 2345 N NE . ARG A 1 295 ? -27.838 158.582 14.055 1.00 20.06 ? 310 ARG A NE 1 ATOM 2346 C CZ . ARG A 1 295 ? -28.589 158.123 13.074 1.00 15.90 ? 310 ARG A CZ 1 ATOM 2347 N NH1 . ARG A 1 295 ? -28.418 156.857 12.673 1.00 17.28 ? 310 ARG A NH1 1 ATOM 2348 N NH2 . ARG A 1 295 ? -29.513 158.923 12.514 1.00 21.09 ? 310 ARG A NH2 1 ATOM 2349 N N . ILE A 1 296 ? -21.967 158.047 18.093 1.00 16.37 ? 311 ILE A N 1 ATOM 2350 C CA . ILE A 1 296 ? -20.940 157.417 18.916 1.00 16.29 ? 311 ILE A CA 1 ATOM 2351 C C . ILE A 1 296 ? -20.624 158.335 20.085 1.00 15.36 ? 311 ILE A C 1 ATOM 2352 O O . ILE A 1 296 ? -20.309 159.518 19.893 1.00 17.83 ? 311 ILE A O 1 ATOM 2353 C CB . ILE A 1 296 ? -19.683 157.098 18.057 1.00 16.14 ? 311 ILE A CB 1 ATOM 2354 C CG1 . ILE A 1 296 ? -20.054 156.040 16.991 1.00 17.65 ? 311 ILE A CG1 1 ATOM 2355 C CG2 . ILE A 1 296 ? -18.528 156.616 18.932 1.00 17.63 ? 311 ILE A CG2 1 ATOM 2356 C CD1 . ILE A 1 296 ? -19.048 155.923 15.841 1.00 18.62 ? 311 ILE A CD1 1 ATOM 2357 N N . GLN A 1 297 ? -20.719 157.802 21.304 1.00 16.77 ? 312 GLN A N 1 ATOM 2358 C CA . GLN A 1 297 ? -20.661 158.632 22.521 1.00 14.11 ? 312 GLN A CA 1 ATOM 2359 C C . GLN A 1 297 ? -19.230 159.095 22.838 1.00 15.24 ? 312 GLN A C 1 ATOM 2360 O O . GLN A 1 297 ? -18.268 158.614 22.217 1.00 17.43 ? 312 GLN A O 1 ATOM 2361 C CB . GLN A 1 297 ? -21.273 157.844 23.697 1.00 18.09 ? 312 GLN A CB 1 ATOM 2362 C CG . GLN A 1 297 ? -22.739 157.466 23.488 1.00 18.19 ? 312 GLN A CG 1 ATOM 2363 C CD . GLN A 1 297 ? -23.616 158.710 23.303 1.00 18.76 ? 312 GLN A CD 1 ATOM 2364 O OE1 . GLN A 1 297 ? -23.318 159.783 23.848 1.00 18.91 ? 312 GLN A OE1 1 ATOM 2365 N NE2 . GLN A 1 297 ? -24.708 158.578 22.543 1.00 18.28 ? 312 GLN A NE2 1 ATOM 2366 N N . PRO A 1 298 ? -19.076 160.059 23.770 1.00 16.71 ? 313 PRO A N 1 ATOM 2367 C CA . PRO A 1 298 ? -17.727 160.601 23.973 1.00 20.88 ? 313 PRO A CA 1 ATOM 2368 C C . PRO A 1 298 ? -16.671 159.619 24.503 1.00 17.55 ? 313 PRO A C 1 ATOM 2369 O O . PRO A 1 298 ? -15.470 159.891 24.335 1.00 16.33 ? 313 PRO A O 1 ATOM 2370 C CB . PRO A 1 298 ? -17.961 161.726 24.986 1.00 24.54 ? 313 PRO A CB 1 ATOM 2371 C CG . PRO A 1 298 ? -19.369 162.187 24.683 1.00 20.53 ? 313 PRO A CG 1 ATOM 2372 C CD . PRO A 1 298 ? -20.107 160.892 24.418 1.00 25.86 ? 313 PRO A CD 1 ATOM 2373 N N . ILE A 1 299 ? -17.092 158.532 25.143 1.00 15.48 ? 314 ILE A N 1 ATOM 2374 C CA . ILE A 1 299 ? -16.166 157.508 25.629 1.00 17.83 ? 314 ILE A CA 1 ATOM 2375 C C . ILE A 1 299 ? -16.776 156.171 25.294 1.00 16.84 ? 314 ILE A C 1 ATOM 2376 O O . ILE A 1 299 ? -17.978 155.994 25.496 1.00 16.41 ? 314 ILE A O 1 ATOM 2377 C CB . ILE A 1 299 ? -15.987 157.553 27.169 1.00 16.31 ? 314 ILE A CB 1 ATOM 2378 C CG1 . ILE A 1 299 ? -15.228 158.825 27.589 1.00 20.78 ? 314 ILE A CG1 1 ATOM 2379 C CG2 . ILE A 1 299 ? -15.260 156.282 27.690 1.00 17.69 ? 314 ILE A CG2 1 ATOM 2380 C CD1 . ILE A 1 299 ? -15.164 159.039 29.111 1.00 21.16 ? 314 ILE A CD1 1 ATOM 2381 N N . ILE A 1 300 ? -15.982 155.220 24.800 1.00 14.52 ? 315 ILE A N 1 ATOM 2382 C CA . ILE A 1 300 ? -16.470 153.845 24.754 1.00 14.57 ? 315 ILE A CA 1 ATOM 2383 C C . ILE A 1 300 ? -15.553 152.905 25.505 1.00 15.28 ? 315 ILE A C 1 ATOM 2384 O O . ILE A 1 300 ? -14.326 153.127 25.607 1.00 16.29 ? 315 ILE A O 1 ATOM 2385 C CB . ILE A 1 300 ? -16.740 153.319 23.308 1.00 20.84 ? 315 ILE A CB 1 ATOM 2386 C CG1 . ILE A 1 300 ? -15.443 153.138 22.529 1.00 19.08 ? 315 ILE A CG1 1 ATOM 2387 C CG2 . ILE A 1 300 ? -17.722 154.240 22.547 1.00 18.63 ? 315 ILE A CG2 1 ATOM 2388 C CD1 . ILE A 1 300 ? -15.672 152.422 21.191 1.00 20.47 ? 315 ILE A CD1 1 ATOM 2389 N N . LEU A 1 301 ? -16.147 151.857 26.064 1.00 16.13 ? 316 LEU A N 1 ATOM 2390 C CA . LEU A 1 301 ? -15.400 150.829 26.788 1.00 13.73 ? 316 LEU A CA 1 ATOM 2391 C C . LEU A 1 301 ? -15.529 149.543 26.001 1.00 11.42 ? 316 LEU A C 1 ATOM 2392 O O . LEU A 1 301 ? -16.641 149.141 25.661 1.00 18.31 ? 316 LEU A O 1 ATOM 2393 C CB . LEU A 1 301 ? -15.986 150.648 28.193 1.00 14.78 ? 316 LEU A CB 1 ATOM 2394 C CG . LEU A 1 301 ? -16.275 151.919 28.985 1.00 13.48 ? 316 LEU A CG 1 ATOM 2395 C CD1 . LEU A 1 301 ? -16.856 151.531 30.356 1.00 16.34 ? 316 LEU A CD1 1 ATOM 2396 C CD2 . LEU A 1 301 ? -15.008 152.772 29.212 1.00 20.76 ? 316 LEU A CD2 1 ATOM 2397 N N . VAL A 1 302 ? -14.401 148.926 25.668 1.00 13.07 ? 317 VAL A N 1 ATOM 2398 C CA . VAL A 1 302 ? -14.424 147.706 24.871 1.00 14.28 ? 317 VAL A CA 1 ATOM 2399 C C . VAL A 1 302 ? -13.829 146.570 25.669 1.00 10.83 ? 317 VAL A C 1 ATOM 2400 O O . VAL A 1 302 ? -12.598 146.530 25.908 1.00 13.35 ? 317 VAL A O 1 ATOM 2401 C CB . VAL A 1 302 ? -13.631 147.878 23.564 1.00 12.16 ? 317 VAL A CB 1 ATOM 2402 C CG1 . VAL A 1 302 ? -13.747 146.602 22.697 1.00 14.76 ? 317 VAL A CG1 1 ATOM 2403 C CG2 . VAL A 1 302 ? -14.125 149.121 22.803 1.00 15.45 ? 317 VAL A CG2 1 ATOM 2404 N N . ALA A 1 303 ? -14.687 145.657 26.112 1.00 12.88 ? 318 ALA A N 1 ATOM 2405 C CA . ALA A 1 303 ? -14.217 144.515 26.898 1.00 12.46 ? 318 ALA A CA 1 ATOM 2406 C C . ALA A 1 303 ? -13.474 143.518 26.038 1.00 15.30 ? 318 ALA A C 1 ATOM 2407 O O . ALA A 1 303 ? -13.830 143.313 24.874 1.00 13.15 ? 318 ALA A O 1 ATOM 2408 C CB . ALA A 1 303 ? -15.385 143.820 27.574 1.00 14.63 ? 318 ALA A CB 1 ATOM 2409 N N . ASP A 1 304 ? -12.435 142.901 26.606 1.00 14.99 ? 319 ASP A N 1 ATOM 2410 C CA . ASP A 1 304 ? -11.740 141.817 25.911 1.00 13.30 ? 319 ASP A CA 1 ATOM 2411 C C . ASP A 1 304 ? -12.704 140.645 25.687 1.00 12.85 ? 319 ASP A C 1 ATOM 2412 O O . ASP A 1 304 ? -13.667 140.461 26.434 1.00 14.15 ? 319 ASP A O 1 ATOM 2413 C CB . ASP A 1 304 ? -10.561 141.300 26.736 1.00 15.29 ? 319 ASP A CB 1 ATOM 2414 C CG . ASP A 1 304 ? -9.444 142.312 26.892 1.00 15.35 ? 319 ASP A CG 1 ATOM 2415 O OD1 . ASP A 1 304 ? -9.410 143.350 26.186 1.00 20.10 ? 319 ASP A OD1 1 ATOM 2416 O OD2 . ASP A 1 304 ? -8.566 142.050 27.730 1.00 19.28 ? 319 ASP A OD2 1 ATOM 2417 N N . GLU A 1 305 ? -12.398 139.829 24.686 1.00 14.49 ? 320 GLU A N 1 ATOM 2418 C CA . GLU A 1 305 ? -13.184 138.638 24.377 1.00 13.10 ? 320 GLU A CA 1 ATOM 2419 C C . GLU A 1 305 ? -13.542 137.811 25.609 1.00 11.78 ? 320 GLU A C 1 ATOM 2420 O O . GLU A 1 305 ? -12.670 137.437 26.412 1.00 15.46 ? 320 GLU A O 1 ATOM 2421 C CB . GLU A 1 305 ? -12.450 137.768 23.380 1.00 11.83 ? 320 GLU A CB 1 ATOM 2422 C CG . GLU A 1 305 ? -13.249 136.515 22.966 1.00 17.58 ? 320 GLU A CG 1 ATOM 2423 C CD . GLU A 1 305 ? -12.455 135.626 22.016 1.00 16.98 ? 320 GLU A CD 1 ATOM 2424 O OE1 . GLU A 1 305 ? -11.271 135.313 22.334 1.00 20.76 ? 320 GLU A OE1 1 ATOM 2425 O OE2 . GLU A 1 305 ? -12.987 135.261 20.939 1.00 20.56 ? 320 GLU A OE2 1 ATOM 2426 N N . GLY A 1 306 ? -14.845 137.592 25.786 1.00 12.99 ? 321 GLY A N 1 ATOM 2427 C CA . GLY A 1 306 ? -15.329 136.727 26.847 1.00 14.61 ? 321 GLY A CA 1 ATOM 2428 C C . GLY A 1 306 ? -15.529 137.433 28.177 1.00 14.63 ? 321 GLY A C 1 ATOM 2429 O O . GLY A 1 306 ? -15.964 136.814 29.141 1.00 15.27 ? 321 GLY A O 1 ATOM 2430 N N . TRP A 1 307 ? -15.229 138.726 28.224 1.00 10.29 ? 322 TRP A N 1 ATOM 2431 C CA . TRP A 1 307 ? -15.474 139.554 29.404 1.00 16.43 ? 322 TRP A CA 1 ATOM 2432 C C . TRP A 1 307 ? -16.780 140.320 29.228 1.00 14.55 ? 322 TRP A C 1 ATOM 2433 O O . TRP A 1 307 ? -17.163 140.702 28.103 1.00 14.01 ? 322 TRP A O 1 ATOM 2434 C CB . TRP A 1 307 ? -14.291 140.496 29.692 1.00 14.00 ? 322 TRP A CB 1 ATOM 2435 C CG . TRP A 1 307 ? -13.110 139.753 30.282 1.00 13.80 ? 322 TRP A CG 1 ATOM 2436 C CD1 . TRP A 1 307 ? -12.248 138.908 29.622 1.00 17.63 ? 322 TRP A CD1 1 ATOM 2437 C CD2 . TRP A 1 307 ? -12.703 139.737 31.661 1.00 17.08 ? 322 TRP A CD2 1 ATOM 2438 N NE1 . TRP A 1 307 ? -11.313 138.390 30.508 1.00 18.43 ? 322 TRP A NE1 1 ATOM 2439 C CE2 . TRP A 1 307 ? -11.584 138.877 31.761 1.00 19.49 ? 322 TRP A CE2 1 ATOM 2440 C CE3 . TRP A 1 307 ? -13.171 140.376 32.811 1.00 15.28 ? 322 TRP A CE3 1 ATOM 2441 C CZ2 . TRP A 1 307 ? -10.936 138.632 32.965 1.00 18.72 ? 322 TRP A CZ2 1 ATOM 2442 C CZ3 . TRP A 1 307 ? -12.520 140.135 34.019 1.00 19.57 ? 322 TRP A CZ3 1 ATOM 2443 C CH2 . TRP A 1 307 ? -11.419 139.266 34.085 1.00 16.49 ? 322 TRP A CH2 1 ATOM 2444 N N . THR A 1 308 ? -17.467 140.546 30.338 1.00 14.77 ? 323 THR A N 1 ATOM 2445 C CA . THR A 1 308 ? -18.773 141.210 30.337 1.00 14.33 ? 323 THR A CA 1 ATOM 2446 C C . THR A 1 308 ? -18.723 142.426 31.247 1.00 13.05 ? 323 THR A C 1 ATOM 2447 O O . THR A 1 308 ? -18.262 142.333 32.396 1.00 13.77 ? 323 THR A O 1 ATOM 2448 C CB . THR A 1 308 ? -19.829 140.264 30.882 1.00 12.50 ? 323 THR A CB 1 ATOM 2449 O OG1 . THR A 1 308 ? -19.876 139.107 30.043 1.00 13.77 ? 323 THR A OG1 1 ATOM 2450 C CG2 . THR A 1 308 ? -21.215 140.920 30.923 1.00 13.91 ? 323 THR A CG2 1 ATOM 2451 N N . ILE A 1 309 ? -19.216 143.548 30.747 1.00 12.93 ? 324 ILE A N 1 ATOM 2452 C CA . ILE A 1 309 ? -19.338 144.770 31.527 1.00 12.56 ? 324 ILE A CA 1 ATOM 2453 C C . ILE A 1 309 ? -20.699 144.698 32.194 1.00 15.92 ? 324 ILE A C 1 ATOM 2454 O O . ILE A 1 309 ? -21.692 144.411 31.529 1.00 14.29 ? 324 ILE A O 1 ATOM 2455 C CB . ILE A 1 309 ? -19.249 146.012 30.626 1.00 10.30 ? 324 ILE A CB 1 ATOM 2456 C CG1 . ILE A 1 309 ? -17.923 145.964 29.845 1.00 15.04 ? 324 ILE A CG1 1 ATOM 2457 C CG2 . ILE A 1 309 ? -19.274 147.284 31.469 1.00 14.77 ? 324 ILE A CG2 1 ATOM 2458 C CD1 . ILE A 1 309 ? -17.692 147.137 28.900 1.00 15.04 ? 324 ILE A CD1 1 ATOM 2459 N N . VAL A 1 310 ? -20.754 144.916 33.513 1.00 14.67 ? 325 VAL A N 1 ATOM 2460 C CA . VAL A 1 310 ? -22.007 144.758 34.244 1.00 16.91 ? 325 VAL A CA 1 ATOM 2461 C C . VAL A 1 310 ? -22.300 145.936 35.144 1.00 13.61 ? 325 VAL A C 1 ATOM 2462 O O . VAL A 1 310 ? -21.412 146.726 35.459 1.00 17.35 ? 325 VAL A O 1 ATOM 2463 C CB . VAL A 1 310 ? -22.023 143.471 35.130 1.00 16.70 ? 325 VAL A CB 1 ATOM 2464 C CG1 . VAL A 1 310 ? -21.797 142.206 34.301 1.00 16.29 ? 325 VAL A CG1 1 ATOM 2465 C CG2 . VAL A 1 310 ? -21.015 143.551 36.270 1.00 18.02 ? 325 VAL A CG2 1 ATOM 2466 N N . LEU A 1 311 ? -23.564 146.046 35.561 1.00 17.27 ? 326 LEU A N 1 ATOM 2467 C CA . LEU A 1 311 ? -23.934 146.900 36.680 1.00 20.26 ? 326 LEU A CA 1 ATOM 2468 C C . LEU A 1 311 ? -24.267 145.944 37.804 1.00 19.53 ? 326 LEU A C 1 ATOM 2469 O O . LEU A 1 311 ? -24.245 144.733 37.608 1.00 19.61 ? 326 LEU A O 1 ATOM 2470 C CB . LEU A 1 311 ? -25.156 147.752 36.325 1.00 22.89 ? 326 LEU A CB 1 ATOM 2471 C CG . LEU A 1 311 ? -24.905 148.711 35.157 1.00 21.99 ? 326 LEU A CG 1 ATOM 2472 C CD1 . LEU A 1 311 ? -26.174 149.502 34.761 1.00 30.89 ? 326 LEU A CD1 1 ATOM 2473 C CD2 . LEU A 1 311 ? -23.749 149.650 35.472 1.00 25.00 ? 326 LEU A CD2 1 ATOM 2474 N N . ASN A 1 312 ? -24.579 146.470 38.983 1.00 20.42 ? 327 ASN A N 1 ATOM 2475 C CA . ASN A 1 312 ? -24.880 145.603 40.123 1.00 21.35 ? 327 ASN A CA 1 ATOM 2476 C C . ASN A 1 312 ? -25.942 144.521 39.865 1.00 23.79 ? 327 ASN A C 1 ATOM 2477 O O . ASN A 1 312 ? -25.806 143.392 40.338 1.00 27.17 ? 327 ASN A O 1 ATOM 2478 C CB . ASN A 1 312 ? -25.264 146.450 41.341 1.00 25.18 ? 327 ASN A CB 1 ATOM 2479 C CG . ASN A 1 312 ? -24.061 147.129 41.985 1.00 31.28 ? 327 ASN A CG 1 ATOM 2480 O OD1 . ASN A 1 312 ? -22.917 146.652 41.881 1.00 29.60 ? 327 ASN A OD1 1 ATOM 2481 N ND2 . ASN A 1 312 ? -24.314 148.246 42.663 1.00 30.55 ? 327 ASN A ND2 1 ATOM 2482 N N . GLU A 1 313 ? -26.990 144.855 39.113 1.00 21.00 ? 328 GLU A N 1 ATOM 2483 C CA . GLU A 1 313 ? -28.084 143.903 38.894 1.00 26.45 ? 328 GLU A CA 1 ATOM 2484 C C . GLU A 1 313 ? -28.192 143.308 37.498 1.00 23.07 ? 328 GLU A C 1 ATOM 2485 O O . GLU A 1 313 ? -29.178 142.637 37.202 1.00 25.14 ? 328 GLU A O 1 ATOM 2486 C CB . GLU A 1 313 ? -29.427 144.535 39.277 1.00 27.41 ? 328 GLU A CB 1 ATOM 2487 C CG . GLU A 1 313 ? -29.393 145.178 40.646 1.00 28.43 ? 328 GLU A CG 1 ATOM 2488 C CD . GLU A 1 313 ? -30.753 145.271 41.294 1.00 46.30 ? 328 GLU A CD 1 ATOM 2489 O OE1 . GLU A 1 313 ? -31.774 144.977 40.620 1.00 46.54 ? 328 GLU A OE1 1 ATOM 2490 O OE2 . GLU A 1 313 ? -30.792 145.638 42.491 1.00 50.95 ? 328 GLU A OE2 1 ATOM 2491 N N . SER A 1 314 ? -27.194 143.535 36.651 1.00 20.93 ? 329 SER A N 1 ATOM 2492 C CA . SER A 1 314 ? -27.229 143.029 35.276 1.00 18.02 ? 329 SER A CA 1 ATOM 2493 C C . SER A 1 314 ? -27.362 141.516 35.276 1.00 20.19 ? 329 SER A C 1 ATOM 2494 O O . SER A 1 314 ? -26.610 140.833 35.971 1.00 26.15 ? 329 SER A O 1 ATOM 2495 C CB . SER A 1 314 ? -25.947 143.403 34.527 1.00 18.52 ? 329 SER A CB 1 ATOM 2496 O OG . SER A 1 314 ? -25.807 144.795 34.506 1.00 22.47 ? 329 SER A OG 1 ATOM 2497 N N . SER A 1 315 ? -28.294 140.990 34.481 1.00 22.14 ? 330 SER A N 1 ATOM 2498 C CA . SER A 1 315 ? -28.537 139.564 34.486 1.00 23.56 ? 330 SER A CA 1 ATOM 2499 C C . SER A 1 315 ? -27.444 138.807 33.732 1.00 18.84 ? 330 SER A C 1 ATOM 2500 O O . SER A 1 315 ? -26.770 139.334 32.820 1.00 21.64 ? 330 SER A O 1 ATOM 2501 C CB . SER A 1 315 ? -29.930 139.235 33.944 1.00 33.14 ? 330 SER A CB 1 ATOM 2502 O OG . SER A 1 315 ? -30.169 139.917 32.735 1.00 43.06 ? 330 SER A OG 1 ATOM 2503 N N . GLN A 1 316 ? -27.231 137.576 34.170 1.00 20.20 ? 331 GLN A N 1 ATOM 2504 C CA . GLN A 1 316 ? -26.238 136.694 33.582 1.00 21.27 ? 331 GLN A CA 1 ATOM 2505 C C . GLN A 1 316 ? -26.619 136.351 32.143 1.00 18.84 ? 331 GLN A C 1 ATOM 2506 O O . GLN A 1 316 ? -27.801 136.161 31.827 1.00 21.11 ? 331 GLN A O 1 ATOM 2507 C CB . GLN A 1 316 ? -26.145 135.434 34.444 1.00 22.10 ? 331 GLN A CB 1 ATOM 2508 C CG . GLN A 1 316 ? -25.498 134.254 33.787 1.00 24.44 ? 331 GLN A CG 1 ATOM 2509 C CD . GLN A 1 316 ? -25.271 133.123 34.765 1.00 31.04 ? 331 GLN A CD 1 ATOM 2510 O OE1 . GLN A 1 316 ? -25.694 131.984 34.539 1.00 36.37 ? 331 GLN A OE1 1 ATOM 2511 N NE2 . GLN A 1 316 ? -24.593 133.431 35.863 1.00 32.46 ? 331 GLN A NE2 1 ATOM 2512 N N . LYS A 1 317 ? -25.614 136.311 31.275 1.00 16.80 ? 332 LYS A N 1 ATOM 2513 C CA . LYS A 1 317 ? -25.802 135.880 29.902 1.00 15.07 ? 332 LYS A CA 1 ATOM 2514 C C . LYS A 1 317 ? -24.549 135.108 29.500 1.00 17.01 ? 332 LYS A C 1 ATOM 2515 O O . LYS A 1 317 ? -23.477 135.703 29.377 1.00 14.74 ? 332 LYS A O 1 ATOM 2516 C CB . LYS A 1 317 ? -25.988 137.107 28.992 1.00 20.76 ? 332 LYS A CB 1 ATOM 2517 C CG . LYS A 1 317 ? -26.683 136.813 27.681 1.00 22.64 ? 332 LYS A CG 1 ATOM 2518 C CD . LYS A 1 317 ? -27.352 138.059 27.058 1.00 25.96 ? 332 LYS A CD 1 ATOM 2519 C CE . LYS A 1 317 ? -26.377 139.183 26.795 1.00 27.36 ? 332 LYS A CE 1 ATOM 2520 N NZ . LYS A 1 317 ? -27.045 140.360 26.143 1.00 31.24 ? 332 LYS A NZ 1 ATOM 2521 N N . LEU A 1 318 ? -24.679 133.788 29.339 1.00 16.43 ? 333 LEU A N 1 ATOM 2522 C CA . LEU A 1 318 ? -23.518 132.908 29.118 1.00 14.35 ? 333 LEU A CA 1 ATOM 2523 C C . LEU A 1 318 ? -22.822 133.031 27.778 1.00 14.14 ? 333 LEU A C 1 ATOM 2524 O O . LEU A 1 318 ? -21.639 132.686 27.664 1.00 15.30 ? 333 LEU A O 1 ATOM 2525 C CB . LEU A 1 318 ? -23.878 131.444 29.383 1.00 16.65 ? 333 LEU A CB 1 ATOM 2526 C CG . LEU A 1 318 ? -24.232 131.113 30.837 1.00 21.13 ? 333 LEU A CG 1 ATOM 2527 C CD1 . LEU A 1 318 ? -24.632 129.646 30.964 1.00 22.26 ? 333 LEU A CD1 1 ATOM 2528 C CD2 . LEU A 1 318 ? -23.080 131.462 31.768 1.00 25.38 ? 333 LEU A CD2 1 ATOM 2529 N N . GLY A 1 319 ? -23.534 133.525 26.766 1.00 14.89 ? 334 GLY A N 1 ATOM 2530 C CA . GLY A 1 319 ? -22.903 133.839 25.493 1.00 13.38 ? 334 GLY A CA 1 ATOM 2531 C C . GLY A 1 319 ? -23.125 135.294 25.158 1.00 12.56 ? 334 GLY A C 1 ATOM 2532 O O . GLY A 1 319 ? -24.182 135.843 25.475 1.00 15.41 ? 334 GLY A O 1 ATOM 2533 N N . ASP A 1 320 ? -22.149 135.921 24.502 1.00 11.04 ? 335 ASP A N 1 ATOM 2534 C CA . ASP A 1 320 ? -22.349 137.279 23.992 1.00 14.00 ? 335 ASP A CA 1 ATOM 2535 C C . ASP A 1 320 ? -21.502 137.584 22.769 1.00 13.88 ? 335 ASP A C 1 ATOM 2536 O O . ASP A 1 320 ? -20.571 136.835 22.414 1.00 11.78 ? 335 ASP A O 1 ATOM 2537 C CB . ASP A 1 320 ? -22.115 138.341 25.076 1.00 13.45 ? 335 ASP A CB 1 ATOM 2538 C CG . ASP A 1 320 ? -22.984 139.591 24.869 1.00 17.38 ? 335 ASP A CG 1 ATOM 2539 O OD1 . ASP A 1 320 ? -23.837 139.630 23.951 1.00 14.52 ? 335 ASP A OD1 1 ATOM 2540 O OD2 . ASP A 1 320 ? -22.863 140.544 25.670 1.00 17.22 ? 335 ASP A OD2 1 ATOM 2541 N N . HIS A 1 321 ? -21.831 138.697 22.124 1.00 14.96 ? 336 HIS A N 1 ATOM 2542 C CA . HIS A 1 321 ? -21.073 139.183 20.973 1.00 9.15 ? 336 HIS A CA 1 ATOM 2543 C C . HIS A 1 321 ? -21.093 140.713 21.029 1.00 10.96 ? 336 HIS A C 1 ATOM 2544 O O . HIS A 1 321 ? -21.764 141.289 21.877 1.00 13.06 ? 336 HIS A O 1 ATOM 2545 C CB . HIS A 1 321 ? -21.714 138.673 19.676 1.00 10.24 ? 336 HIS A CB 1 ATOM 2546 C CG . HIS A 1 321 ? -23.177 138.964 19.598 1.00 8.67 ? 336 HIS A CG 1 ATOM 2547 N ND1 . HIS A 1 321 ? -23.671 140.123 19.037 1.00 10.37 ? 336 HIS A ND1 1 ATOM 2548 C CD2 . HIS A 1 321 ? -24.240 138.312 20.125 1.00 13.42 ? 336 HIS A CD2 1 ATOM 2549 C CE1 . HIS A 1 321 ? -24.993 140.135 19.163 1.00 12.17 ? 336 HIS A CE1 1 ATOM 2550 N NE2 . HIS A 1 321 ? -25.361 139.052 19.836 1.00 12.99 ? 336 HIS A NE2 1 ATOM 2551 N N . GLY A 1 322 ? -20.332 141.367 20.153 1.00 11.84 ? 337 GLY A N 1 ATOM 2552 C CA . GLY A 1 322 ? -20.184 142.828 20.168 1.00 11.52 ? 337 GLY A CA 1 ATOM 2553 C C . GLY A 1 322 ? -18.707 143.179 20.117 1.00 10.94 ? 337 GLY A C 1 ATOM 2554 O O . GLY A 1 322 ? -18.314 144.288 19.698 1.00 14.23 ? 337 GLY A O 1 ATOM 2555 N N . TYR A 1 323 ? -17.898 142.205 20.513 1.00 12.26 ? 338 TYR A N 1 ATOM 2556 C CA . TYR A 1 323 ? -16.441 142.348 20.619 1.00 12.25 ? 338 TYR A CA 1 ATOM 2557 C C . TYR A 1 323 ? -15.743 142.663 19.301 1.00 13.63 ? 338 TYR A C 1 ATOM 2558 O O . TYR A 1 323 ? -16.354 142.578 18.239 1.00 14.68 ? 338 TYR A O 1 ATOM 2559 C CB . TYR A 1 323 ? -15.836 141.061 21.182 1.00 12.05 ? 338 TYR A CB 1 ATOM 2560 C CG . TYR A 1 323 ? -16.437 140.594 22.476 1.00 10.17 ? 338 TYR A CG 1 ATOM 2561 C CD1 . TYR A 1 323 ? -15.909 141.020 23.703 1.00 13.33 ? 338 TYR A CD1 1 ATOM 2562 C CD2 . TYR A 1 323 ? -17.524 139.720 22.491 1.00 14.76 ? 338 TYR A CD2 1 ATOM 2563 C CE1 . TYR A 1 323 ? -16.439 140.596 24.900 1.00 14.97 ? 338 TYR A CE1 1 ATOM 2564 C CE2 . TYR A 1 323 ? -18.094 139.297 23.691 1.00 13.08 ? 338 TYR A CE2 1 ATOM 2565 C CZ . TYR A 1 323 ? -17.550 139.738 24.894 1.00 13.54 ? 338 TYR A CZ 1 ATOM 2566 O OH . TYR A 1 323 ? -18.098 139.307 26.086 1.00 15.87 ? 338 TYR A OH 1 ATOM 2567 N N . ASP A 1 324 ? -14.463 143.025 19.412 1.00 11.81 ? 339 ASP A N 1 ATOM 2568 C CA . ASP A 1 324 ? -13.517 143.215 18.312 1.00 12.68 ? 339 ASP A CA 1 ATOM 2569 C C . ASP A 1 324 ? -13.858 142.318 17.121 1.00 14.86 ? 339 ASP A C 1 ATOM 2570 O O . ASP A 1 324 ? -13.914 141.093 17.265 1.00 13.93 ? 339 ASP A O 1 ATOM 2571 C CB . ASP A 1 324 ? -12.146 142.870 18.893 1.00 14.09 ? 339 ASP A CB 1 ATOM 2572 C CG . ASP A 1 324 ? -10.997 143.049 17.927 1.00 19.35 ? 339 ASP A CG 1 ATOM 2573 O OD1 . ASP A 1 324 ? -11.216 143.236 16.713 1.00 15.09 ? 339 ASP A OD1 1 ATOM 2574 O OD2 . ASP A 1 324 ? -9.839 142.986 18.403 1.00 21.26 ? 339 ASP A OD2 1 ATOM 2575 N N . ASN A 1 325 ? -14.089 142.937 15.951 1.00 12.93 ? 340 ASN A N 1 ATOM 2576 C CA . ASN A 1 325 ? -14.504 142.207 14.759 1.00 13.87 ? 340 ASN A CA 1 ATOM 2577 C C . ASN A 1 325 ? -13.359 141.439 14.111 1.00 11.10 ? 340 ASN A C 1 ATOM 2578 O O . ASN A 1 325 ? -13.575 140.709 13.146 1.00 14.56 ? 340 ASN A O 1 ATOM 2579 C CB . ASN A 1 325 ? -15.126 143.168 13.721 1.00 13.29 ? 340 ASN A CB 1 ATOM 2580 C CG . ASN A 1 325 ? -14.152 144.228 13.251 1.00 12.12 ? 340 ASN A CG 1 ATOM 2581 O OD1 . ASN A 1 325 ? -13.369 144.775 14.045 1.00 15.60 ? 340 ASN A OD1 1 ATOM 2582 N ND2 . ASN A 1 325 ? -14.163 144.508 11.949 1.00 13.45 ? 340 ASN A ND2 1 ATOM 2583 N N . SER A 1 326 ? -12.156 141.541 14.668 1.00 13.45 ? 341 SER A N 1 ATOM 2584 C CA . SER A 1 326 ? -11.071 140.660 14.198 1.00 16.48 ? 341 SER A CA 1 ATOM 2585 C C . SER A 1 326 ? -11.087 139.261 14.843 1.00 18.54 ? 341 SER A C 1 ATOM 2586 O O . SER A 1 326 ? -10.405 138.347 14.365 1.00 18.87 ? 341 SER A O 1 ATOM 2587 C CB . SER A 1 326 ? -9.714 141.309 14.403 1.00 16.72 ? 341 SER A CB 1 ATOM 2588 O OG . SER A 1 326 ? -9.560 142.337 13.435 1.00 21.55 ? 341 SER A OG 1 ATOM 2589 N N . LEU A 1 327 ? -11.858 139.090 15.914 1.00 15.92 ? 342 LEU A N 1 ATOM 2590 C CA . LEU A 1 327 ? -11.912 137.802 16.612 1.00 12.98 ? 342 LEU A CA 1 ATOM 2591 C C . LEU A 1 327 ? -12.696 136.769 15.807 1.00 12.63 ? 342 LEU A C 1 ATOM 2592 O O . LEU A 1 327 ? -13.853 137.019 15.459 1.00 13.29 ? 342 LEU A O 1 ATOM 2593 C CB . LEU A 1 327 ? -12.610 137.982 17.958 1.00 12.58 ? 342 LEU A CB 1 ATOM 2594 C CG . LEU A 1 327 ? -11.861 138.857 18.978 1.00 14.57 ? 342 LEU A CG 1 ATOM 2595 C CD1 . LEU A 1 327 ? -12.833 139.264 20.076 1.00 15.16 ? 342 LEU A CD1 1 ATOM 2596 C CD2 . LEU A 1 327 ? -10.648 138.142 19.554 1.00 18.07 ? 342 LEU A CD2 1 ATOM 2597 N N . PRO A 1 328 ? -12.095 135.606 15.527 1.00 16.30 ? 343 PRO A N 1 ATOM 2598 C CA . PRO A 1 328 ? -12.827 134.543 14.827 1.00 18.75 ? 343 PRO A CA 1 ATOM 2599 C C . PRO A 1 328 ? -14.173 134.207 15.457 1.00 13.30 ? 343 PRO A C 1 ATOM 2600 O O . PRO A 1 328 ? -15.142 133.924 14.727 1.00 14.53 ? 343 PRO A O 1 ATOM 2601 C CB . PRO A 1 328 ? -11.878 133.346 14.932 1.00 19.13 ? 343 PRO A CB 1 ATOM 2602 C CG . PRO A 1 328 ? -10.528 133.960 14.931 1.00 21.25 ? 343 PRO A CG 1 ATOM 2603 C CD . PRO A 1 328 ? -10.664 135.267 15.687 1.00 17.73 ? 343 PRO A CD 1 ATOM 2604 N N . SER A 1 329 ? -14.267 134.282 16.783 1.00 11.74 ? 344 SER A N 1 ATOM 2605 C CA . SER A 1 329 ? -15.531 133.970 17.457 1.00 12.74 ? 344 SER A CA 1 ATOM 2606 C C . SER A 1 329 ? -16.687 134.873 17.049 1.00 15.47 ? 344 SER A C 1 ATOM 2607 O O . SER A 1 329 ? -17.858 134.467 17.146 1.00 13.70 ? 344 SER A O 1 ATOM 2608 C CB . SER A 1 329 ? -15.355 134.007 18.980 1.00 15.45 ? 344 SER A CB 1 ATOM 2609 O OG . SER A 1 329 ? -15.069 135.325 19.418 1.00 14.81 ? 344 SER A OG 1 ATOM 2610 N N . MET A 1 330 ? -16.365 136.074 16.561 1.00 12.45 ? 345 MET A N 1 ATOM 2611 C CA . MET A 1 330 ? -17.384 137.030 16.151 1.00 11.96 ? 345 MET A CA 1 ATOM 2612 C C . MET A 1 330 ? -17.793 136.910 14.699 1.00 10.82 ? 345 MET A C 1 ATOM 2613 O O . MET A 1 330 ? -18.767 137.524 14.296 1.00 13.23 ? 345 MET A O 1 ATOM 2614 C CB . MET A 1 330 ? -16.884 138.448 16.410 1.00 11.18 ? 345 MET A CB 1 ATOM 2615 C CG . MET A 1 330 ? -16.671 138.778 17.905 1.00 12.16 ? 345 MET A CG 1 ATOM 2616 S SD . MET A 1 330 ? -18.225 138.684 18.850 1.00 11.81 ? 345 MET A SD 1 ATOM 2617 C CE . MET A 1 330 ? -18.105 137.084 19.628 1.00 13.56 ? 345 MET A CE 1 ATOM 2618 N N . HIS A 1 331 ? -17.086 136.095 13.926 1.00 13.06 ? 346 HIS A N 1 ATOM 2619 C CA . HIS A 1 331 ? -17.335 136.048 12.480 1.00 13.61 ? 346 HIS A CA 1 ATOM 2620 C C . HIS A 1 331 ? -18.477 135.108 12.150 1.00 13.78 ? 346 HIS A C 1 ATOM 2621 O O . HIS A 1 331 ? -18.552 134.011 12.719 1.00 15.05 ? 346 HIS A O 1 ATOM 2622 C CB . HIS A 1 331 ? -16.088 135.595 11.746 1.00 15.15 ? 346 HIS A CB 1 ATOM 2623 C CG . HIS A 1 331 ? -14.933 136.527 11.914 1.00 12.87 ? 346 HIS A CG 1 ATOM 2624 N ND1 . HIS A 1 331 ? -13.627 136.154 11.660 1.00 20.31 ? 346 HIS A ND1 1 ATOM 2625 C CD2 . HIS A 1 331 ? -14.883 137.826 12.319 1.00 12.44 ? 346 HIS A CD2 1 ATOM 2626 C CE1 . HIS A 1 331 ? -12.824 137.176 11.907 1.00 18.46 ? 346 HIS A CE1 1 ATOM 2627 N NE2 . HIS A 1 331 ? -13.558 138.203 12.302 1.00 17.45 ? 346 HIS A NE2 1 ATOM 2628 N N . PRO A 1 332 ? -19.395 135.542 11.254 1.00 11.34 ? 347 PRO A N 1 ATOM 2629 C CA . PRO A 1 332 ? -20.363 134.627 10.634 1.00 12.26 ? 347 PRO A CA 1 ATOM 2630 C C . PRO A 1 332 ? -19.745 133.925 9.426 1.00 14.81 ? 347 PRO A C 1 ATOM 2631 O O . PRO A 1 332 ? -18.549 134.092 9.158 1.00 16.85 ? 347 PRO A O 1 ATOM 2632 C CB . PRO A 1 332 ? -21.489 135.576 10.179 1.00 16.60 ? 347 PRO A CB 1 ATOM 2633 C CG . PRO A 1 332 ? -20.755 136.846 9.799 1.00 12.06 ? 347 PRO A CG 1 ATOM 2634 C CD . PRO A 1 332 ? -19.519 136.921 10.717 1.00 12.19 ? 347 PRO A CD 1 ATOM 2635 N N . PHE A 1 333 ? -20.519 133.088 8.750 1.00 16.83 ? 348 PHE A N 1 ATOM 2636 C CA . PHE A 1 333 ? -20.069 132.494 7.490 1.00 15.05 ? 348 PHE A CA 1 ATOM 2637 C C . PHE A 1 333 ? -20.993 132.992 6.382 1.00 18.23 ? 348 PHE A C 1 ATOM 2638 O O . PHE A 1 333 ? -21.992 133.676 6.656 1.00 16.05 ? 348 PHE A O 1 ATOM 2639 C CB . PHE A 1 333 ? -20.182 130.960 7.555 1.00 15.65 ? 348 PHE A CB 1 ATOM 2640 C CG . PHE A 1 333 ? -21.602 130.457 7.460 1.00 16.49 ? 348 PHE A CG 1 ATOM 2641 C CD1 . PHE A 1 333 ? -22.459 130.543 8.540 1.00 20.54 ? 348 PHE A CD1 1 ATOM 2642 C CD2 . PHE A 1 333 ? -22.075 129.924 6.267 1.00 18.95 ? 348 PHE A CD2 1 ATOM 2643 C CE1 . PHE A 1 333 ? -23.771 130.098 8.454 1.00 22.63 ? 348 PHE A CE1 1 ATOM 2644 C CE2 . PHE A 1 333 ? -23.383 129.474 6.160 1.00 19.44 ? 348 PHE A CE2 1 ATOM 2645 C CZ . PHE A 1 333 ? -24.239 129.560 7.267 1.00 23.39 ? 348 PHE A CZ 1 ATOM 2646 N N . LEU A 1 334 ? -20.688 132.626 5.144 1.00 16.97 ? 349 LEU A N 1 ATOM 2647 C CA . LEU A 1 334 ? -21.633 132.831 4.062 1.00 14.60 ? 349 LEU A CA 1 ATOM 2648 C C . LEU A 1 334 ? -21.683 131.619 3.125 1.00 17.11 ? 349 LEU A C 1 ATOM 2649 O O . LEU A 1 334 ? -20.642 131.080 2.743 1.00 20.73 ? 349 LEU A O 1 ATOM 2650 C CB . LEU A 1 334 ? -21.305 134.105 3.267 1.00 16.10 ? 349 LEU A CB 1 ATOM 2651 C CG . LEU A 1 334 ? -22.250 134.417 2.093 1.00 17.87 ? 349 LEU A CG 1 ATOM 2652 C CD1 . LEU A 1 334 ? -22.387 135.926 1.952 1.00 17.13 ? 349 LEU A CD1 1 ATOM 2653 C CD2 . LEU A 1 334 ? -21.760 133.823 0.756 1.00 16.03 ? 349 LEU A CD2 1 ATOM 2654 N N . ALA A 1 335 ? -22.891 131.196 2.746 1.00 16.03 ? 350 ALA A N 1 ATOM 2655 C CA . ALA A 1 335 ? -23.031 130.169 1.720 1.00 15.69 ? 350 ALA A CA 1 ATOM 2656 C C . ALA A 1 335 ? -24.019 130.668 0.674 1.00 18.27 ? 350 ALA A C 1 ATOM 2657 O O . ALA A 1 335 ? -24.874 131.490 0.978 1.00 20.76 ? 350 ALA A O 1 ATOM 2658 C CB . ALA A 1 335 ? -23.513 128.871 2.344 1.00 19.27 ? 350 ALA A CB 1 ATOM 2659 N N . ALA A 1 336 ? -23.914 130.175 -0.562 1.00 17.02 ? 351 ALA A N 1 ATOM 2660 C CA . ALA A 1 336 ? -24.821 130.612 -1.609 1.00 16.13 ? 351 ALA A CA 1 ATOM 2661 C C . ALA A 1 336 ? -25.023 129.535 -2.657 1.00 16.80 ? 351 ALA A C 1 ATOM 2662 O O . ALA A 1 336 ? -24.173 128.676 -2.859 1.00 20.58 ? 351 ALA A O 1 ATOM 2663 C CB . ALA A 1 336 ? -24.308 131.906 -2.249 1.00 18.83 ? 351 ALA A CB 1 ATOM 2664 N N . HIS A 1 337 ? -26.190 129.583 -3.289 1.00 19.10 ? 352 HIS A N 1 ATOM 2665 C CA . HIS A 1 337 ? -26.521 128.655 -4.354 1.00 21.94 ? 352 HIS A CA 1 ATOM 2666 C C . HIS A 1 337 ? -27.370 129.378 -5.383 1.00 22.62 ? 352 HIS A C 1 ATOM 2667 O O . HIS A 1 337 ? -28.225 130.194 -5.037 1.00 22.94 ? 352 HIS A O 1 ATOM 2668 C CB . HIS A 1 337 ? -27.293 127.441 -3.804 1.00 23.63 ? 352 HIS A CB 1 ATOM 2669 C CG . HIS A 1 337 ? -27.801 126.515 -4.874 1.00 23.09 ? 352 HIS A CG 1 ATOM 2670 N ND1 . HIS A 1 337 ? -29.026 126.686 -5.481 1.00 26.17 ? 352 HIS A ND1 1 ATOM 2671 C CD2 . HIS A 1 337 ? -27.246 125.417 -5.444 1.00 30.44 ? 352 HIS A CD2 1 ATOM 2672 C CE1 . HIS A 1 337 ? -29.200 125.741 -6.393 1.00 21.45 ? 352 HIS A CE1 1 ATOM 2673 N NE2 . HIS A 1 337 ? -28.139 124.950 -6.384 1.00 29.49 ? 352 HIS A NE2 1 ATOM 2674 N N . GLY A 1 338 ? -27.156 129.047 -6.653 1.00 25.81 ? 353 GLY A N 1 ATOM 2675 C CA . GLY A 1 338 ? -28.012 129.555 -7.704 1.00 23.43 ? 353 GLY A CA 1 ATOM 2676 C C . GLY A 1 338 ? -27.247 129.846 -8.983 1.00 16.27 ? 353 GLY A C 1 ATOM 2677 O O . GLY A 1 338 ? -26.029 129.651 -9.046 1.00 21.65 ? 353 GLY A O 1 ATOM 2678 N N . PRO A 1 339 ? -27.962 130.323 -10.008 1.00 23.46 ? 354 PRO A N 1 ATOM 2679 C CA . PRO A 1 339 ? -27.335 130.485 -11.327 1.00 24.96 ? 354 PRO A CA 1 ATOM 2680 C C . PRO A 1 339 ? -26.162 131.450 -11.352 1.00 28.16 ? 354 PRO A C 1 ATOM 2681 O O . PRO A 1 339 ? -25.312 131.316 -12.227 1.00 28.15 ? 354 PRO A O 1 ATOM 2682 C CB . PRO A 1 339 ? -28.480 130.979 -12.221 1.00 27.85 ? 354 PRO A CB 1 ATOM 2683 C CG . PRO A 1 339 ? -29.606 131.335 -11.316 1.00 33.91 ? 354 PRO A CG 1 ATOM 2684 C CD . PRO A 1 339 ? -29.418 130.560 -10.041 1.00 25.19 ? 354 PRO A CD 1 ATOM 2685 N N . ALA A 1 340 ? -26.097 132.385 -10.403 1.00 25.68 ? 355 ALA A N 1 ATOM 2686 C CA . ALA A 1 340 ? -24.983 133.330 -10.358 1.00 22.32 ? 355 ALA A CA 1 ATOM 2687 C C . ALA A 1 340 ? -23.744 132.742 -9.709 1.00 27.77 ? 355 ALA A C 1 ATOM 2688 O O . ALA A 1 340 ? -22.659 133.308 -9.831 1.00 24.35 ? 355 ALA A O 1 ATOM 2689 C CB . ALA A 1 340 ? -25.385 134.591 -9.622 1.00 23.69 ? 355 ALA A CB 1 ATOM 2690 N N . PHE A 1 341 ? -23.903 131.608 -9.033 1.00 24.37 ? 356 PHE A N 1 ATOM 2691 C CA . PHE A 1 341 ? -22.850 131.070 -8.166 1.00 23.99 ? 356 PHE A CA 1 ATOM 2692 C C . PHE A 1 341 ? -22.247 129.772 -8.691 1.00 29.82 ? 356 PHE A C 1 ATOM 2693 O O . PHE A 1 341 ? -22.940 128.939 -9.275 1.00 29.62 ? 356 PHE A O 1 ATOM 2694 C CB . PHE A 1 341 ? -23.394 130.850 -6.756 1.00 21.04 ? 356 PHE A CB 1 ATOM 2695 C CG . PHE A 1 341 ? -23.812 132.118 -6.062 1.00 18.29 ? 356 PHE A CG 1 ATOM 2696 C CD1 . PHE A 1 341 ? -25.163 132.409 -5.860 1.00 19.28 ? 356 PHE A CD1 1 ATOM 2697 C CD2 . PHE A 1 341 ? -22.862 133.021 -5.614 1.00 19.55 ? 356 PHE A CD2 1 ATOM 2698 C CE1 . PHE A 1 341 ? -25.558 133.580 -5.192 1.00 23.23 ? 356 PHE A CE1 1 ATOM 2699 C CE2 . PHE A 1 341 ? -23.241 134.197 -4.957 1.00 19.62 ? 356 PHE A CE2 1 ATOM 2700 C CZ . PHE A 1 341 ? -24.595 134.474 -4.745 1.00 24.55 ? 356 PHE A CZ 1 ATOM 2701 N N . HIS A 1 342 ? -20.944 129.604 -8.485 1.00 24.93 ? 357 HIS A N 1 ATOM 2702 C CA . HIS A 1 342 ? -20.269 128.363 -8.860 1.00 25.97 ? 357 HIS A CA 1 ATOM 2703 C C . HIS A 1 342 ? -20.822 127.202 -8.058 1.00 26.37 ? 357 HIS A C 1 ATOM 2704 O O . HIS A 1 342 ? -21.551 127.399 -7.082 1.00 29.31 ? 357 HIS A O 1 ATOM 2705 C CB . HIS A 1 342 ? -18.767 128.461 -8.609 1.00 24.20 ? 357 HIS A CB 1 ATOM 2706 C CG . HIS A 1 342 ? -18.047 129.314 -9.597 1.00 24.26 ? 357 HIS A CG 1 ATOM 2707 N ND1 . HIS A 1 342 ? -17.997 129.014 -10.945 1.00 26.29 ? 357 HIS A ND1 1 ATOM 2708 C CD2 . HIS A 1 342 ? -17.335 130.454 -9.434 1.00 24.36 ? 357 HIS A CD2 1 ATOM 2709 C CE1 . HIS A 1 342 ? -17.296 129.944 -11.570 1.00 30.34 ? 357 HIS A CE1 1 ATOM 2710 N NE2 . HIS A 1 342 ? -16.871 130.821 -10.676 1.00 29.31 ? 357 HIS A NE2 1 ATOM 2711 N N . LYS A 1 343 ? -20.473 125.989 -8.479 1.00 29.28 ? 358 LYS A N 1 ATOM 2712 C CA . LYS A 1 343 ? -20.930 124.772 -7.810 1.00 28.75 ? 358 LYS A CA 1 ATOM 2713 C C . LYS A 1 343 ? -19.739 124.019 -7.206 1.00 32.38 ? 358 LYS A C 1 ATOM 2714 O O . LYS A 1 343 ? -18.847 123.583 -7.928 1.00 37.46 ? 358 LYS A O 1 ATOM 2715 C CB . LYS A 1 343 ? -21.688 123.887 -8.806 1.00 36.58 ? 358 LYS A CB 1 ATOM 2716 C CG . LYS A 1 343 ? -21.490 124.287 -10.263 1.00 52.23 ? 358 LYS A CG 1 ATOM 2717 C CD . LYS A 1 343 ? -20.097 123.914 -10.795 1.00 58.96 ? 358 LYS A CD 1 ATOM 2718 C CE . LYS A 1 343 ? -19.593 124.903 -11.864 1.00 55.46 ? 358 LYS A CE 1 ATOM 2719 N NZ . LYS A 1 343 ? -19.090 126.188 -11.280 1.00 40.95 ? 358 LYS A NZ 1 ATOM 2720 N N . GLY A 1 344 ? -19.705 123.908 -5.879 1.00 26.26 ? 359 GLY A N 1 ATOM 2721 C CA . GLY A 1 344 ? -18.695 123.115 -5.208 1.00 31.22 ? 359 GLY A CA 1 ATOM 2722 C C . GLY A 1 344 ? -17.417 123.887 -4.973 1.00 28.82 ? 359 GLY A C 1 ATOM 2723 O O . GLY A 1 344 ? -16.330 123.306 -4.955 1.00 39.17 ? 359 GLY A O 1 ATOM 2724 N N . TYR A 1 345 ? -17.543 125.202 -4.795 1.00 29.43 ? 360 TYR A N 1 ATOM 2725 C CA . TYR A 1 345 ? -16.376 126.033 -4.538 1.00 25.18 ? 360 TYR A CA 1 ATOM 2726 C C . TYR A 1 345 ? -16.365 126.476 -3.092 1.00 25.90 ? 360 TYR A C 1 ATOM 2727 O O . TYR A 1 345 ? -17.404 126.845 -2.530 1.00 28.88 ? 360 TYR A O 1 ATOM 2728 C CB . TYR A 1 345 ? -16.349 127.263 -5.452 1.00 26.71 ? 360 TYR A CB 1 ATOM 2729 C CG . TYR A 1 345 ? -15.189 128.197 -5.147 1.00 26.49 ? 360 TYR A CG 1 ATOM 2730 C CD1 . TYR A 1 345 ? -13.884 127.872 -5.519 1.00 32.70 ? 360 TYR A CD1 1 ATOM 2731 C CD2 . TYR A 1 345 ? -15.394 129.404 -4.485 1.00 24.40 ? 360 TYR A CD2 1 ATOM 2732 C CE1 . TYR A 1 345 ? -12.819 128.727 -5.234 1.00 35.68 ? 360 TYR A CE1 1 ATOM 2733 C CE2 . TYR A 1 345 ? -14.336 130.259 -4.199 1.00 28.29 ? 360 TYR A CE2 1 ATOM 2734 C CZ . TYR A 1 345 ? -13.055 129.919 -4.578 1.00 28.72 ? 360 TYR A CZ 1 ATOM 2735 O OH . TYR A 1 345 ? -12.008 130.777 -4.278 1.00 32.22 ? 360 TYR A OH 1 ATOM 2736 N N . LYS A 1 346 ? -15.187 126.451 -2.481 1.00 24.65 ? 361 LYS A N 1 ATOM 2737 C CA . LYS A 1 346 ? -15.057 126.974 -1.127 1.00 26.45 ? 361 LYS A CA 1 ATOM 2738 C C . LYS A 1 346 ? -13.954 128.035 -1.081 1.00 24.45 ? 361 LYS A C 1 ATOM 2739 O O . LYS A 1 346 ? -12.905 127.882 -1.711 1.00 30.21 ? 361 LYS A O 1 ATOM 2740 C CB . LYS A 1 346 ? -14.841 125.841 -0.112 1.00 33.10 ? 361 LYS A CB 1 ATOM 2741 C CG . LYS A 1 346 ? -13.627 124.958 -0.365 1.00 48.64 ? 361 LYS A CG 1 ATOM 2742 C CD . LYS A 1 346 ? -12.386 125.437 0.403 1.00 58.41 ? 361 LYS A CD 1 ATOM 2743 C CE . LYS A 1 346 ? -11.168 124.546 0.127 1.00 60.85 ? 361 LYS A CE 1 ATOM 2744 N NZ . LYS A 1 346 ? -11.354 123.160 0.657 1.00 61.93 ? 361 LYS A NZ 1 ATOM 2745 N N . HIS A 1 347 ? -14.222 129.126 -0.363 1.00 23.69 ? 362 HIS A N 1 ATOM 2746 C CA . HIS A 1 347 ? -13.348 130.285 -0.314 1.00 28.24 ? 362 HIS A CA 1 ATOM 2747 C C . HIS A 1 347 ? -13.137 130.566 1.166 1.00 22.76 ? 362 HIS A C 1 ATOM 2748 O O . HIS A 1 347 ? -14.020 130.313 1.979 1.00 21.96 ? 362 HIS A O 1 ATOM 2749 C CB . HIS A 1 347 ? -14.059 131.464 -0.980 1.00 27.71 ? 362 HIS A CB 1 ATOM 2750 C CG . HIS A 1 347 ? -13.183 132.643 -1.271 1.00 33.01 ? 362 HIS A CG 1 ATOM 2751 N ND1 . HIS A 1 347 ? -12.347 132.702 -2.366 1.00 35.57 ? 362 HIS A ND1 1 ATOM 2752 C CD2 . HIS A 1 347 ? -13.054 133.834 -0.636 1.00 28.04 ? 362 HIS A CD2 1 ATOM 2753 C CE1 . HIS A 1 347 ? -11.724 133.869 -2.380 1.00 31.16 ? 362 HIS A CE1 1 ATOM 2754 N NE2 . HIS A 1 347 ? -12.132 134.572 -1.338 1.00 31.32 ? 362 HIS A NE2 1 ATOM 2755 N N . SER A 1 348 ? -11.968 131.076 1.521 1.00 24.06 ? 363 SER A N 1 ATOM 2756 C CA . SER A 1 348 ? -11.621 131.289 2.924 1.00 20.66 ? 363 SER A CA 1 ATOM 2757 C C . SER A 1 348 ? -12.409 132.428 3.594 1.00 19.94 ? 363 SER A C 1 ATOM 2758 O O . SER A 1 348 ? -13.088 132.231 4.636 1.00 19.20 ? 363 SER A O 1 ATOM 2759 C CB . SER A 1 348 ? -10.124 131.568 3.013 1.00 30.77 ? 363 SER A CB 1 ATOM 2760 O OG . SER A 1 348 ? -9.816 132.153 4.255 1.00 41.62 ? 363 SER A OG 1 ATOM 2761 N N . THR A 1 349 ? -12.343 133.616 2.990 1.00 20.57 ? 364 THR A N 1 ATOM 2762 C CA . THR A 1 349 ? -12.886 134.807 3.648 1.00 16.58 ? 364 THR A CA 1 ATOM 2763 C C . THR A 1 349 ? -13.273 135.933 2.676 1.00 19.97 ? 364 THR A C 1 ATOM 2764 O O . THR A 1 349 ? -12.678 136.084 1.605 1.00 21.69 ? 364 THR A O 1 ATOM 2765 C CB . THR A 1 349 ? -11.891 135.344 4.695 1.00 20.66 ? 364 THR A CB 1 ATOM 2766 O OG1 . THR A 1 349 ? -12.517 136.357 5.504 1.00 22.13 ? 364 THR A OG1 1 ATOM 2767 C CG2 . THR A 1 349 ? -10.685 135.922 4.030 1.00 24.68 ? 364 THR A CG2 1 ATOM 2768 N N . ILE A 1 350 ? -14.319 136.675 3.042 1.00 16.85 ? 365 ILE A N 1 ATOM 2769 C CA . ILE A 1 350 ? -14.625 137.974 2.465 1.00 15.32 ? 365 ILE A CA 1 ATOM 2770 C C . ILE A 1 350 ? -14.963 138.897 3.632 1.00 12.99 ? 365 ILE A C 1 ATOM 2771 O O . ILE A 1 350 ? -15.134 138.428 4.781 1.00 14.46 ? 365 ILE A O 1 ATOM 2772 C CB . ILE A 1 350 ? -15.811 137.943 1.474 1.00 16.74 ? 365 ILE A CB 1 ATOM 2773 C CG1 . ILE A 1 350 ? -17.136 137.654 2.194 1.00 17.15 ? 365 ILE A CG1 1 ATOM 2774 C CG2 . ILE A 1 350 ? -15.543 136.969 0.344 1.00 18.65 ? 365 ILE A CG2 1 ATOM 2775 C CD1 . ILE A 1 350 ? -18.334 137.682 1.256 1.00 17.46 ? 365 ILE A CD1 1 ATOM 2776 N N . ASN A 1 351 ? -15.039 140.195 3.371 1.00 15.41 ? 366 ASN A N 1 ATOM 2777 C CA . ASN A 1 351 ? -15.514 141.135 4.374 1.00 12.58 ? 366 ASN A CA 1 ATOM 2778 C C . ASN A 1 351 ? -17.024 141.312 4.238 1.00 12.38 ? 366 ASN A C 1 ATOM 2779 O O . ASN A 1 351 ? -17.583 141.182 3.131 1.00 15.31 ? 366 ASN A O 1 ATOM 2780 C CB . ASN A 1 351 ? -14.761 142.456 4.239 1.00 16.70 ? 366 ASN A CB 1 ATOM 2781 C CG . ASN A 1 351 ? -13.259 142.279 4.489 1.00 24.14 ? 366 ASN A CG 1 ATOM 2782 O OD1 . ASN A 1 351 ? -12.854 141.517 5.388 1.00 29.82 ? 366 ASN A OD1 1 ATOM 2783 N ND2 . ASN A 1 351 ? -12.430 142.959 3.706 1.00 26.88 ? 366 ASN A ND2 1 ATOM 2784 N N . ILE A 1 352 ? -17.706 141.588 5.344 1.00 13.15 ? 367 ILE A N 1 ATOM 2785 C CA . ILE A 1 352 ? -19.171 141.640 5.296 1.00 12.64 ? 367 ILE A CA 1 ATOM 2786 C C . ILE A 1 352 ? -19.644 142.798 4.412 1.00 12.93 ? 367 ILE A C 1 ATOM 2787 O O . ILE A 1 352 ? -20.729 142.708 3.801 1.00 13.38 ? 367 ILE A O 1 ATOM 2788 C CB . ILE A 1 352 ? -19.752 141.737 6.719 1.00 11.60 ? 367 ILE A CB 1 ATOM 2789 C CG1 . ILE A 1 352 ? -21.252 141.397 6.744 1.00 14.45 ? 367 ILE A CG1 1 ATOM 2790 C CG2 . ILE A 1 352 ? -19.554 143.136 7.298 1.00 11.27 ? 367 ILE A CG2 1 ATOM 2791 C CD1 . ILE A 1 352 ? -21.768 141.217 8.162 1.00 16.99 ? 367 ILE A CD1 1 ATOM 2792 N N . VAL A 1 353 ? -18.831 143.850 4.263 1.00 13.78 ? 368 VAL A N 1 ATOM 2793 C CA . VAL A 1 353 ? -19.194 144.977 3.387 1.00 15.94 ? 368 VAL A CA 1 ATOM 2794 C C . VAL A 1 353 ? -19.057 144.639 1.893 1.00 14.11 ? 368 VAL A C 1 ATOM 2795 O O . VAL A 1 353 ? -19.481 145.414 1.024 1.00 16.96 ? 368 VAL A O 1 ATOM 2796 C CB . VAL A 1 353 ? -18.385 146.269 3.709 1.00 15.15 ? 368 VAL A CB 1 ATOM 2797 C CG1 . VAL A 1 353 ? -18.812 146.846 5.075 1.00 14.35 ? 368 VAL A CG1 1 ATOM 2798 C CG2 . VAL A 1 353 ? -16.884 145.981 3.669 1.00 15.45 ? 368 VAL A CG2 1 ATOM 2799 N N . ASP A 1 354 ? -18.486 143.474 1.589 1.00 15.06 ? 369 ASP A N 1 ATOM 2800 C CA . ASP A 1 354 ? -18.314 143.044 0.192 1.00 15.51 ? 369 ASP A CA 1 ATOM 2801 C C . ASP A 1 354 ? -19.580 142.387 -0.364 1.00 16.65 ? 369 ASP A C 1 ATOM 2802 O O . ASP A 1 354 ? -19.727 142.199 -1.579 1.00 18.08 ? 369 ASP A O 1 ATOM 2803 C CB . ASP A 1 354 ? -17.191 142.021 0.082 1.00 16.11 ? 369 ASP A CB 1 ATOM 2804 C CG . ASP A 1 354 ? -15.860 142.533 0.556 1.00 17.33 ? 369 ASP A CG 1 ATOM 2805 O OD1 . ASP A 1 354 ? -15.621 143.765 0.570 1.00 17.60 ? 369 ASP A OD1 1 ATOM 2806 O OD2 . ASP A 1 354 ? -15.022 141.683 0.923 1.00 18.09 ? 369 ASP A OD2 1 ATOM 2807 N N . ILE A 1 355 ? -20.491 142.005 0.520 1.00 15.90 ? 370 ILE A N 1 ATOM 2808 C CA . ILE A 1 355 ? -21.694 141.297 0.081 1.00 17.34 ? 370 ILE A CA 1 ATOM 2809 C C . ILE A 1 355 ? -22.582 142.218 -0.747 1.00 19.23 ? 370 ILE A C 1 ATOM 2810 O O . ILE A 1 355 ? -23.155 141.800 -1.769 1.00 17.07 ? 370 ILE A O 1 ATOM 2811 C CB . ILE A 1 355 ? -22.468 140.724 1.288 1.00 13.71 ? 370 ILE A CB 1 ATOM 2812 C CG1 . ILE A 1 355 ? -21.627 139.652 1.994 1.00 16.19 ? 370 ILE A CG1 1 ATOM 2813 C CG2 . ILE A 1 355 ? -23.799 140.089 0.853 1.00 17.16 ? 370 ILE A CG2 1 ATOM 2814 C CD1 . ILE A 1 355 ? -22.159 139.272 3.398 1.00 15.41 ? 370 ILE A CD1 1 ATOM 2815 N N . TYR A 1 356 ? -22.647 143.485 -0.345 1.00 18.15 ? 371 TYR A N 1 ATOM 2816 C CA . TYR A 1 356 ? -23.480 144.471 -1.041 1.00 18.96 ? 371 TYR A CA 1 ATOM 2817 C C . TYR A 1 356 ? -23.115 144.675 -2.502 1.00 20.26 ? 371 TYR A C 1 ATOM 2818 O O . TYR A 1 356 ? -24.000 144.561 -3.362 1.00 20.83 ? 371 TYR A O 1 ATOM 2819 C CB . TYR A 1 356 ? -23.475 145.797 -0.284 1.00 17.11 ? 371 TYR A CB 1 ATOM 2820 C CG . TYR A 1 356 ? -24.184 146.960 -0.959 1.00 15.96 ? 371 TYR A CG 1 ATOM 2821 C CD1 . TYR A 1 356 ? -25.569 147.060 -0.927 1.00 15.29 ? 371 TYR A CD1 1 ATOM 2822 C CD2 . TYR A 1 356 ? -23.462 147.967 -1.619 1.00 18.49 ? 371 TYR A CD2 1 ATOM 2823 C CE1 . TYR A 1 356 ? -26.220 148.124 -1.499 1.00 19.10 ? 371 TYR A CE1 1 ATOM 2824 C CE2 . TYR A 1 356 ? -24.105 149.035 -2.197 1.00 18.93 ? 371 TYR A CE2 1 ATOM 2825 C CZ . TYR A 1 356 ? -25.493 149.100 -2.146 1.00 16.08 ? 371 TYR A CZ 1 ATOM 2826 O OH . TYR A 1 356 ? -26.171 150.159 -2.717 1.00 19.32 ? 371 TYR A OH 1 ATOM 2827 N N . PRO A 1 357 ? -21.834 144.988 -2.807 1.00 14.96 ? 372 PRO A N 1 ATOM 2828 C CA . PRO A 1 357 ? -21.566 145.147 -4.246 1.00 18.06 ? 372 PRO A CA 1 ATOM 2829 C C . PRO A 1 357 ? -21.778 143.849 -5.021 1.00 15.69 ? 372 PRO A C 1 ATOM 2830 O O . PRO A 1 357 ? -22.170 143.911 -6.205 1.00 19.26 ? 372 PRO A O 1 ATOM 2831 C CB . PRO A 1 357 ? -20.088 145.606 -4.306 1.00 20.07 ? 372 PRO A CB 1 ATOM 2832 C CG . PRO A 1 357 ? -19.522 145.224 -2.935 1.00 22.03 ? 372 PRO A CG 1 ATOM 2833 C CD . PRO A 1 357 ? -20.656 145.330 -1.978 1.00 16.09 ? 372 PRO A CD 1 ATOM 2834 N N . MET A 1 358 ? -21.581 142.695 -4.393 1.00 15.73 ? 373 MET A N 1 ATOM 2835 C CA . MET A 1 358 ? -21.850 141.429 -5.077 1.00 18.68 ? 373 MET A CA 1 ATOM 2836 C C . MET A 1 358 ? -23.341 141.286 -5.376 1.00 14.88 ? 373 MET A C 1 ATOM 2837 O O . MET A 1 358 ? -23.730 140.855 -6.474 1.00 19.37 ? 373 MET A O 1 ATOM 2838 C CB . MET A 1 358 ? -21.369 140.245 -4.229 1.00 24.01 ? 373 MET A CB 1 ATOM 2839 C CG . MET A 1 358 ? -21.643 138.884 -4.867 1.00 20.23 ? 373 MET A CG 1 ATOM 2840 S SD . MET A 1 358 ? -21.304 137.499 -3.756 1.00 21.32 ? 373 MET A SD 1 ATOM 2841 C CE . MET A 1 358 ? -22.639 137.643 -2.589 1.00 26.03 ? 373 MET A CE 1 ATOM 2842 N N . MET A 1 359 ? -24.183 141.595 -4.385 1.00 17.88 ? 374 MET A N 1 ATOM 2843 C CA . MET A 1 359 ? -25.629 141.496 -4.604 1.00 15.01 ? 374 MET A CA 1 ATOM 2844 C C . MET A 1 359 ? -26.108 142.477 -5.660 1.00 19.73 ? 374 MET A C 1 ATOM 2845 O O . MET A 1 359 ? -26.981 142.130 -6.464 1.00 21.83 ? 374 MET A O 1 ATOM 2846 C CB . MET A 1 359 ? -26.421 141.701 -3.308 1.00 17.98 ? 374 MET A CB 1 ATOM 2847 C CG . MET A 1 359 ? -26.141 140.661 -2.221 1.00 17.91 ? 374 MET A CG 1 ATOM 2848 S SD . MET A 1 359 ? -27.281 140.733 -0.834 1.00 19.84 ? 374 MET A SD 1 ATOM 2849 C CE . MET A 1 359 ? -26.859 142.356 -0.215 1.00 17.17 ? 374 MET A CE 1 ATOM 2850 N N . CYS A 1 360 ? -25.578 143.702 -5.661 1.00 19.89 ? 375 CYS A N 1 ATOM 2851 C CA . CYS A 1 360 ? -25.980 144.652 -6.708 1.00 23.16 ? 375 CYS A CA 1 ATOM 2852 C C . CYS A 1 360 ? -25.595 144.106 -8.066 1.00 18.00 ? 375 CYS A C 1 ATOM 2853 O O . CYS A 1 360 ? -26.356 144.214 -9.032 1.00 22.07 ? 375 CYS A O 1 ATOM 2854 C CB . CYS A 1 360 ? -25.366 146.047 -6.510 1.00 19.62 ? 375 CYS A CB 1 ATOM 2855 S SG . CYS A 1 360 ? -26.002 146.931 -5.040 1.00 20.40 ? 375 CYS A SG 1 ATOM 2856 N N . HIS A 1 361 ? -24.416 143.504 -8.166 1.00 20.76 ? 376 HIS A N 1 ATOM 2857 C CA . HIS A 1 361 ? -24.007 142.945 -9.447 1.00 22.28 ? 376 HIS A CA 1 ATOM 2858 C C . HIS A 1 361 ? -24.974 141.848 -9.912 1.00 23.71 ? 376 HIS A C 1 ATOM 2859 O O . HIS A 1 361 ? -25.397 141.838 -11.064 1.00 25.29 ? 376 HIS A O 1 ATOM 2860 C CB . HIS A 1 361 ? -22.573 142.414 -9.375 1.00 22.71 ? 376 HIS A CB 1 ATOM 2861 C CG . HIS A 1 361 ? -22.133 141.704 -10.611 1.00 20.81 ? 376 HIS A CG 1 ATOM 2862 N ND1 . HIS A 1 361 ? -21.582 142.361 -11.688 1.00 26.52 ? 376 HIS A ND1 1 ATOM 2863 C CD2 . HIS A 1 361 ? -22.160 140.391 -10.939 1.00 23.11 ? 376 HIS A CD2 1 ATOM 2864 C CE1 . HIS A 1 361 ? -21.285 141.481 -12.630 1.00 33.68 ? 376 HIS A CE1 1 ATOM 2865 N NE2 . HIS A 1 361 ? -21.626 140.277 -12.200 1.00 26.87 ? 376 HIS A NE2 1 ATOM 2866 N N . ILE A 1 362 ? -25.328 140.927 -9.019 1.00 22.63 ? 377 ILE A N 1 ATOM 2867 C CA . ILE A 1 362 ? -26.250 139.844 -9.370 1.00 21.55 ? 377 ILE A CA 1 ATOM 2868 C C . ILE A 1 362 ? -27.591 140.374 -9.872 1.00 23.83 ? 377 ILE A C 1 ATOM 2869 O O . ILE A 1 362 ? -28.168 139.834 -10.823 1.00 28.51 ? 377 ILE A O 1 ATOM 2870 C CB . ILE A 1 362 ? -26.480 138.897 -8.174 1.00 22.01 ? 377 ILE A CB 1 ATOM 2871 C CG1 . ILE A 1 362 ? -25.186 138.153 -7.864 1.00 23.90 ? 377 ILE A CG1 1 ATOM 2872 C CG2 . ILE A 1 362 ? -27.639 137.918 -8.467 1.00 25.67 ? 377 ILE A CG2 1 ATOM 2873 C CD1 . ILE A 1 362 ? -25.155 137.458 -6.520 1.00 23.11 ? 377 ILE A CD1 1 ATOM 2874 N N . LEU A 1 363 ? -28.063 141.460 -9.260 1.00 21.66 ? 378 LEU A N 1 ATOM 2875 C CA . LEU A 1 363 ? -29.393 142.008 -9.543 1.00 24.58 ? 378 LEU A CA 1 ATOM 2876 C C . LEU A 1 363 ? -29.389 143.061 -10.626 1.00 23.21 ? 378 LEU A C 1 ATOM 2877 O O . LEU A 1 363 ? -30.453 143.540 -11.020 1.00 30.36 ? 378 LEU A O 1 ATOM 2878 C CB . LEU A 1 363 ? -29.997 142.629 -8.277 1.00 26.72 ? 378 LEU A CB 1 ATOM 2879 C CG . LEU A 1 363 ? -30.404 141.647 -7.185 1.00 23.23 ? 378 LEU A CG 1 ATOM 2880 C CD1 . LEU A 1 363 ? -30.903 142.378 -5.933 1.00 23.24 ? 378 LEU A CD1 1 ATOM 2881 C CD2 . LEU A 1 363 ? -31.467 140.697 -7.737 1.00 30.69 ? 378 LEU A CD2 1 ATOM 2882 N N . GLY A 1 364 ? -28.204 143.439 -11.103 1.00 24.92 ? 379 GLY A N 1 ATOM 2883 C CA . GLY A 1 364 ? -28.093 144.492 -12.107 1.00 26.27 ? 379 GLY A CA 1 ATOM 2884 C C . GLY A 1 364 ? -28.463 145.872 -11.576 1.00 26.58 ? 379 GLY A C 1 ATOM 2885 O O . GLY A 1 364 ? -29.077 146.676 -12.285 1.00 29.64 ? 379 GLY A O 1 ATOM 2886 N N . LEU A 1 365 ? -28.098 146.140 -10.322 1.00 25.24 ? 380 LEU A N 1 ATOM 2887 C CA . LEU A 1 365 ? -28.369 147.429 -9.683 1.00 22.75 ? 380 LEU A CA 1 ATOM 2888 C C . LEU A 1 365 ? -27.094 148.233 -9.606 1.00 29.52 ? 380 LEU A C 1 ATOM 2889 O O . LEU A 1 365 ? -26.021 147.662 -9.395 1.00 25.98 ? 380 LEU A O 1 ATOM 2890 C CB . LEU A 1 365 ? -28.892 147.216 -8.259 1.00 24.88 ? 380 LEU A CB 1 ATOM 2891 C CG . LEU A 1 365 ? -30.254 146.532 -8.125 1.00 25.30 ? 380 LEU A CG 1 ATOM 2892 C CD1 . LEU A 1 365 ? -30.636 146.361 -6.657 1.00 28.99 ? 380 LEU A CD1 1 ATOM 2893 C CD2 . LEU A 1 365 ? -31.334 147.320 -8.851 1.00 29.67 ? 380 LEU A CD2 1 ATOM 2894 N N . LYS A 1 366 ? -27.207 149.552 -9.739 1.00 31.15 ? 381 LYS A N 1 ATOM 2895 C CA . LYS A 1 366 ? -26.068 150.436 -9.465 1.00 29.78 ? 381 LYS A CA 1 ATOM 2896 C C . LYS A 1 366 ? -25.897 150.622 -7.972 1.00 24.19 ? 381 LYS A C 1 ATOM 2897 O O . LYS A 1 366 ? -26.781 151.151 -7.292 1.00 31.48 ? 381 LYS A O 1 ATOM 2898 C CB . LYS A 1 366 ? -26.229 151.783 -10.148 1.00 36.19 ? 381 LYS A CB 1 ATOM 2899 C CG . LYS A 1 366 ? -25.652 151.759 -11.546 1.00 54.10 ? 381 LYS A CG 1 ATOM 2900 C CD . LYS A 1 366 ? -26.448 152.596 -12.528 1.00 56.35 ? 381 LYS A CD 1 ATOM 2901 C CE . LYS A 1 366 ? -25.739 152.616 -13.874 1.00 57.79 ? 381 LYS A CE 1 ATOM 2902 N NZ . LYS A 1 366 ? -26.515 153.357 -14.903 1.00 57.36 ? 381 LYS A NZ 1 ATOM 2903 N N . PRO A 1 367 ? -24.745 150.198 -7.454 1.00 24.50 ? 382 PRO A N 1 ATOM 2904 C CA . PRO A 1 367 ? -24.528 150.334 -6.015 1.00 25.35 ? 382 PRO A CA 1 ATOM 2905 C C . PRO A 1 367 ? -24.342 151.802 -5.618 1.00 21.51 ? 382 PRO A C 1 ATOM 2906 O O . PRO A 1 367 ? -23.806 152.597 -6.391 1.00 23.12 ? 382 PRO A O 1 ATOM 2907 C CB . PRO A 1 367 ? -23.235 149.532 -5.780 1.00 24.85 ? 382 PRO A CB 1 ATOM 2908 C CG . PRO A 1 367 ? -22.531 149.573 -7.083 1.00 32.19 ? 382 PRO A CG 1 ATOM 2909 C CD . PRO A 1 367 ? -23.618 149.533 -8.132 1.00 26.68 ? 382 PRO A CD 1 ATOM 2910 N N . HIS A 1 368 ? -24.825 152.160 -4.433 1.00 21.88 ? 383 HIS A N 1 ATOM 2911 C CA . HIS A 1 368 ? -24.425 153.412 -3.816 1.00 21.22 ? 383 HIS A CA 1 ATOM 2912 C C . HIS A 1 368 ? -22.961 153.300 -3.420 1.00 22.89 ? 383 HIS A C 1 ATOM 2913 O O . HIS A 1 368 ? -22.439 152.186 -3.246 1.00 24.41 ? 383 HIS A O 1 ATOM 2914 C CB . HIS A 1 368 ? -25.279 153.714 -2.593 1.00 26.64 ? 383 HIS A CB 1 ATOM 2915 C CG . HIS A 1 368 ? -26.674 154.142 -2.927 1.00 32.29 ? 383 HIS A CG 1 ATOM 2916 N ND1 . HIS A 1 368 ? -27.165 155.392 -2.616 1.00 33.28 ? 383 HIS A ND1 1 ATOM 2917 C CD2 . HIS A 1 368 ? -27.674 153.494 -3.572 1.00 36.21 ? 383 HIS A CD2 1 ATOM 2918 C CE1 . HIS A 1 368 ? -28.413 155.490 -3.042 1.00 34.70 ? 383 HIS A CE1 1 ATOM 2919 N NE2 . HIS A 1 368 ? -28.747 154.352 -3.624 1.00 35.58 ? 383 HIS A NE2 1 ATOM 2920 N N . PRO A 1 369 ? -22.283 154.449 -3.279 1.00 23.27 ? 384 PRO A N 1 ATOM 2921 C CA . PRO A 1 369 ? -20.898 154.425 -2.795 1.00 22.02 ? 384 PRO A CA 1 ATOM 2922 C C . PRO A 1 369 ? -20.831 153.617 -1.507 1.00 22.34 ? 384 PRO A C 1 ATOM 2923 O O . PRO A 1 369 ? -21.712 153.745 -0.640 1.00 21.45 ? 384 PRO A O 1 ATOM 2924 C CB . PRO A 1 369 ? -20.616 155.895 -2.518 1.00 25.77 ? 384 PRO A CB 1 ATOM 2925 C CG . PRO A 1 369 ? -21.420 156.598 -3.572 1.00 27.92 ? 384 PRO A CG 1 ATOM 2926 C CD . PRO A 1 369 ? -22.723 155.817 -3.607 1.00 30.56 ? 384 PRO A CD 1 ATOM 2927 N N . ASN A 1 370 ? -19.811 152.775 -1.385 1.00 20.84 ? 385 ASN A N 1 ATOM 2928 C CA . ASN A 1 370 ? -19.766 151.853 -0.258 1.00 17.52 ? 385 ASN A CA 1 ATOM 2929 C C . ASN A 1 370 ? -18.331 151.510 0.075 1.00 14.49 ? 385 ASN A C 1 ATOM 2930 O O . ASN A 1 370 ? -17.416 152.010 -0.581 1.00 20.87 ? 385 ASN A O 1 ATOM 2931 C CB . ASN A 1 370 ? -20.600 150.596 -0.559 1.00 20.59 ? 385 ASN A CB 1 ATOM 2932 C CG . ASN A 1 370 ? -20.029 149.769 -1.718 1.00 16.45 ? 385 ASN A CG 1 ATOM 2933 O OD1 . ASN A 1 370 ? -19.164 148.918 -1.513 1.00 22.12 ? 385 ASN A OD1 1 ATOM 2934 N ND2 . ASN A 1 370 ? -20.529 150.008 -2.938 1.00 18.71 ? 385 ASN A ND2 1 ATOM 2935 N N . ASN A 1 371 ? -18.131 150.679 1.096 1.00 16.62 ? 386 ASN A N 1 ATOM 2936 C CA . ASN A 1 371 ? -16.792 150.384 1.584 1.00 16.96 ? 386 ASN A CA 1 ATOM 2937 C C . ASN A 1 371 ? -16.348 148.985 1.220 1.00 15.13 ? 386 ASN A C 1 ATOM 2938 O O . ASN A 1 371 ? -15.266 148.559 1.599 1.00 20.39 ? 386 ASN A O 1 ATOM 2939 C CB . ASN A 1 371 ? -16.741 150.524 3.100 1.00 17.38 ? 386 ASN A CB 1 ATOM 2940 C CG . ASN A 1 371 ? -17.138 151.898 3.563 1.00 16.80 ? 386 ASN A CG 1 ATOM 2941 O OD1 . ASN A 1 371 ? -18.062 152.045 4.386 1.00 15.63 ? 386 ASN A OD1 1 ATOM 2942 N ND2 . ASN A 1 371 ? -16.429 152.923 3.065 1.00 21.60 ? 386 ASN A ND2 1 ATOM 2943 N N . GLY A 1 372 ? -17.189 148.286 0.461 1.00 17.60 ? 387 GLY A N 1 ATOM 2944 C CA . GLY A 1 372 ? -16.894 146.938 0.034 1.00 19.92 ? 387 GLY A CA 1 ATOM 2945 C C . GLY A 1 372 ? -16.002 146.870 -1.194 1.00 19.20 ? 387 GLY A C 1 ATOM 2946 O O . GLY A 1 372 ? -15.823 147.862 -1.931 1.00 20.77 ? 387 GLY A O 1 ATOM 2947 N N . THR A 1 373 ? -15.439 145.678 -1.398 1.00 20.56 ? 388 THR A N 1 ATOM 2948 C CA . THR A 1 373 ? -14.571 145.418 -2.535 1.00 19.66 ? 388 THR A CA 1 ATOM 2949 C C . THR A 1 373 ? -15.149 144.253 -3.324 1.00 16.80 ? 388 THR A C 1 ATOM 2950 O O . THR A 1 373 ? -15.084 143.112 -2.870 1.00 20.67 ? 388 THR A O 1 ATOM 2951 C CB . THR A 1 373 ? -13.170 145.038 -2.074 1.00 22.28 ? 388 THR A CB 1 ATOM 2952 O OG1 . THR A 1 373 ? -12.613 146.114 -1.304 1.00 28.28 ? 388 THR A OG1 1 ATOM 2953 C CG2 . THR A 1 373 ? -12.275 144.740 -3.281 1.00 24.25 ? 388 THR A CG2 1 ATOM 2954 N N . PHE A 1 374 ? -15.750 144.550 -4.472 1.00 23.09 ? 389 PHE A N 1 ATOM 2955 C CA . PHE A 1 374 ? -16.373 143.525 -5.304 1.00 21.21 ? 389 PHE A CA 1 ATOM 2956 C C . PHE A 1 374 ? -15.387 142.423 -5.644 1.00 19.19 ? 389 PHE A C 1 ATOM 2957 O O . PHE A 1 374 ? -15.765 141.257 -5.699 1.00 22.18 ? 389 PHE A O 1 ATOM 2958 C CB . PHE A 1 374 ? -16.905 144.135 -6.608 1.00 20.58 ? 389 PHE A CB 1 ATOM 2959 C CG . PHE A 1 374 ? -17.503 143.130 -7.560 1.00 19.24 ? 389 PHE A CG 1 ATOM 2960 C CD1 . PHE A 1 374 ? -16.844 142.778 -8.718 1.00 23.74 ? 389 PHE A CD1 1 ATOM 2961 C CD2 . PHE A 1 374 ? -18.735 142.555 -7.309 1.00 23.93 ? 389 PHE A CD2 1 ATOM 2962 C CE1 . PHE A 1 374 ? -17.397 141.867 -9.604 1.00 25.10 ? 389 PHE A CE1 1 ATOM 2963 C CE2 . PHE A 1 374 ? -19.281 141.628 -8.188 1.00 24.14 ? 389 PHE A CE2 1 ATOM 2964 C CZ . PHE A 1 374 ? -18.617 141.292 -9.344 1.00 22.76 ? 389 PHE A CZ 1 ATOM 2965 N N . GLY A 1 375 ? -14.134 142.806 -5.896 1.00 22.53 ? 390 GLY A N 1 ATOM 2966 C CA . GLY A 1 375 ? -13.081 141.851 -6.202 1.00 24.06 ? 390 GLY A CA 1 ATOM 2967 C C . GLY A 1 375 ? -12.987 140.670 -5.257 1.00 23.96 ? 390 GLY A C 1 ATOM 2968 O O . GLY A 1 375 ? -12.673 139.552 -5.673 1.00 22.46 ? 390 GLY A O 1 ATOM 2969 N N . HIS A 1 376 ? -13.272 140.903 -3.982 1.00 19.27 ? 391 HIS A N 1 ATOM 2970 C CA . HIS A 1 376 ? -13.168 139.824 -3.001 1.00 18.77 ? 391 HIS A CA 1 ATOM 2971 C C . HIS A 1 376 ? -14.168 138.702 -3.256 1.00 18.20 ? 391 HIS A C 1 ATOM 2972 O O . HIS A 1 376 ? -13.974 137.577 -2.763 1.00 21.35 ? 391 HIS A O 1 ATOM 2973 C CB . HIS A 1 376 ? -13.386 140.371 -1.587 1.00 23.47 ? 391 HIS A CB 1 ATOM 2974 C CG . HIS A 1 376 ? -12.316 141.308 -1.113 1.00 21.43 ? 391 HIS A CG 1 ATOM 2975 N ND1 . HIS A 1 376 ? -12.453 142.047 0.043 1.00 19.47 ? 391 HIS A ND1 1 ATOM 2976 C CD2 . HIS A 1 376 ? -11.087 141.609 -1.606 1.00 25.00 ? 391 HIS A CD2 1 ATOM 2977 C CE1 . HIS A 1 376 ? -11.363 142.770 0.238 1.00 21.38 ? 391 HIS A CE1 1 ATOM 2978 N NE2 . HIS A 1 376 ? -10.515 142.520 -0.744 1.00 25.14 ? 391 HIS A NE2 1 ATOM 2979 N N . THR A 1 377 ? -15.231 138.992 -4.020 1.00 17.33 ? 392 THR A N 1 ATOM 2980 C CA . THR A 1 377 ? -16.314 138.018 -4.211 1.00 20.31 ? 392 THR A CA 1 ATOM 2981 C C . THR A 1 377 ? -16.302 137.339 -5.574 1.00 19.69 ? 392 THR A C 1 ATOM 2982 O O . THR A 1 377 ? -17.113 136.450 -5.828 1.00 22.79 ? 392 THR A O 1 ATOM 2983 C CB . THR A 1 377 ? -17.711 138.628 -3.995 1.00 18.38 ? 392 THR A CB 1 ATOM 2984 O OG1 . THR A 1 377 ? -18.027 139.513 -5.069 1.00 19.94 ? 392 THR A OG1 1 ATOM 2985 C CG2 . THR A 1 377 ? -17.770 139.397 -2.667 1.00 22.64 ? 392 THR A CG2 1 ATOM 2986 N N . LYS A 1 378 ? -15.378 137.746 -6.440 1.00 19.38 ? 393 LYS A N 1 ATOM 2987 C CA . LYS A 1 378 ? -15.383 137.268 -7.831 1.00 20.32 ? 393 LYS A CA 1 ATOM 2988 C C . LYS A 1 378 ? -15.266 135.750 -7.957 1.00 19.87 ? 393 LYS A C 1 ATOM 2989 O O . LYS A 1 378 ? -15.894 135.136 -8.836 1.00 21.53 ? 393 LYS A O 1 ATOM 2990 C CB . LYS A 1 378 ? -14.298 137.972 -8.656 1.00 23.78 ? 393 LYS A CB 1 ATOM 2991 C CG . LYS A 1 378 ? -14.594 139.440 -8.889 1.00 28.14 ? 393 LYS A CG 1 ATOM 2992 C CD . LYS A 1 378 ? -13.393 140.193 -9.451 1.00 28.04 ? 393 LYS A CD 1 ATOM 2993 C CE . LYS A 1 378 ? -13.539 140.397 -10.932 1.00 33.83 ? 393 LYS A CE 1 ATOM 2994 N NZ . LYS A 1 378 ? -12.525 141.367 -11.421 1.00 34.57 ? 393 LYS A NZ 1 ATOM 2995 N N . CYS A 1 379 ? -14.485 135.124 -7.079 1.00 18.78 ? 394 CYS A N 1 ATOM 2996 C CA . CYS A 1 379 ? -14.370 133.671 -7.125 1.00 19.16 ? 394 CYS A CA 1 ATOM 2997 C C . CYS A 1 379 ? -15.669 132.916 -6.846 1.00 22.44 ? 394 CYS A C 1 ATOM 2998 O O . CYS A 1 379 ? -15.770 131.740 -7.165 1.00 23.30 ? 394 CYS A O 1 ATOM 2999 C CB . CYS A 1 379 ? -13.238 133.179 -6.220 1.00 22.22 ? 394 CYS A CB 1 ATOM 3000 S SG . CYS A 1 379 ? -11.641 133.612 -6.896 1.00 28.89 ? 394 CYS A SG 1 ATOM 3001 N N . LEU A 1 380 ? -16.653 133.589 -6.258 1.00 21.27 ? 395 LEU A N 1 ATOM 3002 C CA . LEU A 1 380 ? -17.952 132.975 -6.011 1.00 22.89 ? 395 LEU A CA 1 ATOM 3003 C C . LEU A 1 380 ? -18.875 132.990 -7.236 1.00 18.55 ? 395 LEU A C 1 ATOM 3004 O O . LEU A 1 380 ? -19.861 132.243 -7.281 1.00 20.74 ? 395 LEU A O 1 ATOM 3005 C CB . LEU A 1 380 ? -18.661 133.710 -4.882 1.00 19.79 ? 395 LEU A CB 1 ATOM 3006 C CG . LEU A 1 380 ? -17.887 133.930 -3.594 1.00 18.58 ? 395 LEU A CG 1 ATOM 3007 C CD1 . LEU A 1 380 ? -18.801 134.619 -2.594 1.00 22.92 ? 395 LEU A CD1 1 ATOM 3008 C CD2 . LEU A 1 380 ? -17.380 132.600 -3.034 1.00 25.27 ? 395 LEU A CD2 1 ATOM 3009 N N . LEU A 1 381 ? -18.570 133.843 -8.214 1.00 20.41 ? 396 LEU A N 1 ATOM 3010 C CA . LEU A 1 381 ? -19.532 134.177 -9.262 1.00 21.54 ? 396 LEU A CA 1 ATOM 3011 C C . LEU A 1 381 ? -19.178 133.588 -10.615 1.00 22.57 ? 396 LEU A C 1 ATOM 3012 O O . LEU A 1 381 ? -18.043 133.717 -11.069 1.00 22.90 ? 396 LEU A O 1 ATOM 3013 C CB . LEU A 1 381 ? -19.632 135.693 -9.408 1.00 18.91 ? 396 LEU A CB 1 ATOM 3014 C CG . LEU A 1 381 ? -20.015 136.472 -8.141 1.00 18.38 ? 396 LEU A CG 1 ATOM 3015 C CD1 . LEU A 1 381 ? -19.765 137.965 -8.280 1.00 23.95 ? 396 LEU A CD1 1 ATOM 3016 C CD2 . LEU A 1 381 ? -21.490 136.218 -7.852 1.00 22.50 ? 396 LEU A CD2 1 ATOM 3017 N N . VAL A 1 382 ? -20.164 132.963 -11.258 1.00 24.09 ? 397 VAL A N 1 ATOM 3018 C CA . VAL A 1 382 ? -19.953 132.281 -12.555 1.00 25.41 ? 397 VAL A CA 1 ATOM 3019 C C . VAL A 1 382 ? -19.496 133.180 -13.701 1.00 27.80 ? 397 VAL A C 1 ATOM 3020 O O . VAL A 1 382 ? -18.819 132.714 -14.627 1.00 36.31 ? 397 VAL A O 1 ATOM 3021 C CB . VAL A 1 382 ? -21.201 131.509 -13.012 1.00 31.67 ? 397 VAL A CB 1 ATOM 3022 C CG1 . VAL A 1 382 ? -21.504 130.359 -12.055 1.00 31.63 ? 397 VAL A CG1 1 ATOM 3023 C CG2 . VAL A 1 382 ? -22.384 132.436 -13.102 1.00 32.94 ? 397 VAL A CG2 1 ATOM 3024 N N . ASP A 1 383 ? -19.869 134.453 -13.681 1.00 26.84 ? 398 ASP A N 1 ATOM 3025 C CA . ASP A 1 383 ? -19.499 135.299 -14.819 1.00 34.43 ? 398 ASP A CA 1 ATOM 3026 C C . ASP A 1 383 ? -18.144 135.987 -14.653 1.00 23.22 ? 398 ASP A C 1 ATOM 3027 O O . ASP A 1 383 ? -17.785 136.814 -15.476 1.00 22.16 ? 398 ASP A O 1 ATOM 3028 C CB . ASP A 1 383 ? -20.577 136.363 -15.078 1.00 31.82 ? 398 ASP A CB 1 ATOM 3029 C CG . ASP A 1 383 ? -20.721 137.343 -13.917 1.00 32.57 ? 398 ASP A CG 1 ATOM 3030 O OD1 . ASP A 1 383 ? -20.453 136.934 -12.773 1.00 44.76 ? 398 ASP A OD1 1 ATOM 3031 O OD2 . ASP A 1 383 ? -21.096 138.517 -14.130 1.00 38.99 ? 398 ASP A OD2 1 ATOM 3032 N N . GLN A 1 384 ? -17.408 135.647 -13.595 1.00 21.52 ? 399 GLN A N 1 ATOM 3033 C CA . GLN A 1 384 ? -16.272 136.449 -13.162 1.00 18.97 ? 399 GLN A CA 1 ATOM 3034 C C . GLN A 1 384 ? -14.922 135.708 -13.201 1.00 21.14 ? 399 GLN A C 1 ATOM 3035 O O . GLN A 1 384 ? -14.842 134.492 -12.961 1.00 22.45 ? 399 GLN A O 1 ATOM 3036 C CB . GLN A 1 384 ? -16.541 136.981 -11.741 1.00 22.26 ? 399 GLN A CB 1 ATOM 3037 C CG . GLN A 1 384 ? -17.733 137.923 -11.669 1.00 24.68 ? 399 GLN A CG 1 ATOM 3038 C CD . GLN A 1 384 ? -17.447 139.256 -12.336 1.00 24.12 ? 399 GLN A CD 1 ATOM 3039 O OE1 . GLN A 1 384 ? -16.402 139.863 -12.103 1.00 26.75 ? 399 GLN A OE1 1 ATOM 3040 N NE2 . GLN A 1 384 ? -18.361 139.708 -13.185 1.00 25.22 ? 399 GLN A NE2 1 ATOM 3041 N N . TRP A 1 385 ? -13.865 136.453 -13.506 1.00 20.73 ? 400 TRP A N 1 ATOM 3042 C CA . TRP A 1 385 ? -12.509 135.928 -13.403 1.00 20.93 ? 400 TRP A CA 1 ATOM 3043 C C . TRP A 1 385 ? -12.185 135.588 -11.947 1.00 23.01 ? 400 TRP A C 1 ATOM 3044 O O . TRP A 1 385 ? -12.486 136.364 -11.033 1.00 22.74 ? 400 TRP A O 1 ATOM 3045 C CB . TRP A 1 385 ? -11.488 136.957 -13.902 1.00 20.12 ? 400 TRP A CB 1 ATOM 3046 C CG . TRP A 1 385 ? -11.578 137.395 -15.364 1.00 17.13 ? 400 TRP A CG 1 ATOM 3047 C CD1 . TRP A 1 385 ? -11.957 138.630 -15.830 1.00 21.71 ? 400 TRP A CD1 1 ATOM 3048 C CD2 . TRP A 1 385 ? -11.250 136.617 -16.516 1.00 19.37 ? 400 TRP A CD2 1 ATOM 3049 N NE1 . TRP A 1 385 ? -11.878 138.663 -17.202 1.00 19.95 ? 400 TRP A NE1 1 ATOM 3050 C CE2 . TRP A 1 385 ? -11.436 137.443 -17.647 1.00 18.62 ? 400 TRP A CE2 1 ATOM 3051 C CE3 . TRP A 1 385 ? -10.794 135.313 -16.701 1.00 18.76 ? 400 TRP A CE3 1 ATOM 3052 C CZ2 . TRP A 1 385 ? -11.196 136.998 -18.942 1.00 25.28 ? 400 TRP A CZ2 1 ATOM 3053 C CZ3 . TRP A 1 385 ? -10.552 134.870 -17.994 1.00 21.17 ? 400 TRP A CZ3 1 ATOM 3054 C CH2 . TRP A 1 385 ? -10.759 135.709 -19.092 1.00 20.29 ? 400 TRP A CH2 1 ATOM 3055 N N . CYS A 1 386 ? -11.585 134.425 -11.727 1.00 21.95 ? 401 CYS A N 1 ATOM 3056 C CA . CYS A 1 386 ? -11.154 134.039 -10.392 1.00 23.85 ? 401 CYS A CA 1 ATOM 3057 C C . CYS A 1 386 ? -9.658 133.912 -10.373 1.00 24.93 ? 401 CYS A C 1 ATOM 3058 O O . CYS A 1 386 ? -9.112 132.936 -10.884 1.00 28.51 ? 401 CYS A O 1 ATOM 3059 C CB . CYS A 1 386 ? -11.748 132.703 -9.986 1.00 22.61 ? 401 CYS A CB 1 ATOM 3060 S SG . CYS A 1 386 ? -11.188 132.217 -8.322 1.00 26.59 ? 401 CYS A SG 1 ATOM 3061 N N . ILE A 1 387 ? -8.993 134.899 -9.792 1.00 25.75 ? 402 ILE A N 1 ATOM 3062 C CA . ILE A 1 387 ? -7.569 134.773 -9.528 1.00 34.74 ? 402 ILE A CA 1 ATOM 3063 C C . ILE A 1 387 ? -7.468 134.439 -8.048 1.00 43.23 ? 402 ILE A C 1 ATOM 3064 O O . ILE A 1 387 ? -7.167 133.306 -7.661 1.00 51.81 ? 402 ILE A O 1 ATOM 3065 C CB . ILE A 1 387 ? -6.811 136.070 -9.829 1.00 38.99 ? 402 ILE A CB 1 ATOM 3066 C CG1 . ILE A 1 387 ? -7.621 136.950 -10.777 1.00 39.42 ? 402 ILE A CG1 1 ATOM 3067 C CG2 . ILE A 1 387 ? -5.444 135.756 -10.440 1.00 49.08 ? 402 ILE A CG2 1 ATOM 3068 C CD1 . ILE A 1 387 ? -7.162 138.390 -10.837 1.00 40.77 ? 402 ILE A CD1 1 HETATM 3069 C C1 . NAG B 2 . ? -16.961 154.224 3.359 1.00 20.90 ? 501 NAG A C1 1 HETATM 3070 C C2 . NAG B 2 . ? -15.815 155.210 3.559 1.00 21.15 ? 501 NAG A C2 1 HETATM 3071 C C3 . NAG B 2 . ? -16.366 156.619 3.761 1.00 23.14 ? 501 NAG A C3 1 HETATM 3072 C C4 . NAG B 2 . ? -17.346 156.984 2.650 1.00 24.80 ? 501 NAG A C4 1 HETATM 3073 C C5 . NAG B 2 . ? -18.389 155.886 2.474 1.00 24.59 ? 501 NAG A C5 1 HETATM 3074 C C6 . NAG B 2 . ? -19.284 156.107 1.279 1.00 26.96 ? 501 NAG A C6 1 HETATM 3075 C C7 . NAG B 2 . ? -13.675 154.610 4.597 1.00 19.32 ? 501 NAG A C7 1 HETATM 3076 C C8 . NAG B 2 . ? -12.978 154.235 5.868 1.00 22.62 ? 501 NAG A C8 1 HETATM 3077 N N2 . NAG B 2 . ? -14.989 154.832 4.693 1.00 19.03 ? 501 NAG A N2 1 HETATM 3078 O O3 . NAG B 2 . ? -15.279 157.541 3.829 1.00 23.13 ? 501 NAG A O3 1 HETATM 3079 O O4 . NAG B 2 . ? -18.062 158.159 3.010 1.00 30.92 ? 501 NAG A O4 1 HETATM 3080 O O5 . NAG B 2 . ? -17.739 154.630 2.260 1.00 20.92 ? 501 NAG A O5 1 HETATM 3081 O O6 . NAG B 2 . ? -18.510 156.455 0.139 1.00 25.68 ? 501 NAG A O6 1 HETATM 3082 O O7 . NAG B 2 . ? -13.077 154.683 3.522 1.00 26.20 ? 501 NAG A O7 1 HETATM 3083 C C1 . NAG C 2 . ? -17.477 159.324 2.409 1.00 43.21 ? 502 NAG A C1 1 HETATM 3084 C C2 . NAG C 2 . ? -18.529 160.420 2.275 1.00 49.94 ? 502 NAG A C2 1 HETATM 3085 C C3 . NAG C 2 . ? -17.908 161.667 1.655 1.00 57.48 ? 502 NAG A C3 1 HETATM 3086 C C4 . NAG C 2 . ? -16.676 162.083 2.449 1.00 65.63 ? 502 NAG A C4 1 HETATM 3087 C C5 . NAG C 2 . ? -15.718 160.901 2.537 1.00 63.07 ? 502 NAG A C5 1 HETATM 3088 C C6 . NAG C 2 . ? -14.465 161.183 3.332 1.00 59.34 ? 502 NAG A C6 1 HETATM 3089 C C7 . NAG C 2 . ? -20.738 159.378 2.040 1.00 53.50 ? 502 NAG A C7 1 HETATM 3090 C C8 . NAG C 2 . ? -21.822 158.963 1.083 1.00 54.04 ? 502 NAG A C8 1 HETATM 3091 N N2 . NAG C 2 . ? -19.667 159.965 1.493 1.00 54.53 ? 502 NAG A N2 1 HETATM 3092 O O3 . NAG C 2 . ? -18.864 162.721 1.638 1.00 57.65 ? 502 NAG A O3 1 HETATM 3093 O O4 . NAG C 2 . ? -16.021 163.181 1.825 1.00 75.61 ? 502 NAG A O4 1 HETATM 3094 O O5 . NAG C 2 . ? -16.385 159.803 3.172 1.00 52.75 ? 502 NAG A O5 1 HETATM 3095 O O6 . NAG C 2 . ? -13.312 161.045 2.512 1.00 62.94 ? 502 NAG A O6 1 HETATM 3096 O O7 . NAG C 2 . ? -20.830 159.191 3.257 1.00 51.76 ? 502 NAG A O7 1 HETATM 3097 C C1 . NAG D 2 . ? -47.219 137.962 16.856 1.00 37.55 ? 503 NAG A C1 1 HETATM 3098 C C2 . NAG D 2 . ? -48.554 138.672 17.064 1.00 41.05 ? 503 NAG A C2 1 HETATM 3099 C C3 . NAG D 2 . ? -49.509 137.762 17.825 1.00 50.92 ? 503 NAG A C3 1 HETATM 3100 C C4 . NAG D 2 . ? -49.670 136.439 17.086 1.00 54.24 ? 503 NAG A C4 1 HETATM 3101 C C5 . NAG D 2 . ? -48.307 135.793 16.837 1.00 52.40 ? 503 NAG A C5 1 HETATM 3102 C C6 . NAG D 2 . ? -48.395 134.576 15.944 1.00 55.27 ? 503 NAG A C6 1 HETATM 3103 C C7 . NAG D 2 . ? -48.770 141.111 17.265 1.00 51.48 ? 503 NAG A C7 1 HETATM 3104 C C8 . NAG D 2 . ? -48.491 142.312 18.115 1.00 45.75 ? 503 NAG A C8 1 HETATM 3105 N N2 . NAG D 2 . ? -48.375 139.935 17.764 1.00 46.27 ? 503 NAG A N2 1 HETATM 3106 O O3 . NAG D 2 . ? -50.772 138.402 17.962 1.00 54.41 ? 503 NAG A O3 1 HETATM 3107 O O4 . NAG D 2 . ? -50.478 135.548 17.845 1.00 63.29 ? 503 NAG A O4 1 HETATM 3108 O O5 . NAG D 2 . ? -47.437 136.718 16.168 1.00 45.28 ? 503 NAG A O5 1 HETATM 3109 O O6 . NAG D 2 . ? -48.783 134.937 14.624 1.00 59.98 ? 503 NAG A O6 1 HETATM 3110 O O7 . NAG D 2 . ? -49.330 141.200 16.175 1.00 59.18 ? 503 NAG A O7 1 HETATM 3111 C C1 . NAG E 2 . ? -48.217 134.952 5.357 1.00 44.70 ? 504 NAG A C1 1 HETATM 3112 C C2 . NAG E 2 . ? -48.627 136.229 6.138 1.00 42.37 ? 504 NAG A C2 1 HETATM 3113 C C3 . NAG E 2 . ? -50.154 136.285 6.355 1.00 51.06 ? 504 NAG A C3 1 HETATM 3114 C C4 . NAG E 2 . ? -50.898 136.045 5.049 1.00 51.50 ? 504 NAG A C4 1 HETATM 3115 C C5 . NAG E 2 . ? -50.459 134.698 4.506 1.00 52.63 ? 504 NAG A C5 1 HETATM 3116 C C6 . NAG E 2 . ? -51.177 134.291 3.241 1.00 53.57 ? 504 NAG A C6 1 HETATM 3117 C C7 . NAG E 2 . ? -47.273 137.354 7.867 1.00 46.57 ? 504 NAG A C7 1 HETATM 3118 C C8 . NAG E 2 . ? -47.251 138.545 6.955 1.00 39.91 ? 504 NAG A C8 1 HETATM 3119 N N2 . NAG E 2 . ? -47.932 136.280 7.418 1.00 41.96 ? 504 NAG A N2 1 HETATM 3120 O O3 . NAG E 2 . ? -50.539 137.543 6.904 1.00 48.06 ? 504 NAG A O3 1 HETATM 3121 O O4 . NAG E 2 . ? -52.310 136.065 5.235 1.00 55.16 ? 504 NAG A O4 1 HETATM 3122 O O5 . NAG E 2 . ? -49.064 134.788 4.194 1.00 53.01 ? 504 NAG A O5 1 HETATM 3123 O O6 . NAG E 2 . ? -50.262 133.823 2.260 1.00 56.54 ? 504 NAG A O6 1 HETATM 3124 O O7 . NAG E 2 . ? -46.706 137.359 8.959 1.00 48.20 ? 504 NAG A O7 1 HETATM 3125 P P . AMP F 3 . ? -28.109 141.153 20.009 1.00 22.21 ? 505 AMP A P 1 HETATM 3126 O O1P . AMP F 3 . ? -27.548 141.114 21.429 1.00 31.93 ? 505 AMP A O1P 1 HETATM 3127 O O2P . AMP F 3 . ? -28.439 139.808 19.386 1.00 27.44 ? 505 AMP A O2P 1 HETATM 3128 O O3P . AMP F 3 . ? -27.441 142.037 18.950 1.00 17.91 ? 505 AMP A O3P 1 HETATM 3129 O "O5'" . AMP F 3 . ? -29.542 141.818 20.165 1.00 29.63 ? 505 AMP A "O5'" 1 HETATM 3130 C "C5'" . AMP F 3 . ? -30.356 142.074 19.024 1.00 37.40 ? 505 AMP A "C5'" 1 HETATM 3131 C "C4'" . AMP F 3 . ? -31.549 141.148 18.986 1.00 47.65 ? 505 AMP A "C4'" 1 HETATM 3132 O "O4'" . AMP F 3 . ? -32.771 141.889 18.790 1.00 36.74 ? 505 AMP A "O4'" 1 HETATM 3133 C "C3'" . AMP F 3 . ? -31.585 140.133 17.857 1.00 48.19 ? 505 AMP A "C3'" 1 HETATM 3134 O "O3'" . AMP F 3 . ? -30.670 139.061 18.030 1.00 38.16 ? 505 AMP A "O3'" 1 HETATM 3135 C "C2'" . AMP F 3 . ? -33.065 139.725 17.818 1.00 39.87 ? 505 AMP A "C2'" 1 HETATM 3136 O "O2'" . AMP F 3 . ? -33.362 138.731 18.782 1.00 38.65 ? 505 AMP A "O2'" 1 HETATM 3137 C "C1'" . AMP F 3 . ? -33.764 141.016 18.260 1.00 29.33 ? 505 AMP A "C1'" 1 HETATM 3138 N N9 . AMP F 3 . ? -34.406 141.675 17.116 1.00 28.93 ? 505 AMP A N9 1 HETATM 3139 C C8 . AMP F 3 . ? -34.055 141.504 15.818 1.00 25.35 ? 505 AMP A C8 1 HETATM 3140 N N7 . AMP F 3 . ? -34.832 142.281 15.012 1.00 32.84 ? 505 AMP A N7 1 HETATM 3141 C C5 . AMP F 3 . ? -35.695 142.949 15.823 1.00 32.68 ? 505 AMP A C5 1 HETATM 3142 C C6 . AMP F 3 . ? -36.788 143.932 15.668 1.00 38.77 ? 505 AMP A C6 1 HETATM 3143 N N6 . AMP F 3 . ? -37.148 144.396 14.446 1.00 31.71 ? 505 AMP A N6 1 HETATM 3144 N N1 . AMP F 3 . ? -37.420 144.365 16.783 1.00 39.16 ? 505 AMP A N1 1 HETATM 3145 C C2 . AMP F 3 . ? -37.089 143.935 18.013 1.00 37.90 ? 505 AMP A C2 1 HETATM 3146 N N3 . AMP F 3 . ? -36.102 143.050 18.230 1.00 35.87 ? 505 AMP A N3 1 HETATM 3147 C C4 . AMP F 3 . ? -35.401 142.535 17.195 1.00 33.54 ? 505 AMP A C4 1 HETATM 3148 ZN ZN . ZN G 4 . ? -27.356 139.225 15.725 1.00 16.41 ? 506 ZN A ZN 1 HETATM 3149 ZN ZN . ZN H 4 . ? -27.293 138.432 20.216 1.00 15.40 ? 507 ZN A ZN 1 HETATM 3150 O O . HOH I 5 . ? -30.172 146.753 10.717 1.00 16.48 ? 601 HOH A O 1 HETATM 3151 O O . HOH I 5 . ? -30.765 145.758 8.155 1.00 14.73 ? 602 HOH A O 1 HETATM 3152 O O . HOH I 5 . ? -22.105 138.055 6.644 1.00 15.88 ? 603 HOH A O 1 HETATM 3153 O O . HOH I 5 . ? -22.255 144.261 2.284 1.00 14.95 ? 604 HOH A O 1 HETATM 3154 O O . HOH I 5 . ? -17.859 149.882 11.643 1.00 14.98 ? 605 HOH A O 1 HETATM 3155 O O . HOH I 5 . ? -12.527 154.077 14.232 1.00 16.66 ? 606 HOH A O 1 HETATM 3156 O O . HOH I 5 . ? -22.253 146.664 23.518 1.00 16.57 ? 607 HOH A O 1 HETATM 3157 O O . HOH I 5 . ? -22.235 150.345 22.285 1.00 15.72 ? 608 HOH A O 1 HETATM 3158 O O . HOH I 5 . ? -22.183 152.577 20.821 1.00 15.42 ? 609 HOH A O 1 HETATM 3159 O O . HOH I 5 . ? -24.847 153.666 21.261 1.00 18.76 ? 610 HOH A O 1 HETATM 3160 O O . HOH I 5 . ? -25.562 156.243 20.868 1.00 16.55 ? 611 HOH A O 1 HETATM 3161 O O . HOH I 5 . ? -31.851 153.644 23.703 1.00 37.83 ? 612 HOH A O 1 HETATM 3162 O O . HOH I 5 . ? -25.363 161.278 20.508 1.00 27.08 ? 613 HOH A O 1 HETATM 3163 O O . HOH I 5 . ? -28.624 150.383 -1.950 1.00 19.82 ? 614 HOH A O 1 HETATM 3164 O O . HOH I 5 . ? -32.517 126.748 16.878 1.00 21.65 ? 615 HOH A O 1 HETATM 3165 O O . HOH I 5 . ? -24.808 127.395 -7.394 1.00 25.54 ? 616 HOH A O 1 HETATM 3166 O O . HOH I 5 . ? -25.680 147.372 21.030 1.00 15.84 ? 617 HOH A O 1 HETATM 3167 O O . HOH I 5 . ? -28.858 155.827 9.487 1.00 21.21 ? 618 HOH A O 1 HETATM 3168 O O . HOH I 5 . ? -24.107 152.142 0.207 1.00 21.18 ? 619 HOH A O 1 HETATM 3169 O O . HOH I 5 . ? -26.317 153.233 0.991 1.00 27.32 ? 620 HOH A O 1 HETATM 3170 O O . HOH I 5 . ? -25.116 131.516 18.616 1.00 14.93 ? 621 HOH A O 1 HETATM 3171 O O . HOH I 5 . ? -37.715 150.119 3.689 1.00 21.83 ? 622 HOH A O 1 HETATM 3172 O O . HOH I 5 . ? -32.279 134.369 -10.851 1.00 31.05 ? 623 HOH A O 1 HETATM 3173 O O . HOH I 5 . ? -38.271 157.296 5.204 1.00 31.65 ? 624 HOH A O 1 HETATM 3174 O O . HOH I 5 . ? -36.190 143.007 1.702 1.00 24.36 ? 625 HOH A O 1 HETATM 3175 O O . HOH I 5 . ? -13.179 143.159 22.091 1.00 15.74 ? 626 HOH A O 1 HETATM 3176 O O . HOH I 5 . ? -16.361 154.619 7.109 1.00 20.54 ? 627 HOH A O 1 HETATM 3177 O O . HOH I 5 . ? -18.919 124.487 -1.797 1.00 30.55 ? 628 HOH A O 1 HETATM 3178 O O . HOH I 5 . ? -38.850 147.660 3.311 1.00 20.28 ? 629 HOH A O 1 HETATM 3179 O O . HOH I 5 . ? -24.004 142.748 31.197 1.00 17.98 ? 630 HOH A O 1 HETATM 3180 O O . HOH I 5 . ? -6.343 147.795 28.558 1.00 25.68 ? 631 HOH A O 1 HETATM 3181 O O . HOH I 5 . ? -6.559 148.263 18.391 1.00 21.45 ? 632 HOH A O 1 HETATM 3182 O O . HOH I 5 . ? -17.919 137.316 30.940 1.00 15.12 ? 633 HOH A O 1 HETATM 3183 O O . HOH I 5 . ? -11.966 134.215 18.761 1.00 17.25 ? 634 HOH A O 1 HETATM 3184 O O . HOH I 5 . ? -22.680 138.326 29.309 1.00 18.82 ? 635 HOH A O 1 HETATM 3185 O O . HOH I 5 . ? -13.064 146.738 10.630 1.00 16.39 ? 636 HOH A O 1 HETATM 3186 O O . HOH I 5 . ? -27.418 132.733 30.086 1.00 20.43 ? 637 HOH A O 1 HETATM 3187 O O . HOH I 5 . ? -10.132 140.392 22.947 1.00 21.54 ? 638 HOH A O 1 HETATM 3188 O O . HOH I 5 . ? -6.156 150.939 14.149 1.00 19.83 ? 639 HOH A O 1 HETATM 3189 O O . HOH I 5 . ? -16.300 130.748 23.393 1.00 21.31 ? 640 HOH A O 1 HETATM 3190 O O . HOH I 5 . ? -15.753 131.234 14.232 1.00 18.45 ? 641 HOH A O 1 HETATM 3191 O O . HOH I 5 . ? -15.287 138.290 37.559 1.00 25.06 ? 642 HOH A O 1 HETATM 3192 O O . HOH I 5 . ? -15.583 147.581 11.544 1.00 16.37 ? 643 HOH A O 1 HETATM 3193 O O . HOH I 5 . ? -10.648 145.150 24.530 1.00 19.39 ? 644 HOH A O 1 HETATM 3194 O O . HOH I 5 . ? -22.848 162.165 12.410 1.00 26.05 ? 645 HOH A O 1 HETATM 3195 O O . HOH I 5 . ? -40.298 142.236 7.295 1.00 18.34 ? 646 HOH A O 1 HETATM 3196 O O . HOH I 5 . ? -8.297 157.171 24.858 1.00 22.44 ? 647 HOH A O 1 HETATM 3197 O O . HOH I 5 . ? -23.208 156.005 0.152 1.00 36.15 ? 648 HOH A O 1 HETATM 3198 O O . HOH I 5 . ? -27.559 161.339 14.479 1.00 24.05 ? 649 HOH A O 1 HETATM 3199 O O . HOH I 5 . ? -13.358 144.693 1.716 1.00 23.33 ? 650 HOH A O 1 HETATM 3200 O O . HOH I 5 . ? -10.673 145.083 13.297 1.00 21.07 ? 651 HOH A O 1 HETATM 3201 O O . HOH I 5 . ? -21.911 155.188 21.137 1.00 24.82 ? 652 HOH A O 1 HETATM 3202 O O . HOH I 5 . ? -6.227 151.940 30.762 1.00 23.45 ? 653 HOH A O 1 HETATM 3203 O O . HOH I 5 . ? -31.976 136.563 18.567 1.00 24.79 ? 654 HOH A O 1 HETATM 3204 O O . HOH I 5 . ? -40.075 152.816 17.224 1.00 26.59 ? 655 HOH A O 1 HETATM 3205 O O . HOH I 5 . ? -15.162 133.028 -10.554 1.00 21.94 ? 656 HOH A O 1 HETATM 3206 O O . HOH I 5 . ? -9.443 142.420 21.060 1.00 25.31 ? 657 HOH A O 1 HETATM 3207 O O . HOH I 5 . ? -15.096 144.402 7.790 1.00 34.00 ? 658 HOH A O 1 HETATM 3208 O O . HOH I 5 . ? -8.389 149.545 31.014 1.00 20.87 ? 659 HOH A O 1 HETATM 3209 O O . HOH I 5 . ? -10.745 144.773 21.951 1.00 24.57 ? 660 HOH A O 1 HETATM 3210 O O . HOH I 5 . ? -34.932 127.565 15.496 1.00 22.90 ? 661 HOH A O 1 HETATM 3211 O O . HOH I 5 . ? -27.362 155.732 33.033 1.00 30.45 ? 662 HOH A O 1 HETATM 3212 O O . HOH I 5 . ? -36.863 154.641 16.602 1.00 25.62 ? 663 HOH A O 1 HETATM 3213 O O . HOH I 5 . ? -7.796 151.217 28.691 1.00 24.79 ? 664 HOH A O 1 HETATM 3214 O O . HOH I 5 . ? -31.661 147.379 22.128 1.00 28.28 ? 665 HOH A O 1 HETATM 3215 O O . HOH I 5 . ? -26.161 164.199 18.244 1.00 31.45 ? 666 HOH A O 1 HETATM 3216 O O . HOH I 5 . ? -24.206 140.680 29.136 1.00 22.99 ? 667 HOH A O 1 HETATM 3217 O O . HOH I 5 . ? -18.117 152.510 -3.775 1.00 25.32 ? 668 HOH A O 1 HETATM 3218 O O . HOH I 5 . ? -25.060 126.349 29.412 1.00 29.53 ? 669 HOH A O 1 HETATM 3219 O O . HOH I 5 . ? -28.708 135.085 -11.871 1.00 30.83 ? 670 HOH A O 1 HETATM 3220 O O . HOH I 5 . ? -27.372 137.496 -12.104 1.00 26.69 ? 671 HOH A O 1 HETATM 3221 O O . HOH I 5 . ? -19.194 148.987 -5.444 1.00 28.43 ? 672 HOH A O 1 HETATM 3222 O O . HOH I 5 . ? -14.177 152.741 1.473 1.00 26.47 ? 673 HOH A O 1 HETATM 3223 O O . HOH I 5 . ? -11.737 132.843 32.946 1.00 25.50 ? 674 HOH A O 1 HETATM 3224 O O . HOH I 5 . ? -13.190 145.369 -6.660 1.00 27.39 ? 675 HOH A O 1 HETATM 3225 O O . HOH I 5 . ? -33.615 116.829 13.653 1.00 41.91 ? 676 HOH A O 1 HETATM 3226 O O . HOH I 5 . ? -14.473 131.926 21.731 1.00 26.16 ? 677 HOH A O 1 HETATM 3227 O O . HOH I 5 . ? -13.101 124.997 -3.721 1.00 34.89 ? 678 HOH A O 1 HETATM 3228 O O . HOH I 5 . ? -12.845 136.215 -4.998 1.00 28.63 ? 679 HOH A O 1 HETATM 3229 O O . HOH I 5 . ? -24.092 141.896 37.563 1.00 26.54 ? 680 HOH A O 1 HETATM 3230 O O . HOH I 5 . ? -19.804 120.918 26.190 1.00 39.26 ? 681 HOH A O 1 HETATM 3231 O O . HOH I 5 . ? -5.508 160.011 24.510 1.00 32.35 ? 682 HOH A O 1 HETATM 3232 O O . HOH I 5 . ? -37.977 161.654 12.320 1.00 34.10 ? 683 HOH A O 1 HETATM 3233 O O . HOH I 5 . ? -36.871 158.692 20.494 1.00 36.79 ? 684 HOH A O 1 HETATM 3234 O O . HOH I 5 . ? -31.220 160.666 9.605 1.00 30.43 ? 685 HOH A O 1 HETATM 3235 O O . HOH I 5 . ? -3.667 147.374 13.660 1.00 35.17 ? 686 HOH A O 1 HETATM 3236 O O . HOH I 5 . ? -22.905 159.029 7.782 1.00 36.07 ? 687 HOH A O 1 HETATM 3237 O O . HOH I 5 . ? -28.504 128.835 30.841 1.00 34.74 ? 688 HOH A O 1 HETATM 3238 O O . HOH I 5 . ? -13.799 130.999 12.180 1.00 24.18 ? 689 HOH A O 1 HETATM 3239 O O . HOH I 5 . ? -26.057 119.795 15.626 1.00 24.51 ? 690 HOH A O 1 HETATM 3240 O O . HOH I 5 . ? -10.592 154.722 10.272 1.00 33.55 ? 691 HOH A O 1 HETATM 3241 O O . HOH I 5 . ? -13.541 130.579 16.160 1.00 37.15 ? 692 HOH A O 1 HETATM 3242 O O . HOH I 5 . ? -37.970 133.306 17.085 1.00 34.12 ? 693 HOH A O 1 HETATM 3243 O O . HOH I 5 . ? -31.576 134.493 24.929 1.00 27.29 ? 694 HOH A O 1 HETATM 3244 O O . HOH I 5 . ? -6.308 154.373 21.263 1.00 23.53 ? 695 HOH A O 1 HETATM 3245 O O . HOH I 5 . ? -22.432 135.309 -11.722 1.00 28.53 ? 696 HOH A O 1 HETATM 3246 O O . HOH I 5 . ? -9.456 147.403 9.655 1.00 35.73 ? 697 HOH A O 1 HETATM 3247 O O . HOH I 5 . ? -29.920 150.719 -10.103 1.00 37.24 ? 698 HOH A O 1 HETATM 3248 O O . HOH I 5 . ? -39.763 125.378 8.745 1.00 33.36 ? 699 HOH A O 1 HETATM 3249 O O . HOH I 5 . ? -15.425 131.708 -13.620 1.00 30.33 ? 700 HOH A O 1 HETATM 3250 O O . HOH I 5 . ? -14.156 129.841 -8.709 1.00 34.97 ? 701 HOH A O 1 HETATM 3251 O O . HOH I 5 . ? -15.087 145.020 38.507 1.00 36.00 ? 702 HOH A O 1 HETATM 3252 O O . HOH I 5 . ? -40.850 128.108 13.824 1.00 29.91 ? 703 HOH A O 1 HETATM 3253 O O . HOH I 5 . ? -27.924 147.613 38.397 1.00 31.90 ? 704 HOH A O 1 HETATM 3254 O O . HOH I 5 . ? -31.232 121.286 24.303 1.00 33.31 ? 705 HOH A O 1 HETATM 3255 O O . HOH I 5 . ? -37.681 121.945 10.702 1.00 35.70 ? 706 HOH A O 1 HETATM 3256 O O . HOH I 5 . ? -9.937 137.717 26.596 1.00 28.28 ? 707 HOH A O 1 HETATM 3257 O O . HOH I 5 . ? -29.892 153.726 25.699 1.00 35.93 ? 708 HOH A O 1 HETATM 3258 O O . HOH I 5 . ? -36.044 123.088 12.827 1.00 36.22 ? 709 HOH A O 1 HETATM 3259 O O . HOH I 5 . ? -25.682 155.717 35.141 1.00 34.30 ? 710 HOH A O 1 HETATM 3260 O O . HOH I 5 . ? -16.095 125.944 7.241 1.00 28.76 ? 711 HOH A O 1 HETATM 3261 O O . HOH I 5 . ? -31.170 153.700 -4.603 1.00 31.09 ? 712 HOH A O 1 HETATM 3262 O O . HOH I 5 . ? -9.441 145.439 11.110 1.00 28.29 ? 713 HOH A O 1 HETATM 3263 O O . HOH I 5 . ? -27.064 144.948 22.476 1.00 27.64 ? 714 HOH A O 1 HETATM 3264 O O . HOH I 5 . ? -20.536 147.363 43.163 1.00 36.39 ? 715 HOH A O 1 HETATM 3265 O O . HOH I 5 . ? -4.614 145.777 29.700 1.00 30.55 ? 716 HOH A O 1 HETATM 3266 O O . HOH I 5 . ? -17.215 123.040 24.639 1.00 35.08 ? 717 HOH A O 1 HETATM 3267 O O . HOH I 5 . ? -8.990 146.631 20.831 1.00 32.69 ? 718 HOH A O 1 HETATM 3268 O O . HOH I 5 . ? -33.697 126.909 19.419 1.00 33.81 ? 719 HOH A O 1 HETATM 3269 O O . HOH I 5 . ? -35.688 130.507 20.522 1.00 39.08 ? 720 HOH A O 1 HETATM 3270 O O . HOH I 5 . ? -10.980 143.332 36.202 1.00 31.54 ? 721 HOH A O 1 HETATM 3271 O O . HOH I 5 . ? -30.353 135.335 33.266 1.00 41.70 ? 722 HOH A O 1 HETATM 3272 O O . HOH I 5 . ? -11.505 132.378 -13.816 1.00 36.95 ? 723 HOH A O 1 HETATM 3273 O O . HOH I 5 . ? -21.472 119.113 8.559 1.00 39.20 ? 724 HOH A O 1 HETATM 3274 O O . HOH I 5 . ? -23.782 162.256 22.845 1.00 30.54 ? 725 HOH A O 1 HETATM 3275 O O . HOH I 5 . ? -43.290 150.881 -2.057 1.00 42.00 ? 726 HOH A O 1 HETATM 3276 O O . HOH I 5 . ? -25.203 153.495 35.169 1.00 35.54 ? 727 HOH A O 1 HETATM 3277 O O . HOH I 5 . ? -20.217 129.689 33.939 1.00 37.47 ? 728 HOH A O 1 HETATM 3278 O O . HOH I 5 . ? -11.582 150.522 3.495 1.00 46.83 ? 729 HOH A O 1 HETATM 3279 O O . HOH I 5 . ? -27.998 146.086 33.376 1.00 34.54 ? 730 HOH A O 1 HETATM 3280 O O . HOH I 5 . ? -7.648 156.349 16.088 1.00 35.72 ? 731 HOH A O 1 HETATM 3281 O O . HOH I 5 . ? -24.348 117.851 15.353 1.00 36.83 ? 732 HOH A O 1 HETATM 3282 O O . HOH I 5 . ? -18.762 162.606 15.174 1.00 38.27 ? 733 HOH A O 1 HETATM 3283 O O . HOH I 5 . ? -48.262 125.172 6.087 1.00 42.88 ? 734 HOH A O 1 HETATM 3284 O O . HOH I 5 . ? -33.446 143.969 -10.022 1.00 38.63 ? 735 HOH A O 1 HETATM 3285 O O . HOH I 5 . ? -38.336 143.839 10.548 1.00 40.01 ? 736 HOH A O 1 HETATM 3286 O O . HOH I 5 . ? -20.782 141.005 27.225 1.00 15.85 ? 737 HOH A O 1 HETATM 3287 O O . HOH I 5 . ? -7.494 141.670 17.404 1.00 31.19 ? 738 HOH A O 1 HETATM 3288 O O . HOH I 5 . ? -18.094 126.210 17.494 1.00 24.28 ? 739 HOH A O 1 HETATM 3289 O O . HOH I 5 . ? -19.950 125.523 19.832 1.00 24.91 ? 740 HOH A O 1 HETATM 3290 O O . HOH I 5 . ? -12.743 133.482 11.395 1.00 23.78 ? 741 HOH A O 1 HETATM 3291 O O . HOH I 5 . ? -6.424 142.277 14.611 1.00 32.40 ? 742 HOH A O 1 HETATM 3292 O O . HOH I 5 . ? -14.358 129.005 10.504 1.00 36.42 ? 743 HOH A O 1 HETATM 3293 O O . HOH I 5 . ? -24.400 140.502 32.663 1.00 30.25 ? 744 HOH A O 1 HETATM 3294 O O . HOH I 5 . ? -29.833 134.164 29.244 1.00 29.72 ? 745 HOH A O 1 HETATM 3295 O O . HOH I 5 . ? -36.523 127.950 17.611 1.00 30.72 ? 746 HOH A O 1 HETATM 3296 O O . HOH I 5 . ? -30.048 135.698 27.054 1.00 32.02 ? 747 HOH A O 1 HETATM 3297 O O . HOH I 5 . ? -8.477 140.662 10.989 1.00 35.14 ? 748 HOH A O 1 HETATM 3298 O O . HOH I 5 . ? -29.069 164.893 15.064 1.00 32.69 ? 749 HOH A O 1 HETATM 3299 O O . HOH I 5 . ? -27.341 126.674 31.075 1.00 43.79 ? 750 HOH A O 1 HETATM 3300 O O . HOH I 5 . ? -12.570 145.579 8.152 1.00 26.82 ? 751 HOH A O 1 HETATM 3301 O O . HOH I 5 . ? -36.416 157.615 17.783 1.00 29.57 ? 752 HOH A O 1 HETATM 3302 O O . HOH I 5 . ? -28.662 139.959 23.736 1.00 31.29 ? 753 HOH A O 1 HETATM 3303 O O . HOH I 5 . ? -20.119 159.309 8.742 1.00 36.96 ? 754 HOH A O 1 HETATM 3304 O O . HOH I 5 . ? -27.659 131.598 32.489 1.00 38.79 ? 755 HOH A O 1 HETATM 3305 O O . HOH I 5 . ? -8.899 136.773 22.479 1.00 41.61 ? 756 HOH A O 1 HETATM 3306 O O . HOH I 5 . ? -36.790 125.535 14.807 1.00 45.50 ? 757 HOH A O 1 HETATM 3307 O O . HOH I 5 . ? -42.691 152.885 -0.843 1.00 32.83 ? 758 HOH A O 1 HETATM 3308 O O . HOH I 5 . ? -18.984 158.091 6.411 1.00 33.82 ? 759 HOH A O 1 HETATM 3309 O O . HOH I 5 . ? -39.608 146.543 14.220 1.00 25.28 ? 760 HOH A O 1 HETATM 3310 O O . HOH I 5 . ? -4.255 143.946 27.339 1.00 35.93 ? 761 HOH A O 1 HETATM 3311 O O . HOH I 5 . ? -10.149 134.504 0.816 1.00 44.32 ? 762 HOH A O 1 HETATM 3312 O O . HOH I 5 . ? -4.503 154.161 10.902 1.00 34.73 ? 763 HOH A O 1 HETATM 3313 O O . HOH I 5 . ? -26.124 155.980 0.387 1.00 44.72 ? 764 HOH A O 1 HETATM 3314 O O . HOH I 5 . ? -46.030 128.103 -7.947 1.00 45.83 ? 765 HOH A O 1 HETATM 3315 O O . HOH I 5 . ? -40.579 123.367 3.392 1.00 36.57 ? 766 HOH A O 1 HETATM 3316 O O . HOH I 5 . ? -9.196 136.464 30.253 1.00 38.36 ? 767 HOH A O 1 HETATM 3317 O O . HOH I 5 . ? -35.826 120.377 13.956 1.00 39.92 ? 768 HOH A O 1 HETATM 3318 O O . HOH I 5 . ? -16.816 155.126 -3.757 1.00 45.82 ? 769 HOH A O 1 HETATM 3319 O O . HOH I 5 . ? -14.189 119.793 11.336 1.00 46.85 ? 770 HOH A O 1 HETATM 3320 O O . HOH I 5 . ? -10.088 139.000 11.192 1.00 32.34 ? 771 HOH A O 1 HETATM 3321 O O . HOH I 5 . ? -43.636 138.311 20.047 1.00 54.28 ? 772 HOH A O 1 HETATM 3322 O O . HOH I 5 . ? -10.584 137.998 -6.941 1.00 40.87 ? 773 HOH A O 1 HETATM 3323 O O . HOH I 5 . ? -34.622 146.176 41.549 1.00 36.04 ? 774 HOH A O 1 HETATM 3324 O O . HOH I 5 . ? -43.389 147.017 12.936 1.00 32.96 ? 775 HOH A O 1 HETATM 3325 O O . HOH I 5 . ? -31.612 119.528 2.100 1.00 40.10 ? 776 HOH A O 1 HETATM 3326 O O . HOH I 5 . ? -26.668 133.887 -13.815 1.00 40.34 ? 777 HOH A O 1 HETATM 3327 O O . HOH I 5 . ? -46.172 140.624 11.705 1.00 35.01 ? 778 HOH A O 1 HETATM 3328 O O . HOH I 5 . ? -13.910 161.704 16.520 1.00 40.49 ? 779 HOH A O 1 HETATM 3329 O O . HOH I 5 . ? -46.555 131.660 13.117 1.00 42.36 ? 780 HOH A O 1 HETATM 3330 O O . HOH I 5 . ? -17.144 149.319 -3.902 1.00 38.08 ? 781 HOH A O 1 HETATM 3331 O O . HOH I 5 . ? -46.583 127.562 11.162 1.00 42.99 ? 782 HOH A O 1 HETATM 3332 O O . HOH I 5 . ? -24.214 137.390 -11.879 1.00 40.11 ? 783 HOH A O 1 HETATM 3333 O O . HOH I 5 . ? -5.162 151.106 11.645 1.00 36.81 ? 784 HOH A O 1 HETATM 3334 O O . HOH I 5 . ? -25.037 145.941 24.255 1.00 19.34 ? 785 HOH A O 1 HETATM 3335 O O . HOH I 5 . ? -25.460 144.652 26.891 1.00 22.20 ? 786 HOH A O 1 HETATM 3336 O O . HOH I 5 . ? -24.791 142.121 26.622 1.00 27.86 ? 787 HOH A O 1 HETATM 3337 O O . HOH I 5 . ? -25.775 141.634 23.368 1.00 28.09 ? 788 HOH A O 1 HETATM 3338 O O . HOH I 5 . ? -16.630 128.029 8.954 1.00 25.84 ? 789 HOH A O 1 HETATM 3339 O O . HOH I 5 . ? -26.304 120.948 13.309 1.00 25.44 ? 790 HOH A O 1 HETATM 3340 O O . HOH I 5 . ? -12.707 155.959 9.679 1.00 32.63 ? 791 HOH A O 1 HETATM 3341 O O . HOH I 5 . ? -31.218 128.086 -5.352 1.00 25.57 ? 792 HOH A O 1 HETATM 3342 O O . HOH I 5 . ? -25.294 160.568 12.873 1.00 22.58 ? 793 HOH A O 1 HETATM 3343 O O . HOH I 5 . ? -21.699 153.001 37.549 1.00 28.64 ? 794 HOH A O 1 HETATM 3344 O O . HOH I 5 . ? -33.100 146.097 43.742 1.00 25.55 ? 795 HOH A O 1 HETATM 3345 O O . HOH I 5 . ? -25.674 139.179 37.763 1.00 27.00 ? 796 HOH A O 1 HETATM 3346 O O . HOH I 5 . ? -14.953 133.803 25.326 1.00 18.74 ? 797 HOH A O 1 HETATM 3347 O O . HOH I 5 . ? -11.932 153.673 38.790 1.00 35.11 ? 798 HOH A O 1 HETATM 3348 O O . HOH I 5 . ? -37.151 146.395 12.050 1.00 18.99 ? 799 HOH A O 1 HETATM 3349 O O . HOH I 5 . ? -6.287 149.467 21.090 1.00 21.86 ? 800 HOH A O 1 HETATM 3350 O O . HOH I 5 . ? -16.853 154.680 -1.106 1.00 27.65 ? 801 HOH A O 1 HETATM 3351 O O . HOH I 5 . ? -15.456 130.074 29.740 1.00 31.17 ? 802 HOH A O 1 HETATM 3352 O O . HOH I 5 . ? -30.250 118.231 10.054 1.00 30.50 ? 803 HOH A O 1 HETATM 3353 O O . HOH I 5 . ? -36.365 139.060 18.799 1.00 29.59 ? 804 HOH A O 1 HETATM 3354 O O . HOH I 5 . ? -19.431 130.261 31.287 1.00 29.53 ? 805 HOH A O 1 HETATM 3355 O O . HOH I 5 . ? -44.965 142.973 -7.041 1.00 33.96 ? 806 HOH A O 1 HETATM 3356 O O . HOH I 5 . ? -40.888 149.249 -8.418 1.00 35.50 ? 807 HOH A O 1 HETATM 3357 O O . HOH I 5 . ? -30.361 139.484 25.386 1.00 35.14 ? 808 HOH A O 1 HETATM 3358 O O . HOH I 5 . ? -31.591 144.640 21.490 1.00 42.34 ? 809 HOH A O 1 HETATM 3359 O O . HOH I 5 . ? -28.242 153.369 -7.043 1.00 35.82 ? 810 HOH A O 1 HETATM 3360 O O . HOH I 5 . ? -47.070 142.860 8.808 1.00 38.56 ? 811 HOH A O 1 HETATM 3361 O O . HOH I 5 . ? -27.846 122.565 -7.876 1.00 39.01 ? 812 HOH A O 1 HETATM 3362 O O . HOH I 5 . ? -24.902 129.181 -13.929 1.00 39.76 ? 813 HOH A O 1 HETATM 3363 O O . HOH I 5 . ? -6.323 155.115 23.793 1.00 38.18 ? 814 HOH A O 1 HETATM 3364 O O . HOH I 5 . ? -18.706 119.409 10.766 1.00 42.07 ? 815 HOH A O 1 HETATM 3365 O O . HOH I 5 . ? -41.809 153.933 10.811 1.00 32.41 ? 816 HOH A O 1 HETATM 3366 O O . HOH I 5 . ? -30.010 121.033 1.249 1.00 39.97 ? 817 HOH A O 1 HETATM 3367 O O . HOH I 5 . ? -13.164 143.083 37.152 1.00 38.51 ? 818 HOH A O 1 HETATM 3368 O O . HOH I 5 . ? -14.066 158.033 1.262 1.00 44.25 ? 819 HOH A O 1 HETATM 3369 O O . HOH I 5 . ? -22.944 164.403 23.626 1.00 39.88 ? 820 HOH A O 1 HETATM 3370 O O . HOH I 5 . ? -25.463 116.400 2.964 1.00 47.78 ? 821 HOH A O 1 HETATM 3371 O O . HOH I 5 . ? -26.833 143.231 30.797 1.00 31.21 ? 822 HOH A O 1 HETATM 3372 O O . HOH I 5 . ? -31.696 150.368 25.294 1.00 41.10 ? 823 HOH A O 1 HETATM 3373 O O . HOH I 5 . ? -28.483 148.252 31.772 1.00 45.50 ? 824 HOH A O 1 HETATM 3374 O O . HOH I 5 . ? -36.978 130.613 18.206 1.00 50.76 ? 825 HOH A O 1 HETATM 3375 O O . HOH I 5 . ? -33.129 141.721 -11.002 1.00 41.36 ? 826 HOH A O 1 HETATM 3376 O O . HOH I 5 . ? -22.963 153.498 41.127 1.00 38.90 ? 827 HOH A O 1 HETATM 3377 O O . HOH I 5 . ? -43.833 145.227 14.959 1.00 38.47 ? 828 HOH A O 1 HETATM 3378 O O . HOH I 5 . ? -44.665 149.076 9.527 1.00 45.01 ? 829 HOH A O 1 HETATM 3379 O O . HOH I 5 . ? -31.996 123.267 23.275 1.00 44.83 ? 830 HOH A O 1 HETATM 3380 O O . HOH I 5 . ? -17.347 128.781 31.241 1.00 41.04 ? 831 HOH A O 1 HETATM 3381 O O . HOH I 5 . ? -11.518 156.241 12.580 1.00 36.95 ? 832 HOH A O 1 HETATM 3382 O O . HOH I 5 . ? -12.449 131.419 18.451 1.00 45.57 ? 833 HOH A O 1 HETATM 3383 O O . HOH I 5 . ? -8.040 143.672 -1.230 1.00 46.09 ? 834 HOH A O 1 HETATM 3384 O O . HOH I 5 . ? -10.620 134.364 11.045 1.00 46.07 ? 835 HOH A O 1 HETATM 3385 O O . HOH I 5 . ? -10.766 135.043 34.880 1.00 36.09 ? 836 HOH A O 1 HETATM 3386 O O . HOH I 5 . ? -29.180 147.018 35.830 1.00 33.65 ? 837 HOH A O 1 HETATM 3387 O O . HOH I 5 . ? -18.557 163.032 12.528 1.00 52.19 ? 838 HOH A O 1 HETATM 3388 O O . HOH I 5 . ? -27.633 147.960 27.073 1.00 33.17 ? 839 HOH A O 1 HETATM 3389 O O . HOH I 5 . ? -33.338 120.082 25.398 1.00 50.85 ? 840 HOH A O 1 HETATM 3390 O O . HOH I 5 . ? -19.238 151.758 -6.368 1.00 46.75 ? 841 HOH A O 1 HETATM 3391 O O . HOH I 5 . ? -9.852 130.888 -0.400 1.00 40.55 ? 842 HOH A O 1 HETATM 3392 O O . HOH I 5 . ? -28.874 144.097 31.910 1.00 47.06 ? 843 HOH A O 1 HETATM 3393 O O . HOH I 5 . ? -35.971 127.497 -11.117 1.00 47.03 ? 844 HOH A O 1 HETATM 3394 O O . HOH I 5 . ? -46.988 140.623 9.035 1.00 39.36 ? 845 HOH A O 1 HETATM 3395 O O . HOH I 5 . ? -35.791 153.126 23.320 1.00 35.71 ? 846 HOH A O 1 HETATM 3396 O O . HOH I 5 . ? -10.609 137.494 8.881 1.00 38.62 ? 847 HOH A O 1 HETATM 3397 O O . HOH I 5 . ? -24.779 121.119 28.963 1.00 39.48 ? 848 HOH A O 1 HETATM 3398 O O . HOH I 5 . ? -11.740 139.257 4.960 1.00 38.83 ? 849 HOH A O 1 HETATM 3399 O O . HOH I 5 . ? -28.032 149.961 28.725 1.00 44.83 ? 850 HOH A O 1 HETATM 3400 O O . HOH I 5 . ? -33.854 119.256 1.815 1.00 49.42 ? 851 HOH A O 1 HETATM 3401 O O . HOH I 5 . ? -14.367 155.049 -0.189 1.00 43.93 ? 852 HOH A O 1 HETATM 3402 O O . HOH I 5 . ? -29.002 126.927 -9.805 1.00 48.06 ? 853 HOH A O 1 HETATM 3403 O O . HOH I 5 . ? -39.350 126.348 14.262 1.00 50.87 ? 854 HOH A O 1 HETATM 3404 O O . HOH I 5 . ? -10.682 137.233 -9.293 1.00 37.95 ? 855 HOH A O 1 HETATM 3405 O O . HOH I 5 . ? -42.284 124.762 4.345 1.00 47.72 ? 856 HOH A O 1 HETATM 3406 O O . HOH I 5 . ? -34.262 126.933 25.522 1.00 43.59 ? 857 HOH A O 1 HETATM 3407 O O . HOH I 5 . ? -28.360 147.623 24.249 1.00 41.51 ? 858 HOH A O 1 HETATM 3408 O O . HOH I 5 . ? -30.739 146.926 44.026 1.00 45.36 ? 859 HOH A O 1 HETATM 3409 O O . HOH I 5 . ? -35.444 141.966 12.680 1.00 33.33 ? 860 HOH A O 1 HETATM 3410 O O . HOH I 5 . ? -41.947 137.161 -8.478 1.00 43.60 ? 861 HOH A O 1 HETATM 3411 O O . HOH I 5 . ? -21.358 165.469 25.302 1.00 46.89 ? 862 HOH A O 1 HETATM 3412 O O . HOH I 5 . ? -22.194 120.009 26.814 1.00 44.80 ? 863 HOH A O 1 HETATM 3413 O O . HOH I 5 . ? -11.454 151.300 40.613 1.00 48.74 ? 864 HOH A O 1 HETATM 3414 O O . HOH I 5 . ? -5.925 142.162 27.722 1.00 40.16 ? 865 HOH A O 1 HETATM 3415 O O . HOH I 5 . ? -26.808 159.188 35.883 1.00 45.62 ? 866 HOH A O 1 HETATM 3416 O O . HOH I 5 . ? -9.613 160.984 15.159 1.00 39.52 ? 867 HOH A O 1 HETATM 3417 O O . HOH I 5 . ? -10.094 128.978 -2.027 1.00 46.72 ? 868 HOH A O 1 HETATM 3418 O O . HOH I 5 . ? -10.314 150.198 32.873 1.00 22.17 ? 869 HOH A O 1 HETATM 3419 O O . HOH I 5 . ? -7.716 144.996 27.564 1.00 27.53 ? 870 HOH A O 1 HETATM 3420 O O . HOH I 5 . ? -9.646 162.842 37.828 1.00 49.37 ? 871 HOH A O 1 HETATM 3421 O O . HOH I 5 . ? -7.481 158.976 15.276 1.00 57.99 ? 872 HOH A O 1 HETATM 3422 O O . HOH I 5 . ? -5.654 145.675 25.757 0.50 44.34 ? 873 HOH A O 1 HETATM 3423 O O . HOH I 5 . ? -29.518 138.924 20.762 1.00 35.43 ? 874 HOH A O 1 HETATM 3424 O O . HOH I 5 . ? -25.724 142.502 29.276 1.00 59.02 ? 875 HOH A O 1 HETATM 3425 O O . HOH I 5 . ? -17.214 123.459 6.586 1.00 46.77 ? 876 HOH A O 1 HETATM 3426 O O . HOH I 5 . ? -10.216 140.329 -10.955 1.00 49.72 ? 877 HOH A O 1 HETATM 3427 O O . HOH I 5 . ? -31.558 142.062 36.114 1.00 39.20 ? 878 HOH A O 1 HETATM 3428 O O . HOH I 5 . ? -42.625 122.552 -8.982 1.00 43.95 ? 879 HOH A O 1 HETATM 3429 O O . HOH I 5 . ? -9.581 130.426 -4.974 1.00 47.64 ? 880 HOH A O 1 HETATM 3430 O O . HOH I 5 . ? -30.748 134.450 -13.070 1.00 37.62 ? 881 HOH A O 1 HETATM 3431 O O . HOH I 5 . ? -42.195 151.282 18.218 1.00 50.95 ? 882 HOH A O 1 HETATM 3432 O O . HOH I 5 . ? -29.784 137.648 30.351 1.00 41.39 ? 883 HOH A O 1 HETATM 3433 O O . HOH I 5 . ? -27.626 152.833 34.250 1.00 45.19 ? 884 HOH A O 1 HETATM 3434 O O . HOH I 5 . ? -27.757 165.021 26.056 1.00 41.15 ? 885 HOH A O 1 HETATM 3435 O O . HOH I 5 . ? -9.141 133.528 18.551 1.00 43.32 ? 886 HOH A O 1 HETATM 3436 O O . HOH I 5 . ? -20.941 153.340 -6.735 1.00 54.38 ? 887 HOH A O 1 HETATM 3437 O O . HOH I 5 . ? -28.139 147.726 43.339 1.00 52.49 ? 888 HOH A O 1 HETATM 3438 O O . HOH I 5 . ? -41.437 146.612 16.390 1.00 48.82 ? 889 HOH A O 1 HETATM 3439 O O . HOH I 5 . ? -11.601 161.375 38.143 1.00 43.38 ? 890 HOH A O 1 HETATM 3440 O O . HOH I 5 . ? -18.079 122.360 3.968 1.00 53.72 ? 891 HOH A O 1 HETATM 3441 O O . HOH I 5 . ? -9.463 142.444 3.582 1.00 50.31 ? 892 HOH A O 1 HETATM 3442 O O . HOH I 5 . ? -47.526 145.119 7.045 1.00 45.21 ? 893 HOH A O 1 HETATM 3443 O O . HOH I 5 . ? -38.178 163.039 18.406 1.00 44.72 ? 894 HOH A O 1 HETATM 3444 O O . HOH I 5 . ? -27.518 144.718 28.177 1.00 45.65 ? 895 HOH A O 1 HETATM 3445 O O . HOH I 5 . ? -15.268 147.266 -5.543 1.00 42.89 ? 896 HOH A O 1 HETATM 3446 O O . HOH I 5 . ? -22.237 127.206 29.037 1.00 38.38 ? 897 HOH A O 1 HETATM 3447 O O . HOH I 5 . ? -15.283 159.662 -0.386 1.00 53.84 ? 898 HOH A O 1 HETATM 3448 O O . HOH I 5 . ? -31.698 153.830 -7.273 1.00 44.29 ? 899 HOH A O 1 HETATM 3449 O O . HOH I 5 . ? -32.297 137.018 31.917 1.00 54.49 ? 900 HOH A O 1 HETATM 3450 O O . HOH I 5 . ? -21.331 152.718 42.639 1.00 45.45 ? 901 HOH A O 1 HETATM 3451 O O . HOH I 5 . ? -28.135 137.604 -14.964 1.00 46.29 ? 902 HOH A O 1 HETATM 3452 O O . HOH I 5 . ? -32.573 146.822 24.627 1.00 50.56 ? 903 HOH A O 1 HETATM 3453 O O . HOH I 5 . ? -19.862 165.785 23.086 1.00 56.38 ? 904 HOH A O 1 HETATM 3454 O O . HOH I 5 . ? -13.500 125.785 16.959 1.00 49.29 ? 905 HOH A O 1 HETATM 3455 O O . HOH I 5 . ? -4.502 148.984 15.264 1.00 30.11 ? 906 HOH A O 1 HETATM 3456 O O . HOH I 5 . ? -20.777 162.164 20.994 1.00 40.60 ? 907 HOH A O 1 HETATM 3457 O O . HOH I 5 . ? -8.210 142.218 -10.965 1.00 40.52 ? 908 HOH A O 1 HETATM 3458 O O . HOH I 5 . ? -13.071 147.071 1.020 1.00 44.42 ? 909 HOH A O 1 HETATM 3459 O O . HOH I 5 . ? -47.847 131.058 -9.681 1.00 45.10 ? 910 HOH A O 1 HETATM 3460 O O . HOH I 5 . ? -6.756 139.589 19.363 1.00 56.54 ? 911 HOH A O 1 HETATM 3461 O O . HOH I 5 . ? -22.979 128.863 34.772 1.00 47.80 ? 912 HOH A O 1 HETATM 3462 O O . HOH I 5 . ? -20.908 154.478 44.273 1.00 49.34 ? 913 HOH A O 1 HETATM 3463 O O . HOH I 5 . ? -38.687 159.004 17.989 1.00 54.78 ? 914 HOH A O 1 HETATM 3464 O O . HOH I 5 . ? -18.397 164.635 27.056 1.00 36.84 ? 915 HOH A O 1 HETATM 3465 O O . HOH I 5 . ? -5.202 159.553 14.451 1.00 64.15 ? 916 HOH A O 1 HETATM 3466 O O . HOH I 5 . ? -13.616 129.637 31.751 1.00 55.89 ? 917 HOH A O 1 HETATM 3467 O O . HOH I 5 . ? -24.420 135.488 -14.734 1.00 54.89 ? 918 HOH A O 1 HETATM 3468 O O . HOH I 5 . ? -4.573 143.347 30.137 1.00 55.08 ? 919 HOH A O 1 HETATM 3469 O O . HOH I 5 . ? -6.521 141.463 21.029 1.00 53.79 ? 920 HOH A O 1 HETATM 3470 O O . HOH I 5 . ? -31.283 132.902 -14.652 1.00 51.26 ? 921 HOH A O 1 HETATM 3471 O O . HOH I 5 . ? -39.823 163.505 1.627 1.00 46.36 ? 922 HOH A O 1 HETATM 3472 O O . HOH I 5 . ? -26.832 149.797 38.897 1.00 37.47 ? 923 HOH A O 1 HETATM 3473 O O . HOH I 5 . ? -20.767 121.630 8.356 1.00 43.78 ? 924 HOH A O 1 HETATM 3474 O O . HOH I 5 . ? -10.298 139.628 2.360 1.00 57.75 ? 925 HOH A O 1 HETATM 3475 O O . HOH I 5 . ? -30.927 138.469 27.866 1.00 48.64 ? 926 HOH A O 1 HETATM 3476 O O . HOH I 5 . ? -29.226 144.707 23.175 1.00 41.16 ? 927 HOH A O 1 HETATM 3477 O O . HOH I 5 . ? -30.320 142.975 33.175 1.00 44.26 ? 928 HOH A O 1 HETATM 3478 O O . HOH I 5 . ? -25.352 165.465 25.810 1.00 52.29 ? 929 HOH A O 1 HETATM 3479 O O . HOH I 5 . ? -47.710 137.894 -4.553 1.00 44.66 ? 930 HOH A O 1 HETATM 3480 O O . HOH I 5 . ? -14.330 128.375 21.394 1.00 49.80 ? 931 HOH A O 1 HETATM 3481 O O . HOH I 5 . ? -42.086 162.559 3.438 1.00 56.41 ? 932 HOH A O 1 HETATM 3482 O O . HOH I 5 . ? -40.855 160.624 5.002 1.00 57.35 ? 933 HOH A O 1 HETATM 3483 O O . HOH I 5 . ? -7.777 138.361 16.862 1.00 43.99 ? 934 HOH A O 1 HETATM 3484 O O . HOH I 5 . ? -35.198 119.328 7.094 1.00 36.93 ? 935 HOH A O 1 HETATM 3485 O O . HOH I 5 . ? -13.060 138.907 37.749 1.00 49.44 ? 936 HOH A O 1 HETATM 3486 O O . HOH I 5 . ? -19.786 121.719 6.156 1.00 47.60 ? 937 HOH A O 1 HETATM 3487 O O . HOH I 5 . ? -27.145 140.693 30.446 1.00 36.63 ? 938 HOH A O 1 HETATM 3488 O O . HOH I 5 . ? -27.027 149.277 42.309 1.00 49.17 ? 939 HOH A O 1 HETATM 3489 O O . HOH I 5 . ? -24.876 164.624 29.291 1.00 47.33 ? 940 HOH A O 1 HETATM 3490 O O . HOH I 5 . ? -28.864 141.137 28.395 1.00 46.55 ? 941 HOH A O 1 HETATM 3491 O O . HOH I 5 . ? -24.394 126.456 33.506 1.00 55.85 ? 942 HOH A O 1 HETATM 3492 O O . HOH I 5 . ? -33.709 137.470 27.853 1.00 51.86 ? 943 HOH A O 1 HETATM 3493 O O . HOH I 5 . ? -43.033 124.098 -10.994 1.00 55.00 ? 944 HOH A O 1 HETATM 3494 O O . HOH I 5 . ? -11.689 143.517 -9.138 1.00 39.98 ? 945 HOH A O 1 HETATM 3495 O O . HOH I 5 . ? -10.098 143.753 -7.660 1.00 57.08 ? 946 HOH A O 1 HETATM 3496 O O . HOH I 5 . ? -9.171 136.764 11.931 1.00 43.43 ? 947 HOH A O 1 HETATM 3497 O O . HOH I 5 . ? -9.973 141.901 -7.974 1.00 60.27 ? 948 HOH A O 1 HETATM 3498 O O . HOH I 5 . ? -45.639 124.670 5.087 1.00 57.39 ? 949 HOH A O 1 HETATM 3499 O O . HOH I 5 . ? -9.922 136.027 -4.483 1.00 55.47 ? 950 HOH A O 1 HETATM 3500 O O . HOH I 5 . ? -7.047 149.747 33.526 1.00 26.17 ? 951 HOH A O 1 HETATM 3501 O O . HOH I 5 . ? -47.326 141.940 5.873 1.00 46.21 ? 952 HOH A O 1 HETATM 3502 O O . HOH I 5 . ? -20.312 164.777 27.547 1.00 52.83 ? 953 HOH A O 1 HETATM 3503 O O . HOH I 5 . ? -11.873 129.489 14.208 1.00 53.83 ? 954 HOH A O 1 HETATM 3504 O O . HOH I 5 . ? -11.741 127.917 -8.483 1.00 48.11 ? 955 HOH A O 1 HETATM 3505 O O . HOH I 5 . ? -9.547 137.758 -3.197 1.00 66.11 ? 956 HOH A O 1 HETATM 3506 O O . HOH I 5 . ? -38.734 164.112 14.774 1.00 55.96 ? 957 HOH A O 1 HETATM 3507 O O . HOH I 5 . ? -34.072 118.091 -0.556 1.00 56.19 ? 958 HOH A O 1 HETATM 3508 O O . HOH I 5 . ? -27.112 162.703 38.616 1.00 60.67 ? 959 HOH A O 1 HETATM 3509 O O . HOH I 5 . ? -6.721 137.128 29.397 1.00 52.93 ? 960 HOH A O 1 HETATM 3510 O O . HOH I 5 . ? -26.986 162.575 30.541 1.00 44.41 ? 961 HOH A O 1 HETATM 3511 O O . HOH I 5 . ? -8.244 152.551 6.211 1.00 56.61 ? 962 HOH A O 1 HETATM 3512 O O . HOH I 5 . ? -37.797 143.435 -14.655 1.00 55.55 ? 963 HOH A O 1 HETATM 3513 O O . HOH I 5 . ? -15.528 165.530 3.790 1.00 55.20 ? 964 HOH A O 1 HETATM 3514 O O . HOH I 5 . ? -43.175 147.405 -7.677 1.00 44.46 ? 965 HOH A O 1 HETATM 3515 O O . HOH I 5 . ? -29.092 162.116 10.522 1.00 48.86 ? 966 HOH A O 1 HETATM 3516 O O . HOH I 5 . ? -36.217 144.622 -14.102 1.00 59.19 ? 967 HOH A O 1 HETATM 3517 O O . HOH I 5 . ? -31.516 130.723 -14.394 1.00 61.97 ? 968 HOH A O 1 HETATM 3518 O O . HOH I 5 . ? -37.848 134.345 18.935 1.00 61.55 ? 969 HOH A O 1 HETATM 3519 O O . HOH I 5 . ? -10.491 134.266 37.866 1.00 60.30 ? 970 HOH A O 1 HETATM 3520 O O . HOH I 5 . ? -16.896 167.280 38.944 1.00 64.81 ? 971 HOH A O 1 HETATM 3521 O O . HOH I 5 . ? -44.271 138.489 -12.799 1.00 62.06 ? 972 HOH A O 1 HETATM 3522 O O . HOH I 5 . ? -28.659 121.544 30.203 1.00 57.41 ? 973 HOH A O 1 HETATM 3523 O O . HOH I 5 . ? -6.837 151.349 9.469 1.00 56.12 ? 974 HOH A O 1 HETATM 3524 O O . HOH I 5 . ? -32.454 117.073 -0.958 1.00 65.95 ? 975 HOH A O 1 HETATM 3525 O O . HOH I 5 . ? -35.897 125.737 -14.063 1.00 60.73 ? 976 HOH A O 1 HETATM 3526 O O . HOH I 5 . ? -27.249 155.771 -6.593 1.00 60.14 ? 977 HOH A O 1 HETATM 3527 O O . HOH I 5 . ? -28.584 158.738 2.771 1.00 49.83 ? 978 HOH A O 1 HETATM 3528 O O . HOH I 5 . ? -50.994 135.122 -8.795 1.00 56.71 ? 979 HOH A O 1 HETATM 3529 O O . HOH I 5 . ? -15.018 150.409 -1.659 1.00 41.25 ? 980 HOH A O 1 HETATM 3530 O O . HOH I 5 . ? -5.654 140.215 25.757 0.50 47.54 ? 981 HOH A O 1 HETATM 3531 O O . HOH I 5 . ? -36.055 124.571 -9.691 1.00 41.62 ? 982 HOH A O 1 HETATM 3532 O O . HOH I 5 . ? -32.724 139.558 20.680 1.00 46.54 ? 983 HOH A O 1 HETATM 3533 O O . HOH I 5 . ? -9.791 138.735 6.908 1.00 52.28 ? 984 HOH A O 1 HETATM 3534 O O . HOH I 5 . ? -9.366 143.849 -5.459 1.00 51.75 ? 985 HOH A O 1 HETATM 3535 O O . HOH I 5 . ? -9.715 141.955 -4.937 1.00 50.59 ? 986 HOH A O 1 HETATM 3536 O O . HOH I 5 . ? -20.785 124.670 29.192 1.00 51.24 ? 987 HOH A O 1 HETATM 3537 O O . HOH I 5 . ? -47.632 140.430 13.584 1.00 48.63 ? 988 HOH A O 1 HETATM 3538 O O . HOH I 5 . ? -35.872 132.463 19.652 1.00 57.11 ? 989 HOH A O 1 HETATM 3539 O O . HOH I 5 . ? -32.747 163.510 26.813 1.00 49.66 ? 990 HOH A O 1 HETATM 3540 O O . HOH I 5 . ? -30.406 153.301 -8.986 1.00 54.92 ? 991 HOH A O 1 HETATM 3541 O O . HOH I 5 . ? -10.082 133.268 21.429 1.00 51.25 ? 992 HOH A O 1 HETATM 3542 O O . HOH I 5 . ? -49.006 135.274 0.252 1.00 46.98 ? 993 HOH A O 1 HETATM 3543 O O . HOH I 5 . ? -30.080 132.209 33.842 1.00 52.39 ? 994 HOH A O 1 HETATM 3544 O O . HOH I 5 . ? -22.437 126.337 31.260 1.00 56.43 ? 995 HOH A O 1 HETATM 3545 O O . HOH I 5 . ? -4.040 140.749 26.908 1.00 57.12 ? 996 HOH A O 1 HETATM 3546 O O . HOH I 5 . ? -42.725 143.129 17.983 1.00 53.06 ? 997 HOH A O 1 HETATM 3547 O O . HOH I 5 . ? -29.914 140.214 29.740 1.00 56.84 ? 998 HOH A O 1 HETATM 3548 O O . HOH I 5 . ? -12.301 130.865 34.388 1.00 50.51 ? 999 HOH A O 1 HETATM 3549 O O . HOH I 5 . ? -26.430 158.195 1.970 1.00 51.19 ? 1000 HOH A O 1 HETATM 3550 O O . HOH I 5 . ? -42.677 156.682 -1.953 1.00 50.50 ? 1001 HOH A O 1 HETATM 3551 O O . HOH I 5 . ? -40.245 155.261 -3.256 1.00 50.42 ? 1002 HOH A O 1 HETATM 3552 O O . HOH I 5 . ? -49.329 134.180 -9.619 1.00 54.83 ? 1003 HOH A O 1 HETATM 3553 O O . HOH I 5 . ? -32.137 156.243 -3.381 1.00 46.99 ? 1004 HOH A O 1 HETATM 3554 O O . HOH I 5 . ? -23.218 163.932 19.516 1.00 51.00 ? 1005 HOH A O 1 HETATM 3555 O O . HOH I 5 . ? -16.957 126.199 28.765 1.00 55.12 ? 1006 HOH A O 1 HETATM 3556 O O . HOH I 5 . ? -38.143 156.891 21.566 1.00 56.26 ? 1007 HOH A O 1 HETATM 3557 O O . HOH I 5 . ? -6.965 151.323 7.567 1.00 55.68 ? 1008 HOH A O 1 HETATM 3558 O O . HOH I 5 . ? -7.940 132.761 -4.916 1.00 55.95 ? 1009 HOH A O 1 HETATM 3559 O O . HOH I 5 . ? -2.250 157.867 12.029 1.00 54.85 ? 1010 HOH A O 1 HETATM 3560 O O . HOH I 5 . ? -6.129 130.904 -8.585 1.00 56.94 ? 1011 HOH A O 1 HETATM 3561 O O . HOH I 5 . ? -14.843 163.659 18.005 1.00 56.28 ? 1012 HOH A O 1 HETATM 3562 O O . HOH I 5 . ? -21.957 122.828 29.672 1.00 56.68 ? 1013 HOH A O 1 HETATM 3563 O O . HOH I 5 . ? -39.004 127.122 17.208 1.00 54.36 ? 1014 HOH A O 1 HETATM 3564 O O . HOH I 5 . ? -20.537 127.510 33.484 1.00 57.50 ? 1015 HOH A O 1 HETATM 3565 O O . HOH I 5 . ? -22.523 111.869 4.107 1.00 55.24 ? 1016 HOH A O 1 HETATM 3566 O O . HOH I 5 . ? -15.201 129.688 33.213 1.00 57.65 ? 1017 HOH A O 1 HETATM 3567 O O . HOH I 5 . ? -7.311 137.435 5.712 1.00 53.24 ? 1018 HOH A O 1 HETATM 3568 O O . HOH I 5 . ? -40.534 162.298 14.512 1.00 58.33 ? 1019 HOH A O 1 HETATM 3569 O O . HOH I 5 . ? -29.421 150.392 27.253 1.00 57.22 ? 1020 HOH A O 1 HETATM 3570 O O . HOH I 5 . ? -25.707 157.697 -1.292 1.00 55.08 ? 1021 HOH A O 1 HETATM 3571 O O . HOH I 5 . ? -34.487 162.315 26.196 1.00 58.27 ? 1022 HOH A O 1 HETATM 3572 O O . HOH I 5 . ? -8.473 139.785 29.080 1.00 32.59 ? 1023 HOH A O 1 HETATM 3573 O O . HOH I 5 . ? -33.404 169.428 19.107 1.00 41.94 ? 1024 HOH A O 1 HETATM 3574 O O . HOH I 5 . ? -31.414 137.735 23.756 1.00 44.76 ? 1025 HOH A O 1 HETATM 3575 O O . HOH I 5 . ? -41.064 126.329 11.681 1.00 45.37 ? 1026 HOH A O 1 HETATM 3576 O O . HOH I 5 . ? -9.295 164.046 28.301 1.00 47.01 ? 1027 HOH A O 1 HETATM 3577 O O . HOH I 5 . ? -22.516 149.541 44.111 1.00 52.14 ? 1028 HOH A O 1 HETATM 3578 O O . HOH I 5 . ? -16.685 167.559 29.307 1.00 46.93 ? 1029 HOH A O 1 HETATM 3579 O O . HOH I 5 . ? -14.923 123.361 4.520 1.00 51.48 ? 1030 HOH A O 1 HETATM 3580 O O . HOH I 5 . ? -35.674 135.307 20.318 1.00 53.22 ? 1031 HOH A O 1 HETATM 3581 O O . HOH I 5 . ? -12.534 131.565 22.084 1.00 51.92 ? 1032 HOH A O 1 HETATM 3582 O O . HOH I 5 . ? -29.956 119.579 -6.596 1.00 56.86 ? 1033 HOH A O 1 HETATM 3583 O O . HOH I 5 . ? -20.421 121.053 4.430 1.00 57.16 ? 1034 HOH A O 1 HETATM 3584 O O . HOH I 5 . ? -52.972 137.097 19.208 1.00 55.90 ? 1035 HOH A O 1 HETATM 3585 O O . HOH I 5 . ? -18.117 163.528 21.253 1.00 55.92 ? 1036 HOH A O 1 HETATM 3586 O O . HOH I 5 . ? -32.877 159.071 -1.502 1.00 52.39 ? 1037 HOH A O 1 HETATM 3587 O O . HOH I 5 . ? -7.682 140.844 -1.209 1.00 55.08 ? 1038 HOH A O 1 HETATM 3588 O O . HOH I 5 . ? -23.463 114.240 5.503 1.00 56.21 ? 1039 HOH A O 1 HETATM 3589 O O . HOH I 5 . ? -10.711 146.356 3.399 1.00 54.68 ? 1040 HOH A O 1 HETATM 3590 O O . HOH I 5 . ? -16.287 117.904 14.544 1.00 55.02 ? 1041 HOH A O 1 HETATM 3591 O O . HOH I 5 . ? -32.950 142.556 22.310 1.00 50.22 ? 1042 HOH A O 1 HETATM 3592 O O . HOH I 5 . ? -30.247 119.542 27.676 1.00 54.90 ? 1043 HOH A O 1 HETATM 3593 O O . HOH I 5 . ? -38.199 163.694 2.926 1.00 54.47 ? 1044 HOH A O 1 HETATM 3594 O O . HOH I 5 . ? -4.751 158.285 13.071 1.00 56.86 ? 1045 HOH A O 1 HETATM 3595 O O . HOH I 5 . ? -23.703 109.468 3.064 1.00 55.45 ? 1046 HOH A O 1 HETATM 3596 O O . HOH I 5 . ? -10.037 146.284 -6.009 1.00 55.90 ? 1047 HOH A O 1 HETATM 3597 O O . HOH I 5 . ? -37.424 157.346 23.969 1.00 56.65 ? 1048 HOH A O 1 HETATM 3598 O O . HOH I 5 . ? -38.644 125.839 -12.837 1.00 53.79 ? 1049 HOH A O 1 HETATM 3599 O O . HOH I 5 . ? -42.035 150.726 20.229 1.00 58.01 ? 1050 HOH A O 1 HETATM 3600 O O . HOH I 5 . ? -10.244 132.273 11.162 1.00 53.13 ? 1051 HOH A O 1 HETATM 3601 O O . HOH I 5 . ? -8.183 133.060 9.527 1.00 57.31 ? 1052 HOH A O 1 HETATM 3602 O O . HOH I 5 . ? -27.753 132.044 -15.644 1.00 57.99 ? 1053 HOH A O 1 HETATM 3603 O O . HOH I 5 . ? -48.664 137.000 1.623 1.00 53.94 ? 1054 HOH A O 1 HETATM 3604 O O . HOH I 5 . ? -33.873 161.551 8.564 1.00 51.79 ? 1055 HOH A O 1 HETATM 3605 O O . HOH I 5 . ? -11.442 126.151 7.635 1.00 59.47 ? 1056 HOH A O 1 HETATM 3606 O O . HOH I 5 . ? -11.003 164.630 27.824 1.00 54.87 ? 1057 HOH A O 1 HETATM 3607 O O . HOH I 5 . ? -23.111 162.010 10.161 1.00 57.78 ? 1058 HOH A O 1 HETATM 3608 O O . HOH I 5 . ? -30.972 162.203 5.025 1.00 56.04 ? 1059 HOH A O 1 HETATM 3609 O O . HOH I 5 . ? -37.078 163.651 4.449 1.00 56.90 ? 1060 HOH A O 1 HETATM 3610 O O . HOH I 5 . ? -16.891 157.792 41.205 1.00 52.48 ? 1061 HOH A O 1 HETATM 3611 O O . HOH I 5 . ? -16.688 163.298 10.688 1.00 58.47 ? 1062 HOH A O 1 HETATM 3612 O O . HOH I 5 . ? -8.624 154.859 7.691 1.00 55.98 ? 1063 HOH A O 1 HETATM 3613 O O . HOH I 5 . ? -29.694 161.933 6.654 1.00 53.11 ? 1064 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 . LEU A 9 ? 0.6720 0.7576 0.7836 -0.0173 0.0136 0.1051 24 LEU A N 2 C CA . LEU A 9 ? 0.6386 0.7629 0.7231 -0.0257 -0.0377 -0.0062 24 LEU A CA 3 C C . LEU A 9 ? 0.5706 0.7085 0.5668 -0.0329 -0.1047 -0.0668 24 LEU A C 4 O O . LEU A 9 ? 0.6091 0.7600 0.4853 -0.0588 -0.0795 -0.0169 24 LEU A O 5 C CB . LEU A 9 ? 0.6524 0.7558 0.7559 0.0452 0.0216 -0.0193 24 LEU A CB 6 N N . PRO A 10 ? 0.5152 0.5980 0.4941 -0.0531 -0.1095 -0.0168 25 PRO A N 7 C CA . PRO A 10 ? 0.4825 0.5319 0.4018 0.0058 -0.1568 0.0555 25 PRO A CA 8 C C . PRO A 10 ? 0.4277 0.4798 0.3909 -0.1654 -0.0069 0.0633 25 PRO A C 9 O O . PRO A 10 ? 0.3994 0.7346 0.2833 -0.1197 -0.1117 0.0250 25 PRO A O 10 C CB . PRO A 10 ? 0.5484 0.5330 0.3496 -0.1016 -0.1754 -0.0807 25 PRO A CB 11 C CG . PRO A 10 ? 0.5301 0.5993 0.6075 -0.0622 -0.0810 -0.0069 25 PRO A CG 12 C CD . PRO A 10 ? 0.5563 0.6187 0.4951 0.0244 -0.1529 0.0247 25 PRO A CD 13 N N . PRO A 11 ? 0.3864 0.5056 0.2859 -0.1361 -0.0466 0.0726 26 PRO A N 14 C CA . PRO A 11 ? 0.4145 0.5355 0.2154 -0.1092 -0.1025 0.0460 26 PRO A CA 15 C C . PRO A 11 ? 0.3321 0.4602 0.2152 -0.0970 0.0133 -0.0927 26 PRO A C 16 O O . PRO A 11 ? 0.3453 0.4371 0.2265 -0.0389 -0.0451 -0.0690 26 PRO A O 17 C CB . PRO A 11 ? 0.3733 0.4808 0.2874 -0.2235 -0.0125 0.0498 26 PRO A CB 18 C CG . PRO A 11 ? 0.4327 0.4846 0.4192 -0.1042 -0.0619 0.2288 26 PRO A CG 19 C CD . PRO A 11 ? 0.3632 0.5871 0.3112 -0.1608 -0.1302 0.0872 26 PRO A CD 20 N N . LYS A 12 ? 0.3401 0.4427 0.2117 -0.0904 -0.0712 -0.0429 27 LYS A N 21 C CA . LYS A 12 ? 0.2602 0.4935 0.2120 -0.1040 -0.0134 0.0659 27 LYS A CA 22 C C . LYS A 12 ? 0.2308 0.3358 0.1666 -0.0058 0.0232 0.0323 27 LYS A C 23 O O . LYS A 12 ? 0.2036 0.5221 0.1735 -0.1003 0.0189 -0.0769 27 LYS A O 24 C CB . LYS A 12 ? 0.2390 0.5528 0.2126 -0.0912 -0.0327 -0.0618 27 LYS A CB 25 C CG . LYS A 12 ? 0.3305 0.4036 0.2482 -0.1271 -0.0701 -0.0740 27 LYS A CG 26 C CD . LYS A 12 ? 0.3115 0.5691 0.4039 -0.1503 -0.1028 -0.0611 27 LYS A CD 27 C CE . LYS A 12 ? 0.3799 0.5966 0.4891 -0.1181 -0.1317 -0.1443 27 LYS A CE 28 N NZ . LYS A 12 ? 0.2788 0.6391 0.7124 -0.0983 -0.0461 0.0032 27 LYS A NZ 29 N N . LEU A 13 ? 0.2652 0.4654 0.1928 -0.1715 -0.0255 0.0100 28 LEU A N 30 C CA . LEU A 13 ? 0.2008 0.3981 0.1513 -0.1168 -0.0121 -0.0199 28 LEU A CA 31 C C . LEU A 13 ? 0.2183 0.4531 0.2313 -0.1006 0.0154 0.0039 28 LEU A C 32 O O . LEU A 13 ? 0.2401 0.4439 0.1723 -0.1021 -0.0547 0.0244 28 LEU A O 33 C CB . LEU A 13 ? 0.1857 0.3511 0.2371 -0.0875 -0.0756 0.0339 28 LEU A CB 34 C CG . LEU A 13 ? 0.2097 0.4501 0.3524 -0.1025 -0.0631 0.0956 28 LEU A CG 35 C CD1 . LEU A 13 ? 0.3363 0.4098 0.2790 -0.1012 -0.0698 -0.0663 28 LEU A CD1 36 C CD2 . LEU A 13 ? 0.3026 0.3134 0.4198 -0.1264 -0.1046 0.0313 28 LEU A CD2 37 N N . LEU A 14 ? 0.2476 0.3650 0.1395 -0.1218 -0.0189 0.0505 29 LEU A N 38 C CA . LEU A 14 ? 0.2353 0.3548 0.1447 -0.1495 -0.0310 0.0464 29 LEU A CA 39 C C . LEU A 14 ? 0.2139 0.2916 0.1819 -0.0692 -0.0811 0.0298 29 LEU A C 40 O O . LEU A 14 ? 0.2483 0.3274 0.1706 -0.1346 -0.0079 -0.0077 29 LEU A O 41 C CB . LEU A 14 ? 0.2484 0.3768 0.2084 -0.1408 0.0414 0.0174 29 LEU A CB 42 C CG . LEU A 14 ? 0.3134 0.3261 0.1751 -0.0932 0.0941 -0.0267 29 LEU A CG 43 C CD1 . LEU A 14 ? 0.2438 0.2771 0.1692 -0.0310 0.0182 -0.0085 29 LEU A CD1 44 C CD2 . LEU A 14 ? 0.3124 0.2243 0.3852 -0.1187 -0.0544 0.0808 29 LEU A CD2 45 N N . LEU A 15 ? 0.2538 0.3503 0.1514 -0.1456 -0.0338 0.0152 30 LEU A N 46 C CA . LEU A 15 ? 0.2270 0.2888 0.1466 -0.1376 0.0068 -0.0043 30 LEU A CA 47 C C . LEU A 15 ? 0.2043 0.2899 0.1698 -0.1249 0.0185 -0.0046 30 LEU A C 48 O O . LEU A 15 ? 0.2189 0.3173 0.1560 -0.0718 -0.0032 -0.0010 30 LEU A O 49 C CB . LEU A 15 ? 0.2034 0.3148 0.1550 -0.0990 -0.0467 0.0009 30 LEU A CB 50 C CG . LEU A 15 ? 0.1576 0.2614 0.1403 -0.0699 -0.0264 -0.0354 30 LEU A CG 51 C CD1 . LEU A 15 ? 0.1388 0.4053 0.1688 -0.0230 0.0052 0.0377 30 LEU A CD1 52 C CD2 . LEU A 15 ? 0.2252 0.2430 0.1829 -0.0950 -0.0115 0.0470 30 LEU A CD2 53 N N . VAL A 16 ? 0.2266 0.2403 0.1348 -0.0837 -0.0160 0.0246 31 VAL A N 54 C CA . VAL A 16 ? 0.1673 0.3033 0.2195 -0.0775 -0.0656 0.0510 31 VAL A CA 55 C C . VAL A 16 ? 0.1250 0.2197 0.1586 -0.0631 -0.0011 -0.0233 31 VAL A C 56 O O . VAL A 16 ? 0.1479 0.2706 0.1628 -0.0747 -0.0116 -0.0066 31 VAL A O 57 C CB . VAL A 16 ? 0.2017 0.2361 0.1523 -0.1070 0.0184 0.0205 31 VAL A CB 58 C CG1 . VAL A 16 ? 0.2043 0.4165 0.1785 -0.1173 -0.0034 0.0648 31 VAL A CG1 59 C CG2 . VAL A 16 ? 0.2183 0.2425 0.1873 -0.1070 -0.0613 0.0128 31 VAL A CG2 60 N N . SER A 17 ? 0.1655 0.2387 0.1502 -0.0917 -0.0191 -0.0210 32 SER A N 61 C CA . SER A 17 ? 0.1622 0.1678 0.1614 -0.0777 -0.0095 0.0029 32 SER A CA 62 C C . SER A 17 ? 0.1471 0.2652 0.1687 -0.0572 -0.0033 0.0294 32 SER A C 63 O O . SER A 17 ? 0.1854 0.2741 0.1642 -0.0523 -0.0160 0.0071 32 SER A O 64 C CB . SER A 17 ? 0.1236 0.1847 0.1813 -0.0350 -0.0654 0.0026 32 SER A CB 65 O OG . SER A 17 ? 0.1520 0.2329 0.1638 -0.0544 -0.0195 0.0512 32 SER A OG 66 N N . PHE A 18 ? 0.1993 0.2531 0.1122 -0.0845 -0.0160 0.0382 33 PHE A N 67 C CA . PHE A 18 ? 0.2014 0.2630 0.1703 -0.0579 -0.0286 -0.0547 33 PHE A CA 68 C C . PHE A 18 ? 0.1780 0.1904 0.1011 -0.0539 0.0407 0.0065 33 PHE A C 69 O O . PHE A 18 ? 0.1317 0.2876 0.2073 -0.0382 0.0267 -0.0363 33 PHE A O 70 C CB . PHE A 18 ? 0.1616 0.2651 0.2083 -0.0884 0.0245 -0.0299 33 PHE A CB 71 C CG . PHE A 18 ? 0.1897 0.1925 0.2123 -0.1023 0.0056 -0.0018 33 PHE A CG 72 C CD1 . PHE A 18 ? 0.1766 0.2948 0.2978 -0.1110 0.0100 0.0162 33 PHE A CD1 73 C CD2 . PHE A 18 ? 0.2283 0.2754 0.1535 -0.1364 -0.0018 -0.0060 33 PHE A CD2 74 C CE1 . PHE A 18 ? 0.2409 0.2797 0.2882 -0.0784 0.0675 0.0926 33 PHE A CE1 75 C CE2 . PHE A 18 ? 0.2091 0.2542 0.2242 -0.1095 -0.0207 0.0049 33 PHE A CE2 76 C CZ . PHE A 18 ? 0.2397 0.2386 0.2165 -0.1312 0.0047 -0.0022 33 PHE A CZ 77 N N . ASP A 19 ? 0.2157 0.2366 0.0909 -0.0468 0.0116 0.0241 34 ASP A N 78 C CA . ASP A 19 ? 0.1648 0.1817 0.1899 -0.0045 0.0282 -0.0016 34 ASP A CA 79 C C . ASP A 19 ? 0.1247 0.1271 0.2346 0.0023 0.0216 -0.0557 34 ASP A C 80 O O . ASP A 19 ? 0.1836 0.2169 0.1751 -0.0746 -0.0089 0.0569 34 ASP A O 81 C CB . ASP A 19 ? 0.1786 0.1273 0.2043 -0.0390 0.0071 0.0199 34 ASP A CB 82 C CG . ASP A 19 ? 0.1995 0.0702 0.1014 -0.0121 -0.0308 0.0089 34 ASP A CG 83 O OD1 . ASP A 19 ? 0.2836 0.1359 0.1538 -0.0161 -0.0349 0.0382 34 ASP A OD1 84 O OD2 . ASP A 19 ? 0.2575 0.2477 0.2489 0.0292 -0.0412 0.0848 34 ASP A OD2 85 N N . GLY A 20 ? 0.1957 0.1939 0.0800 -0.0314 -0.0023 -0.0140 35 GLY A N 86 C CA . GLY A 20 ? 0.2037 0.2465 0.1305 -0.0628 0.0065 0.0368 35 GLY A CA 87 C C . GLY A 20 ? 0.1972 0.1216 0.1016 -0.0697 0.0047 -0.0081 35 GLY A C 88 O O . GLY A 20 ? 0.1675 0.2203 0.1429 -0.0142 0.0390 0.0381 35 GLY A O 89 N N . PHE A 21 ? 0.1712 0.1780 0.1315 -0.0145 0.0166 -0.0641 36 PHE A N 90 C CA . PHE A 21 ? 0.1633 0.1598 0.1889 -0.0646 0.0155 -0.0639 36 PHE A CA 91 C C . PHE A 21 ? 0.2175 0.1589 0.2067 -0.0906 -0.0153 -0.0038 36 PHE A C 92 O O . PHE A 21 ? 0.1748 0.2440 0.1934 -0.0564 0.0056 0.0443 36 PHE A O 93 C CB . PHE A 21 ? 0.1660 0.0957 0.2337 -0.0234 -0.0050 -0.0103 36 PHE A CB 94 C CG . PHE A 21 ? 0.2716 0.1188 0.2083 -0.0365 0.0651 -0.0366 36 PHE A CG 95 C CD1 . PHE A 21 ? 0.3233 0.1158 0.2258 -0.0266 0.0497 -0.0388 36 PHE A CD1 96 C CD2 . PHE A 21 ? 0.2917 0.1143 0.2910 -0.0412 0.0179 -0.0447 36 PHE A CD2 97 C CE1 . PHE A 21 ? 0.3012 0.1875 0.2442 -0.0576 0.0339 0.0236 36 PHE A CE1 98 C CE2 . PHE A 21 ? 0.3026 0.1446 0.3092 -0.0278 0.0822 -0.0724 36 PHE A CE2 99 C CZ . PHE A 21 ? 0.3392 0.1801 0.2331 -0.0770 0.1169 -0.0343 36 PHE A CZ 100 N N . ARG A 22 ? 0.1594 0.1224 0.2013 0.0083 0.0455 -0.0525 37 ARG A N 101 C CA . ARG A 22 ? 0.1495 0.1763 0.1589 0.0646 0.0326 0.0148 37 ARG A CA 102 C C . ARG A 22 ? 0.1182 0.2173 0.1324 -0.0386 0.0225 0.0351 37 ARG A C 103 O O . ARG A 22 ? 0.1845 0.1897 0.2105 -0.0081 0.0405 0.0136 37 ARG A O 104 C CB . ARG A 22 ? 0.2064 0.0836 0.1775 0.0187 -0.0254 0.0292 37 ARG A CB 105 C CG . ARG A 22 ? 0.1760 0.2209 0.1816 0.0399 -0.0647 0.0381 37 ARG A CG 106 C CD . ARG A 22 ? 0.1729 0.3190 0.1818 0.0786 -0.0574 -0.0071 37 ARG A CD 107 N NE . ARG A 22 ? 0.2488 0.1769 0.2498 0.0243 -0.0457 -0.0276 37 ARG A NE 108 C CZ . ARG A 22 ? 0.2018 0.3665 0.2413 -0.0524 -0.0306 -0.0267 37 ARG A CZ 109 N NH1 . ARG A 22 ? 0.3046 0.1775 0.2407 0.0700 -0.0696 -0.0106 37 ARG A NH1 110 N NH2 . ARG A 22 ? 0.2365 0.2750 0.4028 0.0424 0.0159 -0.1076 37 ARG A NH2 111 N N . ALA A 23 ? 0.1460 0.2807 0.1557 -0.0125 0.0645 -0.0045 38 ALA A N 112 C CA . ALA A 23 ? 0.2226 0.2127 0.2033 -0.0152 0.1144 -0.0030 38 ALA A CA 113 C C . ALA A 23 ? 0.2179 0.1909 0.1612 0.0066 0.0740 -0.0571 38 ALA A C 114 O O . ALA A 23 ? 0.3136 0.1984 0.2303 0.0052 0.0700 -0.0756 38 ALA A O 115 C CB . ALA A 23 ? 0.2204 0.2000 0.2031 -0.0203 0.0782 0.0386 38 ALA A CB 116 N N . ASP A 24 ? 0.2738 0.1713 0.1452 0.0000 0.0109 0.0106 39 ASP A N 117 C CA . ASP A 24 ? 0.2642 0.1466 0.2068 -0.0186 0.0525 0.0512 39 ASP A CA 118 C C . ASP A 24 ? 0.2700 0.3092 0.2112 0.0161 0.0411 -0.0257 39 ASP A C 119 O O . ASP A 24 ? 0.2843 0.2799 0.2498 0.0352 0.0190 -0.0258 39 ASP A O 120 C CB . ASP A 24 ? 0.2808 0.2648 0.2521 0.0330 -0.0075 -0.1085 39 ASP A CB 121 C CG . ASP A 24 ? 0.2658 0.1320 0.2881 0.0652 -0.0418 -0.0401 39 ASP A CG 122 O OD1 . ASP A 24 ? 0.3056 0.3467 0.3292 0.0891 -0.0497 -0.1286 39 ASP A OD1 123 O OD2 . ASP A 24 ? 0.3052 0.2252 0.2846 0.0911 -0.0229 -0.0446 39 ASP A OD2 124 N N . TYR A 25 ? 0.2917 0.1867 0.2499 -0.0420 0.0655 -0.0428 40 TYR A N 125 C CA . TYR A 25 ? 0.2293 0.2902 0.2224 0.0011 0.0212 -0.0849 40 TYR A CA 126 C C . TYR A 25 ? 0.2922 0.2023 0.2288 -0.0238 0.0833 -0.0947 40 TYR A C 127 O O . TYR A 25 ? 0.3697 0.1691 0.3162 -0.0293 0.0975 -0.0099 40 TYR A O 128 C CB . TYR A 25 ? 0.2156 0.2205 0.2809 -0.0274 0.0234 -0.1052 40 TYR A CB 129 C CG . TYR A 25 ? 0.2442 0.2109 0.2040 -0.0335 -0.0585 0.0233 40 TYR A CG 130 C CD1 . TYR A 25 ? 0.2162 0.2041 0.1797 -0.0300 0.0539 0.0196 40 TYR A CD1 131 C CD2 . TYR A 25 ? 0.2539 0.1113 0.2489 0.0406 0.0807 0.0173 40 TYR A CD2 132 C CE1 . TYR A 25 ? 0.2344 0.2354 0.1265 -0.0191 0.0720 0.0272 40 TYR A CE1 133 C CE2 . TYR A 25 ? 0.2351 0.1407 0.2855 0.0289 0.0320 -0.0321 40 TYR A CE2 134 C CZ . TYR A 25 ? 0.2267 0.2478 0.1235 -0.0031 0.0663 0.0060 40 TYR A CZ 135 O OH . TYR A 25 ? 0.1808 0.1869 0.1782 -0.0214 0.0436 0.0275 40 TYR A OH 136 N N . LEU A 26 ? 0.2928 0.1555 0.2292 -0.0296 0.0393 -0.0849 41 LEU A N 137 C CA . LEU A 26 ? 0.3578 0.2016 0.1962 -0.0380 0.0648 -0.0677 41 LEU A CA 138 C C . LEU A 26 ? 0.3266 0.2248 0.3705 -0.1305 0.0667 -0.0245 41 LEU A C 139 O O . LEU A 26 ? 0.4668 0.1838 0.3639 -0.0448 0.0804 -0.0225 41 LEU A O 140 C CB . LEU A 26 ? 0.3510 0.1865 0.2068 -0.0696 0.0739 0.0138 41 LEU A CB 141 C CG . LEU A 26 ? 0.3677 0.1828 0.2640 -0.0679 0.0118 -0.0167 41 LEU A CG 142 C CD1 . LEU A 26 ? 0.3927 0.2781 0.2831 0.0041 0.1057 -0.0966 41 LEU A CD1 143 C CD2 . LEU A 26 ? 0.3423 0.2934 0.3150 -0.0613 0.0541 -0.1363 41 LEU A CD2 144 N N . LYS A 27 ? 0.3136 0.1834 0.3409 -0.0828 0.0610 -0.0148 42 LYS A N 145 C CA . LYS A 27 ? 0.4131 0.3044 0.3950 -0.0233 0.0905 -0.0733 42 LYS A CA 146 C C . LYS A 27 ? 0.4330 0.3087 0.3892 -0.0019 0.0990 0.1085 42 LYS A C 147 O O . LYS A 27 ? 0.5047 0.4161 0.5589 -0.0352 0.0801 -0.0169 42 LYS A O 148 C CB . LYS A 27 ? 0.4209 0.2228 0.4763 0.0946 0.0525 -0.0268 42 LYS A CB 149 C CG . LYS A 27 ? 0.4725 0.5311 0.5775 0.0746 0.0841 0.0790 42 LYS A CG 150 C CD . LYS A 27 ? 0.5855 0.6403 0.6490 0.0747 0.0751 0.0317 42 LYS A CD 151 C CE . LYS A 27 ? 0.6016 0.7003 0.6979 -0.0205 0.1084 -0.0229 42 LYS A CE 152 N NZ . LYS A 27 ? 0.6237 0.7751 0.7858 0.0132 0.0942 -0.0071 42 LYS A NZ 153 N N . ASN A 28 ? 0.3937 0.1837 0.3468 0.0515 0.0650 0.0417 43 ASN A N 154 C CA . ASN A 28 ? 0.3933 0.4619 0.3039 -0.0287 0.0505 0.0755 43 ASN A CA 155 C C . ASN A 28 ? 0.3804 0.2571 0.3884 -0.0206 0.1109 0.0309 43 ASN A C 156 O O . ASN A 28 ? 0.3648 0.2669 0.3580 -0.0038 0.0646 -0.0098 43 ASN A O 157 C CB . ASN A 28 ? 0.4414 0.3357 0.2581 0.0326 0.0333 0.0369 43 ASN A CB 158 C CG . ASN A 28 ? 0.4239 0.3515 0.4635 0.0424 0.0061 0.0060 43 ASN A CG 159 O OD1 . ASN A 28 ? 0.4197 0.4298 0.6646 -0.0236 -0.0337 0.0203 43 ASN A OD1 160 N ND2 . ASN A 28 ? 0.4610 0.2508 0.3905 0.0190 0.0433 -0.0049 43 ASN A ND2 161 N N . TYR A 29 ? 0.3758 0.2305 0.3910 0.0536 0.1273 -0.0093 44 TYR A N 162 C CA . TYR A 29 ? 0.3889 0.2710 0.3120 0.0253 0.0108 0.0033 44 TYR A CA 163 C C . TYR A 29 ? 0.3926 0.3417 0.2760 -0.0296 0.0307 -0.0679 44 TYR A C 164 O O . TYR A 29 ? 0.4627 0.3560 0.2748 0.0194 0.0742 -0.1525 44 TYR A O 165 C CB . TYR A 29 ? 0.4495 0.2305 0.2381 -0.0405 -0.0217 0.0665 44 TYR A CB 166 C CG . TYR A 29 ? 0.4346 0.1619 0.2743 0.0330 0.0788 0.0596 44 TYR A CG 167 C CD1 . TYR A 29 ? 0.3867 0.3543 0.2938 -0.0834 -0.0062 0.0769 44 TYR A CD1 168 C CD2 . TYR A 29 ? 0.3672 0.2851 0.1779 -0.0488 0.0447 0.0572 44 TYR A CD2 169 C CE1 . TYR A 29 ? 0.3519 0.2562 0.3839 -0.0259 0.1108 0.0156 44 TYR A CE1 170 C CE2 . TYR A 29 ? 0.3177 0.3741 0.1096 0.0067 -0.0092 0.0011 44 TYR A CE2 171 C CZ . TYR A 29 ? 0.3000 0.2757 0.2507 -0.0253 0.0578 0.1098 44 TYR A CZ 172 O OH . TYR A 29 ? 0.3228 0.3445 0.2684 0.0074 0.0758 0.0161 44 TYR A OH 173 N N . GLU A 30 ? 0.4593 0.4148 0.2760 -0.1538 0.0327 -0.1425 45 GLU A N 174 C CA . GLU A 30 ? 0.4908 0.3561 0.3065 -0.2116 0.0387 -0.0286 45 GLU A CA 175 C C . GLU A 30 ? 0.4450 0.2391 0.3181 -0.1123 0.1495 -0.0046 45 GLU A C 176 O O . GLU A 30 ? 0.4989 0.2474 0.2995 -0.1330 0.0876 -0.0900 45 GLU A O 177 C CB . GLU A 30 ? 0.5194 0.3714 0.3916 -0.1006 0.0965 -0.0885 45 GLU A CB 178 C CG . GLU A 30 ? 0.5789 0.4881 0.4899 -0.0957 -0.0068 0.0085 45 GLU A CG 179 C CD . GLU A 30 ? 0.6004 0.6406 0.6591 0.0414 -0.0424 -0.0936 45 GLU A CD 180 O OE1 . GLU A 30 ? 0.6766 0.6915 0.8196 0.0668 0.0206 -0.0212 45 GLU A OE1 181 O OE2 . GLU A 30 ? 0.6050 0.8032 0.7882 0.0119 -0.0109 -0.0867 45 GLU A OE2 182 N N . PHE A 31 ? 0.4558 0.2798 0.2351 -0.1727 0.0788 -0.0734 46 PHE A N 183 C CA . PHE A 31 ? 0.3654 0.2777 0.2987 -0.1057 -0.0426 -0.1111 46 PHE A CA 184 C C . PHE A 31 ? 0.4165 0.2941 0.3549 -0.1533 0.0301 -0.1107 46 PHE A C 185 O O . PHE A 31 ? 0.4662 0.2593 0.2913 -0.1407 0.0303 -0.0281 46 PHE A O 186 C CB . PHE A 31 ? 0.3812 0.2184 0.3163 -0.1158 0.0939 -0.0925 46 PHE A CB 187 C CG . PHE A 31 ? 0.3620 0.2744 0.2005 -0.1321 0.0844 -0.0020 46 PHE A CG 188 C CD1 . PHE A 31 ? 0.3735 0.2037 0.3140 -0.0794 0.1215 -0.0211 46 PHE A CD1 189 C CD2 . PHE A 31 ? 0.4279 0.3013 0.2897 -0.1670 0.1243 -0.1153 46 PHE A CD2 190 C CE1 . PHE A 31 ? 0.2577 0.1729 0.3386 -0.0919 0.0346 -0.0492 46 PHE A CE1 191 C CE2 . PHE A 31 ? 0.3721 0.2600 0.2257 -0.1512 0.0912 -0.0831 46 PHE A CE2 192 C CZ . PHE A 31 ? 0.3430 0.2075 0.2730 -0.1108 0.0434 0.0520 46 PHE A CZ 193 N N . PRO A 32 ? 0.4416 0.2961 0.2299 -0.0695 -0.0064 -0.0486 47 PRO A N 194 C CA . PRO A 32 ? 0.4334 0.4005 0.2222 -0.1146 0.1019 -0.1027 47 PRO A CA 195 C C . PRO A 32 ? 0.4292 0.2648 0.2783 -0.1284 0.0937 -0.1097 47 PRO A C 196 O O . PRO A 32 ? 0.4747 0.2622 0.3658 -0.1216 0.0860 -0.1252 47 PRO A O 197 C CB . PRO A 32 ? 0.4115 0.3539 0.4325 -0.1739 0.0576 -0.0253 47 PRO A CB 198 C CG . PRO A 32 ? 0.4223 0.4301 0.3897 -0.1520 0.1550 -0.0120 47 PRO A CG 199 C CD . PRO A 32 ? 0.4308 0.2832 0.4057 -0.1814 0.0342 0.0065 47 PRO A CD 200 N N . HIS A 33 ? 0.4338 0.2344 0.2692 -0.1206 0.1191 -0.0916 48 HIS A N 201 C CA . HIS A 33 ? 0.3949 0.1582 0.3418 -0.0625 0.0397 -0.0287 48 HIS A CA 202 C C . HIS A 33 ? 0.3821 0.3964 0.2764 -0.1907 0.0894 -0.0448 48 HIS A C 203 O O . HIS A 33 ? 0.4869 0.2646 0.2666 -0.1553 0.0481 -0.0550 48 HIS A O 204 C CB . HIS A 33 ? 0.3857 0.4056 0.3730 -0.2153 0.0231 -0.0636 48 HIS A CB 205 C CG . HIS A 33 ? 0.3923 0.2673 0.2948 -0.1389 0.0244 -0.0979 48 HIS A CG 206 N ND1 . HIS A 33 ? 0.4428 0.4000 0.3302 -0.1460 0.0482 -0.1097 48 HIS A ND1 207 C CD2 . HIS A 33 ? 0.4318 0.3322 0.4075 -0.1458 0.1080 -0.1691 48 HIS A CD2 208 C CE1 . HIS A 33 ? 0.4658 0.3017 0.4624 -0.1424 0.0716 -0.1521 48 HIS A CE1 209 N NE2 . HIS A 33 ? 0.4625 0.3765 0.3529 -0.1860 0.0752 -0.0179 48 HIS A NE2 210 N N . LEU A 34 ? 0.3598 0.1736 0.2875 -0.1137 -0.0169 -0.0042 49 LEU A N 211 C CA . LEU A 34 ? 0.4040 0.2426 0.3396 -0.1561 0.0193 0.0154 49 LEU A CA 212 C C . LEU A 34 ? 0.3485 0.3741 0.2581 -0.0991 0.0308 -0.0142 49 LEU A C 213 O O . LEU A 34 ? 0.3393 0.3414 0.2510 -0.1490 0.0120 0.0027 49 LEU A O 214 C CB . LEU A 34 ? 0.4685 0.3534 0.2823 -0.0281 -0.0481 -0.1665 49 LEU A CB 215 C CG . LEU A 34 ? 0.5295 0.4224 0.4947 -0.0849 -0.0018 0.0030 49 LEU A CG 216 C CD1 . LEU A 34 ? 0.5601 0.3627 0.3821 -0.2170 -0.0514 -0.0198 49 LEU A CD1 217 C CD2 . LEU A 34 ? 0.3962 0.3934 0.2370 -0.2074 0.1045 -0.1020 49 LEU A CD2 218 N N . GLN A 35 ? 0.3726 0.3442 0.2905 -0.1062 0.0133 -0.1066 50 GLN A N 219 C CA . GLN A 35 ? 0.4855 0.2272 0.3813 -0.0302 0.0672 -0.0932 50 GLN A CA 220 C C . GLN A 35 ? 0.5191 0.4646 0.4028 -0.0172 0.1195 -0.0184 50 GLN A C 221 O O . GLN A 35 ? 0.5743 0.3891 0.4392 -0.0207 0.2282 -0.0968 50 GLN A O 222 C CB . GLN A 35 ? 0.5295 0.4683 0.5213 0.0433 0.2004 0.0195 50 GLN A CB 223 C CG . GLN A 35 ? 0.6582 0.7206 0.8459 -0.0682 0.0269 0.1012 50 GLN A CG 224 C CD . GLN A 35 ? 0.7058 0.9319 0.9773 0.0302 0.0670 0.0516 50 GLN A CD 225 O OE1 . GLN A 35 ? 0.7740 0.9567 1.0310 0.0181 0.0725 0.1408 50 GLN A OE1 226 N NE2 . GLN A 35 ? 0.6770 0.9368 0.9748 0.0427 0.1022 -0.0285 50 GLN A NE2 227 N N . ASN A 36 ? 0.5284 0.3864 0.2060 -0.0103 0.0647 -0.0183 51 ASN A N 228 C CA . ASN A 36 ? 0.4944 0.3433 0.2639 -0.1410 0.0768 -0.0690 51 ASN A CA 229 C C . ASN A 36 ? 0.4828 0.4410 0.2941 -0.1226 0.1300 -0.1153 51 ASN A C 230 O O . ASN A 36 ? 0.6467 0.4392 0.2103 -0.0666 0.0829 -0.0563 51 ASN A O 231 C CB . ASN A 36 ? 0.4859 0.4347 0.3151 -0.1004 -0.0750 -0.0846 51 ASN A CB 232 C CG . ASN A 36 ? 0.5956 0.5740 0.6049 0.0090 0.0878 -0.0118 51 ASN A CG 233 O OD1 . ASN A 36 ? 0.7264 0.6657 0.6410 -0.0931 0.0259 -0.0216 51 ASN A OD1 234 N ND2 . ASN A 36 ? 0.5805 0.4956 0.5556 -0.0711 0.0282 -0.1389 51 ASN A ND2 235 N N . PHE A 37 ? 0.4553 0.3233 0.3337 -0.1206 0.0224 -0.1507 52 PHE A N 236 C CA . PHE A 37 ? 0.4372 0.2955 0.2915 -0.1364 0.0172 -0.1117 52 PHE A CA 237 C C . PHE A 37 ? 0.4867 0.3871 0.3681 -0.0919 0.0920 -0.0674 52 PHE A C 238 O O . PHE A 37 ? 0.5882 0.3424 0.3032 -0.1509 0.1047 -0.0518 52 PHE A O 239 C CB . PHE A 37 ? 0.3664 0.3161 0.2613 -0.1085 -0.0271 -0.1168 52 PHE A CB 240 C CG . PHE A 37 ? 0.2753 0.2615 0.2176 -0.0826 0.0469 -0.0633 52 PHE A CG 241 C CD1 . PHE A 37 ? 0.2689 0.3232 0.2852 -0.1584 0.0404 -0.0079 52 PHE A CD1 242 C CD2 . PHE A 37 ? 0.2815 0.2807 0.2894 -0.0811 0.0033 -0.1368 52 PHE A CD2 243 C CE1 . PHE A 37 ? 0.2439 0.2649 0.1983 -0.0916 0.0311 -0.0421 52 PHE A CE1 244 C CE2 . PHE A 37 ? 0.2555 0.3583 0.2866 -0.1547 0.0394 -0.0281 52 PHE A CE2 245 C CZ . PHE A 37 ? 0.2799 0.4234 0.2176 -0.1370 0.0448 -0.1238 52 PHE A CZ 246 N N . ILE A 38 ? 0.4139 0.4632 0.3037 -0.1205 0.1629 0.0027 53 ILE A N 247 C CA . ILE A 38 ? 0.4308 0.2745 0.3564 -0.0973 0.2065 -0.0572 53 ILE A CA 248 C C . ILE A 38 ? 0.4932 0.4254 0.3843 -0.1059 0.1409 -0.0011 53 ILE A C 249 O O . ILE A 38 ? 0.4536 0.3975 0.3276 -0.0489 0.0878 -0.0569 53 ILE A O 250 C CB . ILE A 38 ? 0.4166 0.3476 0.4324 -0.0806 0.1508 -0.1272 53 ILE A CB 251 C CG1 . ILE A 38 ? 0.4175 0.4420 0.4409 -0.1556 0.0678 -0.1445 53 ILE A CG1 252 C CG2 . ILE A 38 ? 0.4697 0.3888 0.4878 -0.1072 0.1461 -0.0935 53 ILE A CG2 253 C CD1 . ILE A 38 ? 0.4449 0.3705 0.3770 -0.1285 -0.0717 0.0601 53 ILE A CD1 254 N N . LYS A 39 ? 0.5239 0.3021 0.4604 -0.0663 0.2098 0.0672 54 LYS A N 255 C CA . LYS A 39 ? 0.6138 0.4754 0.3178 -0.0200 0.1353 -0.0789 54 LYS A CA 256 C C . LYS A 39 ? 0.5532 0.3804 0.5357 -0.0712 0.0904 -0.0699 54 LYS A C 257 O O . LYS A 39 ? 0.5502 0.4461 0.3258 -0.0858 0.1216 -0.0124 54 LYS A O 258 C CB . LYS A 39 ? 0.6356 0.5902 0.6439 -0.0974 0.1045 -0.0479 54 LYS A CB 259 C CG . LYS A 39 ? 0.6466 0.6714 0.6298 -0.0857 0.0857 -0.0690 54 LYS A CG 260 C CD . LYS A 39 ? 0.6854 0.7736 0.7166 -0.0004 0.0515 -0.0542 54 LYS A CD 261 C CE . LYS A 39 ? 0.6922 0.7874 0.8420 -0.0500 0.0259 -0.0631 54 LYS A CE 262 N NZ . LYS A 39 ? 0.6883 0.8738 0.8473 -0.0234 0.0088 -0.0425 54 LYS A NZ 263 N N . GLU A 40 ? 0.4957 0.2854 0.5783 -0.1680 0.0780 0.0378 55 GLU A N 264 C CA . GLU A 40 ? 0.5303 0.5233 0.5727 -0.2139 -0.1138 -0.0479 55 GLU A CA 265 C C . GLU A 40 ? 0.4971 0.3398 0.4307 -0.1313 0.0335 -0.0329 55 GLU A C 266 O O . GLU A 40 ? 0.4068 0.4632 0.3132 -0.1545 0.0510 -0.1056 55 GLU A O 267 C CB . GLU A 40 ? 0.6370 0.6911 0.8653 -0.0991 -0.1481 0.0081 55 GLU A CB 268 C CG . GLU A 40 ? 0.6490 0.7811 0.9022 -0.0989 -0.1698 0.0252 55 GLU A CG 269 C CD . GLU A 40 ? 0.7662 0.9432 0.9830 -0.0445 -0.0166 -0.0468 55 GLU A CD 270 O OE1 . GLU A 40 ? 0.7725 0.9602 0.8696 0.0072 0.1117 -0.0807 55 GLU A OE1 271 O OE2 . GLU A 40 ? 0.7998 1.0203 1.0226 -0.0208 0.0300 0.0180 55 GLU A OE2 272 N N . GLY A 41 ? 0.3889 0.3841 0.3816 -0.1822 0.0610 -0.0437 56 GLY A N 273 C CA . GLY A 41 ? 0.3873 0.3549 0.2103 -0.2020 0.0903 -0.0809 56 GLY A CA 274 C C . GLY A 41 ? 0.3237 0.3156 0.3257 -0.0650 0.0202 -0.0759 56 GLY A C 275 O O . GLY A 41 ? 0.3864 0.2554 0.2290 -0.0880 0.0273 -0.1057 56 GLY A O 276 N N . VAL A 42 ? 0.2959 0.3205 0.1678 -0.1584 0.0309 -0.0173 57 VAL A N 277 C CA . VAL A 42 ? 0.3032 0.3461 0.1699 -0.1514 0.0622 -0.0347 57 VAL A CA 278 C C . VAL A 42 ? 0.2999 0.3054 0.2240 -0.1276 0.1134 -0.0853 57 VAL A C 279 O O . VAL A 42 ? 0.2946 0.3456 0.1813 -0.1310 0.0685 -0.0889 57 VAL A O 280 C CB . VAL A 42 ? 0.2919 0.4050 0.1865 -0.0897 0.0894 -0.0315 57 VAL A CB 281 C CG1 . VAL A 42 ? 0.3477 0.3469 0.1595 -0.1179 0.0600 0.0056 57 VAL A CG1 282 C CG2 . VAL A 42 ? 0.2710 0.4402 0.2346 -0.0882 0.0582 -0.1228 57 VAL A CG2 283 N N . LEU A 43 ? 0.3331 0.2404 0.1908 -0.1256 0.0050 -0.0339 58 LEU A N 284 C CA . LEU A 43 ? 0.3101 0.3165 0.1499 -0.0964 0.0477 -0.0115 58 LEU A CA 285 C C . LEU A 43 ? 0.2782 0.2583 0.2136 -0.0078 0.0828 -0.0679 58 LEU A C 286 O O . LEU A 43 ? 0.2807 0.3521 0.2293 -0.0272 0.0652 -0.1358 58 LEU A O 287 C CB . LEU A 43 ? 0.3989 0.2551 0.1417 -0.0516 0.0076 -0.0256 58 LEU A CB 288 C CG . LEU A 43 ? 0.3661 0.3495 0.2056 0.0173 -0.0025 -0.1130 58 LEU A CG 289 C CD1 . LEU A 43 ? 0.2809 0.3419 0.2009 -0.0008 0.0686 -0.0311 58 LEU A CD1 290 C CD2 . LEU A 43 ? 0.4104 0.2335 0.2937 -0.0449 0.1148 -0.0748 58 LEU A CD2 291 N N . VAL A 44 ? 0.2558 0.2382 0.2459 -0.0794 0.0356 -0.0808 59 VAL A N 292 C CA . VAL A 44 ? 0.2928 0.2064 0.2501 0.0176 0.0932 -0.0787 59 VAL A CA 293 C C . VAL A 44 ? 0.2519 0.2531 0.1673 -0.0697 0.0732 -0.0660 59 VAL A C 294 O O . VAL A 44 ? 0.2197 0.2437 0.1728 -0.0610 0.0565 -0.0334 59 VAL A O 295 C CB . VAL A 44 ? 0.1927 0.3699 0.1633 -0.0616 0.0503 -0.0810 59 VAL A CB 296 C CG1 . VAL A 44 ? 0.1776 0.3173 0.1564 -0.0848 0.0038 -0.0398 59 VAL A CG1 297 C CG2 . VAL A 44 ? 0.2730 0.3335 0.1160 -0.0520 0.0363 -0.0219 59 VAL A CG2 298 N N . GLU A 45 ? 0.2494 0.2442 0.1862 -0.0434 0.0247 0.0004 60 GLU A N 299 C CA . GLU A 45 ? 0.2966 0.2030 0.1764 0.0248 0.0359 -0.0198 60 GLU A CA 300 C C . GLU A 45 ? 0.3139 0.1794 0.1634 -0.0137 -0.0564 -0.0541 60 GLU A C 301 O O . GLU A 45 ? 0.3325 0.2042 0.1672 0.0057 0.0625 -0.0367 60 GLU A O 302 C CB . GLU A 45 ? 0.2807 0.2501 0.2679 0.0373 0.0449 -0.1268 60 GLU A CB 303 C CG . GLU A 45 ? 0.3329 0.3558 0.3340 0.0506 0.0641 -0.1620 60 GLU A CG 304 C CD . GLU A 45 ? 0.5042 0.6454 0.6769 0.0437 0.0841 -0.0084 60 GLU A CD 305 O OE1 . GLU A 45 ? 0.4367 0.6982 0.6435 0.0333 0.1879 -0.0205 60 GLU A OE1 306 O OE2 . GLU A 45 ? 0.6107 0.4857 0.8010 -0.0412 0.0094 -0.0041 60 GLU A OE2 307 N N . HIS A 46 ? 0.2228 0.1767 0.2082 0.0078 0.0455 -0.0298 61 HIS A N 308 C CA . HIS A 46 ? 0.2103 0.0998 0.2628 0.0114 -0.0018 -0.0483 61 HIS A CA 309 C C . HIS A 46 ? 0.1669 0.1771 0.2912 -0.0331 0.0722 -0.0930 61 HIS A C 310 O O . HIS A 46 ? 0.2536 0.3128 0.2791 -0.0153 0.1266 -0.0132 61 HIS A O 311 C CB . HIS A 46 ? 0.1581 0.4251 0.2532 0.0339 -0.0470 -0.0456 61 HIS A CB 312 C CG . HIS A 46 ? 0.2785 0.4273 0.3835 0.0376 -0.0461 -0.1533 61 HIS A CG 313 N ND1 . HIS A 46 ? 0.3129 0.5463 0.5281 0.0338 -0.0311 -0.0651 61 HIS A ND1 314 C CD2 . HIS A 46 ? 0.3503 0.4597 0.2707 0.0035 -0.0728 0.1592 61 HIS A CD2 315 C CE1 . HIS A 46 ? 0.3619 0.5241 0.5429 0.0081 -0.0078 -0.0016 61 HIS A CE1 316 N NE2 . HIS A 46 ? 0.3978 0.5050 0.4698 -0.0405 -0.0102 0.0346 61 HIS A NE2 317 N N . VAL A 47 ? 0.1678 0.2276 0.1770 -0.0174 0.0095 -0.0189 62 VAL A N 318 C CA . VAL A 47 ? 0.1796 0.1695 0.1651 0.0262 -0.0144 0.0142 62 VAL A CA 319 C C . VAL A 47 ? 0.1701 0.1299 0.1657 0.0086 -0.0044 -0.0455 62 VAL A C 320 O O . VAL A 47 ? 0.1944 0.1918 0.1694 -0.0361 0.0259 -0.0733 62 VAL A O 321 C CB . VAL A 47 ? 0.1998 0.1235 0.1200 -0.0121 -0.0164 -0.0100 62 VAL A CB 322 C CG1 . VAL A 47 ? 0.1661 0.1930 0.2124 -0.0160 -0.0106 -0.0253 62 VAL A CG1 323 C CG2 . VAL A 47 ? 0.2367 0.1670 0.1795 -0.0977 0.0377 -0.0393 62 VAL A CG2 324 N N . LYS A 48 ? 0.1679 0.1914 0.1802 -0.0900 -0.0007 -0.0308 63 LYS A N 325 C CA . LYS A 48 ? 0.1027 0.1816 0.1831 -0.0262 0.0101 0.0179 63 LYS A CA 326 C C . LYS A 48 ? 0.1082 0.1884 0.1617 -0.0355 -0.0334 0.0492 63 LYS A C 327 O O . LYS A 48 ? 0.1471 0.2187 0.1459 0.0099 -0.0107 0.0007 63 LYS A O 328 C CB . LYS A 48 ? 0.1041 0.1995 0.2287 -0.0622 0.0065 0.0010 63 LYS A CB 329 C CG . LYS A 48 ? 0.1277 0.2305 0.2375 -0.0626 -0.0434 -0.0280 63 LYS A CG 330 C CD . LYS A 48 ? 0.1480 0.2808 0.3253 -0.0509 0.0097 -0.1175 63 LYS A CD 331 C CE . LYS A 48 ? 0.1922 0.2431 0.3075 -0.0778 -0.0008 -0.0384 63 LYS A CE 332 N NZ . LYS A 48 ? 0.2290 0.5464 0.4982 -0.1242 0.0164 -0.1239 63 LYS A NZ 333 N N . ASN A 49 ? 0.1614 0.1985 0.1943 -0.0190 0.0522 0.0321 64 ASN A N 334 C CA . ASN A 49 ? 0.1657 0.1741 0.1729 -0.0768 0.0624 -0.0462 64 ASN A CA 335 C C . ASN A 49 ? 0.1584 0.1021 0.1179 -0.0252 0.0149 0.0437 64 ASN A C 336 O O . ASN A 49 ? 0.1454 0.1922 0.1808 -0.0404 0.0079 -0.0123 64 ASN A O 337 C CB . ASN A 49 ? 0.1463 0.1335 0.1214 -0.0177 0.0100 0.0060 64 ASN A CB 338 C CG . ASN A 49 ? 0.1574 0.1222 0.0905 -0.0423 0.0103 0.0181 64 ASN A CG 339 O OD1 . ASN A 49 ? 0.1271 0.2235 0.1674 -0.0052 -0.0137 0.0279 64 ASN A OD1 340 N ND2 . ASN A 49 ? 0.1795 0.1760 0.1036 -0.0291 0.0322 -0.0051 64 ASN A ND2 341 N N . VAL A 50 ? 0.1749 0.1382 0.1704 -0.0138 -0.0038 -0.0054 65 VAL A N 342 C CA . VAL A 50 ? 0.1981 0.1058 0.1296 -0.0263 0.0269 -0.0340 65 VAL A CA 343 C C . VAL A 50 ? 0.1647 0.1543 0.0978 -0.0279 0.0419 -0.0167 65 VAL A C 344 O O . VAL A 50 ? 0.1211 0.1989 0.1448 -0.0250 -0.0066 0.0149 65 VAL A O 345 C CB . VAL A 50 ? 0.1958 0.2256 0.1445 -0.0284 -0.0183 0.0016 65 VAL A CB 346 C CG1 . VAL A 50 ? 0.2966 0.2544 0.0973 -0.0244 0.0130 -0.0258 65 VAL A CG1 347 C CG2 . VAL A 50 ? 0.2257 0.1354 0.2603 0.0028 -0.0750 0.0420 65 VAL A CG2 348 N N . PHE A 51 ? 0.1844 0.1790 0.1577 -0.0433 -0.0562 -0.0248 66 PHE A N 349 C CA . PHE A 51 ? 0.1673 0.2055 0.0976 -0.0276 -0.0383 -0.0284 66 PHE A CA 350 C C . PHE A 51 ? 0.1435 0.0897 0.1585 -0.0231 0.0324 0.0164 66 PHE A C 351 O O . PHE A 51 ? 0.1584 0.1895 0.1505 -0.0050 0.0105 0.0635 66 PHE A O 352 C CB . PHE A 51 ? 0.1763 0.2177 0.1295 -0.0156 -0.0701 0.0144 66 PHE A CB 353 C CG . PHE A 51 ? 0.1342 0.2442 0.1131 -0.0691 -0.0048 -0.0193 66 PHE A CG 354 C CD1 . PHE A 51 ? 0.1637 0.3071 0.1247 -0.0232 0.0141 0.0646 66 PHE A CD1 355 C CD2 . PHE A 51 ? 0.1819 0.2051 0.1489 -0.0903 -0.0023 -0.0408 66 PHE A CD2 356 C CE1 . PHE A 51 ? 0.1303 0.4105 0.1699 -0.0241 -0.0187 0.0167 66 PHE A CE1 357 C CE2 . PHE A 51 ? 0.1633 0.1311 0.1747 -0.0146 -0.0175 -0.0044 66 PHE A CE2 358 C CZ . PHE A 51 ? 0.1468 0.2558 0.1821 -0.0246 -0.0188 0.0203 66 PHE A CZ 359 N N . ILE A 52 ? 0.1190 0.0954 0.1956 -0.0175 0.0026 0.0493 67 ILE A N 360 C CA . ILE A 52 ? 0.1343 0.0773 0.1389 -0.0297 -0.0131 -0.0064 67 ILE A CA 361 C C . ILE A 52 ? 0.1302 0.1830 0.1188 -0.0479 0.0074 0.0089 67 ILE A C 362 O O . ILE A 52 ? 0.1269 0.1623 0.1258 -0.0228 -0.0066 -0.0066 67 ILE A O 363 C CB . ILE A 52 ? 0.0968 0.1831 0.1668 -0.0120 0.0340 -0.0372 67 ILE A CB 364 C CG1 . ILE A 52 ? 0.1222 0.1890 0.1397 0.0187 0.0617 -0.0163 67 ILE A CG1 365 C CG2 . ILE A 52 ? 0.1790 0.0994 0.2123 -0.0330 -0.0023 -0.0060 67 ILE A CG2 366 C CD1 . ILE A 52 ? 0.1345 0.1729 0.2363 0.0475 0.0589 0.0327 67 ILE A CD1 367 N N . THR A 53 ? 0.1515 0.1318 0.1530 -0.0254 0.0360 0.0378 68 THR A N 368 C CA . THR A 53 ? 0.1552 0.1500 0.1966 -0.0576 -0.0128 0.0621 68 THR A CA 369 C C . THR A 53 ? 0.2231 0.1463 0.1213 -0.0412 -0.0028 0.0242 68 THR A C 370 O O . THR A 53 ? 0.1405 0.2476 0.1327 -0.0265 0.0044 0.0016 68 THR A O 371 C CB . THR A 53 ? 0.1278 0.1894 0.0832 -0.0122 0.0267 0.0258 68 THR A CB 372 O OG1 . THR A 53 ? 0.1800 0.1821 0.1061 0.0071 0.0084 -0.0029 68 THR A OG1 373 C CG2 . THR A 53 ? 0.1093 0.2003 0.1495 0.0118 0.0299 0.0779 68 THR A CG2 374 N N . LYS A 54 ? 0.1623 0.1422 0.1584 -0.0412 0.0027 0.0653 69 LYS A N 375 C CA . LYS A 54 ? 0.1000 0.1359 0.1587 -0.0165 0.0245 0.0165 69 LYS A CA 376 C C . LYS A 54 ? 0.0797 0.2218 0.2251 -0.0275 0.0000 -0.0086 69 LYS A C 377 O O . LYS A 54 ? 0.1274 0.2416 0.1711 -0.0030 0.0145 -0.0488 69 LYS A O 378 C CB . LYS A 54 ? 0.1178 0.1712 0.1352 0.0239 -0.0140 0.0167 69 LYS A CB 379 C CG . LYS A 54 ? 0.1486 0.2599 0.1104 -0.0120 -0.0425 0.0196 69 LYS A CG 380 C CD . LYS A 54 ? 0.1468 0.2318 0.0996 -0.0040 -0.0372 0.0302 69 LYS A CD 381 C CE . LYS A 54 ? 0.2147 0.3095 0.1628 0.0389 -0.0293 0.0280 69 LYS A CE 382 N NZ . LYS A 54 ? 0.2819 0.3191 0.1734 0.1208 0.0286 0.0848 69 LYS A NZ 383 N N . THR A 55 ? 0.0791 0.1617 0.1437 -0.0231 -0.0196 0.0281 70 THR A N 384 C CA . THR A 55 ? 0.1193 0.1815 0.2256 -0.0196 -0.0397 0.0143 70 THR A CA 385 C C . THR A 55 ? 0.1022 0.2553 0.1949 0.0044 0.0236 -0.0608 70 THR A C 386 O O . THR A 55 ? 0.1600 0.2059 0.1444 -0.0204 -0.0050 -0.0005 70 THR A O 387 C CB . THR A 55 ? 0.1401 0.2149 0.1692 0.0176 0.0054 0.0926 70 THR A CB 388 O OG1 . THR A 55 ? 0.1578 0.1270 0.1481 -0.0073 -0.0030 -0.0126 70 THR A OG1 389 C CG2 . THR A 55 ? 0.2096 0.1583 0.1868 -0.0714 -0.0669 0.0381 70 THR A CG2 390 N N . PHE A 56 ? 0.0879 0.1634 0.1872 -0.0113 -0.0105 0.0410 71 PHE A N 391 C CA . PHE A 56 ? 0.1121 0.2520 0.2060 0.0336 0.0376 0.0007 71 PHE A CA 392 C C . PHE A 56 ? 0.1271 0.2025 0.1467 0.0502 -0.0411 0.0233 71 PHE A C 393 O O . PHE A 56 ? 0.1728 0.1974 0.1501 0.0016 0.0044 0.0321 71 PHE A O 394 C CB . PHE A 56 ? 0.1075 0.2765 0.2069 0.0491 0.0281 -0.0026 71 PHE A CB 395 C CG . PHE A 56 ? 0.1123 0.2339 0.2220 0.0232 0.0458 0.0342 71 PHE A CG 396 C CD1 . PHE A 56 ? 0.2118 0.2510 0.4070 0.0156 0.0730 0.1540 71 PHE A CD1 397 C CD2 . PHE A 56 ? 0.1727 0.2413 0.1769 -0.0010 -0.0145 -0.0062 71 PHE A CD2 398 C CE1 . PHE A 56 ? 0.2167 0.2346 0.4838 0.0349 0.1000 0.1486 71 PHE A CE1 399 C CE2 . PHE A 56 ? 0.1651 0.2374 0.3550 -0.0755 0.0244 0.0358 71 PHE A CE2 400 C CZ . PHE A 56 ? 0.1605 0.2435 0.3713 -0.0657 0.0534 0.0106 71 PHE A CZ 401 N N . PRO A 57 ? 0.1022 0.1816 0.1378 -0.0339 -0.0325 0.0270 72 PRO A N 402 C CA . PRO A 57 ? 0.1356 0.1828 0.1532 -0.0231 -0.0194 0.0706 72 PRO A CA 403 C C . PRO A 57 ? 0.1471 0.1590 0.2448 -0.0701 0.0223 0.0144 72 PRO A C 404 O O . PRO A 57 ? 0.1725 0.1414 0.2122 -0.0024 0.0385 0.0735 72 PRO A O 405 C CB . PRO A 57 ? 0.1713 0.1919 0.0986 0.0504 -0.0278 -0.0472 72 PRO A CB 406 C CG . PRO A 57 ? 0.1432 0.2178 0.1633 -0.0401 -0.0176 -0.0041 72 PRO A CG 407 C CD . PRO A 57 ? 0.1124 0.2623 0.1854 -0.0268 -0.0455 -0.0270 72 PRO A CD 408 N N . ASN A 58 ? 0.1402 0.1450 0.1729 -0.0136 -0.0152 -0.0569 73 ASN A N 409 C CA . ASN A 58 ? 0.1978 0.1222 0.1524 0.0240 -0.0232 0.0386 73 ASN A CA 410 C C . ASN A 58 ? 0.1126 0.2089 0.1279 0.0472 -0.0302 0.0161 73 ASN A C 411 O O . ASN A 58 ? 0.1733 0.2169 0.1215 -0.0169 0.0181 0.0044 73 ASN A O 412 C CB . ASN A 58 ? 0.1665 0.1520 0.1561 -0.0208 -0.0575 0.0574 73 ASN A CB 413 C CG . ASN A 58 ? 0.1285 0.1079 0.2002 -0.0261 -0.0611 0.0569 73 ASN A CG 414 O OD1 . ASN A 58 ? 0.1261 0.2076 0.1854 -0.0131 0.0161 -0.0205 73 ASN A OD1 415 N ND2 . ASN A 58 ? 0.1666 0.2248 0.1166 -0.0005 -0.0334 0.0229 73 ASN A ND2 416 N N . HIS A 59 ? 0.0989 0.1930 0.1857 0.0284 -0.0343 0.0406 74 HIS A N 417 C CA . HIS A 59 ? 0.0960 0.2195 0.1845 -0.0138 -0.0480 0.0212 74 HIS A CA 418 C C . HIS A 59 ? 0.1508 0.2945 0.2606 -0.0772 -0.0045 0.0482 74 HIS A C 419 O O . HIS A 59 ? 0.1894 0.2220 0.1264 -0.0078 -0.0111 0.0105 74 HIS A O 420 C CB . HIS A 59 ? 0.0837 0.1989 0.2556 -0.0131 -0.0151 -0.0177 74 HIS A CB 421 C CG . HIS A 59 ? 0.1069 0.1911 0.1365 0.0105 -0.0156 0.0036 74 HIS A CG 422 N ND1 . HIS A 59 ? 0.1223 0.2180 0.1498 -0.0172 -0.0232 0.0729 74 HIS A ND1 423 C CD2 . HIS A 59 ? 0.1693 0.2448 0.1345 -0.0610 0.0050 0.0278 74 HIS A CD2 424 C CE1 . HIS A 59 ? 0.0945 0.2166 0.1695 -0.0268 0.0168 0.0004 74 HIS A CE1 425 N NE2 . HIS A 59 ? 0.1657 0.2211 0.0940 -0.0416 -0.0281 0.0333 74 HIS A NE2 426 N N . TYR A 60 ? 0.1104 0.2237 0.2269 -0.0242 -0.0121 0.1136 75 TYR A N 427 C CA . TYR A 60 ? 0.1065 0.1059 0.2131 -0.0313 0.0001 0.0262 75 TYR A CA 428 C C . TYR A 60 ? 0.0915 0.1727 0.1756 -0.0250 -0.0447 0.0282 75 TYR A C 429 O O . TYR A 60 ? 0.1752 0.2601 0.1526 0.0125 -0.0358 0.0662 75 TYR A O 430 C CB . TYR A 60 ? 0.1386 0.2099 0.1939 -0.0220 -0.0746 0.0475 75 TYR A CB 431 C CG . TYR A 60 ? 0.1342 0.2784 0.1482 -0.0023 -0.0518 0.0315 75 TYR A CG 432 C CD1 . TYR A 60 ? 0.1648 0.1665 0.1768 0.0211 -0.0553 0.0597 75 TYR A CD1 433 C CD2 . TYR A 60 ? 0.1822 0.3502 0.2017 0.0227 -0.0269 0.0338 75 TYR A CD2 434 C CE1 . TYR A 60 ? 0.2446 0.2811 0.2221 0.0236 0.0090 0.0332 75 TYR A CE1 435 C CE2 . TYR A 60 ? 0.1505 0.3527 0.1793 0.0291 0.0026 0.0506 75 TYR A CE2 436 C CZ . TYR A 60 ? 0.2264 0.3481 0.1994 0.0516 -0.0458 0.0948 75 TYR A CZ 437 O OH . TYR A 60 ? 0.2234 0.3310 0.2299 -0.0146 -0.0224 0.1013 75 TYR A OH 438 N N . SER A 61 ? 0.1107 0.2013 0.1813 -0.0278 0.0005 -0.0098 76 SER A N 439 C CA . SER A 61 ? 0.1154 0.2285 0.1646 0.0414 -0.0191 -0.0468 76 SER A CA 440 C C . SER A 61 ? 0.1642 0.1794 0.1528 -0.0360 0.0331 0.0636 76 SER A C 441 O O . SER A 61 ? 0.1599 0.2539 0.1404 -0.0327 0.0081 0.0542 76 SER A O 442 C CB . SER A 61 ? 0.1645 0.0816 0.2456 -0.0142 0.0018 -0.0190 76 SER A CB 443 O OG . SER A 61 ? 0.1392 0.1753 0.1798 -0.0027 -0.0036 0.0189 76 SER A OG 444 N N . ILE A 62 ? 0.1966 0.1176 0.1849 -0.0293 -0.0437 0.0615 77 ILE A N 445 C CA . ILE A 62 ? 0.1834 0.1868 0.2106 -0.0934 -0.0243 0.0247 77 ILE A CA 446 C C . ILE A 62 ? 0.1041 0.2211 0.1367 0.0042 0.0385 -0.0066 77 ILE A C 447 O O . ILE A 62 ? 0.1562 0.3105 0.1357 -0.0446 0.0144 0.0635 77 ILE A O 448 C CB . ILE A 62 ? 0.1964 0.1789 0.1860 -0.0610 -0.0147 -0.0718 77 ILE A CB 449 C CG1 . ILE A 62 ? 0.1788 0.2180 0.2292 -0.0140 -0.0643 0.0428 77 ILE A CG1 450 C CG2 . ILE A 62 ? 0.2268 0.1480 0.1933 -0.0619 0.0228 0.0156 77 ILE A CG2 451 C CD1 . ILE A 62 ? 0.2252 0.1922 0.2144 -0.0674 0.0333 -0.0261 77 ILE A CD1 452 N N . VAL A 63 ? 0.1252 0.2992 0.1289 -0.0038 -0.0271 0.0263 78 VAL A N 453 C CA . VAL A 63 ? 0.1470 0.2750 0.1323 -0.0498 -0.0241 0.0791 78 VAL A CA 454 C C . VAL A 63 ? 0.1607 0.2505 0.1434 -0.0100 -0.0189 0.0891 78 VAL A C 455 O O . VAL A 63 ? 0.1817 0.2986 0.1666 -0.0148 -0.0288 0.0481 78 VAL A O 456 C CB . VAL A 63 ? 0.1326 0.2157 0.2097 -0.0551 0.0099 -0.0351 78 VAL A CB 457 C CG1 . VAL A 63 ? 0.1641 0.2932 0.1781 -0.1054 -0.0139 0.0017 78 VAL A CG1 458 C CG2 . VAL A 63 ? 0.1260 0.3874 0.1855 0.0074 -0.0317 -0.0039 78 VAL A CG2 459 N N . THR A 64 ? 0.1437 0.2344 0.1814 -0.0486 -0.0311 0.0349 79 THR A N 460 C CA . THR A 64 ? 0.1345 0.3313 0.1634 -0.0524 -0.0037 -0.0074 79 THR A CA 461 C C . THR A 64 ? 0.1635 0.3086 0.1204 -0.0119 -0.0354 0.0436 79 THR A C 462 O O . THR A 64 ? 0.1928 0.2854 0.1476 -0.0174 -0.0020 0.0738 79 THR A O 463 C CB . THR A 64 ? 0.1563 0.2952 0.1242 -0.0162 -0.0448 0.0135 79 THR A CB 464 O OG1 . THR A 64 ? 0.1718 0.2398 0.1770 -0.0333 -0.0192 0.0479 79 THR A OG1 465 C CG2 . THR A 64 ? 0.1808 0.2471 0.2099 -0.0486 0.0152 0.1033 79 THR A CG2 466 N N . GLY A 65 ? 0.1255 0.2722 0.1421 -0.0271 -0.0406 0.0017 80 GLY A N 467 C CA . GLY A 65 ? 0.1408 0.3829 0.1702 -0.0618 -0.0295 0.0253 80 GLY A CA 468 C C . GLY A 65 ? 0.1811 0.3081 0.1400 -0.0501 0.0369 0.0457 80 GLY A C 469 O O . GLY A 65 ? 0.2147 0.1791 0.1457 -0.0450 0.0258 0.0171 80 GLY A O 470 N N . LEU A 66 ? 0.1549 0.2254 0.1355 -0.0469 -0.0098 0.0597 81 LEU A N 471 C CA . LEU A 66 ? 0.1562 0.1733 0.1908 -0.0028 -0.0463 -0.0092 81 LEU A CA 472 C C . LEU A 66 ? 0.1488 0.2496 0.2282 -0.0337 -0.0273 0.0867 81 LEU A C 473 O O . LEU A 66 ? 0.1510 0.2770 0.1625 -0.0535 -0.0217 0.0019 81 LEU A O 474 C CB . LEU A 66 ? 0.1908 0.2405 0.1680 0.0546 -0.0104 0.0869 81 LEU A CB 475 C CG . LEU A 66 ? 0.1825 0.2264 0.1460 0.0288 -0.0007 0.0874 81 LEU A CG 476 C CD1 . LEU A 66 ? 0.1851 0.2107 0.2256 0.0158 -0.0417 0.0180 81 LEU A CD1 477 C CD2 . LEU A 66 ? 0.2345 0.3491 0.1862 -0.0865 0.0185 0.0883 81 LEU A CD2 478 N N . TYR A 67 ? 0.1500 0.2292 0.1393 -0.0215 0.0068 0.0551 82 TYR A N 479 C CA . TYR A 67 ? 0.1407 0.2505 0.0861 -0.0430 -0.0088 0.0240 82 TYR A CA 480 C C . TYR A 67 ? 0.1974 0.1978 0.1095 -0.0083 0.0392 0.0284 82 TYR A C 481 O O . TYR A 67 ? 0.1881 0.1588 0.1996 0.0010 -0.0025 0.0774 82 TYR A O 482 C CB . TYR A 67 ? 0.1245 0.2373 0.1680 -0.0455 -0.0216 0.0397 82 TYR A CB 483 C CG . TYR A 67 ? 0.1278 0.2177 0.2148 -0.0143 0.0083 -0.0379 82 TYR A CG 484 C CD1 . TYR A 67 ? 0.2092 0.3200 0.3586 0.0008 0.0362 -0.0911 82 TYR A CD1 485 C CD2 . TYR A 67 ? 0.1533 0.3779 0.2034 0.0153 0.0567 0.0569 82 TYR A CD2 486 C CE1 . TYR A 67 ? 0.2252 0.4091 0.3507 0.0011 -0.0446 -0.1301 82 TYR A CE1 487 C CE2 . TYR A 67 ? 0.2189 0.4104 0.1590 -0.0067 -0.0165 -0.0316 82 TYR A CE2 488 C CZ . TYR A 67 ? 0.1960 0.4984 0.2756 0.0027 -0.0110 -0.1828 82 TYR A CZ 489 O OH . TYR A 67 ? 0.2011 0.5025 0.4169 -0.0113 0.0043 -0.1690 82 TYR A OH 490 N N . GLU A 68 ? 0.1758 0.2410 0.1220 -0.0261 0.0415 0.0423 83 GLU A N 491 C CA . GLU A 68 ? 0.2164 0.1455 0.1448 -0.0237 0.0184 0.0666 83 GLU A CA 492 C C . GLU A 68 ? 0.1643 0.1863 0.2117 -0.0786 0.0027 0.0438 83 GLU A C 493 O O . GLU A 68 ? 0.1873 0.2030 0.1931 -0.0114 -0.0002 0.0399 83 GLU A O 494 C CB . GLU A 68 ? 0.2141 0.1118 0.1295 0.0198 -0.0071 0.0441 83 GLU A CB 495 C CG . GLU A 68 ? 0.2061 0.1305 0.1700 -0.0133 0.0115 0.0735 83 GLU A CG 496 C CD . GLU A 68 ? 0.1651 0.2088 0.2526 -0.0858 -0.0100 0.0341 83 GLU A CD 497 O OE1 . GLU A 68 ? 0.1718 0.1373 0.2153 -0.0105 -0.0167 0.0609 83 GLU A OE1 498 O OE2 . GLU A 68 ? 0.1422 0.1946 0.1789 -0.0356 -0.0031 -0.0018 83 GLU A OE2 499 N N . GLU A 69 ? 0.1575 0.1285 0.1730 -0.0348 -0.0356 0.0251 84 GLU A N 500 C CA . GLU A 69 ? 0.1600 0.1509 0.1643 -0.0270 -0.0559 0.0225 84 GLU A CA 501 C C . GLU A 69 ? 0.2312 0.2251 0.1396 -0.0288 -0.0697 -0.0113 84 GLU A C 502 O O . GLU A 69 ? 0.2783 0.1590 0.2258 -0.0001 0.0081 0.0277 84 GLU A O 503 C CB . GLU A 69 ? 0.2301 0.1795 0.1919 -0.0565 0.0268 0.0605 84 GLU A CB 504 C CG . GLU A 69 ? 0.1906 0.1352 0.2007 -0.0255 0.0111 0.0751 84 GLU A CG 505 C CD . GLU A 69 ? 0.2265 0.2102 0.1993 -0.0560 -0.0346 0.0510 84 GLU A CD 506 O OE1 . GLU A 69 ? 0.2330 0.1865 0.2152 -0.0365 -0.0406 0.0247 84 GLU A OE1 507 O OE2 . GLU A 69 ? 0.2553 0.2540 0.2236 -0.0304 0.0295 0.0103 84 GLU A OE2 508 N N . SER A 70 ? 0.2301 0.2202 0.1267 -0.0580 -0.0318 0.0593 85 SER A N 509 C CA . SER A 70 ? 0.1945 0.2226 0.1354 -0.0313 0.0066 0.0332 85 SER A CA 510 C C . SER A 70 ? 0.1555 0.2334 0.2286 -0.0654 -0.0214 0.0506 85 SER A C 511 O O . SER A 70 ? 0.2048 0.3607 0.3313 -0.0073 -0.0478 0.1243 85 SER A O 512 C CB . SER A 70 ? 0.2303 0.1432 0.2316 -0.0242 0.0512 0.0708 85 SER A CB 513 O OG . SER A 70 ? 0.2004 0.2485 0.2338 -0.0408 0.0370 0.0273 85 SER A OG 514 N N . HIS A 71 ? 0.1425 0.1814 0.1794 -0.0679 -0.0212 0.0643 86 HIS A N 515 C CA . HIS A 71 ? 0.1748 0.1002 0.1957 -0.0276 0.0100 0.0461 86 HIS A CA 516 C C . HIS A 71 ? 0.2573 0.2072 0.1623 0.0380 0.0434 0.0827 86 HIS A C 517 O O . HIS A 71 ? 0.2438 0.1817 0.2580 0.0047 0.0238 0.0239 86 HIS A O 518 C CB . HIS A 71 ? 0.2292 0.1619 0.1945 -0.0608 -0.0071 0.0743 86 HIS A CB 519 C CG . HIS A 71 ? 0.1678 0.1692 0.1598 -0.0222 0.0743 0.0161 86 HIS A CG 520 N ND1 . HIS A 71 ? 0.1590 0.2403 0.2144 0.0670 0.0475 0.0814 86 HIS A ND1 521 C CD2 . HIS A 71 ? 0.1324 0.1653 0.2279 -0.0205 -0.0471 0.0630 86 HIS A CD2 522 C CE1 . HIS A 71 ? 0.1027 0.2092 0.2385 0.0082 -0.0410 -0.0305 86 HIS A CE1 523 N NE2 . HIS A 71 ? 0.1740 0.1863 0.1555 -0.0429 0.0020 0.0788 86 HIS A NE2 524 N N . GLY A 72 ? 0.2395 0.2673 0.1181 -0.0136 -0.0167 0.0268 87 GLY A N 525 C CA . GLY A 72 ? 0.2244 0.1409 0.1949 -0.0030 -0.0448 -0.0113 87 GLY A CA 526 C C . GLY A 72 ? 0.2404 0.2602 0.1868 0.0357 -0.0008 0.0605 87 GLY A C 527 O O . GLY A 72 ? 0.2209 0.2703 0.2085 0.0574 -0.0092 0.0342 87 GLY A O 528 N N . ILE A 73 ? 0.1805 0.2412 0.2023 0.0039 -0.0186 0.1113 88 ILE A N 529 C CA . ILE A 73 ? 0.2422 0.1506 0.2916 -0.0135 -0.0081 0.0438 88 ILE A CA 530 C C . ILE A 73 ? 0.2384 0.2403 0.1664 0.0749 0.0029 0.0829 88 ILE A C 531 O O . ILE A 73 ? 0.2067 0.1783 0.1768 0.0048 -0.0170 0.0240 88 ILE A O 532 C CB . ILE A 73 ? 0.2291 0.2367 0.2291 0.0365 0.0050 0.1230 88 ILE A CB 533 C CG1 . ILE A 73 ? 0.2305 0.1475 0.1571 -0.0171 -0.0332 -0.0517 88 ILE A CG1 534 C CG2 . ILE A 73 ? 0.2327 0.2073 0.1919 -0.0354 -0.0461 0.0957 88 ILE A CG2 535 C CD1 . ILE A 73 ? 0.2023 0.4489 0.1901 0.0234 -0.0643 0.0134 88 ILE A CD1 536 N N . VAL A 74 ? 0.2096 0.1862 0.1503 0.0013 -0.0212 0.0413 89 VAL A N 537 C CA . VAL A 74 ? 0.2280 0.1859 0.1958 0.0071 -0.0359 0.0035 89 VAL A CA 538 C C . VAL A 74 ? 0.2200 0.1013 0.1521 0.0150 -0.0064 0.0480 89 VAL A C 539 O O . VAL A 74 ? 0.1755 0.1846 0.1897 0.0076 0.0116 -0.0009 89 VAL A O 540 C CB . VAL A 74 ? 0.2732 0.1167 0.1619 0.0272 0.0552 0.0252 89 VAL A CB 541 C CG1 . VAL A 74 ? 0.2617 0.2265 0.1509 -0.0332 0.0198 0.0543 89 VAL A CG1 542 C CG2 . VAL A 74 ? 0.1450 0.2673 0.2177 0.0006 0.0263 0.0276 89 VAL A CG2 543 N N . ALA A 75 ? 0.2166 0.1447 0.1645 -0.0158 0.0643 0.0299 90 ALA A N 544 C CA . ALA A 75 ? 0.1484 0.2033 0.1633 -0.0400 0.0659 0.0267 90 ALA A CA 545 C C . ALA A 75 ? 0.1261 0.1240 0.2048 0.0236 0.0512 0.0703 90 ALA A C 546 O O . ALA A 75 ? 0.2075 0.2287 0.1734 0.0888 -0.0155 0.0526 90 ALA A O 547 C CB . ALA A 75 ? 0.2435 0.1824 0.0953 -0.0375 0.0120 -0.0294 90 ALA A CB 548 N N . ASN A 76 ? 0.1239 0.2457 0.1806 -0.0476 0.0142 0.0317 91 ASN A N 549 C CA . ASN A 76 ? 0.1398 0.1166 0.2414 0.0453 -0.0044 -0.0162 91 ASN A CA 550 C C . ASN A 76 ? 0.2364 0.2210 0.1304 0.1110 0.0090 0.0250 91 ASN A C 551 O O . ASN A 76 ? 0.2306 0.2417 0.2770 0.1041 -0.0090 -0.0169 91 ASN A O 552 C CB . ASN A 76 ? 0.1943 0.0938 0.2114 0.0448 -0.0118 0.0289 91 ASN A CB 553 C CG . ASN A 76 ? 0.2879 0.2719 0.3122 0.0341 0.1373 0.0578 91 ASN A CG 554 O OD1 . ASN A 76 ? 0.2156 0.2724 0.2005 0.0194 0.0530 0.0472 91 ASN A OD1 555 N ND2 . ASN A 76 ? 0.2794 0.4311 0.3126 0.0010 0.0594 0.1646 91 ASN A ND2 556 N N . SER A 77 ? 0.2234 0.1309 0.1826 0.0201 -0.0015 -0.0128 92 SER A N 557 C CA . SER A 77 ? 0.2663 0.2751 0.1672 0.0113 0.0317 0.0379 92 SER A CA 558 C C . SER A 77 ? 0.1853 0.1602 0.1696 0.0167 -0.0458 0.0703 92 SER A C 559 O O . SER A 77 ? 0.1630 0.2614 0.2048 0.0159 -0.0082 0.0380 92 SER A O 560 C CB . SER A 77 ? 0.2657 0.2949 0.2564 -0.0061 -0.0095 0.0829 92 SER A CB 561 O OG . SER A 77 ? 0.3424 0.2409 0.2635 0.0218 0.0141 0.0296 92 SER A OG 562 N N . MET A 78 ? 0.2586 0.1363 0.1883 0.0302 0.0166 0.0468 93 MET A N 563 C CA . MET A 78 ? 0.2337 0.1719 0.2071 -0.0015 0.0553 -0.0283 93 MET A CA 564 C C . MET A 78 ? 0.2625 0.3344 0.1407 0.0509 0.0704 0.0038 93 MET A C 565 O O . MET A 78 ? 0.2373 0.1788 0.2271 0.0494 0.0763 0.0377 93 MET A O 566 C CB . MET A 78 ? 0.2473 0.2299 0.1618 0.0180 0.0583 -0.0213 93 MET A CB 567 C CG . MET A 78 ? 0.2305 0.1836 0.1579 0.0853 0.0358 0.0146 93 MET A CG 568 S SD . MET A 78 ? 0.2089 0.2195 0.1904 0.0174 0.0108 0.0261 93 MET A SD 569 C CE . MET A 78 ? 0.1405 0.3352 0.1871 0.0514 0.0031 0.0260 93 MET A CE 570 N N . TYR A 79 ? 0.2598 0.2625 0.2379 0.0424 -0.0469 0.0538 94 TYR A N 571 C CA . TYR A 79 ? 0.3190 0.1681 0.2484 0.0033 -0.0168 0.1013 94 TYR A CA 572 C C . TYR A 79 ? 0.2465 0.1014 0.2372 0.0435 0.0151 0.0336 94 TYR A C 573 O O . TYR A 79 ? 0.1751 0.2763 0.2468 0.0407 0.0068 0.0497 94 TYR A O 574 C CB . TYR A 79 ? 0.3043 0.1060 0.2836 0.0474 -0.0132 0.0044 94 TYR A CB 575 C CG . TYR A 79 ? 0.3870 0.2245 0.2342 0.1233 0.0486 0.0079 94 TYR A CG 576 C CD1 . TYR A 79 ? 0.3533 0.2158 0.2301 0.0618 0.0237 0.1030 94 TYR A CD1 577 C CD2 . TYR A 79 ? 0.2974 0.1679 0.2667 0.1057 0.0076 0.0297 94 TYR A CD2 578 C CE1 . TYR A 79 ? 0.3518 0.1424 0.3557 0.0802 0.0191 -0.0280 94 TYR A CE1 579 C CE2 . TYR A 79 ? 0.3907 0.2586 0.2496 0.1668 0.0267 -0.0057 94 TYR A CE2 580 C CZ . TYR A 79 ? 0.4223 0.3123 0.2590 0.1157 0.0472 -0.0992 94 TYR A CZ 581 O OH . TYR A 79 ? 0.4730 0.2664 0.2829 0.1031 0.0290 -0.0105 94 TYR A OH 582 N N . ASP A 80 ? 0.3655 0.1261 0.2401 0.0103 0.0479 0.0130 95 ASP A N 583 C CA . ASP A 80 ? 0.3191 0.1574 0.2937 0.0436 -0.0720 0.0292 95 ASP A CA 584 C C . ASP A 80 ? 0.3376 0.1141 0.2082 0.0430 -0.0197 0.0173 95 ASP A C 585 O O . ASP A 80 ? 0.3895 0.1570 0.3543 0.0734 0.0019 0.0636 95 ASP A O 586 C CB . ASP A 80 ? 0.3645 0.1640 0.2621 -0.0209 -0.0662 0.0765 95 ASP A CB 587 C CG . ASP A 80 ? 0.4340 0.2469 0.3566 0.0222 0.0697 0.1439 95 ASP A CG 588 O OD1 . ASP A 80 ? 0.4846 0.1979 0.4055 -0.0506 0.0076 -0.0310 95 ASP A OD1 589 O OD2 . ASP A 80 ? 0.4532 0.1504 0.3666 0.0266 0.0080 0.0649 95 ASP A OD2 590 N N . ALA A 81 ? 0.2923 0.1798 0.3144 -0.0224 -0.0336 -0.0107 96 ALA A N 591 C CA . ALA A 81 ? 0.3307 0.1657 0.3882 -0.0234 -0.0627 0.0925 96 ALA A CA 592 C C . ALA A 81 ? 0.3472 0.3105 0.3983 -0.1017 -0.0139 0.0539 96 ALA A C 593 O O . ALA A 81 ? 0.4894 0.3170 0.3903 0.0309 0.0392 0.0915 96 ALA A O 594 C CB . ALA A 81 ? 0.3929 0.4142 0.4897 -0.0098 -0.0473 0.0554 96 ALA A CB 595 N N . VAL A 82 ? 0.4525 0.1979 0.3498 -0.0465 0.0285 0.0636 97 VAL A N 596 C CA . VAL A 82 ? 0.4399 0.1419 0.2378 -0.0360 0.0340 -0.0091 97 VAL A CA 597 C C . VAL A 82 ? 0.4290 0.1510 0.3441 0.0497 -0.0939 -0.0353 97 VAL A C 598 O O . VAL A 82 ? 0.4962 0.1665 0.5214 0.0307 0.0295 0.0363 97 VAL A O 599 C CB . VAL A 82 ? 0.4421 0.3009 0.3019 -0.0780 -0.0284 0.0770 97 VAL A CB 600 C CG1 . VAL A 82 ? 0.4790 0.1679 0.4615 -0.0355 -0.0057 0.0887 97 VAL A CG1 601 C CG2 . VAL A 82 ? 0.4976 0.3142 0.4306 -0.0375 -0.0497 -0.0136 97 VAL A CG2 602 N N . THR A 83 ? 0.4930 0.2222 0.3044 -0.1144 -0.0218 0.0451 98 THR A N 603 C CA . THR A 83 ? 0.4078 0.2059 0.3563 0.0304 0.0172 0.0334 98 THR A CA 604 C C . THR A 83 ? 0.4073 0.1662 0.3349 0.0476 0.0482 -0.0738 98 THR A C 605 O O . THR A 83 ? 0.3894 0.1827 0.4064 0.0299 0.0031 0.0369 98 THR A O 606 C CB . THR A 83 ? 0.4428 0.2741 0.3530 0.0893 0.0026 -0.0363 98 THR A CB 607 O OG1 . THR A 83 ? 0.4845 0.1928 0.3245 0.0455 -0.0530 -0.0075 98 THR A OG1 608 C CG2 . THR A 83 ? 0.4438 0.3447 0.3052 -0.0012 -0.1168 0.0610 98 THR A CG2 609 N N . LYS A 84 ? 0.3828 0.2604 0.3566 0.0913 0.0089 0.0218 99 LYS A N 610 C CA . LYS A 84 ? 0.3275 0.1602 0.3619 0.0628 0.0217 -0.0166 99 LYS A CA 611 C C . LYS A 84 ? 0.3265 0.2436 0.3285 0.0430 -0.0254 0.0670 99 LYS A C 612 O O . LYS A 84 ? 0.3527 0.2828 0.3115 -0.0102 0.0469 0.0368 99 LYS A O 613 C CB . LYS A 84 ? 0.3940 0.3218 0.3518 -0.0392 -0.0096 -0.0218 99 LYS A CB 614 C CG . LYS A 84 ? 0.4024 0.3734 0.3893 0.0353 0.0995 -0.1170 99 LYS A CG 615 C CD . LYS A 84 ? 0.4644 0.4790 0.4967 0.0018 0.1307 -0.1992 99 LYS A CD 616 C CE . LYS A 84 ? 0.5187 0.6375 0.7093 -0.0316 0.1067 -0.1343 99 LYS A CE 617 N NZ . LYS A 84 ? 0.5754 0.7426 0.7638 -0.0735 0.0997 -0.0626 99 LYS A NZ 618 N N . LYS A 85 ? 0.2507 0.1744 0.3168 0.0852 -0.0211 -0.0072 100 LYS A N 619 C CA . LYS A 85 ? 0.2624 0.2343 0.2727 0.0275 -0.0067 -0.0286 100 LYS A CA 620 C C . LYS A 85 ? 0.2818 0.2581 0.2707 0.0973 -0.0201 0.0551 100 LYS A C 621 O O . LYS A 85 ? 0.2878 0.2190 0.2730 0.0683 0.0070 0.0304 100 LYS A O 622 C CB . LYS A 85 ? 0.3870 0.1976 0.2287 0.0593 -0.0320 0.0249 100 LYS A CB 623 C CG . LYS A 85 ? 0.3744 0.3867 0.2529 0.1244 -0.0429 0.0681 100 LYS A CG 624 C CD . LYS A 85 ? 0.3473 0.2662 0.3660 0.0998 -0.0735 0.0648 100 LYS A CD 625 C CE . LYS A 85 ? 0.3839 0.2929 0.4336 0.0781 -0.0954 0.0007 100 LYS A CE 626 N NZ . LYS A 85 ? 0.2704 0.3649 0.5501 0.0810 -0.1087 -0.0717 100 LYS A NZ 627 N N . HIS A 86 ? 0.3410 0.1429 0.2762 0.0274 0.0234 0.0209 101 HIS A N 628 C CA . HIS A 86 ? 0.2595 0.1520 0.2789 0.0348 0.0319 0.0914 101 HIS A CA 629 C C . HIS A 86 ? 0.2896 0.4455 0.2362 0.0733 0.0834 -0.0389 101 HIS A C 630 O O . HIS A 86 ? 0.2596 0.1729 0.3806 0.0225 -0.0437 -0.0008 101 HIS A O 631 C CB . HIS A 86 ? 0.3459 0.4380 0.2848 -0.0529 0.0886 0.1361 101 HIS A CB 632 C CG . HIS A 86 ? 0.3577 0.2618 0.3188 0.0120 0.0254 0.0956 101 HIS A CG 633 N ND1 . HIS A 86 ? 0.4461 0.3257 0.3350 0.0580 0.1214 0.0709 101 HIS A ND1 634 C CD2 . HIS A 86 ? 0.4092 0.4409 0.3684 0.0173 0.0078 -0.1041 101 HIS A CD2 635 C CE1 . HIS A 86 ? 0.4124 0.2193 0.3695 -0.0006 0.1032 -0.1128 101 HIS A CE1 636 N NE2 . HIS A 86 ? 0.3701 0.4101 0.4278 0.0585 0.0809 -0.0573 101 HIS A NE2 637 N N . PHE A 87 ? 0.2384 0.1953 0.2400 0.0004 0.0335 -0.0139 102 PHE A N 638 C CA . PHE A 87 ? 0.3002 0.1306 0.2373 -0.0198 0.0453 0.0604 102 PHE A CA 639 C C . PHE A 87 ? 0.2224 0.2258 0.2172 -0.0098 0.0067 0.0195 102 PHE A C 640 O O . PHE A 87 ? 0.2036 0.2562 0.2374 0.0307 -0.0122 0.0247 102 PHE A O 641 C CB . PHE A 87 ? 0.2564 0.2682 0.2691 -0.0417 0.0121 0.0694 102 PHE A CB 642 C CG . PHE A 87 ? 0.2640 0.2173 0.2776 0.0100 0.0628 0.0533 102 PHE A CG 643 C CD1 . PHE A 87 ? 0.2487 0.1407 0.3454 0.0090 -0.0337 -0.0322 102 PHE A CD1 644 C CD2 . PHE A 87 ? 0.2270 0.1672 0.2591 -0.0515 -0.0302 -0.0203 102 PHE A CD2 645 C CE1 . PHE A 87 ? 0.2406 0.2873 0.2755 0.0122 0.0016 0.1561 102 PHE A CE1 646 C CE2 . PHE A 87 ? 0.1978 0.2671 0.2908 -0.0538 -0.0334 -0.0691 102 PHE A CE2 647 C CZ . PHE A 87 ? 0.2266 0.3003 0.1920 -0.0280 -0.0546 0.0063 102 PHE A CZ 648 N N . SER A 88 ? 0.2171 0.2956 0.2830 0.0546 0.0791 0.0004 103 SER A N 649 C CA . SER A 88 ? 0.2823 0.1018 0.2898 0.0075 0.0584 -0.0011 103 SER A CA 650 C C . SER A 88 ? 0.3394 0.3868 0.4122 -0.0524 0.0940 0.0645 103 SER A C 651 O O . SER A 88 ? 0.2743 0.2342 0.3410 -0.0082 0.0340 -0.0569 103 SER A O 652 C CB . SER A 88 ? 0.3193 0.3007 0.2743 0.0297 0.1620 0.0316 103 SER A CB 653 O OG . SER A 88 ? 0.2852 0.3454 0.4694 0.0589 0.1481 0.0980 103 SER A OG 654 N N . ASP A 89 ? 0.3708 0.3742 0.3784 -0.0122 0.1001 0.0566 104 ASP A N 655 C CA . ASP A 89 ? 0.3771 0.4531 0.5840 -0.0180 -0.0149 0.1273 104 ASP A CA 656 C C . ASP A 89 ? 0.3747 0.3732 0.5597 -0.0476 0.0286 0.0455 104 ASP A C 657 O O . ASP A 89 ? 0.3830 0.5736 0.6766 0.0922 0.0722 -0.2161 104 ASP A O 658 C CB . ASP A 89 ? 0.4374 0.3119 0.6552 0.0751 -0.0483 0.0372 104 ASP A CB 659 C CG . ASP A 89 ? 0.4959 0.4547 0.6583 0.0861 -0.0354 0.0671 104 ASP A CG 660 O OD1 . ASP A 89 ? 0.5585 0.6032 0.7889 -0.0255 0.0347 0.0202 104 ASP A OD1 661 O OD2 . ASP A 89 ? 0.6660 0.7662 0.8272 -0.1021 -0.0269 -0.0744 104 ASP A OD2 662 N N . SER A 90 ? 0.4045 0.2882 0.5105 0.0433 0.0906 0.1048 105 SER A N 663 C CA . SER A 90 ? 0.3628 0.4444 0.5881 -0.0073 0.0908 0.1507 105 SER A CA 664 C C . SER A 90 ? 0.4153 0.5241 0.5854 0.0197 0.0811 0.0286 105 SER A C 665 O O . SER A 90 ? 0.4658 0.5665 0.7573 -0.0775 0.2042 -0.1512 105 SER A O 666 C CB . SER A 90 ? 0.4594 0.5165 0.4761 -0.0990 0.0917 -0.0072 105 SER A CB 667 O OG . SER A 90 ? 0.4957 0.5105 0.7221 -0.0104 0.0667 0.0651 105 SER A OG 668 N N . ASN A 91 ? 0.2643 0.3209 0.4515 -0.0139 0.0198 0.0778 106 ASN A N 669 C CA . ASN A 91 ? 0.3251 0.3372 0.3376 -0.0120 0.1210 0.0541 106 ASN A CA 670 C C . ASN A 91 ? 0.2413 0.4049 0.2345 -0.0848 0.0920 -0.0023 106 ASN A C 671 O O . ASN A 91 ? 0.2007 0.2935 0.3142 0.0124 0.0166 0.0131 106 ASN A O 672 C CB . ASN A 91 ? 0.3002 0.3317 0.3555 0.0033 0.0812 -0.0970 106 ASN A CB 673 C CG . ASN A 91 ? 0.3459 0.4749 0.4277 0.0700 0.0913 -0.0234 106 ASN A CG 674 O OD1 . ASN A 91 ? 0.4161 0.5807 0.4071 0.2042 -0.0487 -0.0029 106 ASN A OD1 675 N ND2 . ASN A 91 ? 0.3886 0.5154 0.4372 0.0142 0.1408 -0.0526 106 ASN A ND2 676 N N . ASP A 92 ? 0.2245 0.3509 0.2520 0.0552 0.0680 0.0164 107 ASP A N 677 C CA . ASP A 92 ? 0.2147 0.4793 0.2860 -0.0109 0.0343 0.0067 107 ASP A CA 678 C C . ASP A 92 ? 0.2473 0.3987 0.3432 0.1004 -0.0434 -0.0409 107 ASP A C 679 O O . ASP A 92 ? 0.2944 0.4570 0.3186 -0.0598 0.0624 -0.0364 107 ASP A O 680 C CB . ASP A 92 ? 0.1752 0.4012 0.3952 -0.0866 -0.0319 0.0209 107 ASP A CB 681 C CG . ASP A 92 ? 0.1771 0.4130 0.4118 0.0896 0.0623 -0.0023 107 ASP A CG 682 O OD1 . ASP A 92 ? 0.1945 0.3845 0.4661 0.0165 0.0123 -0.0536 107 ASP A OD1 683 O OD2 . ASP A 92 ? 0.2050 0.5950 0.4343 0.0391 0.0026 -0.0829 107 ASP A OD2 684 N N . LYS A 93 ? 0.1897 0.3698 0.3763 0.0109 -0.0169 0.0917 108 LYS A N 685 C CA . LYS A 93 ? 0.1917 0.3682 0.3735 -0.0225 -0.0149 0.0281 108 LYS A CA 686 C C . LYS A 93 ? 0.2013 0.4105 0.4085 -0.0756 0.0110 0.0368 108 LYS A C 687 O O . LYS A 93 ? 0.2345 0.4486 0.4602 0.0383 -0.0132 0.0944 108 LYS A O 688 C CB . LYS A 93 ? 0.3077 0.4640 0.3465 -0.0691 -0.0690 0.1304 108 LYS A CB 689 C CG . LYS A 93 ? 0.3744 0.4206 0.4805 -0.0084 -0.0515 0.2504 108 LYS A CG 690 C CD . LYS A 93 ? 0.4932 0.5584 0.5967 -0.0045 -0.0924 0.0573 108 LYS A CD 691 C CE . LYS A 93 ? 0.5322 0.5249 0.4136 0.0113 -0.0079 0.0118 108 LYS A CE 692 N NZ . LYS A 93 ? 0.5331 0.6617 0.5970 0.0173 -0.0998 0.0647 108 LYS A NZ 693 N N . ASP A 94 ? 0.1932 0.2365 0.2730 0.0271 -0.0077 0.0174 109 ASP A N 694 C CA . ASP A 94 ? 0.2082 0.2971 0.3825 -0.0340 0.0219 0.0540 109 ASP A CA 695 C C . ASP A 94 ? 0.2024 0.3118 0.3453 -0.0284 -0.0750 0.1628 109 ASP A C 696 O O . ASP A 94 ? 0.2643 0.3308 0.3085 0.0537 -0.0702 0.1064 109 ASP A O 697 C CB . ASP A 94 ? 0.2148 0.3301 0.3452 0.0514 -0.0488 -0.0414 109 ASP A CB 698 C CG . ASP A 94 ? 0.2413 0.4469 0.4236 0.0372 0.0009 0.0431 109 ASP A CG 699 O OD1 . ASP A 94 ? 0.2574 0.3824 0.3628 0.0720 -0.0227 0.0182 109 ASP A OD1 700 O OD2 . ASP A 94 ? 0.3587 0.4114 0.3694 -0.0092 -0.0256 0.0691 109 ASP A OD2 701 N N . PRO A 95 ? 0.1937 0.3238 0.3067 0.1000 -0.0202 -0.0095 110 PRO A N 702 C CA . PRO A 95 ? 0.2371 0.3767 0.2926 0.1373 -0.0332 0.0495 110 PRO A CA 703 C C . PRO A 95 ? 0.3161 0.2699 0.3461 0.1040 0.0296 0.1168 110 PRO A C 704 O O . PRO A 95 ? 0.2743 0.3139 0.2156 0.0964 -0.0259 0.0098 110 PRO A O 705 C CB . PRO A 95 ? 0.1850 0.3734 0.3114 0.0485 -0.0711 0.0475 110 PRO A CB 706 C CG . PRO A 95 ? 0.1824 0.4722 0.3803 0.0629 0.0272 0.1641 110 PRO A CG 707 C CD . PRO A 95 ? 0.2067 0.3628 0.2813 0.0387 -0.0151 -0.0133 110 PRO A CD 708 N N . PHE A 96 ? 0.3365 0.2002 0.2537 0.0443 -0.0907 0.0130 111 PHE A N 709 C CA . PHE A 96 ? 0.2791 0.2355 0.3287 0.0179 -0.0832 0.0230 111 PHE A CA 710 C C . PHE A 96 ? 0.2529 0.2072 0.2490 -0.0004 0.0091 0.1010 111 PHE A C 711 O O . PHE A 96 ? 0.1841 0.2868 0.2674 -0.0287 -0.0258 0.0841 111 PHE A O 712 C CB . PHE A 96 ? 0.3153 0.3063 0.3610 0.1491 0.0016 0.0421 111 PHE A CB 713 C CG . PHE A 96 ? 0.4082 0.3068 0.2889 0.1071 0.0052 -0.0178 111 PHE A CG 714 C CD1 . PHE A 96 ? 0.3732 0.3820 0.2441 0.1208 -0.0252 0.0099 111 PHE A CD1 715 C CD2 . PHE A 96 ? 0.3591 0.2871 0.3261 0.0740 -0.0585 0.0003 111 PHE A CD2 716 C CE1 . PHE A 96 ? 0.3386 0.1981 0.3462 0.0772 -0.0296 0.0226 111 PHE A CE1 717 C CE2 . PHE A 96 ? 0.4412 0.2870 0.2812 -0.0271 -0.0139 0.0302 111 PHE A CE2 718 C CZ . PHE A 96 ? 0.3974 0.1944 0.3257 0.0000 -0.0373 -0.0344 111 PHE A CZ 719 N N . TRP A 97 ? 0.2736 0.2369 0.2216 0.0321 -0.0362 0.0443 112 TRP A N 720 C CA . TRP A 97 ? 0.2031 0.2815 0.2900 0.0070 -0.0132 0.1044 112 TRP A CA 721 C C . TRP A 97 ? 0.2130 0.2645 0.2618 -0.0227 0.0994 0.0379 112 TRP A C 722 O O . TRP A 97 ? 0.1653 0.3795 0.2609 0.0536 0.0202 -0.0201 112 TRP A O 723 C CB . TRP A 97 ? 0.2317 0.2434 0.2199 0.0236 -0.0489 0.0725 112 TRP A CB 724 C CG . TRP A 97 ? 0.2564 0.2374 0.1713 0.0565 -0.0304 0.0229 112 TRP A CG 725 C CD1 . TRP A 97 ? 0.3068 0.2268 0.4015 0.0730 0.1146 0.0433 112 TRP A CD1 726 C CD2 . TRP A 97 ? 0.2315 0.1517 0.2350 0.0361 -0.0386 0.0357 112 TRP A CD2 727 N NE1 . TRP A 97 ? 0.3025 0.2107 0.3069 0.1189 0.0334 0.0679 112 TRP A NE1 728 C CE2 . TRP A 97 ? 0.2600 0.2885 0.3500 0.0536 0.0120 0.1163 112 TRP A CE2 729 C CE3 . TRP A 97 ? 0.1870 0.2576 0.3152 0.0028 -0.0632 0.1006 112 TRP A CE3 730 C CZ2 . TRP A 97 ? 0.2871 0.1189 0.2834 0.0091 0.0136 0.0680 112 TRP A CZ2 731 C CZ3 . TRP A 97 ? 0.2614 0.2484 0.3612 -0.0145 -0.0231 0.1356 112 TRP A CZ3 732 C CH2 . TRP A 97 ? 0.2937 0.2476 0.2736 0.0509 -0.0004 0.1258 112 TRP A CH2 733 N N . TRP A 98 ? 0.2810 0.2870 0.1599 -0.0420 -0.0474 0.0438 113 TRP A N 734 C CA . TRP A 98 ? 0.2867 0.1717 0.1870 -0.0170 -0.0448 0.0676 113 TRP A CA 735 C C . TRP A 98 ? 0.2280 0.2924 0.2729 0.0452 -0.0975 0.0784 113 TRP A C 736 O O . TRP A 98 ? 0.2213 0.3580 0.2832 -0.0295 -0.0204 0.0876 113 TRP A O 737 C CB . TRP A 98 ? 0.1483 0.2878 0.2636 -0.0405 0.0119 0.1029 113 TRP A CB 738 C CG . TRP A 98 ? 0.1893 0.2167 0.2371 -0.0910 0.0279 0.0420 113 TRP A CG 739 C CD1 . TRP A 98 ? 0.1479 0.4472 0.2098 -0.0504 -0.0149 0.0343 113 TRP A CD1 740 C CD2 . TRP A 98 ? 0.2243 0.1814 0.3079 0.0160 -0.0079 0.0038 113 TRP A CD2 741 N NE1 . TRP A 98 ? 0.2033 0.3014 0.1952 0.0057 0.0354 0.0539 113 TRP A NE1 742 C CE2 . TRP A 98 ? 0.1587 0.2274 0.3659 0.0523 -0.0321 -0.0766 113 TRP A CE2 743 C CE3 . TRP A 98 ? 0.2174 0.1162 0.2090 -0.0071 -0.0626 0.0490 113 TRP A CE3 744 C CZ2 . TRP A 98 ? 0.2096 0.1130 0.2411 0.0636 -0.0161 -0.0159 113 TRP A CZ2 745 C CZ3 . TRP A 98 ? 0.1558 0.1770 0.1782 -0.0024 -0.0021 0.0434 113 TRP A CZ3 746 C CH2 . TRP A 98 ? 0.1462 0.3130 0.1940 0.0141 -0.0157 0.0493 113 TRP A CH2 747 N N . ASN A 99 ? 0.2723 0.2253 0.2639 -0.0063 0.0110 0.0695 114 ASN A N 748 C CA . ASN A 99 ? 0.2831 0.2023 0.2295 0.0027 -0.0138 0.1151 114 ASN A CA 749 C C . ASN A 99 ? 0.2563 0.2652 0.2618 0.0077 -0.0234 0.1040 114 ASN A C 750 O O . ASN A 99 ? 0.2776 0.4818 0.3715 0.0501 -0.0422 0.1952 114 ASN A O 751 C CB . ASN A 99 ? 0.2451 0.2799 0.2674 0.0284 -0.0585 0.1273 114 ASN A CB 752 C CG . ASN A 99 ? 0.2327 0.2749 0.2190 0.0551 -0.0898 0.0576 114 ASN A CG 753 O OD1 . ASN A 99 ? 0.2876 0.4031 0.2682 0.0093 -0.0670 -0.0186 114 ASN A OD1 754 N ND2 . ASN A 99 ? 0.3337 0.4895 0.3567 0.1616 0.0528 0.1912 114 ASN A ND2 755 N N . GLU A 100 ? 0.2136 0.2301 0.3211 0.0305 -0.0007 0.0995 115 GLU A N 756 C CA . GLU A 100 ? 0.2264 0.2261 0.2169 -0.0281 -0.0565 0.0422 115 GLU A CA 757 C C . GLU A 100 ? 0.2686 0.1655 0.2980 -0.0370 -0.0612 0.0463 115 GLU A C 758 O O . GLU A 100 ? 0.2608 0.2941 0.4032 -0.0451 0.0224 -0.0050 115 GLU A O 759 C CB . GLU A 100 ? 0.2523 0.1767 0.2775 -0.0104 -0.0905 0.0181 115 GLU A CB 760 C CG . GLU A 100 ? 0.3523 0.1881 0.2821 0.0803 -0.0281 0.0796 115 GLU A CG 761 C CD . GLU A 100 ? 0.3404 0.3418 0.3170 0.0123 0.1127 0.0855 115 GLU A CD 762 O OE1 . GLU A 100 ? 0.3258 0.4483 0.2629 0.0768 -0.0088 0.0579 115 GLU A OE1 763 O OE2 . GLU A 100 ? 0.3081 0.2929 0.2927 0.0200 -0.0345 -0.0396 115 GLU A OE2 764 N N . ALA A 101 ? 0.2128 0.2466 0.2217 0.0344 -0.0343 0.0522 116 ALA A N 765 C CA . ALA A 101 ? 0.2345 0.2780 0.1729 -0.0483 -0.0750 0.0838 116 ALA A CA 766 C C . ALA A 101 ? 0.2252 0.3314 0.1676 0.0586 -0.0579 0.0477 116 ALA A C 767 O O . ALA A 101 ? 0.2204 0.2878 0.3370 0.0316 -0.0594 0.0621 116 ALA A O 768 C CB . ALA A 101 ? 0.2229 0.3254 0.1749 -0.0023 -0.0697 0.0776 116 ALA A CB 769 N N . VAL A 102 ? 0.2409 0.2976 0.1542 -0.0150 -0.0381 0.0605 117 VAL A N 770 C CA . VAL A 102 ? 0.2219 0.1986 0.1703 0.0262 -0.0429 0.0827 117 VAL A CA 771 C C . VAL A 102 ? 0.2149 0.2407 0.2104 0.0620 -0.0850 0.0263 117 VAL A C 772 O O . VAL A 102 ? 0.2130 0.3222 0.2210 -0.0122 -0.0279 0.0647 117 VAL A O 773 C CB . VAL A 102 ? 0.2110 0.2587 0.2496 -0.0207 -0.0645 0.1263 117 VAL A CB 774 C CG1 . VAL A 102 ? 0.2577 0.3886 0.2295 -0.0083 -0.0947 0.0986 117 VAL A CG1 775 C CG2 . VAL A 102 ? 0.2893 0.3613 0.3174 -0.0277 -0.0484 0.1801 117 VAL A CG2 776 N N . PRO A 103 ? 0.2414 0.2620 0.1815 -0.0480 -0.0359 0.1077 118 PRO A N 777 C CA . PRO A 103 ? 0.2114 0.2831 0.2051 -0.0628 -0.0777 0.1069 118 PRO A CA 778 C C . PRO A 103 ? 0.2350 0.2138 0.1964 0.0059 -0.0659 0.0890 118 PRO A C 779 O O . PRO A 103 ? 0.2398 0.3329 0.1992 -0.0324 -0.0602 0.0568 118 PRO A O 780 C CB . PRO A 103 ? 0.2000 0.3864 0.1660 -0.0035 -0.0560 0.0604 118 PRO A CB 781 C CG . PRO A 103 ? 0.1645 0.3898 0.2895 0.0203 -0.0406 0.1238 118 PRO A CG 782 C CD . PRO A 103 ? 0.2147 0.3019 0.2196 -0.0417 0.0723 0.0816 118 PRO A CD 783 N N . ILE A 104 ? 0.1854 0.3729 0.2604 -0.0848 -0.0780 0.0219 119 ILE A N 784 C CA . ILE A 104 ? 0.1932 0.4243 0.2419 -0.0206 -0.0676 -0.0854 119 ILE A CA 785 C C . ILE A 104 ? 0.1519 0.2678 0.2472 -0.0655 -0.0664 0.0425 119 ILE A C 786 O O . ILE A 104 ? 0.1976 0.4370 0.1950 -0.0256 -0.0651 0.0574 119 ILE A O 787 C CB . ILE A 104 ? 0.1748 0.3275 0.1788 -0.0731 0.0470 -0.0033 119 ILE A CB 788 C CG1 . ILE A 104 ? 0.1959 0.3266 0.2228 -0.0072 -0.0200 -0.0750 119 ILE A CG1 789 C CG2 . ILE A 104 ? 0.1462 0.3084 0.2140 -0.0603 0.0133 0.0187 119 ILE A CG2 790 C CD1 . ILE A 104 ? 0.2451 0.3692 0.1766 -0.0253 -0.0268 0.0242 119 ILE A CD1 791 N N . TRP A 105 ? 0.1203 0.2784 0.2436 -0.0596 0.0050 0.0381 120 TRP A N 792 C CA . TRP A 105 ? 0.1483 0.3896 0.1545 -0.0170 -0.0291 0.0659 120 TRP A CA 793 C C . TRP A 105 ? 0.1949 0.4454 0.3103 -0.1218 -0.0362 0.0249 120 TRP A C 794 O O . TRP A 105 ? 0.2104 0.4166 0.2474 -0.0929 -0.0473 0.1429 120 TRP A O 795 C CB . TRP A 105 ? 0.1692 0.3972 0.1699 -0.0766 -0.0305 0.0813 120 TRP A CB 796 C CG . TRP A 105 ? 0.1781 0.2822 0.2434 -0.0406 -0.0508 0.0119 120 TRP A CG 797 C CD1 . TRP A 105 ? 0.2374 0.4413 0.2018 -0.0353 0.0283 0.1165 120 TRP A CD1 798 C CD2 . TRP A 105 ? 0.1620 0.4385 0.2184 -0.0272 -0.0531 0.0586 120 TRP A CD2 799 N NE1 . TRP A 105 ? 0.1865 0.4651 0.2036 0.0236 -0.0394 0.0843 120 TRP A NE1 800 C CE2 . TRP A 105 ? 0.1684 0.2360 0.1605 0.0130 -0.0593 -0.0032 120 TRP A CE2 801 C CE3 . TRP A 105 ? 0.1519 0.2987 0.2123 -0.0604 -0.0638 0.0710 120 TRP A CE3 802 C CZ2 . TRP A 105 ? 0.1494 0.4391 0.1978 -0.0252 -0.0375 0.0551 120 TRP A CZ2 803 C CZ3 . TRP A 105 ? 0.1509 0.3567 0.1813 -0.0611 -0.0338 0.0472 120 TRP A CZ3 804 C CH2 . TRP A 105 ? 0.1829 0.2229 0.2226 -0.0307 -0.0046 0.0253 120 TRP A CH2 805 N N . VAL A 106 ? 0.1904 0.3375 0.2267 -0.0275 -0.0454 0.0985 121 VAL A N 806 C CA . VAL A 106 ? 0.2145 0.4903 0.2977 -0.0574 -0.0166 0.1862 121 VAL A CA 807 C C . VAL A 106 ? 0.2137 0.2417 0.3336 -0.0908 -0.0339 0.0956 121 VAL A C 808 O O . VAL A 106 ? 0.2937 0.4080 0.2729 -0.0370 -0.0652 0.1225 121 VAL A O 809 C CB . VAL A 106 ? 0.2685 0.2538 0.1967 0.0064 -0.0079 0.1182 121 VAL A CB 810 C CG1 . VAL A 106 ? 0.2298 0.4095 0.3537 -0.0091 -0.0975 0.1512 121 VAL A CG1 811 C CG2 . VAL A 106 ? 0.1951 0.5281 0.3219 0.0495 -0.0665 0.0546 121 VAL A CG2 812 N N . THR A 107 ? 0.2223 0.4806 0.2490 -0.0903 -0.0662 0.0794 122 THR A N 813 C CA . THR A 107 ? 0.2961 0.4066 0.2270 0.0212 -0.0061 0.0368 122 THR A CA 814 C C . THR A 107 ? 0.2487 0.3203 0.2898 -0.0245 -0.0449 0.1660 122 THR A C 815 O O . THR A 107 ? 0.2853 0.3775 0.2422 -0.0260 -0.0805 0.0847 122 THR A O 816 C CB . THR A 107 ? 0.2146 0.4498 0.1931 -0.0906 -0.0297 0.1157 122 THR A CB 817 O OG1 . THR A 107 ? 0.2721 0.4562 0.2056 -0.1000 -0.0632 0.0513 122 THR A OG1 818 C CG2 . THR A 107 ? 0.2337 0.4862 0.2216 -0.0968 0.0233 0.0935 122 THR A CG2 819 N N . ASN A 108 ? 0.2920 0.3813 0.2471 -0.1346 -0.0673 0.1390 123 ASN A N 820 C CA . ASN A 108 ? 0.2593 0.3176 0.2644 -0.0325 -0.0614 0.0707 123 ASN A CA 821 C C . ASN A 108 ? 0.2334 0.3475 0.2100 0.0043 -0.0812 0.0835 123 ASN A C 822 O O . ASN A 108 ? 0.3127 0.4460 0.2437 -0.0711 -0.0984 0.1293 123 ASN A O 823 C CB . ASN A 108 ? 0.2778 0.4311 0.2442 -0.0651 -0.0510 0.0335 123 ASN A CB 824 C CG . ASN A 108 ? 0.2426 0.4375 0.3218 -0.0363 -0.0357 -0.0435 123 ASN A CG 825 O OD1 . ASN A 108 ? 0.3171 0.5818 0.2613 -0.1378 -0.0946 0.1262 123 ASN A OD1 826 N ND2 . ASN A 108 ? 0.2309 0.5184 0.2208 -0.0931 -0.0648 0.0320 123 ASN A ND2 827 N N . GLN A 109 ? 0.2282 0.4824 0.2462 0.0027 -0.0290 0.0667 124 GLN A N 828 C CA . GLN A 109 ? 0.1884 0.3427 0.2616 0.0042 -0.0306 0.1153 124 GLN A CA 829 C C . GLN A 109 ? 0.2906 0.3731 0.3214 0.0202 -0.1223 0.1226 124 GLN A C 830 O O . GLN A 109 ? 0.3567 0.5297 0.3227 0.0160 -0.1155 0.1590 124 GLN A O 831 C CB . GLN A 109 ? 0.2256 0.5727 0.2758 -0.0120 -0.0352 0.0701 124 GLN A CB 832 C CG . GLN A 109 ? 0.2888 0.4594 0.3521 -0.0275 -0.1132 0.1351 124 GLN A CG 833 C CD . GLN A 109 ? 0.2670 0.4589 0.4140 0.0539 -0.1387 0.0958 124 GLN A CD 834 O OE1 . GLN A 109 ? 0.2678 0.5653 0.2985 -0.1129 -0.1031 0.0881 124 GLN A OE1 835 N NE2 . GLN A 109 ? 0.2750 0.5953 0.4455 0.0055 -0.1402 -0.0333 124 GLN A NE2 836 N N . LEU A 110 ? 0.3094 0.3823 0.4125 -0.1036 -0.1691 0.1618 125 LEU A N 837 C CA . LEU A 110 ? 0.3623 0.5151 0.3845 -0.0308 -0.1091 0.1449 125 LEU A CA 838 C C . LEU A 110 ? 0.3124 0.3184 0.3694 0.0548 -0.0666 0.0210 125 LEU A C 839 O O . LEU A 110 ? 0.4321 0.6347 0.4121 -0.0249 -0.1091 0.2115 125 LEU A O 840 C CB . LEU A 110 ? 0.4072 0.3352 0.3863 -0.0363 -0.0275 0.0475 125 LEU A CB 841 C CG . LEU A 110 ? 0.5132 0.5428 0.4847 -0.0031 -0.0085 0.2778 125 LEU A CG 842 C CD1 . LEU A 110 ? 0.4687 0.5994 0.6548 0.0370 -0.1430 0.0255 125 LEU A CD1 843 C CD2 . LEU A 110 ? 0.5799 0.6692 0.7539 -0.0080 0.0761 0.0360 125 LEU A CD2 844 N N . GLN A 111 ? 0.3016 0.4595 0.3405 -0.0398 -0.1572 0.0342 126 GLN A N 845 C CA . GLN A 111 ? 0.4308 0.4768 0.2581 -0.0599 -0.0696 -0.0106 126 GLN A CA 846 C C . GLN A 111 ? 0.4558 0.5613 0.3090 -0.0712 -0.1190 0.1789 126 GLN A C 847 O O . GLN A 111 ? 0.4098 0.5758 0.3000 -0.1659 -0.1262 0.0654 126 GLN A O 848 C CB . GLN A 111 ? 0.4297 0.5688 0.2494 -0.0622 -0.1362 0.0604 126 GLN A CB 849 C CG . GLN A 111 ? 0.4371 0.5243 0.3034 -0.0825 -0.0979 0.1612 126 GLN A CG 850 C CD . GLN A 111 ? 0.5303 0.6286 0.5932 -0.0161 0.0114 0.0484 126 GLN A CD 851 O OE1 . GLN A 111 ? 0.5600 0.7491 0.5498 -0.0725 -0.0715 0.1494 126 GLN A OE1 852 N NE2 . GLN A 111 ? 0.4984 0.4463 0.5605 -0.0680 0.0421 -0.0323 126 GLN A NE2 853 N N . GLU A 112 ? 0.5255 0.4822 0.3724 -0.0313 -0.1992 0.1292 127 GLU A N 854 C CA . GLU A 112 ? 0.5380 0.4878 0.3467 -0.0036 -0.2269 0.0530 127 GLU A CA 855 C C . GLU A 112 ? 0.5553 0.5901 0.3401 -0.0070 -0.1971 0.1255 127 GLU A C 856 O O . GLU A 112 ? 0.5738 0.6968 0.2950 -0.1025 -0.1373 0.1364 127 GLU A O 857 C CB . GLU A 112 ? 0.6721 0.5749 0.5723 -0.0370 -0.0870 0.0285 127 GLU A CB 858 C CG . GLU A 112 ? 0.7353 0.8293 0.7386 0.0029 -0.0577 0.0226 127 GLU A CG 859 C CD . GLU A 112 ? 0.7567 0.9078 0.9268 0.0421 0.0120 0.0133 127 GLU A CD 860 O OE1 . GLU A 112 ? 0.7598 0.9149 0.9408 0.0535 0.0006 0.0178 127 GLU A OE1 861 O OE2 . GLU A 112 ? 0.7531 0.9797 1.0110 0.0250 0.0809 -0.0263 127 GLU A OE2 862 N N . ASN A 113 ? 0.4975 0.6017 0.3961 -0.1381 -0.1954 0.1199 128 ASN A N 863 C CA . ASN A 113 ? 0.5714 0.4446 0.5321 0.0256 -0.1099 -0.0265 128 ASN A CA 864 C C . ASN A 113 ? 0.5176 0.4102 0.3164 -0.0479 -0.1177 -0.0267 128 ASN A C 865 O O . ASN A 113 ? 0.4168 0.6226 0.2493 -0.1052 -0.1198 0.0451 128 ASN A O 866 C CB . ASN A 113 ? 0.6250 0.6214 0.4846 0.0677 -0.0560 0.1138 128 ASN A CB 867 C CG . ASN A 113 ? 0.6625 0.7926 0.7759 -0.0069 0.0003 -0.0606 128 ASN A CG 868 O OD1 . ASN A 113 ? 0.6575 0.8808 0.8419 -0.0719 -0.0586 -0.0428 128 ASN A OD1 869 N ND2 . ASN A 113 ? 0.6909 0.8526 0.8362 -0.0648 -0.0714 0.0313 128 ASN A ND2 870 N N . ARG A 114 ? 0.4523 0.6260 0.3714 -0.0257 -0.0777 0.1519 129 ARG A N 871 C CA . ARG A 114 ? 0.3702 0.5830 0.3063 0.0203 0.0377 0.2080 129 ARG A CA 872 C C . ARG A 114 ? 0.2389 0.4022 0.3513 0.0064 0.0145 0.1193 129 ARG A C 873 O O . ARG A 114 ? 0.4052 0.5530 0.3763 -0.0293 -0.0935 0.1357 129 ARG A O 874 C CB . ARG A 114 ? 0.3557 0.5906 0.3055 0.0015 0.0176 0.0426 129 ARG A CB 875 C CG . ARG A 114 ? 0.4138 0.6810 0.5859 0.0129 -0.0042 0.0373 129 ARG A CG 876 C CD . ARG A 114 ? 0.5928 0.7928 0.7449 -0.0491 0.1197 0.0400 129 ARG A CD 877 N NE . ARG A 114 ? 0.6778 0.8569 0.8702 -0.0017 0.0816 -0.0159 129 ARG A NE 878 C CZ . ARG A 114 ? 0.7101 0.8648 0.8343 -0.0148 0.0750 0.0071 129 ARG A CZ 879 N NH1 . ARG A 114 ? 0.7381 0.8865 0.9110 0.0777 0.0444 0.0075 129 ARG A NH1 880 N NH2 . ARG A 114 ? 0.7272 0.8381 0.7077 -0.0579 -0.0096 0.0236 129 ARG A NH2 881 N N . SER A 115 ? 0.2668 0.4144 0.3284 -0.0721 -0.1122 0.1432 130 SER A N 882 C CA . SER A 115 ? 0.2408 0.5604 0.2852 -0.0374 -0.0688 0.0328 130 SER A CA 883 C C . SER A 115 ? 0.2628 0.4831 0.3273 -0.0044 -0.1478 0.0438 130 SER A C 884 O O . SER A 115 ? 0.2736 0.5087 0.2623 -0.0791 -0.1115 0.0611 130 SER A O 885 C CB . SER A 115 ? 0.1975 0.4026 0.2792 -0.0636 -0.0898 0.0875 130 SER A CB 886 O OG . SER A 115 ? 0.2864 0.6230 0.5256 -0.0589 -0.1874 -0.0330 130 SER A OG 887 N N . SER A 116 ? 0.2338 0.3818 0.2610 -0.1160 -0.0761 0.0346 131 SER A N 888 C CA . SER A 116 ? 0.2197 0.3555 0.2938 -0.0804 -0.1126 0.0944 131 SER A CA 889 C C . SER A 116 ? 0.2654 0.3642 0.3472 -0.1053 -0.0262 0.1428 131 SER A C 890 O O . SER A 116 ? 0.2600 0.5293 0.2459 -0.0358 -0.0755 0.1232 131 SER A O 891 C CB . SER A 116 ? 0.2140 0.3642 0.2354 -0.1272 -0.0631 0.0700 131 SER A CB 892 O OG . SER A 116 ? 0.2290 0.5708 0.2318 -0.1347 -0.0480 0.1389 131 SER A OG 893 N N . ALA A 117 ? 0.2264 0.3952 0.2125 -0.1100 -0.0018 0.0984 132 ALA A N 894 C CA . ALA A 117 ? 0.2394 0.3864 0.1616 -0.1057 -0.0550 0.0694 132 ALA A CA 895 C C . ALA A 117 ? 0.2138 0.3826 0.2147 -0.1080 -0.0718 0.0359 132 ALA A C 896 O O . ALA A 117 ? 0.1693 0.4024 0.1984 -0.0784 -0.0509 0.0533 132 ALA A O 897 C CB . ALA A 117 ? 0.2727 0.4727 0.2154 -0.0656 -0.0856 -0.0401 132 ALA A CB 898 N N . ALA A 118 ? 0.2086 0.4301 0.2033 0.0132 -0.0767 0.0157 133 ALA A N 899 C CA . ALA A 118 ? 0.1966 0.2979 0.2320 -0.1035 -0.0562 0.1125 133 ALA A CA 900 C C . ALA A 118 ? 0.1685 0.2634 0.2267 0.0034 -0.0259 0.0539 133 ALA A C 901 O O . ALA A 118 ? 0.1399 0.4448 0.2931 -0.0150 -0.0269 0.0792 133 ALA A O 902 C CB . ALA A 118 ? 0.2121 0.2447 0.2295 -0.0432 -0.0747 0.0360 133 ALA A CB 903 N N . ALA A 119 ? 0.2189 0.4364 0.1823 -0.1034 -0.0530 0.0853 134 ALA A N 904 C CA . ALA A 119 ? 0.2010 0.3723 0.2338 -0.0691 -0.0738 0.0493 134 ALA A CA 905 C C . ALA A 119 ? 0.1777 0.5091 0.2446 -0.0910 0.0031 0.0339 134 ALA A C 906 O O . ALA A 119 ? 0.1563 0.4686 0.2027 -0.0719 -0.0154 0.0693 134 ALA A O 907 C CB . ALA A 119 ? 0.1770 0.4360 0.2510 -0.0969 0.0000 0.0792 134 ALA A CB 908 N N . MET A 120 ? 0.1849 0.3392 0.2217 -0.0187 -0.0484 0.0708 135 MET A N 909 C CA . MET A 120 ? 0.1577 0.4305 0.2270 -0.0745 -0.0301 0.1031 135 MET A CA 910 C C . MET A 120 ? 0.1217 0.3661 0.2719 -0.0275 -0.0161 0.0627 135 MET A C 911 O O . MET A 120 ? 0.1397 0.4761 0.2145 -0.0193 -0.0004 0.0661 135 MET A O 912 C CB . MET A 120 ? 0.1967 0.4341 0.2400 -0.1252 -0.0141 0.0639 135 MET A CB 913 C CG . MET A 120 ? 0.2127 0.5429 0.3155 -0.0756 0.0671 0.0574 135 MET A CG 914 S SD . MET A 120 ? 0.1917 0.6411 0.3825 -0.0678 -0.0054 -0.0566 135 MET A SD 915 C CE . MET A 120 ? 0.1319 0.3960 0.3356 0.0100 -0.0537 0.0305 135 MET A CE 916 N N . TRP A 121 ? 0.1413 0.3878 0.2091 -0.0204 0.0209 0.0987 136 TRP A N 917 C CA . TRP A 121 ? 0.1336 0.3139 0.2008 -0.0221 0.0593 0.0200 136 TRP A CA 918 C C . TRP A 121 ? 0.1478 0.1744 0.1510 0.0562 -0.0051 -0.0167 136 TRP A C 919 O O . TRP A 121 ? 0.1600 0.3024 0.2180 0.0255 -0.0108 0.0262 136 TRP A O 920 C CB . TRP A 121 ? 0.1282 0.3608 0.1888 -0.0140 0.0346 0.0457 136 TRP A CB 921 C CG . TRP A 121 ? 0.1675 0.3543 0.1803 0.0311 0.0384 -0.0415 136 TRP A CG 922 C CD1 . TRP A 121 ? 0.1928 0.2561 0.1545 -0.0279 -0.0791 0.0190 136 TRP A CD1 923 C CD2 . TRP A 121 ? 0.1603 0.3497 0.1587 -0.0432 -0.0172 0.0227 136 TRP A CD2 924 N NE1 . TRP A 121 ? 0.0926 0.2702 0.1590 -0.0049 -0.0270 0.0073 136 TRP A NE1 925 C CE2 . TRP A 121 ? 0.1006 0.2561 0.2216 -0.0039 0.0236 -0.0175 136 TRP A CE2 926 C CE3 . TRP A 121 ? 0.1930 0.3131 0.1500 0.0286 0.0225 0.0738 136 TRP A CE3 927 C CZ2 . TRP A 121 ? 0.1690 0.1334 0.1049 -0.0384 -0.0243 0.0163 136 TRP A CZ2 928 C CZ3 . TRP A 121 ? 0.1890 0.2432 0.1365 -0.1044 -0.0012 -0.0298 136 TRP A CZ3 929 C CH2 . TRP A 121 ? 0.1933 0.1111 0.1811 -0.0572 -0.0537 0.0280 136 TRP A CH2 930 N N . PRO A 122 ? 0.1629 0.2665 0.1540 -0.0597 -0.0592 0.0042 137 PRO A N 931 C CA . PRO A 122 ? 0.1300 0.2119 0.1865 -0.0402 -0.0648 -0.0183 137 PRO A CA 932 C C . PRO A 122 ? 0.1554 0.2998 0.2211 0.0186 -0.0788 0.0375 137 PRO A C 933 O O . PRO A 122 ? 0.2065 0.2569 0.1833 0.0274 0.0030 0.0365 137 PRO A O 934 C CB . PRO A 122 ? 0.1781 0.2121 0.2257 -0.0488 -0.0341 0.0490 137 PRO A CB 935 C CG . PRO A 122 ? 0.2624 0.1371 0.3122 -0.0350 -0.0429 0.0502 137 PRO A CG 936 C CD . PRO A 122 ? 0.1338 0.3265 0.2129 -0.0088 -0.0509 -0.0131 137 PRO A CD 937 N N . GLY A 123 ? 0.1785 0.2763 0.1943 0.0444 -0.0597 0.0656 138 GLY A N 938 C CA . GLY A 123 ? 0.1445 0.2253 0.1796 0.0671 -0.0312 0.0418 138 GLY A CA 939 C C . GLY A 123 ? 0.1400 0.2926 0.2108 -0.0061 -0.0563 0.0672 138 GLY A C 940 O O . GLY A 123 ? 0.1382 0.4469 0.2128 0.0373 -0.0014 0.0675 138 GLY A O 941 N N . THR A 124 ? 0.1848 0.4028 0.2297 -0.0929 -0.0634 0.1000 139 THR A N 942 C CA . THR A 124 ? 0.1929 0.1453 0.2314 -0.0035 0.0064 0.0270 139 THR A CA 943 C C . THR A 124 ? 0.1379 0.3541 0.2842 0.0317 0.0165 0.1172 139 THR A C 944 O O . THR A 124 ? 0.1727 0.4644 0.2756 0.0265 -0.0667 0.0454 139 THR A O 945 C CB . THR A 124 ? 0.1310 0.3452 0.1740 -0.0450 0.0087 0.0686 139 THR A CB 946 O OG1 . THR A 124 ? 0.1459 0.4391 0.2018 -0.0624 -0.0179 0.0691 139 THR A OG1 947 C CG2 . THR A 124 ? 0.1269 0.3719 0.1965 -0.0200 0.0116 0.0455 139 THR A CG2 948 N N . ASP A 125 ? 0.1614 0.3981 0.2776 0.0208 0.0582 0.1015 140 ASP A N 949 C CA . ASP A 125 ? 0.2280 0.3426 0.2958 -0.0370 0.0151 0.0787 140 ASP A CA 950 C C . ASP A 125 ? 0.1881 0.2671 0.3498 0.0694 -0.0869 -0.0145 140 ASP A C 951 O O . ASP A 125 ? 0.2186 0.4701 0.3309 0.1275 0.0068 0.1064 140 ASP A O 952 C CB . ASP A 125 ? 0.2215 0.4722 0.2677 -0.0165 -0.0725 0.0682 140 ASP A CB 953 C CG . ASP A 125 ? 0.2227 0.4805 0.3149 0.0157 0.0221 0.1134 140 ASP A CG 954 O OD1 . ASP A 125 ? 0.2350 0.4879 0.2179 0.0345 0.0367 0.1046 140 ASP A OD1 955 O OD2 . ASP A 125 ? 0.2393 0.5851 0.2767 0.0173 -0.0232 0.0587 140 ASP A OD2 956 N N . VAL A 126 ? 0.1831 0.3801 0.3001 -0.0001 -0.1175 0.0003 141 VAL A N 957 C CA . VAL A 126 ? 0.1711 0.2840 0.2132 0.0693 -0.0671 -0.0143 141 VAL A CA 958 C C . VAL A 126 ? 0.2705 0.3034 0.2369 0.0253 0.0036 0.0984 141 VAL A C 959 O O . VAL A 126 ? 0.2097 0.4524 0.2705 -0.0183 -0.0065 0.0641 141 VAL A O 960 C CB . VAL A 126 ? 0.1994 0.3072 0.2449 0.0945 -0.0217 0.0835 141 VAL A CB 961 C CG1 . VAL A 126 ? 0.1993 0.4108 0.3384 0.0532 -0.0279 0.0616 141 VAL A CG1 962 C CG2 . VAL A 126 ? 0.2135 0.3624 0.2401 0.0493 -0.0620 0.0985 141 VAL A CG2 963 N N . PRO A 127 ? 0.2293 0.4565 0.3634 0.0291 -0.0233 0.1935 142 PRO A N 964 C CA . PRO A 127 ? 0.2237 0.3457 0.3328 0.0894 -0.0629 0.0927 142 PRO A CA 965 C C . PRO A 127 ? 0.2455 0.4230 0.3121 0.0957 0.0076 0.0973 142 PRO A C 966 O O . PRO A 127 ? 0.2096 0.4231 0.3725 0.0674 -0.0024 0.1339 142 PRO A O 967 C CB . PRO A 127 ? 0.2690 0.4060 0.3424 0.0746 -0.1139 0.0971 142 PRO A CB 968 C CG . PRO A 127 ? 0.3284 0.5424 0.4620 0.1686 0.0123 0.0807 142 PRO A CG 969 C CD . PRO A 127 ? 0.3179 0.4480 0.3706 0.1280 -0.0968 0.1067 142 PRO A CD 970 N N . ILE A 128 ? 0.2042 0.4801 0.2783 0.0483 -0.0357 0.1329 143 ILE A N 971 C CA . ILE A 128 ? 0.2498 0.4517 0.3228 -0.0128 0.0220 0.1250 143 ILE A CA 972 C C . ILE A 128 ? 0.2538 0.4247 0.3299 0.0229 0.0904 0.1235 143 ILE A C 973 O O . ILE A 128 ? 0.2945 0.3001 0.2768 0.0479 0.0112 0.0949 143 ILE A O 974 C CB . ILE A 128 ? 0.2399 0.3181 0.2684 0.0049 -0.0465 0.0950 143 ILE A CB 975 C CG1 . ILE A 128 ? 0.2475 0.3885 0.2365 0.0469 -0.0459 0.1264 143 ILE A CG1 976 C CG2 . ILE A 128 ? 0.2860 0.3220 0.2859 -0.0028 -0.0052 0.1451 143 ILE A CG2 977 C CD1 . ILE A 128 ? 0.2711 0.2464 0.2523 0.0530 -0.0737 0.0267 143 ILE A CD1 978 N N . HIS A 129 ? 0.2911 0.3815 0.3409 0.0450 -0.0824 0.1563 144 HIS A N 979 C CA . HIS A 129 ? 0.2983 0.5089 0.2972 0.0827 -0.0887 0.1101 144 HIS A CA 980 C C . HIS A 129 ? 0.2662 0.4180 0.3309 0.0095 -0.1239 0.1128 144 HIS A C 981 O O . HIS A 129 ? 0.3202 0.5934 0.3437 0.0364 -0.1207 0.1303 144 HIS A O 982 C CB . HIS A 129 ? 0.2043 0.5571 0.3703 -0.0113 -0.0526 0.0887 144 HIS A CB 983 C CG . HIS A 129 ? 0.3868 0.4191 0.3551 -0.0525 -0.0066 0.1546 144 HIS A CG 984 N ND1 . HIS A 129 ? 0.4521 0.5637 0.6223 -0.0498 -0.0931 0.1113 144 HIS A ND1 985 C CD2 . HIS A 129 ? 0.4323 0.5252 0.2832 -0.0954 0.0657 0.1029 144 HIS A CD2 986 C CE1 . HIS A 129 ? 0.4477 0.4822 0.5344 0.0370 -0.1197 0.1483 144 HIS A CE1 987 N NE2 . HIS A 129 ? 0.3331 0.6168 0.4061 0.0872 -0.0837 0.1650 144 HIS A NE2 988 N N . ASP A 130 ? 0.2758 0.6081 0.4276 -0.0155 -0.0427 0.2472 145 ASP A N 989 C CA . ASP A 130 ? 0.2488 0.4382 0.3189 -0.0490 -0.1209 0.1079 145 ASP A CA 990 C C . ASP A 130 ? 0.2608 0.5361 0.3948 -0.0399 -0.0803 0.0699 145 ASP A C 991 O O . ASP A 130 ? 0.2707 0.6704 0.5791 -0.0309 -0.1540 0.1043 145 ASP A O 992 C CB . ASP A 130 ? 0.3570 0.6176 0.3839 0.0527 -0.1178 0.1592 145 ASP A CB 993 C CG . ASP A 130 ? 0.4550 0.5126 0.5774 -0.0763 0.0795 0.1182 145 ASP A CG 994 O OD1 . ASP A 130 ? 0.5796 0.5748 0.7495 -0.0256 -0.0107 -0.0736 145 ASP A OD1 995 O OD2 . ASP A 130 ? 0.5603 0.7123 0.7648 -0.0849 -0.0341 -0.0492 145 ASP A OD2 996 N N . THR A 131 ? 0.2404 0.4800 0.3114 0.0170 -0.0337 0.0833 146 THR A N 997 C CA . THR A 131 ? 0.2714 0.2962 0.3180 0.1087 -0.0073 0.0700 146 THR A CA 998 C C . THR A 131 ? 0.2179 0.3781 0.2159 0.0092 -0.0755 0.0901 146 THR A C 999 O O . THR A 131 ? 0.2313 0.5266 0.2810 0.0058 -0.0699 0.1294 146 THR A O 1000 C CB . THR A 131 ? 0.2447 0.4804 0.3228 0.0199 -0.0966 0.0377 146 THR A CB 1001 O OG1 . THR A 131 ? 0.3067 0.6250 0.3973 0.0988 0.0553 0.1706 146 THR A OG1 1002 C CG2 . THR A 131 ? 0.2742 0.5406 0.2795 0.0349 -0.0308 0.0625 146 THR A CG2 1003 N N . ILE A 132 ? 0.2401 0.5075 0.3762 -0.0719 0.0165 0.1833 147 ILE A N 1004 C CA . ILE A 132 ? 0.1863 0.4408 0.2389 0.0437 0.0052 0.0420 147 ILE A CA 1005 C C . ILE A 132 ? 0.2456 0.4816 0.3594 0.0420 -0.0006 0.0943 147 ILE A C 1006 O O . ILE A 132 ? 0.2873 0.4707 0.3142 0.0536 -0.0738 0.0111 147 ILE A O 1007 C CB . ILE A 132 ? 0.2694 0.3423 0.3943 0.1019 -0.0235 0.1445 147 ILE A CB 1008 C CG1 . ILE A 132 ? 0.3593 0.4290 0.3356 0.1081 0.1023 0.1549 147 ILE A CG1 1009 C CG2 . ILE A 132 ? 0.1770 0.3881 0.2770 0.0331 -0.0369 -0.0426 147 ILE A CG2 1010 C CD1 . ILE A 132 ? 0.3054 0.4828 0.4112 0.0958 0.0576 0.1279 147 ILE A CD1 1011 N N . SER A 133 ? 0.1988 0.4526 0.2720 -0.0083 0.0015 0.0123 148 SER A N 1012 C CA . SER A 133 ? 0.1544 0.3588 0.3881 -0.0281 -0.0584 0.0750 148 SER A CA 1013 C C . SER A 133 ? 0.2407 0.4622 0.2733 -0.0115 -0.0437 -0.1098 148 SER A C 1014 O O . SER A 133 ? 0.2629 0.5728 0.3072 0.0327 -0.0308 0.1117 148 SER A O 1015 C CB . SER A 133 ? 0.1368 0.4306 0.4078 -0.0085 -0.0620 -0.0030 148 SER A CB 1016 O OG . SER A 133 ? 0.1630 0.5123 0.3280 -0.0208 -0.0204 0.1293 148 SER A OG 1017 N N . SER A 134 ? 0.1813 0.4631 0.2742 -0.0022 -0.0477 0.0501 149 SER A N 1018 C CA . SER A 134 ? 0.2139 0.5818 0.3183 -0.0690 -0.0649 0.1468 149 SER A CA 1019 C C . SER A 134 ? 0.2126 0.4371 0.4415 0.0106 -0.0384 0.0784 149 SER A C 1020 O O . SER A 134 ? 0.2332 0.6407 0.4452 -0.0186 -0.0562 0.2252 149 SER A O 1021 C CB . SER A 134 ? 0.2580 0.6174 0.5228 -0.1085 -0.0246 0.0435 149 SER A CB 1022 O OG . SER A 134 ? 0.2919 0.3525 0.4077 -0.0569 -0.0805 0.0742 149 SER A OG 1023 N N . TYR A 135 ? 0.2402 0.4155 0.4187 -0.1015 -0.1287 0.0934 150 TYR A N 1024 C CA . TYR A 135 ? 0.1960 0.4269 0.3877 -0.0854 -0.0802 0.1015 150 TYR A CA 1025 C C . TYR A 135 ? 0.2340 0.4647 0.1923 -0.0658 -0.0667 0.0718 150 TYR A C 1026 O O . TYR A 135 ? 0.1784 0.5071 0.2572 -0.0390 -0.0516 0.0845 150 TYR A O 1027 C CB . TYR A 135 ? 0.1907 0.5034 0.3027 -0.0301 -0.0824 0.0420 150 TYR A CB 1028 C CG . TYR A 135 ? 0.2682 0.6260 0.3728 -0.0504 -0.0761 -0.0939 150 TYR A CG 1029 C CD1 . TYR A 135 ? 0.2122 0.3954 0.4902 -0.0438 -0.1108 -0.0454 150 TYR A CD1 1030 C CD2 . TYR A 135 ? 0.3066 0.5086 0.3429 0.0316 -0.1720 -0.0289 150 TYR A CD2 1031 C CE1 . TYR A 135 ? 0.3097 0.4116 0.4492 -0.0570 -0.1506 0.0076 150 TYR A CE1 1032 C CE2 . TYR A 135 ? 0.3631 0.4999 0.3829 0.0562 -0.1628 -0.0138 150 TYR A CE2 1033 C CZ . TYR A 135 ? 0.3942 0.6225 0.5191 -0.0193 -0.2043 0.0015 150 TYR A CZ 1034 O OH . TYR A 135 ? 0.5464 0.8221 0.4819 -0.0058 -0.2545 -0.0111 150 TYR A OH 1035 N N . PHE A 136 ? 0.2083 0.5286 0.2094 -0.0031 -0.0591 0.0347 151 PHE A N 1036 C CA . PHE A 136 ? 0.1834 0.3899 0.2564 -0.0439 -0.0609 0.1430 151 PHE A CA 1037 C C . PHE A 136 ? 0.1424 0.3845 0.2661 -0.0453 -0.0110 0.0733 151 PHE A C 1038 O O . PHE A 136 ? 0.1691 0.5502 0.3496 -0.0453 -0.0147 0.0958 151 PHE A O 1039 C CB . PHE A 136 ? 0.1930 0.4089 0.2485 0.0160 -0.0927 0.0281 151 PHE A CB 1040 C CG . PHE A 136 ? 0.2286 0.4975 0.2809 0.0218 -0.0382 0.1658 151 PHE A CG 1041 C CD1 . PHE A 136 ? 0.2705 0.4522 0.3701 0.0811 -0.1179 0.0964 151 PHE A CD1 1042 C CD2 . PHE A 136 ? 0.1825 0.4734 0.3112 0.0300 -0.0800 0.0007 151 PHE A CD2 1043 C CE1 . PHE A 136 ? 0.2714 0.4915 0.4143 0.1663 -0.0601 0.0412 151 PHE A CE1 1044 C CE2 . PHE A 136 ? 0.2775 0.5479 0.4080 0.0797 -0.0326 0.1470 151 PHE A CE2 1045 C CZ . PHE A 136 ? 0.2465 0.6621 0.4374 0.1062 0.0308 0.1005 151 PHE A CZ 1046 N N . MET A 137 ? 0.2320 0.4462 0.2009 -0.0267 -0.0416 0.1026 152 MET A N 1047 C CA . MET A 137 ? 0.2310 0.4764 0.2666 -0.0467 0.0095 0.0480 152 MET A CA 1048 C C . MET A 137 ? 0.1670 0.4007 0.2659 -0.0164 0.0491 0.0785 152 MET A C 1049 O O . MET A 137 ? 0.1644 0.4773 0.3348 -0.0113 0.0270 -0.0167 152 MET A O 1050 C CB . MET A 137 ? 0.1965 0.5565 0.2332 -0.0675 0.0436 -0.0540 152 MET A CB 1051 C CG . MET A 137 ? 0.2540 0.4764 0.3804 -0.1196 0.0581 0.0472 152 MET A CG 1052 S SD . MET A 137 ? 0.2456 0.4638 0.3393 -0.1169 -0.0164 0.0599 152 MET A SD 1053 C CE . MET A 137 ? 0.3066 0.5005 0.3938 -0.0476 -0.1303 0.0678 152 MET A CE 1054 N N . ASN A 138 ? 0.2762 0.4053 0.2590 0.1044 0.0378 0.0524 153 ASN A N 1055 C CA . ASN A 138 ? 0.1840 0.4706 0.2632 0.0583 0.0319 -0.0445 153 ASN A CA 1056 C C . ASN A 138 ? 0.1571 0.3612 0.3938 -0.0178 -0.0151 0.0619 153 ASN A C 1057 O O . ASN A 138 ? 0.1609 0.4982 0.2955 -0.0194 0.0128 0.1185 153 ASN A O 1058 C CB . ASN A 138 ? 0.2349 0.5525 0.2822 0.0774 0.0140 0.1351 153 ASN A CB 1059 C CG . ASN A 138 ? 0.3036 0.4611 0.5081 0.0633 -0.0437 0.0063 153 ASN A CG 1060 O OD1 . ASN A 138 ? 0.3198 0.7092 0.6928 0.1253 -0.1400 0.1188 153 ASN A OD1 1061 N ND2 . ASN A 138 ? 0.3069 0.4548 0.3300 0.0440 -0.0598 0.1026 153 ASN A ND2 1062 N N . TYR A 139 ? 0.2682 0.4931 0.2499 -0.0214 -0.0055 0.1687 154 TYR A N 1063 C CA . TYR A 139 ? 0.2169 0.2790 0.2601 -0.0026 0.0339 0.1136 154 TYR A CA 1064 C C . TYR A 139 ? 0.2135 0.3449 0.3076 -0.0619 0.0065 0.0323 154 TYR A C 1065 O O . TYR A 139 ? 0.2506 0.5480 0.2546 0.0341 0.0349 0.0923 154 TYR A O 1066 C CB . TYR A 139 ? 0.2631 0.4012 0.2816 -0.0818 -0.0029 0.0412 154 TYR A CB 1067 C CG . TYR A 139 ? 0.2781 0.2991 0.1825 -0.0033 0.0555 0.0542 154 TYR A CG 1068 C CD1 . TYR A 139 ? 0.2128 0.3968 0.1932 0.0579 0.0572 0.0709 154 TYR A CD1 1069 C CD2 . TYR A 139 ? 0.1923 0.3477 0.2726 -0.0163 0.0396 -0.0182 154 TYR A CD2 1070 C CE1 . TYR A 139 ? 0.2787 0.3685 0.2562 -0.0613 -0.0670 0.0351 154 TYR A CE1 1071 C CE2 . TYR A 139 ? 0.2059 0.3631 0.2608 -0.0957 -0.0806 0.0742 154 TYR A CE2 1072 C CZ . TYR A 139 ? 0.2407 0.4579 0.1948 0.0417 -0.0372 0.0174 154 TYR A CZ 1073 O OH . TYR A 139 ? 0.2307 0.4366 0.2853 -0.0484 -0.0459 0.1011 154 TYR A OH 1074 N N . ASN A 140 ? 0.2103 0.2798 0.3183 -0.0151 -0.0085 0.0232 155 ASN A N 1075 C CA . ASN A 140 ? 0.1943 0.4444 0.3971 -0.0441 0.0482 0.1137 155 ASN A CA 1076 C C . ASN A 140 ? 0.1845 0.3827 0.2667 -0.0592 -0.0352 -0.0031 155 ASN A C 1077 O O . ASN A 140 ? 0.1838 0.4439 0.3041 -0.0745 -0.0392 0.0375 155 ASN A O 1078 C CB . ASN A 140 ? 0.1825 0.4669 0.3245 -0.0486 0.0555 0.0905 155 ASN A CB 1079 C CG . ASN A 140 ? 0.2245 0.4326 0.3818 -0.0559 0.0828 0.1117 155 ASN A CG 1080 O OD1 . ASN A 140 ? 0.2497 0.5076 0.4102 0.0720 0.1168 0.1093 155 ASN A OD1 1081 N ND2 . ASN A 140 ? 0.2316 0.5875 0.5906 -0.0746 0.0881 0.0610 155 ASN A ND2 1082 N N . SER A 141 ? 0.1945 0.4341 0.3005 -0.0593 0.0338 0.0050 156 SER A N 1083 C CA . SER A 141 ? 0.2796 0.4565 0.3046 -0.0461 -0.0116 0.1233 156 SER A CA 1084 C C . SER A 141 ? 0.2466 0.4566 0.2223 -0.0126 0.0530 0.1145 156 SER A C 1085 O O . SER A 141 ? 0.2098 0.5609 0.3327 -0.0548 0.0148 0.1142 156 SER A O 1086 C CB . SER A 141 ? 0.3289 0.4859 0.2516 -0.1329 0.0665 0.0697 156 SER A CB 1087 O OG . SER A 141 ? 0.3255 0.5568 0.2527 -0.0149 -0.0222 0.0514 156 SER A OG 1088 N N . SER A 142 ? 0.3466 0.4975 0.3044 -0.0446 0.1703 0.0446 157 SER A N 1089 C CA . SER A 142 ? 0.3584 0.4771 0.2499 0.0459 0.0721 -0.0169 157 SER A CA 1090 C C . SER A 142 ? 0.3204 0.3650 0.3869 -0.1094 0.0150 0.1614 157 SER A C 1091 O O . SER A 142 ? 0.3828 0.5685 0.2851 -0.0732 0.0986 0.0798 157 SER A O 1092 C CB . SER A 142 ? 0.3822 0.5031 0.3140 -0.0157 0.1737 -0.0219 157 SER A CB 1093 O OG . SER A 142 ? 0.4329 0.6125 0.4218 -0.0410 0.2387 0.0348 157 SER A OG 1094 N N . VAL A 143 ? 0.2157 0.5505 0.2641 -0.0841 -0.0137 0.1559 158 VAL A N 1095 C CA . VAL A 143 ? 0.2299 0.5218 0.3496 -0.0748 0.0371 0.0123 158 VAL A CA 1096 C C . VAL A 143 ? 0.2037 0.3625 0.2690 -0.1159 0.0251 0.0469 158 VAL A C 1097 O O . VAL A 143 ? 0.1814 0.3925 0.3259 -0.1004 0.0055 0.0845 158 VAL A O 1098 C CB . VAL A 143 ? 0.2415 0.4325 0.4433 -0.1277 0.0110 0.0258 158 VAL A CB 1099 C CG1 . VAL A 143 ? 0.2106 0.4836 0.3607 -0.0939 -0.0234 -0.0543 158 VAL A CG1 1100 C CG2 . VAL A 143 ? 0.2905 0.4961 0.3905 -0.0450 0.0587 0.2077 158 VAL A CG2 1101 N N . SER A 144 ? 0.2644 0.4142 0.2878 -0.1207 0.0262 0.1158 159 SER A N 1102 C CA . SER A 144 ? 0.2215 0.4704 0.3381 -0.1289 0.0055 0.0567 159 SER A CA 1103 C C . SER A 144 ? 0.2827 0.4080 0.3286 -0.1394 0.0199 0.0860 159 SER A C 1104 O O . SER A 144 ? 0.1871 0.4437 0.2825 -0.1023 -0.0089 0.1016 159 SER A O 1105 C CB . SER A 144 ? 0.2875 0.4671 0.3474 -0.1690 -0.0224 0.1268 159 SER A CB 1106 O OG . SER A 144 ? 0.3395 0.5893 0.3927 -0.2095 0.0208 0.0979 159 SER A OG 1107 N N . PHE A 145 ? 0.2394 0.5008 0.3511 -0.1504 0.0001 0.0607 160 PHE A N 1108 C CA . PHE A 145 ? 0.2739 0.2734 0.3038 -0.1247 0.0336 -0.0889 160 PHE A CA 1109 C C . PHE A 145 ? 0.2992 0.3368 0.3164 -0.1739 -0.0122 -0.0281 160 PHE A C 1110 O O . PHE A 145 ? 0.2774 0.5418 0.2593 -0.1862 -0.0182 0.0580 160 PHE A O 1111 C CB . PHE A 145 ? 0.2952 0.4210 0.2734 -0.0951 0.0905 -0.0157 160 PHE A CB 1112 C CG . PHE A 145 ? 0.3107 0.3722 0.1995 -0.1121 0.0112 -0.0404 160 PHE A CG 1113 C CD1 . PHE A 145 ? 0.2866 0.3343 0.2649 -0.1609 -0.0228 0.0659 160 PHE A CD1 1114 C CD2 . PHE A 145 ? 0.2791 0.4417 0.2347 -0.0725 0.0190 0.0635 160 PHE A CD2 1115 C CE1 . PHE A 145 ? 0.3347 0.3324 0.2209 -0.1828 -0.0034 -0.0263 160 PHE A CE1 1116 C CE2 . PHE A 145 ? 0.2602 0.3412 0.2178 -0.0931 -0.0048 -0.0562 160 PHE A CE2 1117 C CZ . PHE A 145 ? 0.3221 0.3303 0.2649 -0.1438 -0.0856 -0.0215 160 PHE A CZ 1118 N N . GLU A 146 ? 0.3061 0.4298 0.3565 -0.1794 -0.0711 -0.0153 161 GLU A N 1119 C CA . GLU A 146 ? 0.3217 0.3396 0.3853 -0.1620 -0.0886 -0.0173 161 GLU A CA 1120 C C . GLU A 146 ? 0.3143 0.4333 0.3937 -0.1833 -0.0511 -0.0571 161 GLU A C 1121 O O . GLU A 146 ? 0.3144 0.5421 0.3278 -0.1967 -0.0602 -0.0079 161 GLU A O 1122 C CB . GLU A 146 ? 0.3753 0.4561 0.3873 -0.2079 -0.0830 -0.0257 161 GLU A CB 1123 C CG . GLU A 146 ? 0.4074 0.4272 0.4751 -0.2332 -0.0089 -0.0009 161 GLU A CG 1124 C CD . GLU A 146 ? 0.5695 0.6183 0.6124 -0.1317 0.0166 -0.0838 161 GLU A CD 1125 O OE1 . GLU A 146 ? 0.6108 0.6000 0.5964 -0.0636 0.0232 -0.1137 161 GLU A OE1 1126 O OE2 . GLU A 146 ? 0.6126 0.7145 0.6633 -0.2458 -0.0932 -0.0698 161 GLU A OE2 1127 N N . GLU A 147 ? 0.2978 0.3754 0.4156 -0.1831 0.0131 0.0278 162 GLU A N 1128 C CA . GLU A 147 ? 0.3074 0.4659 0.4823 -0.1905 -0.0093 0.0381 162 GLU A CA 1129 C C . GLU A 147 ? 0.2233 0.4046 0.3431 -0.0819 -0.1181 0.0377 162 GLU A C 1130 O O . GLU A 147 ? 0.2416 0.4801 0.4083 -0.1281 -0.0977 0.1413 162 GLU A O 1131 C CB . GLU A 147 ? 0.3607 0.4286 0.4583 -0.1527 0.0528 0.0755 162 GLU A CB 1132 C CG . GLU A 147 ? 0.3501 0.5366 0.4479 -0.1297 -0.0029 0.1998 162 GLU A CG 1133 C CD . GLU A 147 ? 0.3720 0.6343 0.6177 -0.0794 0.1070 0.0841 162 GLU A CD 1134 O OE1 . GLU A 147 ? 0.4291 0.6721 0.5351 -0.0543 -0.0378 0.2224 162 GLU A OE1 1135 O OE2 . GLU A 147 ? 0.4627 0.6952 0.7805 -0.0775 0.0614 -0.0117 162 GLU A OE2 1136 N N . ARG A 148 ? 0.2140 0.3960 0.3176 -0.1401 -0.0351 0.0384 163 ARG A N 1137 C CA . ARG A 148 ? 0.2200 0.3820 0.2121 -0.1056 -0.0717 0.0150 163 ARG A CA 1138 C C . ARG A 148 ? 0.2565 0.2527 0.2255 -0.1172 -0.1039 0.0986 163 ARG A C 1139 O O . ARG A 148 ? 0.2631 0.3995 0.2371 -0.1485 -0.0665 0.1047 163 ARG A O 1140 C CB . ARG A 148 ? 0.2192 0.3927 0.2501 -0.1254 -0.0541 -0.0101 163 ARG A CB 1141 C CG . ARG A 148 ? 0.1945 0.3790 0.2327 -0.1186 -0.0048 -0.0566 163 ARG A CG 1142 C CD . ARG A 148 ? 0.1824 0.3653 0.1814 -0.0600 -0.0580 -0.0200 163 ARG A CD 1143 N NE . ARG A 148 ? 0.1705 0.4027 0.1833 -0.0323 -0.0574 0.0033 163 ARG A NE 1144 C CZ . ARG A 148 ? 0.1479 0.3619 0.1624 -0.0847 -0.0136 0.0205 163 ARG A CZ 1145 N NH1 . ARG A 148 ? 0.1548 0.3486 0.2213 -0.0947 -0.0181 0.0514 163 ARG A NH1 1146 N NH2 . ARG A 148 ? 0.1780 0.5117 0.1904 -0.0926 0.0131 -0.0037 163 ARG A NH2 1147 N N . LEU A 149 ? 0.2315 0.3056 0.2680 -0.1314 -0.0424 -0.0239 164 LEU A N 1148 C CA . LEU A 149 ? 0.2551 0.3665 0.2992 -0.1609 -0.0404 0.0200 164 LEU A CA 1149 C C . LEU A 149 ? 0.2570 0.4229 0.3097 -0.1643 -0.0467 0.0270 164 LEU A C 1150 O O . LEU A 149 ? 0.3179 0.4900 0.2615 -0.1830 -0.0632 0.0639 164 LEU A O 1151 C CB . LEU A 149 ? 0.3326 0.3196 0.2785 -0.0716 0.0009 -0.0886 164 LEU A CB 1152 C CG . LEU A 149 ? 0.3158 0.3330 0.3918 -0.1484 0.0137 0.0012 164 LEU A CG 1153 C CD1 . LEU A 149 ? 0.3338 0.6021 0.3269 -0.2264 -0.0257 -0.0144 164 LEU A CD1 1154 C CD2 . LEU A 149 ? 0.3441 0.4332 0.2331 -0.1460 -0.0326 0.0336 164 LEU A CD2 1155 N N . ASN A 150 ? 0.2680 0.4462 0.3303 -0.1686 -0.0600 0.0100 165 ASN A N 1156 C CA . ASN A 150 ? 0.3210 0.4482 0.3047 -0.1768 -0.0928 0.0148 165 ASN A CA 1157 C C . ASN A 150 ? 0.2849 0.4448 0.4439 -0.1116 -0.1512 0.0693 165 ASN A C 1158 O O . ASN A 150 ? 0.4237 0.6444 0.3682 -0.1899 -0.1558 0.0325 165 ASN A O 1159 C CB . ASN A 150 ? 0.2660 0.4308 0.4153 -0.1699 -0.0175 0.0505 165 ASN A CB 1160 C CG . ASN A 150 ? 0.3021 0.6052 0.4381 -0.1324 -0.0027 -0.0046 165 ASN A CG 1161 O OD1 . ASN A 150 ? 0.3447 0.6441 0.2792 -0.1356 -0.0123 0.0112 165 ASN A OD1 1162 N ND2 . ASN A 150 ? 0.3382 0.3622 0.5301 -0.1817 0.0572 0.0538 165 ASN A ND2 1163 N N . ASN A 151 ? 0.2749 0.4531 0.3674 -0.1859 -0.0021 0.0027 166 ASN A N 1164 C CA . ASN A 151 ? 0.2031 0.5071 0.4322 -0.0969 0.0086 0.1027 166 ASN A CA 1165 C C . ASN A 151 ? 0.2473 0.4616 0.4216 -0.0942 -0.1364 -0.0267 166 ASN A C 1166 O O . ASN A 151 ? 0.2667 0.6585 0.4217 -0.1251 -0.1063 0.0798 166 ASN A O 1167 C CB . ASN A 151 ? 0.1730 0.5296 0.2434 -0.0686 -0.0109 -0.0451 166 ASN A CB 1168 C CG . ASN A 151 ? 0.3254 0.5668 0.3085 -0.0439 -0.0528 0.0397 166 ASN A CG 1169 O OD1 . ASN A 151 ? 0.3451 0.7974 0.4713 0.0182 -0.0247 0.0557 166 ASN A OD1 1170 N ND2 . ASN A 151 ? 0.3982 0.4590 0.4678 0.1658 -0.0289 -0.1509 166 ASN A ND2 1171 N N . ILE A 152 ? 0.2321 0.4274 0.3155 -0.1382 -0.0707 0.1058 167 ILE A N 1172 C CA . ILE A 152 ? 0.2674 0.4193 0.2201 -0.1492 -0.0362 -0.0369 167 ILE A CA 1173 C C . ILE A 152 ? 0.3268 0.2245 0.2652 -0.1176 -0.1165 0.0355 167 ILE A C 1174 O O . ILE A 152 ? 0.3597 0.4872 0.2873 -0.1820 -0.1231 0.1476 167 ILE A O 1175 C CB . ILE A 152 ? 0.2388 0.3306 0.2931 -0.1292 -0.0846 0.1312 167 ILE A CB 1176 C CG1 . ILE A 152 ? 0.2326 0.3721 0.4134 -0.0384 -0.1001 0.0405 167 ILE A CG1 1177 C CG2 . ILE A 152 ? 0.3026 0.3947 0.2331 -0.1870 -0.0451 0.0669 167 ILE A CG2 1178 C CD1 . ILE A 152 ? 0.1982 0.2558 0.3131 -0.0688 -0.0065 0.0221 167 ILE A CD1 1179 N N . THR A 153 ? 0.3566 0.4041 0.2898 -0.2082 0.0071 -0.0506 168 THR A N 1180 C CA . THR A 153 ? 0.3325 0.2423 0.3129 -0.0841 -0.0176 -0.0029 168 THR A CA 1181 C C . THR A 153 ? 0.3031 0.4507 0.3818 -0.1769 -0.0782 -0.0138 168 THR A C 1182 O O . THR A 153 ? 0.3680 0.4065 0.3143 -0.1467 -0.0668 -0.0416 168 THR A O 1183 C CB . THR A 153 ? 0.3345 0.2801 0.2973 -0.1263 -0.1180 0.0073 168 THR A CB 1184 O OG1 . THR A 153 ? 0.4659 0.4133 0.2861 -0.2169 -0.0516 0.0270 168 THR A OG1 1185 C CG2 . THR A 153 ? 0.3139 0.3827 0.2956 -0.0997 -0.1453 0.0079 168 THR A CG2 1186 N N . MET A 154 ? 0.2950 0.4305 0.3613 -0.1336 -0.0845 0.1017 169 MET A N 1187 C CA . MET A 154 ? 0.3478 0.4207 0.3568 -0.0647 -0.1263 0.0181 169 MET A CA 1188 C C . MET A 154 ? 0.3745 0.4675 0.4213 -0.1300 -0.1396 0.0044 169 MET A C 1189 O O . MET A 154 ? 0.3862 0.4677 0.3931 -0.1022 -0.1246 -0.1152 169 MET A O 1190 C CB . MET A 154 ? 0.3750 0.5890 0.3506 -0.1576 -0.0959 -0.0901 169 MET A CB 1191 C CG . MET A 154 ? 0.4690 0.5831 0.5965 -0.0367 -0.0538 -0.3270 169 MET A CG 1192 S SD . MET A 154 ? 0.4622 0.5774 0.7506 -0.0884 -0.2083 -0.2107 169 MET A SD 1193 C CE . MET A 154 ? 0.4637 0.5970 0.6669 -0.1222 -0.2427 0.0008 169 MET A CE 1194 N N . TRP A 155 ? 0.3267 0.4595 0.4483 -0.1336 -0.1414 -0.0876 170 TRP A N 1195 C CA . TRP A 155 ? 0.2765 0.4582 0.3820 -0.0727 -0.1447 -0.0644 170 TRP A CA 1196 C C . TRP A 155 ? 0.3576 0.3658 0.4708 -0.0317 -0.0683 0.1710 170 TRP A C 1197 O O . TRP A 155 ? 0.3757 0.5675 0.2711 -0.1309 -0.0919 0.1051 170 TRP A O 1198 C CB . TRP A 155 ? 0.2702 0.4831 0.3125 -0.0553 -0.0358 -0.0829 170 TRP A CB 1199 C CG . TRP A 155 ? 0.2135 0.5748 0.4274 -0.0356 -0.0821 0.0187 170 TRP A CG 1200 C CD1 . TRP A 155 ? 0.3188 0.5886 0.4408 0.0017 -0.1049 -0.0221 170 TRP A CD1 1201 C CD2 . TRP A 155 ? 0.2212 0.5910 0.4043 -0.1120 0.0344 -0.0794 170 TRP A CD2 1202 N NE1 . TRP A 155 ? 0.3708 0.6249 0.3891 -0.0434 -0.2000 0.0259 170 TRP A NE1 1203 C CE2 . TRP A 155 ? 0.3325 0.5324 0.3767 -0.1030 -0.1109 -0.1304 170 TRP A CE2 1204 C CE3 . TRP A 155 ? 0.2289 0.3529 0.3465 -0.0807 -0.1127 -0.0560 170 TRP A CE3 1205 C CZ2 . TRP A 155 ? 0.3026 0.5237 0.4073 -0.0222 -0.1922 -0.0148 170 TRP A CZ2 1206 C CZ3 . TRP A 155 ? 0.2723 0.6016 0.2850 -0.0364 -0.0859 -0.0554 170 TRP A CZ3 1207 C CH2 . TRP A 155 ? 0.3537 0.6168 0.2844 0.0222 -0.0995 0.0489 170 TRP A CH2 1208 N N . LEU A 156 ? 0.3541 0.2814 0.2229 -0.0455 -0.0343 0.0189 171 LEU A N 1209 C CA . LEU A 156 ? 0.3919 0.4171 0.1710 -0.1126 -0.0742 0.0289 171 LEU A CA 1210 C C . LEU A 156 ? 0.4581 0.5390 0.3018 -0.2075 -0.0981 -0.0171 171 LEU A C 1211 O O . LEU A 156 ? 0.4921 0.6015 0.2674 -0.1734 -0.0539 0.0750 171 LEU A O 1212 C CB . LEU A 156 ? 0.3439 0.4719 0.2321 -0.0738 -0.1243 0.0386 171 LEU A CB 1213 C CG . LEU A 156 ? 0.3571 0.3519 0.2105 -0.1442 -0.0590 -0.0402 171 LEU A CG 1214 C CD1 . LEU A 156 ? 0.3833 0.4153 0.2083 -0.0612 -0.0432 0.0638 171 LEU A CD1 1215 C CD2 . LEU A 156 ? 0.3673 0.4837 0.3195 -0.1855 -0.0048 0.0741 171 LEU A CD2 1216 N N . ASN A 157 ? 0.4497 0.4994 0.2970 -0.1688 -0.1332 0.0052 172 ASN A N 1217 C CA . ASN A 157 ? 0.5154 0.5239 0.4465 -0.0054 -0.1034 0.0475 172 ASN A CA 1218 C C . ASN A 157 ? 0.5072 0.6607 0.5235 -0.0045 -0.0708 0.0532 172 ASN A C 1219 O O . ASN A 157 ? 0.5435 0.6243 0.5549 0.0162 -0.0427 -0.0498 172 ASN A O 1220 C CB . ASN A 157 ? 0.5072 0.4097 0.5363 -0.0824 -0.0817 0.0511 172 ASN A CB 1221 C CG . ASN A 157 ? 0.6034 0.6029 0.6149 0.0221 -0.0470 0.0810 172 ASN A CG 1222 O OD1 . ASN A 157 ? 0.7162 0.5200 0.7072 -0.0947 -0.1368 -0.0838 172 ASN A OD1 1223 N ND2 . ASN A 157 ? 0.6639 0.6506 0.5712 0.0226 0.0707 0.0008 172 ASN A ND2 1224 N N . ASN A 158 ? 0.5849 0.5499 0.5872 -0.0739 -0.0690 -0.0550 173 ASN A N 1225 C CA . ASN A 158 ? 0.5469 0.6714 0.6552 -0.0286 -0.0134 0.0385 173 ASN A CA 1226 C C . ASN A 158 ? 0.5668 0.6764 0.6577 0.0393 0.0533 0.0188 173 ASN A C 1227 O O . ASN A 158 ? 0.7054 0.8732 0.9023 -0.0681 -0.0046 -0.0565 173 ASN A O 1228 C CB . ASN A 158 ? 0.5597 0.7202 0.6400 -0.0469 -0.0439 0.0032 173 ASN A CB 1229 C CG . ASN A 158 ? 0.6646 0.6992 0.7201 -0.0026 -0.0853 0.0936 173 ASN A CG 1230 O OD1 . ASN A 158 ? 0.6441 0.8485 0.8811 -0.1218 -0.1679 0.0130 173 ASN A OD1 1231 N ND2 . ASN A 158 ? 0.5644 0.5881 0.7094 -0.0515 -0.2379 -0.0661 173 ASN A ND2 1232 N N . SER A 159 ? 0.5582 0.7188 0.6726 0.1019 -0.0610 0.0132 174 SER A N 1233 C CA . SER A 159 ? 0.4259 0.4308 0.3810 -0.0608 -0.2080 0.1125 174 SER A CA 1234 C C . SER A 159 ? 0.4667 0.6414 0.4757 -0.0638 -0.1372 -0.0805 174 SER A C 1235 O O . SER A 159 ? 0.4637 0.5985 0.3735 -0.1408 -0.1749 -0.0333 174 SER A O 1236 C CB . SER A 159 ? 0.4662 0.5515 0.3411 -0.0126 -0.2098 -0.0636 174 SER A CB 1237 O OG . SER A 159 ? 0.4624 0.6682 0.5368 -0.0648 -0.1339 -0.0813 174 SER A OG 1238 N N . ASN A 160 ? 0.5750 0.5242 0.4202 -0.0121 -0.1166 0.2038 175 ASN A N 1239 C CA . ASN A 160 ? 0.5075 0.6114 0.4539 -0.1454 -0.2320 0.0081 175 ASN A CA 1240 C C . ASN A 160 ? 0.5234 0.5590 0.4604 0.0167 -0.1751 0.0553 175 ASN A C 1241 O O . ASN A 160 ? 0.5681 0.6739 0.5301 0.0078 -0.0540 0.0435 175 ASN A O 1242 C CB . ASN A 160 ? 0.5319 0.6869 0.6503 -0.0858 -0.1548 -0.0111 175 ASN A CB 1243 C CG . ASN A 160 ? 0.6333 0.7808 0.7543 -0.0360 -0.0274 0.0051 175 ASN A CG 1244 O OD1 . ASN A 160 ? 0.7157 0.8571 0.7457 -0.0085 0.0421 0.1849 175 ASN A OD1 1245 N ND2 . ASN A 160 ? 0.6504 0.7964 0.8468 -0.0107 -0.0362 0.0011 175 ASN A ND2 1246 N N . PRO A 161 ? 0.4613 0.5369 0.4013 -0.0070 -0.1599 0.0218 176 PRO A N 1247 C CA . PRO A 161 ? 0.4881 0.5466 0.5208 0.0285 -0.0261 0.0891 176 PRO A CA 1248 C C . PRO A 161 ? 0.4218 0.5610 0.3372 -0.0373 -0.0964 0.0213 176 PRO A C 1249 O O . PRO A 161 ? 0.3221 0.6429 0.4051 -0.1351 -0.0988 0.1726 176 PRO A O 1250 C CB . PRO A 161 ? 0.4742 0.5424 0.5777 -0.0439 -0.0279 0.0725 176 PRO A CB 1251 C CG . PRO A 161 ? 0.4222 0.6088 0.4176 0.0278 0.1490 0.0458 176 PRO A CG 1252 C CD . PRO A 161 ? 0.4563 0.5427 0.4564 0.0284 -0.1618 0.0834 176 PRO A CD 1253 N N . PRO A 162 ? 0.4019 0.4967 0.2918 -0.0824 -0.1030 0.1364 177 PRO A N 1254 C CA . PRO A 162 ? 0.3747 0.5000 0.2852 -0.0924 -0.1574 0.0214 177 PRO A CA 1255 C C . PRO A 162 ? 0.3130 0.5287 0.3299 -0.1438 -0.0990 0.1028 177 PRO A C 1256 O O . PRO A 162 ? 0.3532 0.6145 0.2307 -0.1625 -0.0769 0.0540 177 PRO A O 1257 C CB . PRO A 162 ? 0.4223 0.4943 0.4777 -0.1288 -0.1218 -0.0211 177 PRO A CB 1258 C CG . PRO A 162 ? 0.4313 0.4320 0.4396 -0.0506 -0.0499 0.1097 177 PRO A CG 1259 C CD . PRO A 162 ? 0.3490 0.5794 0.3745 -0.1117 -0.1041 0.0755 177 PRO A CD 1260 N N . VAL A 163 ? 0.2971 0.5456 0.2514 -0.0935 -0.0960 0.1122 178 VAL A N 1261 C CA . VAL A 163 ? 0.2912 0.3771 0.2607 0.0080 -0.1212 0.0952 178 VAL A CA 1262 C C . VAL A 163 ? 0.3474 0.3704 0.2764 -0.0378 -0.1584 -0.0435 178 VAL A C 1263 O O . VAL A 163 ? 0.2927 0.4807 0.2837 -0.1217 -0.0781 0.0615 178 VAL A O 1264 C CB . VAL A 163 ? 0.2934 0.3565 0.1942 -0.1141 -0.0613 0.1029 178 VAL A CB 1265 C CG1 . VAL A 163 ? 0.2505 0.3476 0.1860 -0.0423 -0.0875 0.0292 178 VAL A CG1 1266 C CG2 . VAL A 163 ? 0.2420 0.4636 0.3761 -0.0200 -0.0091 0.0734 178 VAL A CG2 1267 N N . THR A 164 ? 0.3307 0.4779 0.1917 -0.1074 -0.0828 0.0334 179 THR A N 1268 C CA . THR A 164 ? 0.2821 0.4657 0.1517 -0.1008 -0.0112 0.0480 179 THR A CA 1269 C C . THR A 164 ? 0.2820 0.2975 0.0936 -0.0063 0.0001 0.0205 179 THR A C 1270 O O . THR A 164 ? 0.2869 0.5694 0.1938 -0.1405 0.0095 -0.0624 179 THR A O 1271 C CB . THR A 164 ? 0.2848 0.4730 0.1861 -0.1305 -0.0514 -0.0062 179 THR A CB 1272 O OG1 . THR A 164 ? 0.2652 0.4749 0.1865 -0.0849 -0.0569 0.0458 179 THR A OG1 1273 C CG2 . THR A 164 ? 0.3255 0.5207 0.1934 -0.1355 -0.0580 0.0792 179 THR A CG2 1274 N N . PHE A 165 ? 0.2587 0.3748 0.1512 -0.1156 -0.0383 -0.0103 180 PHE A N 1275 C CA . PHE A 165 ? 0.2646 0.2465 0.1529 -0.1368 -0.0256 0.0230 180 PHE A CA 1276 C C . PHE A 165 ? 0.2514 0.2629 0.1841 -0.1139 -0.0028 0.0677 180 PHE A C 1277 O O . PHE A 165 ? 0.3255 0.4080 0.1420 -0.0577 -0.0190 -0.0079 180 PHE A O 1278 C CB . PHE A 165 ? 0.2413 0.3513 0.1851 -0.0876 -0.0849 0.0549 180 PHE A CB 1279 C CG . PHE A 165 ? 0.2144 0.3376 0.1480 -0.0310 -0.0711 0.0087 180 PHE A CG 1280 C CD1 . PHE A 165 ? 0.1813 0.4493 0.1839 -0.0843 -0.0379 0.0109 180 PHE A CD1 1281 C CD2 . PHE A 165 ? 0.2282 0.3564 0.1803 -0.1237 -0.0255 -0.0342 180 PHE A CD2 1282 C CE1 . PHE A 165 ? 0.2004 0.3299 0.1303 -0.0525 -0.0291 0.0559 180 PHE A CE1 1283 C CE2 . PHE A 165 ? 0.2004 0.3330 0.1307 -0.0816 -0.0028 -0.0524 180 PHE A CE2 1284 C CZ . PHE A 165 ? 0.2027 0.4166 0.1700 -0.0396 -0.0491 -0.0450 180 PHE A CZ 1285 N N . ALA A 166 ? 0.2675 0.3798 0.1694 -0.0872 -0.0400 0.0960 181 ALA A N 1286 C CA . ALA A 166 ? 0.2710 0.3429 0.1295 -0.1034 -0.0318 0.0366 181 ALA A CA 1287 C C . ALA A 166 ? 0.2138 0.3530 0.1681 -0.0278 -0.0196 0.0672 181 ALA A C 1288 O O . ALA A 166 ? 0.2121 0.4260 0.1494 -0.0526 -0.0444 0.0324 181 ALA A O 1289 C CB . ALA A 166 ? 0.2896 0.2410 0.2310 -0.0906 -0.0492 -0.0126 181 ALA A CB 1290 N N . THR A 167 ? 0.1707 0.3447 0.1772 -0.0449 -0.0549 0.0201 182 THR A N 1291 C CA . THR A 167 ? 0.1546 0.3707 0.1923 -0.0858 -0.0313 0.0307 182 THR A CA 1292 C C . THR A 167 ? 0.1712 0.2954 0.1825 -0.0870 -0.0022 0.0762 182 THR A C 1293 O O . THR A 167 ? 0.1601 0.4475 0.2256 -0.0852 -0.0228 0.0489 182 THR A O 1294 C CB . THR A 167 ? 0.1752 0.4050 0.2922 -0.1066 0.0137 -0.0629 182 THR A CB 1295 O OG1 . THR A 167 ? 0.1879 0.5237 0.1631 -0.1081 -0.0149 0.0512 182 THR A OG1 1296 C CG2 . THR A 167 ? 0.1652 0.3932 0.2333 -0.0495 -0.0302 0.0101 182 THR A CG2 1297 N N . LEU A 168 ? 0.2001 0.3919 0.1529 -0.0830 -0.0400 0.0726 183 LEU A N 1298 C CA . LEU A 168 ? 0.2212 0.2341 0.2016 -0.0829 -0.0465 0.0499 183 LEU A CA 1299 C C . LEU A 168 ? 0.2231 0.2563 0.1760 -0.0740 -0.0582 0.0976 183 LEU A C 1300 O O . LEU A 168 ? 0.1903 0.4646 0.1570 -0.0522 0.0051 0.0323 183 LEU A O 1301 C CB . LEU A 168 ? 0.2550 0.2763 0.2499 -0.0978 0.0105 0.1032 183 LEU A CB 1302 C CG . LEU A 168 ? 0.1703 0.2856 0.2187 -0.0673 -0.0647 0.0888 183 LEU A CG 1303 C CD1 . LEU A 168 ? 0.1346 0.4030 0.2291 -0.0583 -0.0124 0.0506 183 LEU A CD1 1304 C CD2 . LEU A 168 ? 0.2376 0.4099 0.3174 -0.1557 -0.0051 -0.0411 183 LEU A CD2 1305 N N . TYR A 169 ? 0.2172 0.3231 0.1507 -0.1245 -0.0225 0.0331 184 TYR A N 1306 C CA . TYR A 169 ? 0.1740 0.4017 0.1334 -0.0980 0.0121 -0.0206 184 TYR A CA 1307 C C . TYR A 169 ? 0.1705 0.3459 0.1158 -0.0289 0.0221 0.0250 184 TYR A C 1308 O O . TYR A 169 ? 0.1416 0.3650 0.2082 -0.0748 0.0249 0.0012 184 TYR A O 1309 C CB . TYR A 169 ? 0.2174 0.2503 0.1212 -0.0348 -0.0523 0.0514 184 TYR A CB 1310 C CG . TYR A 169 ? 0.1541 0.2837 0.1981 -0.0633 -0.0233 0.1085 184 TYR A CG 1311 C CD1 . TYR A 169 ? 0.2198 0.2620 0.1836 -0.0682 -0.0281 0.1052 184 TYR A CD1 1312 C CD2 . TYR A 169 ? 0.1988 0.1510 0.1834 -0.0352 0.0355 0.0074 184 TYR A CD2 1313 C CE1 . TYR A 169 ? 0.2512 0.2785 0.1792 -0.0433 0.0494 0.0525 184 TYR A CE1 1314 C CE2 . TYR A 169 ? 0.1844 0.2222 0.2046 -0.0792 -0.0005 -0.0457 184 TYR A CE2 1315 C CZ . TYR A 169 ? 0.1511 0.3554 0.1657 -0.0238 -0.0405 -0.0309 184 TYR A CZ 1316 O OH . TYR A 169 ? 0.1522 0.4326 0.1725 -0.0299 -0.0143 -0.0262 184 TYR A OH 1317 N N . TRP A 170 ? 0.2463 0.1696 0.1358 -0.0160 -0.0019 0.0716 185 TRP A N 1318 C CA . TRP A 170 ? 0.1898 0.2482 0.1166 -0.0894 -0.0357 0.0181 185 TRP A CA 1319 C C . TRP A 170 ? 0.1978 0.1982 0.1485 -0.1058 -0.0121 0.0080 185 TRP A C 1320 O O . TRP A 170 ? 0.1926 0.2299 0.1798 -0.0979 0.0349 -0.0194 185 TRP A O 1321 C CB . TRP A 170 ? 0.2117 0.3020 0.1990 -0.1149 -0.0023 0.0685 185 TRP A CB 1322 C CG . TRP A 170 ? 0.1638 0.3064 0.1655 -0.0982 0.0188 -0.0043 185 TRP A CG 1323 C CD1 . TRP A 170 ? 0.2593 0.1904 0.2028 -0.0806 -0.0049 0.0433 185 TRP A CD1 1324 C CD2 . TRP A 170 ? 0.1825 0.3363 0.1883 -0.1126 -0.0449 0.0585 185 TRP A CD2 1325 N NE1 . TRP A 170 ? 0.1957 0.4295 0.2256 -0.1207 -0.0190 -0.0078 185 TRP A NE1 1326 C CE2 . TRP A 170 ? 0.2045 0.2921 0.2018 -0.1034 -0.0332 0.0471 185 TRP A CE2 1327 C CE3 . TRP A 170 ? 0.1768 0.4985 0.1930 -0.0859 -0.0163 -0.0091 185 TRP A CE3 1328 C CZ2 . TRP A 170 ? 0.2071 0.4643 0.1616 -0.1359 0.0020 0.0111 185 TRP A CZ2 1329 C CZ3 . TRP A 170 ? 0.2542 0.3588 0.2552 -0.0309 -0.0302 0.1549 185 TRP A CZ3 1330 C CH2 . TRP A 170 ? 0.2295 0.3523 0.2191 -0.1101 -0.0889 0.0886 185 TRP A CH2 1331 N N . GLU A 171 ? 0.1872 0.3105 0.1369 -0.0804 -0.0162 0.0085 186 GLU A N 1332 C CA . GLU A 171 ? 0.1835 0.2925 0.1336 -0.0555 0.0486 0.0158 186 GLU A CA 1333 C C . GLU A 171 ? 0.1853 0.2137 0.1249 -0.0581 -0.0130 0.0298 186 GLU A C 1334 O O . GLU A 171 ? 0.1697 0.2654 0.1611 -0.0404 -0.0221 0.0366 186 GLU A O 1335 C CB . GLU A 171 ? 0.1431 0.2841 0.1871 -0.0597 0.0399 0.0393 186 GLU A CB 1336 C CG . GLU A 171 ? 0.1625 0.3370 0.2218 0.0335 -0.0379 0.0017 186 GLU A CG 1337 C CD . GLU A 171 ? 0.1577 0.2788 0.2365 -0.0233 0.0551 -0.0559 186 GLU A CD 1338 O OE1 . GLU A 171 ? 0.1834 0.3911 0.2603 -0.0036 0.0138 0.0027 186 GLU A OE1 1339 O OE2 . GLU A 171 ? 0.1548 0.4075 0.2144 -0.0271 -0.0039 -0.0017 186 GLU A OE2 1340 N N . GLU A 172 ? 0.1708 0.1794 0.2263 -0.0648 0.0289 -0.0645 187 GLU A N 1341 C CA . GLU A 172 ? 0.1608 0.1498 0.2596 -0.0274 0.0778 0.0043 187 GLU A CA 1342 C C . GLU A 172 ? 0.1357 0.2503 0.2212 -0.0749 -0.0140 -0.0223 187 GLU A C 1343 O O . GLU A 172 ? 0.1678 0.2520 0.1978 -0.0576 0.0047 0.0221 187 GLU A O 1344 C CB . GLU A 172 ? 0.2129 0.2568 0.1871 -0.1017 0.0626 -0.0040 187 GLU A CB 1345 C CG . GLU A 172 ? 0.2411 0.2024 0.1857 -0.1168 0.0054 0.0161 187 GLU A CG 1346 C CD . GLU A 172 ? 0.2233 0.1544 0.1809 -0.0855 0.0396 0.0080 187 GLU A CD 1347 O OE1 . GLU A 172 ? 0.2010 0.2345 0.1990 -0.0897 0.0229 0.0360 187 GLU A OE1 1348 O OE2 . GLU A 172 ? 0.2453 0.5057 0.2331 -0.1183 0.0327 0.0702 187 GLU A OE2 1349 N N . PRO A 173 ? 0.1508 0.2204 0.1793 -0.0715 0.0026 0.0576 188 PRO A N 1350 C CA . PRO A 173 ? 0.1824 0.3547 0.1527 -0.0619 0.0024 0.0526 188 PRO A CA 1351 C C . PRO A 173 ? 0.1515 0.1876 0.1401 -0.0215 0.0040 0.0255 188 PRO A C 1352 O O . PRO A 173 ? 0.1932 0.2001 0.1627 -0.0289 0.0183 0.0039 188 PRO A O 1353 C CB . PRO A 173 ? 0.2073 0.2264 0.2233 -0.0557 0.0779 0.0593 188 PRO A CB 1354 C CG . PRO A 173 ? 0.1776 0.2763 0.1671 -0.0388 0.0335 0.0175 188 PRO A CG 1355 C CD . PRO A 173 ? 0.1632 0.2367 0.1582 -0.0657 0.0442 -0.0204 188 PRO A CD 1356 N N . ASP A 174 ? 0.2250 0.1504 0.1615 -0.0488 0.0306 0.0542 189 ASP A N 1357 C CA . ASP A 174 ? 0.1762 0.1664 0.1751 -0.0856 0.0355 -0.0204 189 ASP A CA 1358 C C . ASP A 174 ? 0.1322 0.1181 0.2246 0.0165 0.0745 0.0316 189 ASP A C 1359 O O . ASP A 174 ? 0.1924 0.1772 0.1702 -0.0382 0.0078 0.0514 189 ASP A O 1360 C CB . ASP A 174 ? 0.2004 0.2114 0.2075 -0.0943 0.0060 -0.0080 189 ASP A CB 1361 C CG . ASP A 174 ? 0.1999 0.0862 0.1633 -0.0396 -0.0145 0.0231 189 ASP A CG 1362 O OD1 . ASP A 174 ? 0.3008 0.2410 0.1440 -0.1470 0.0030 -0.0066 189 ASP A OD1 1363 O OD2 . ASP A 174 ? 0.2304 0.2638 0.2274 0.0695 -0.0063 -0.0861 189 ASP A OD2 1364 N N . ALA A 175 ? 0.1389 0.1705 0.1828 -0.0014 0.0680 0.0460 190 ALA A N 1365 C CA . ALA A 175 ? 0.2059 0.1594 0.1979 -0.0326 0.0635 0.0583 190 ALA A CA 1366 C C . ALA A 175 ? 0.2029 0.1635 0.1695 -0.0639 0.0706 -0.0092 190 ALA A C 1367 O O . ALA A 175 ? 0.1878 0.2492 0.1663 -0.0590 0.0248 0.0215 190 ALA A O 1368 C CB . ALA A 175 ? 0.1200 0.2460 0.2510 -0.0064 0.0331 0.0526 190 ALA A CB 1369 N N . SER A 176 ? 0.2069 0.1461 0.1608 -0.0107 0.0193 0.0084 191 SER A N 1370 C CA . SER A 176 ? 0.1484 0.1666 0.3077 -0.0591 0.0105 -0.0050 191 SER A CA 1371 C C . SER A 176 ? 0.2125 0.0974 0.1908 -0.0288 0.0764 0.0003 191 SER A C 1372 O O . SER A 176 ? 0.3022 0.1751 0.1869 -0.0203 0.0121 0.0594 191 SER A O 1373 C CB . SER A 176 ? 0.1940 0.1736 0.2616 -0.0678 0.0348 0.0063 191 SER A CB 1374 O OG . SER A 176 ? 0.2165 0.2640 0.2691 -0.0877 0.0330 0.0005 191 SER A OG 1375 N N . GLY A 177 ? 0.1694 0.1797 0.1777 -0.0578 0.0561 0.0354 192 GLY A N 1376 C CA . GLY A 177 ? 0.1984 0.1498 0.1318 -0.0816 0.0339 -0.0198 192 GLY A CA 1377 C C . GLY A 177 ? 0.1272 0.1720 0.1846 0.0263 0.0223 0.0162 192 GLY A C 1378 O O . GLY A 177 ? 0.1875 0.1691 0.1982 0.0368 0.0060 0.0135 192 GLY A O 1379 N N . HIS A 178 ? 0.1616 0.2039 0.1388 0.0210 0.0668 0.0069 193 HIS A N 1380 C CA . HIS A 178 ? 0.2178 0.0881 0.1438 -0.0094 0.0747 0.0064 193 HIS A CA 1381 C C . HIS A 178 ? 0.1804 0.1526 0.2159 -0.0709 0.0265 0.0433 193 HIS A C 1382 O O . HIS A 178 ? 0.1694 0.2377 0.1990 -0.0005 -0.0026 -0.0259 193 HIS A O 1383 C CB . HIS A 178 ? 0.2173 0.0924 0.2246 -0.0472 0.0095 -0.0131 193 HIS A CB 1384 C CG . HIS A 178 ? 0.1338 0.1216 0.2281 -0.0456 0.0210 0.0140 193 HIS A CG 1385 N ND1 . HIS A 178 ? 0.1850 0.1652 0.1179 -0.0593 0.0350 0.0156 193 HIS A ND1 1386 C CD2 . HIS A 178 ? 0.1305 0.2914 0.2066 0.0591 0.0291 -0.0174 193 HIS A CD2 1387 C CE1 . HIS A 178 ? 0.1811 0.2422 0.1392 0.0280 0.0250 0.0107 193 HIS A CE1 1388 N NE2 . HIS A 178 ? 0.1650 0.1321 0.1546 -0.0219 0.0424 0.0540 193 HIS A NE2 1389 N N . LYS A 179 ? 0.1907 0.1588 0.1556 -0.0415 0.0534 0.0458 194 LYS A N 1390 C CA . LYS A 179 ? 0.2205 0.1656 0.1714 -0.0328 0.0505 0.0654 194 LYS A CA 1391 C C . LYS A 179 ? 0.3082 0.1027 0.1911 -0.0164 -0.0411 0.0179 194 LYS A C 1392 O O . LYS A 179 ? 0.3299 0.2544 0.1667 -0.0377 -0.0349 0.0286 194 LYS A O 1393 C CB . LYS A 179 ? 0.2309 0.1666 0.3018 -0.0479 0.0747 0.0557 194 LYS A CB 1394 C CG . LYS A 179 ? 0.2635 0.2644 0.2479 -0.0735 0.0770 0.0853 194 LYS A CG 1395 C CD . LYS A 179 ? 0.3123 0.2278 0.3040 -0.0912 0.0534 0.0951 194 LYS A CD 1396 C CE . LYS A 179 ? 0.3426 0.4149 0.4112 -0.0863 0.0762 0.1741 194 LYS A CE 1397 N NZ . LYS A 179 ? 0.4560 0.4456 0.6183 -0.0437 0.1151 -0.0424 194 LYS A NZ 1398 N N . TYR A 180 ? 0.3299 0.1222 0.2241 0.0282 0.0692 -0.0255 195 TYR A N 1399 C CA . TYR A 180 ? 0.3111 0.1370 0.2674 -0.0563 0.0838 -0.0509 195 TYR A CA 1400 C C . TYR A 180 ? 0.3397 0.1818 0.1062 0.0128 -0.0094 0.0202 195 TYR A C 1401 O O . TYR A 180 ? 0.4534 0.2543 0.1896 0.0219 -0.1036 0.0222 195 TYR A O 1402 C CB . TYR A 180 ? 0.2944 0.1830 0.2267 -0.0858 0.0127 0.0666 195 TYR A CB 1403 C CG . TYR A 180 ? 0.3207 0.2372 0.3013 -0.0299 0.1066 -0.0157 195 TYR A CG 1404 C CD1 . TYR A 180 ? 0.3337 0.1596 0.2975 -0.0948 0.0187 0.0337 195 TYR A CD1 1405 C CD2 . TYR A 180 ? 0.3826 0.2198 0.2458 -0.0839 0.1039 0.0344 195 TYR A CD2 1406 C CE1 . TYR A 180 ? 0.3580 0.1750 0.3930 -0.0398 0.0592 0.0909 195 TYR A CE1 1407 C CE2 . TYR A 180 ? 0.3391 0.2941 0.2738 -0.0955 0.0977 0.0641 195 TYR A CE2 1408 C CZ . TYR A 180 ? 0.3798 0.2119 0.4223 -0.0584 0.1156 -0.0003 195 TYR A CZ 1409 O OH . TYR A 180 ? 0.3968 0.3424 0.5807 -0.0680 0.1886 0.0497 195 TYR A OH 1410 N N . GLY A 181 ? 0.3406 0.1618 0.1623 0.0049 0.0062 0.0065 196 GLY A N 1411 C CA . GLY A 181 ? 0.2364 0.2611 0.2645 0.0330 -0.0411 0.0004 196 GLY A CA 1412 C C . GLY A 181 ? 0.2840 0.1026 0.1847 -0.0251 -0.0704 0.0209 196 GLY A C 1413 O O . GLY A 181 ? 0.2948 0.1536 0.2403 -0.0314 0.0018 -0.0179 196 GLY A O 1414 N N . PRO A 182 ? 0.3381 0.1605 0.2226 -0.0382 -0.0286 0.0214 197 PRO A N 1415 C CA . PRO A 182 ? 0.3302 0.1113 0.2839 -0.0048 -0.0477 -0.0303 197 PRO A CA 1416 C C . PRO A 182 ? 0.3728 0.2538 0.2820 0.0200 0.0472 0.0058 197 PRO A C 1417 O O . PRO A 182 ? 0.3503 0.2945 0.3694 0.0121 0.0673 -0.1208 197 PRO A O 1418 C CB . PRO A 182 ? 0.3259 0.1919 0.2773 -0.0999 0.0123 0.0682 197 PRO A CB 1419 C CG . PRO A 182 ? 0.3112 0.2857 0.3133 -0.0599 0.0846 -0.0503 197 PRO A CG 1420 C CD . PRO A 182 ? 0.3346 0.1497 0.3296 -0.0197 -0.0901 0.0638 197 PRO A CD 1421 N N . GLU A 183 ? 0.3345 0.2170 0.3616 0.0149 0.0582 0.1372 198 GLU A N 1422 C CA . GLU A 183 ? 0.3164 0.2260 0.2463 -0.0494 -0.0060 0.0666 198 GLU A CA 1423 C C . GLU A 183 ? 0.3078 0.2871 0.2744 0.0558 0.0473 -0.0105 198 GLU A C 1424 O O . GLU A 183 ? 0.3259 0.3083 0.4205 0.0692 -0.0719 0.0403 198 GLU A O 1425 C CB . GLU A 183 ? 0.2795 0.3248 0.4236 -0.0808 0.0101 0.0953 198 GLU A CB 1426 C CG . GLU A 183 ? 0.3413 0.3163 0.4320 -0.0043 -0.0855 -0.0979 198 GLU A CG 1427 C CD . GLU A 183 ? 0.4101 0.5561 0.5603 0.1103 -0.0087 -0.0122 198 GLU A CD 1428 O OE1 . GLU A 183 ? 0.5104 0.5259 0.6378 0.0936 -0.1584 0.1446 198 GLU A OE1 1429 O OE2 . GLU A 183 ? 0.4455 0.5048 0.6536 0.0519 0.0062 0.1159 198 GLU A OE2 1430 N N . ASP A 184 ? 0.3083 0.1762 0.2702 -0.0325 0.0061 -0.0047 199 ASP A N 1431 C CA . ASP A 184 ? 0.3323 0.1039 0.2493 0.0271 0.0065 -0.0146 199 ASP A CA 1432 C C . ASP A 184 ? 0.3897 0.2414 0.3052 0.0864 -0.0238 0.0838 199 ASP A C 1433 O O . ASP A 184 ? 0.3148 0.1260 0.2778 0.0111 0.0014 0.0548 199 ASP A O 1434 C CB . ASP A 184 ? 0.3408 0.1336 0.2992 0.0051 0.0143 0.0774 199 ASP A CB 1435 C CG . ASP A 184 ? 0.4050 0.2049 0.1867 -0.0044 0.0506 0.0323 199 ASP A CG 1436 O OD1 . ASP A 184 ? 0.4830 0.2080 0.3975 -0.0097 0.0099 0.0415 199 ASP A OD1 1437 O OD2 . ASP A 184 ? 0.4706 0.2269 0.2188 -0.0568 0.0809 0.0075 199 ASP A OD2 1438 N N . LYS A 185 ? 0.4147 0.2735 0.2974 -0.0510 -0.0181 0.0373 200 LYS A N 1439 C CA . LYS A 185 ? 0.4077 0.1342 0.2505 -0.0229 0.0352 0.0342 200 LYS A CA 1440 C C . LYS A 185 ? 0.3917 0.1381 0.3229 -0.0192 0.0681 -0.0462 200 LYS A C 1441 O O . LYS A 185 ? 0.4302 0.1311 0.2692 -0.0005 0.0206 0.0172 200 LYS A O 1442 C CB . LYS A 185 ? 0.4334 0.2651 0.4070 0.0848 0.0858 -0.1276 200 LYS A CB 1443 C CG . LYS A 185 ? 0.4706 0.5197 0.5562 0.1172 0.0745 0.0740 200 LYS A CG 1444 C CD . LYS A 185 ? 0.4502 0.5929 0.6820 0.0686 0.1150 -0.0620 200 LYS A CD 1445 C CE . LYS A 185 ? 0.5173 0.7207 0.7690 0.0535 0.0101 -0.0181 200 LYS A CE 1446 N NZ . LYS A 185 ? 0.5353 0.8727 0.8870 0.0263 0.0033 -0.0301 200 LYS A NZ 1447 N N . GLU A 186 ? 0.3595 0.1825 0.3505 -0.0398 0.0423 -0.0123 201 GLU A N 1448 C CA . GLU A 186 ? 0.4279 0.1704 0.4638 -0.0790 -0.0287 -0.0123 201 GLU A CA 1449 C C . GLU A 186 ? 0.4324 0.2114 0.3771 -0.1202 0.0781 -0.0687 201 GLU A C 1450 O O . GLU A 186 ? 0.4173 0.2100 0.4462 -0.0915 0.1300 -0.0913 201 GLU A O 1451 C CB . GLU A 186 ? 0.4374 0.2690 0.3988 0.0322 0.0430 0.1699 201 GLU A CB 1452 C CG . GLU A 186 ? 0.5465 0.5535 0.4952 -0.0729 0.1247 0.0822 201 GLU A CG 1453 C CD . GLU A 186 ? 0.5972 0.6304 0.5405 -0.0873 -0.0131 0.0461 201 GLU A CD 1454 O OE1 . GLU A 186 ? 0.6119 0.7821 0.7194 -0.0652 0.0050 0.1752 201 GLU A OE1 1455 O OE2 . GLU A 186 ? 0.6332 0.6453 0.5058 -0.0375 -0.0873 0.0493 201 GLU A OE2 1456 N N . ASN A 187 ? 0.4325 0.2698 0.2322 -0.0396 0.0400 0.0539 202 ASN A N 1457 C CA . ASN A 187 ? 0.3998 0.2080 0.1966 -0.0355 0.0995 0.0230 202 ASN A CA 1458 C C . ASN A 187 ? 0.3507 0.1985 0.2535 -0.0829 0.0766 0.0478 202 ASN A C 1459 O O . ASN A 187 ? 0.3618 0.1884 0.2784 -0.0463 0.0561 0.0257 202 ASN A O 1460 C CB . ASN A 187 ? 0.3896 0.1733 0.2831 0.0185 0.1289 0.0473 202 ASN A CB 1461 C CG . ASN A 187 ? 0.3764 0.3656 0.2927 -0.0153 0.1034 0.0706 202 ASN A CG 1462 O OD1 . ASN A 187 ? 0.4257 0.3294 0.2743 -0.0499 0.0874 0.0982 202 ASN A OD1 1463 N ND2 . ASN A 187 ? 0.4328 0.1942 0.2514 -0.0285 0.0373 0.0406 202 ASN A ND2 1464 N N . MET A 188 ? 0.3328 0.1092 0.2668 -0.0187 0.0411 0.0223 203 MET A N 1465 C CA . MET A 188 ? 0.3696 0.1891 0.2142 -0.0508 0.0817 0.0494 203 MET A CA 1466 C C . MET A 188 ? 0.3554 0.2954 0.2991 -0.0423 0.0951 0.1276 203 MET A C 1467 O O . MET A 188 ? 0.3521 0.1627 0.2617 -0.0610 0.0613 0.0053 203 MET A O 1468 C CB . MET A 188 ? 0.2811 0.2147 0.2313 -0.0846 0.0656 0.0564 203 MET A CB 1469 C CG . MET A 188 ? 0.3369 0.1675 0.2336 -0.0518 -0.0107 0.0069 203 MET A CG 1470 S SD . MET A 188 ? 0.3403 0.1966 0.2608 -0.0377 0.0336 0.0468 203 MET A SD 1471 C CE . MET A 188 ? 0.3756 0.2700 0.2054 -0.0600 0.0353 0.0638 203 MET A CE 1472 N N . SER A 189 ? 0.2893 0.1429 0.2476 -0.0752 0.0174 0.0331 204 SER A N 1473 C CA . SER A 189 ? 0.2866 0.1134 0.2979 -0.0565 -0.0097 -0.0323 204 SER A CA 1474 C C . SER A 189 ? 0.3436 0.1204 0.3237 -0.0224 0.0659 -0.0252 204 SER A C 1475 O O . SER A 189 ? 0.4041 0.1728 0.3093 -0.0542 0.0913 0.0126 204 SER A O 1476 C CB . SER A 189 ? 0.2857 0.1748 0.2808 -0.0767 0.0781 0.0362 204 SER A CB 1477 O OG . SER A 189 ? 0.4073 0.1767 0.3677 -0.0968 0.0879 -0.0192 204 SER A OG 1478 N N . ARG A 190 ? 0.3578 0.1327 0.2877 -0.0482 0.0641 0.0225 205 ARG A N 1479 C CA . ARG A 190 ? 0.3059 0.1159 0.2904 -0.0540 0.0345 0.0069 205 ARG A CA 1480 C C . ARG A 190 ? 0.3433 0.1886 0.3600 -0.0828 0.0477 0.0550 205 ARG A C 1481 O O . ARG A 190 ? 0.4348 0.1445 0.2464 -0.0702 0.0075 0.0048 205 ARG A O 1482 C CB . ARG A 190 ? 0.3852 0.3078 0.2355 0.0347 0.0993 0.0450 205 ARG A CB 1483 C CG . ARG A 190 ? 0.4424 0.2166 0.2830 -0.0559 0.0776 0.0315 205 ARG A CG 1484 C CD . ARG A 190 ? 0.4667 0.3852 0.2932 0.0375 0.1672 0.0707 205 ARG A CD 1485 N NE . ARG A 190 ? 0.4594 0.2203 0.5167 -0.0457 0.0757 0.1178 205 ARG A NE 1486 C CZ . ARG A 190 ? 0.4317 0.3275 0.4110 0.0259 0.0653 0.0779 205 ARG A CZ 1487 N NH1 . ARG A 190 ? 0.3965 0.3475 0.3970 0.0272 -0.0137 0.0992 205 ARG A NH1 1488 N NH2 . ARG A 190 ? 0.4216 0.4922 0.4348 0.0076 0.0482 -0.0146 205 ARG A NH2 1489 N N . VAL A 191 ? 0.3444 0.1713 0.2669 -0.0431 0.0946 0.0264 206 VAL A N 1490 C CA . VAL A 191 ? 0.2840 0.2325 0.1974 -0.1062 0.0756 0.0078 206 VAL A CA 1491 C C . VAL A 191 ? 0.2379 0.2414 0.2526 -0.0925 0.0458 0.0567 206 VAL A C 1492 O O . VAL A 191 ? 0.2844 0.2146 0.2543 -0.1157 0.0162 0.0223 206 VAL A O 1493 C CB . VAL A 191 ? 0.3192 0.1341 0.2201 -0.0597 0.0915 -0.0409 206 VAL A CB 1494 C CG1 . VAL A 191 ? 0.3275 0.1445 0.3192 -0.0054 0.0096 0.0508 206 VAL A CG1 1495 C CG2 . VAL A 191 ? 0.3279 0.2366 0.1742 -0.0466 0.0903 -0.0048 206 VAL A CG2 1496 N N . LEU A 192 ? 0.2430 0.1891 0.2142 -0.0704 0.0579 -0.0108 207 LEU A N 1497 C CA . LEU A 192 ? 0.2882 0.1735 0.2440 -0.0871 0.0681 0.0069 207 LEU A CA 1498 C C . LEU A 192 ? 0.3238 0.1543 0.3047 -0.0852 0.0499 0.0235 207 LEU A C 1499 O O . LEU A 192 ? 0.3602 0.1974 0.2308 -0.0626 0.0266 0.0029 207 LEU A O 1500 C CB . LEU A 192 ? 0.2665 0.2422 0.2449 -0.1266 0.0743 -0.0489 207 LEU A CB 1501 C CG . LEU A 192 ? 0.2453 0.1605 0.2161 -0.0906 -0.0007 -0.0293 207 LEU A CG 1502 C CD1 . LEU A 192 ? 0.2975 0.1612 0.2624 -0.1011 0.0395 -0.0174 207 LEU A CD1 1503 C CD2 . LEU A 192 ? 0.2739 0.2191 0.2615 -0.0126 0.0442 0.0933 207 LEU A CD2 1504 N N . LYS A 193 ? 0.3506 0.2002 0.2935 -0.1001 0.0484 -0.0867 208 LYS A N 1505 C CA . LYS A 193 ? 0.4271 0.1609 0.2445 -0.0954 0.0077 -0.0100 208 LYS A CA 1506 C C . LYS A 193 ? 0.4160 0.2292 0.2968 -0.1453 0.0324 0.0285 208 LYS A C 1507 O O . LYS A 193 ? 0.3588 0.3556 0.2748 -0.1572 0.0485 0.0306 208 LYS A O 1508 C CB . LYS A 193 ? 0.4850 0.2220 0.3876 -0.1135 0.0035 0.0629 208 LYS A CB 1509 C CG . LYS A 193 ? 0.5108 0.5009 0.4328 -0.0721 0.1070 -0.0030 208 LYS A CG 1510 C CD . LYS A 193 ? 0.5274 0.5656 0.5356 0.0158 0.0336 -0.1346 208 LYS A CD 1511 C CE . LYS A 193 ? 0.5662 0.4957 0.6243 0.0245 0.0260 -0.0571 208 LYS A CE 1512 N NZ . LYS A 193 ? 0.5579 0.4763 0.6636 -0.0819 0.0349 -0.1586 208 LYS A NZ 1513 N N . LYS A 194 ? 0.3459 0.1572 0.3048 -0.0814 0.0929 -0.0367 209 LYS A N 1514 C CA . LYS A 194 ? 0.3326 0.2427 0.2925 -0.0890 0.1363 0.0036 209 LYS A CA 1515 C C . LYS A 194 ? 0.2766 0.2300 0.2467 -0.0913 0.0954 0.0221 209 LYS A C 1516 O O . LYS A 194 ? 0.3253 0.2744 0.2791 -0.1095 0.0246 -0.0424 209 LYS A O 1517 C CB . LYS A 194 ? 0.3024 0.3158 0.2305 -0.1234 0.0958 0.0022 209 LYS A CB 1518 C CG . LYS A 194 ? 0.3264 0.3557 0.4640 -0.1683 0.0711 -0.0974 209 LYS A CG 1519 C CD . LYS A 194 ? 0.3672 0.3967 0.3528 -0.0993 0.1720 -0.0301 209 LYS A CD 1520 C CE . LYS A 194 ? 0.4733 0.5760 0.4944 -0.0088 0.2196 -0.0595 209 LYS A CE 1521 N NZ . LYS A 194 ? 0.6018 0.6310 0.4784 -0.0228 0.1113 -0.0168 209 LYS A NZ 1522 N N . ILE A 195 ? 0.2683 0.1987 0.2629 -0.1053 0.0656 0.0088 210 ILE A N 1523 C CA . ILE A 195 ? 0.3214 0.2108 0.2132 -0.1324 0.0537 -0.0374 210 ILE A CA 1524 C C . ILE A 195 ? 0.3610 0.2311 0.3183 -0.1223 0.0846 0.0304 210 ILE A C 1525 O O . ILE A 195 ? 0.3582 0.2576 0.2397 -0.1647 0.0147 -0.0092 210 ILE A O 1526 C CB . ILE A 195 ? 0.2792 0.2080 0.2041 -0.1235 0.0478 -0.0471 210 ILE A CB 1527 C CG1 . ILE A 195 ? 0.3028 0.2460 0.1927 -0.0776 0.0334 -0.0847 210 ILE A CG1 1528 C CG2 . ILE A 195 ? 0.2673 0.3248 0.1976 -0.1347 0.0114 0.0606 210 ILE A CG2 1529 C CD1 . ILE A 195 ? 0.3683 0.1899 0.2094 -0.0675 0.0306 0.0535 210 ILE A CD1 1530 N N . ASP A 196 ? 0.3632 0.2510 0.2388 -0.1545 0.0682 -0.0615 211 ASP A N 1531 C CA . ASP A 196 ? 0.3385 0.2536 0.3688 -0.0471 0.0859 -0.0841 211 ASP A CA 1532 C C . ASP A 196 ? 0.3897 0.2208 0.2483 -0.1453 0.0386 -0.0091 211 ASP A C 1533 O O . ASP A 196 ? 0.4021 0.3128 0.2629 -0.1838 0.0396 -0.0712 211 ASP A O 1534 C CB . ASP A 196 ? 0.4068 0.2388 0.1963 -0.0888 0.0837 -0.0767 211 ASP A CB 1535 C CG . ASP A 196 ? 0.4743 0.2868 0.3417 -0.1729 0.0477 -0.0546 211 ASP A CG 1536 O OD1 . ASP A 196 ? 0.3656 0.1974 0.2976 -0.0455 -0.0025 -0.0422 211 ASP A OD1 1537 O OD2 . ASP A 196 ? 0.5328 0.2455 0.2486 -0.0924 0.0959 -0.0193 211 ASP A OD2 1538 N N . ASP A 197 ? 0.3363 0.2300 0.2179 -0.1398 0.0644 -0.0305 212 ASP A N 1539 C CA . ASP A 197 ? 0.3523 0.2910 0.3091 -0.1773 -0.0238 0.0112 212 ASP A CA 1540 C C . ASP A 197 ? 0.3484 0.2707 0.3283 -0.1626 0.0349 0.0212 212 ASP A C 1541 O O . ASP A 197 ? 0.3404 0.4418 0.3439 -0.2141 0.0059 -0.0288 212 ASP A O 1542 C CB . ASP A 197 ? 0.3861 0.3784 0.3672 -0.1620 0.1141 -0.0333 212 ASP A CB 1543 C CG . ASP A 197 ? 0.4804 0.4098 0.4908 -0.2069 0.0501 -0.0656 212 ASP A CG 1544 O OD1 . ASP A 197 ? 0.5214 0.2057 0.4158 -0.1285 -0.0178 0.0297 212 ASP A OD1 1545 O OD2 . ASP A 197 ? 0.5721 0.3110 0.4959 -0.1914 0.0170 0.0908 212 ASP A OD2 1546 N N . LEU A 198 ? 0.3199 0.2217 0.2998 -0.1391 0.0375 -0.0132 213 LEU A N 1547 C CA . LEU A 198 ? 0.3441 0.1789 0.2288 -0.1146 0.0470 -0.0110 213 LEU A CA 1548 C C . LEU A 198 ? 0.3677 0.3229 0.3247 -0.1145 0.0461 -0.0935 213 LEU A C 1549 O O . LEU A 198 ? 0.3108 0.3027 0.2966 -0.1513 0.0265 -0.0920 213 LEU A O 1550 C CB . LEU A 198 ? 0.3095 0.2105 0.2322 -0.1110 0.0253 -0.0731 213 LEU A CB 1551 C CG . LEU A 198 ? 0.2953 0.4175 0.1871 -0.1486 0.0673 -0.0580 213 LEU A CG 1552 C CD1 . LEU A 198 ? 0.3127 0.2148 0.2209 -0.0901 -0.0399 0.0373 213 LEU A CD1 1553 C CD2 . LEU A 198 ? 0.2445 0.4335 0.3160 -0.1629 -0.0016 -0.0295 213 LEU A CD2 1554 N N . ILE A 199 ? 0.3516 0.2063 0.2270 -0.1027 0.0485 -0.0793 214 ILE A N 1555 C CA . ILE A 199 ? 0.3349 0.2454 0.3021 -0.0522 0.0880 -0.1339 214 ILE A CA 1556 C C . ILE A 199 ? 0.3757 0.2725 0.2633 -0.1050 0.1257 -0.0463 214 ILE A C 1557 O O . ILE A 199 ? 0.3813 0.5091 0.2187 -0.2331 -0.0021 0.0276 214 ILE A O 1558 C CB . ILE A 199 ? 0.3223 0.2042 0.2936 -0.0968 0.0829 -0.0955 214 ILE A CB 1559 C CG1 . ILE A 199 ? 0.2711 0.3248 0.2971 -0.1553 -0.0223 -0.0218 214 ILE A CG1 1560 C CG2 . ILE A 199 ? 0.3075 0.4063 0.1926 -0.1879 0.0630 -0.0749 214 ILE A CG2 1561 C CD1 . ILE A 199 ? 0.3193 0.4270 0.2506 -0.1850 -0.0667 0.0179 214 ILE A CD1 1562 N N . GLY A 200 ? 0.3650 0.4196 0.3357 -0.2021 0.0279 -0.0990 215 GLY A N 1563 C CA . GLY A 200 ? 0.4348 0.3233 0.3296 -0.1492 0.0293 -0.1322 215 GLY A CA 1564 C C . GLY A 200 ? 0.4267 0.3129 0.3571 -0.1447 -0.0698 -0.0542 215 GLY A C 1565 O O . GLY A 200 ? 0.4101 0.4119 0.3837 -0.2268 0.0464 -0.0776 215 GLY A O 1566 N N . ASP A 201 ? 0.4476 0.3496 0.3373 -0.1844 -0.0435 -0.0754 216 ASP A N 1567 C CA . ASP A 201 ? 0.3310 0.4449 0.2637 -0.1495 -0.0415 -0.0910 216 ASP A CA 1568 C C . ASP A 201 ? 0.3203 0.4162 0.3673 -0.1982 0.0055 -0.0476 216 ASP A C 1569 O O . ASP A 201 ? 0.3061 0.4196 0.3241 -0.1757 -0.0463 -0.0430 216 ASP A O 1570 C CB . ASP A 201 ? 0.3294 0.4632 0.1835 -0.1495 0.0103 -0.0096 216 ASP A CB 1571 C CG . ASP A 201 ? 0.3931 0.3802 0.4212 -0.0626 0.0186 -0.0821 216 ASP A CG 1572 O OD1 . ASP A 201 ? 0.4117 0.4616 0.3378 -0.2003 0.0489 -0.0440 216 ASP A OD1 1573 O OD2 . ASP A 201 ? 0.4005 0.4447 0.3706 -0.1020 0.0828 -0.0552 216 ASP A OD2 1574 N N . LEU A 202 ? 0.3862 0.4995 0.2556 -0.1896 0.0289 0.0497 217 LEU A N 1575 C CA . LEU A 202 ? 0.3470 0.3680 0.2593 -0.1858 -0.0237 -0.0426 217 LEU A CA 1576 C C . LEU A 202 ? 0.3606 0.3682 0.3490 -0.0810 -0.0871 0.0649 217 LEU A C 1577 O O . LEU A 202 ? 0.3394 0.5118 0.2628 -0.1925 -0.0298 0.0466 217 LEU A O 1578 C CB . LEU A 202 ? 0.3261 0.2970 0.2844 -0.1679 -0.0007 -0.0419 217 LEU A CB 1579 C CG . LEU A 202 ? 0.3849 0.3215 0.2866 -0.1942 -0.0420 0.0325 217 LEU A CG 1580 C CD1 . LEU A 202 ? 0.4460 0.2827 0.2033 -0.1322 0.0242 -0.0058 217 LEU A CD1 1581 C CD2 . LEU A 202 ? 0.3612 0.3989 0.3017 -0.2137 -0.0228 0.0051 217 LEU A CD2 1582 N N . VAL A 203 ? 0.3495 0.2528 0.2450 -0.1452 -0.0356 -0.0325 218 VAL A N 1583 C CA . VAL A 203 ? 0.2989 0.3893 0.2266 -0.0860 -0.0264 -0.0907 218 VAL A CA 1584 C C . VAL A 203 ? 0.3399 0.3885 0.3241 -0.1882 -0.0613 -0.0177 218 VAL A C 1585 O O . VAL A 203 ? 0.2935 0.5505 0.3099 -0.1673 -0.0260 -0.0861 218 VAL A O 1586 C CB . VAL A 203 ? 0.2979 0.4093 0.3759 -0.1446 0.0415 -0.1588 218 VAL A CB 1587 C CG1 . VAL A 203 ? 0.2992 0.5129 0.2301 -0.1586 -0.0265 -0.0277 218 VAL A CG1 1588 C CG2 . VAL A 203 ? 0.2663 0.4436 0.3051 -0.1720 0.0043 -0.0621 218 VAL A CG2 1589 N N . GLN A 204 ? 0.2516 0.3677 0.3109 -0.1358 -0.0315 -0.0775 219 GLN A N 1590 C CA . GLN A 204 ? 0.2870 0.4233 0.3258 -0.1404 -0.0830 -0.0528 219 GLN A CA 1591 C C . GLN A 204 ? 0.3337 0.3120 0.3068 -0.1615 -0.0168 -0.0678 219 GLN A C 1592 O O . GLN A 204 ? 0.3451 0.4922 0.3159 -0.2123 0.0337 -0.1047 219 GLN A O 1593 C CB . GLN A 204 ? 0.3985 0.5382 0.4420 -0.1393 -0.0671 0.1539 219 GLN A CB 1594 C CG . GLN A 204 ? 0.5203 0.7103 0.6988 -0.1607 0.0438 -0.0200 219 GLN A CG 1595 C CD . GLN A 204 ? 0.6033 0.8979 0.8982 -0.0435 0.0616 0.0477 219 GLN A CD 1596 O OE1 . GLN A 204 ? 0.6137 0.9891 1.0384 -0.0407 0.1363 -0.0224 219 GLN A OE1 1597 N NE2 . GLN A 204 ? 0.6406 0.8273 0.8213 -0.0042 -0.0334 0.2207 219 GLN A NE2 1598 N N . ARG A 205 ? 0.3880 0.2197 0.3405 -0.1353 -0.0048 -0.0553 220 ARG A N 1599 C CA . ARG A 205 ? 0.2890 0.4254 0.3061 -0.1675 0.0100 0.0181 220 ARG A CA 1600 C C . ARG A 205 ? 0.3036 0.5524 0.3198 -0.1443 -0.0181 -0.0606 220 ARG A C 1601 O O . ARG A 205 ? 0.3220 0.5304 0.2858 -0.2146 -0.0079 -0.0334 220 ARG A O 1602 C CB . ARG A 205 ? 0.3593 0.3088 0.2430 -0.1215 -0.0015 0.0209 220 ARG A CB 1603 C CG . ARG A 205 ? 0.2645 0.3619 0.3861 -0.0695 -0.0747 0.0462 220 ARG A CG 1604 C CD . ARG A 205 ? 0.3727 0.4716 0.2740 0.0508 -0.0889 -0.0512 220 ARG A CD 1605 N NE . ARG A 205 ? 0.2781 0.3129 0.3815 -0.1101 -0.0816 -0.0353 220 ARG A NE 1606 C CZ . ARG A 205 ? 0.2990 0.5356 0.2489 -0.1108 -0.0973 0.0235 220 ARG A CZ 1607 N NH1 . ARG A 205 ? 0.3824 0.6690 0.5357 -0.1720 -0.0815 -0.0424 220 ARG A NH1 1608 N NH2 . ARG A 205 ? 0.3477 0.4193 0.3631 0.0211 -0.0841 0.0243 220 ARG A NH2 1609 N N . LEU A 206 ? 0.3430 0.3525 0.2855 -0.1934 0.0280 0.0018 221 LEU A N 1610 C CA . LEU A 206 ? 0.3112 0.3144 0.3426 -0.1692 0.0264 -0.0572 221 LEU A CA 1611 C C . LEU A 206 ? 0.3078 0.2257 0.3598 -0.1278 -0.0399 -0.0505 221 LEU A C 1612 O O . LEU A 206 ? 0.3061 0.5836 0.3162 -0.1771 -0.0754 -0.0029 221 LEU A O 1613 C CB . LEU A 206 ? 0.2914 0.3933 0.3287 -0.1469 -0.0283 -0.0988 221 LEU A CB 1614 C CG . LEU A 206 ? 0.3055 0.3831 0.2980 -0.1891 0.0176 -0.0147 221 LEU A CG 1615 C CD1 . LEU A 206 ? 0.3299 0.3975 0.3567 -0.1955 -0.0566 0.0088 221 LEU A CD1 1616 C CD2 . LEU A 206 ? 0.2878 0.3564 0.2649 -0.1239 0.0072 -0.0298 221 LEU A CD2 1617 N N . LYS A 207 ? 0.3621 0.3923 0.2783 -0.1543 0.0292 -0.1207 222 LYS A N 1618 C CA . LYS A 207 ? 0.3174 0.2336 0.2497 -0.0589 0.0057 0.0160 222 LYS A CA 1619 C C . LYS A 207 ? 0.2958 0.3573 0.3680 -0.1662 -0.0069 -0.0709 222 LYS A C 1620 O O . LYS A 207 ? 0.3063 0.5687 0.3598 -0.1849 -0.0277 -0.0891 222 LYS A O 1621 C CB . LYS A 207 ? 0.3428 0.3441 0.3745 -0.0950 0.0961 -0.1267 222 LYS A CB 1622 C CG . LYS A 207 ? 0.3424 0.3827 0.3350 -0.0669 -0.0005 -0.0650 222 LYS A CG 1623 C CD . LYS A 207 ? 0.3928 0.4256 0.4625 -0.0458 -0.0019 -0.0894 222 LYS A CD 1624 C CE . LYS A 207 ? 0.4225 0.3557 0.4546 -0.0906 -0.1800 0.0043 222 LYS A CE 1625 N NZ . LYS A 207 ? 0.4429 0.5269 0.6604 -0.1111 -0.1591 -0.0984 222 LYS A NZ 1626 N N . MET A 208 ? 0.3232 0.4676 0.3249 -0.1792 -0.0234 -0.0954 223 MET A N 1627 C CA . MET A 208 ? 0.3981 0.5413 0.4179 -0.1751 -0.0714 -0.1301 223 MET A CA 1628 C C . MET A 208 ? 0.3577 0.4442 0.3617 -0.2048 -0.0606 -0.0282 223 MET A C 1629 O O . MET A 208 ? 0.3857 0.5793 0.3535 -0.2326 -0.0255 -0.0634 223 MET A O 1630 C CB . MET A 208 ? 0.5008 0.6046 0.3773 -0.1297 0.0968 -0.0380 223 MET A CB 1631 C CG . MET A 208 ? 0.6815 0.7361 0.5740 0.0182 0.0630 0.0288 223 MET A CG 1632 S SD . MET A 208 ? 0.7612 1.0522 1.0052 -0.0291 -0.0721 0.1212 223 MET A SD 1633 C CE . MET A 208 ? 0.7272 0.6657 0.7360 -0.0545 -0.0435 0.0830 223 MET A CE 1634 N N . LEU A 209 ? 0.3841 0.5017 0.4411 -0.2148 0.0654 -0.1310 224 LEU A N 1635 C CA . LEU A 209 ? 0.3368 0.4023 0.3079 -0.1357 -0.0373 -0.0046 224 LEU A CA 1636 C C . LEU A 209 ? 0.3645 0.4669 0.4157 -0.1066 -0.0118 0.0237 224 LEU A C 1637 O O . LEU A 209 ? 0.4144 0.5804 0.4846 -0.1812 -0.0887 0.1276 224 LEU A O 1638 C CB . LEU A 209 ? 0.4119 0.5394 0.3116 -0.1656 0.0100 -0.1180 224 LEU A CB 1639 C CG . LEU A 209 ? 0.4484 0.5382 0.4034 -0.1635 -0.0881 -0.0099 224 LEU A CG 1640 C CD1 . LEU A 209 ? 0.5163 0.4153 0.4827 -0.1796 -0.0213 0.0768 224 LEU A CD1 1641 C CD2 . LEU A 209 ? 0.4172 0.5036 0.5072 -0.1062 0.0981 0.0117 224 LEU A CD2 1642 N N . GLY A 210 ? 0.3334 0.5502 0.3572 -0.1819 -0.0539 -0.0809 225 GLY A N 1643 C CA . GLY A 210 ? 0.4098 0.6170 0.3569 -0.1793 0.0067 -0.1043 225 GLY A CA 1644 C C . GLY A 210 ? 0.4082 0.4965 0.2875 -0.1710 0.0734 0.0750 225 GLY A C 1645 O O . GLY A 210 ? 0.4477 0.6721 0.2600 -0.2949 -0.0318 0.0659 225 GLY A O 1646 N N . LEU A 211 ? 0.3799 0.5161 0.3157 -0.0932 -0.0043 -0.1311 226 LEU A N 1647 C CA . LEU A 211 ? 0.3493 0.4896 0.3201 -0.0899 0.0962 -0.1541 226 LEU A CA 1648 C C . LEU A 211 ? 0.3919 0.3381 0.2301 -0.2012 0.0101 0.0069 226 LEU A C 1649 O O . LEU A 211 ? 0.4091 0.5290 0.2431 -0.2557 0.0482 -0.0774 226 LEU A O 1650 C CB . LEU A 211 ? 0.3812 0.4551 0.4123 -0.1380 -0.0193 -0.0944 226 LEU A CB 1651 C CG . LEU A 211 ? 0.4469 0.3634 0.3367 -0.0249 -0.0409 0.1249 226 LEU A CG 1652 C CD1 . LEU A 211 ? 0.3834 0.4689 0.3681 -0.1811 -0.1243 -0.0140 226 LEU A CD1 1653 C CD2 . LEU A 211 ? 0.4112 0.5566 0.5080 -0.1357 0.0014 -0.0077 226 LEU A CD2 1654 N N . TRP A 212 ? 0.3302 0.4584 0.2919 -0.1928 0.0065 -0.0624 227 TRP A N 1655 C CA . TRP A 212 ? 0.3639 0.3360 0.3208 -0.1542 0.0258 -0.0276 227 TRP A CA 1656 C C . TRP A 212 ? 0.3900 0.4762 0.2542 -0.1435 -0.0340 -0.1141 227 TRP A C 1657 O O . TRP A 212 ? 0.3338 0.5329 0.3787 -0.2102 0.0043 -0.0971 227 TRP A O 1658 C CB . TRP A 212 ? 0.3764 0.2988 0.2659 -0.1029 -0.0609 -0.1012 227 TRP A CB 1659 C CG . TRP A 212 ? 0.4024 0.3603 0.3624 -0.1545 0.0230 -0.1477 227 TRP A CG 1660 C CD1 . TRP A 212 ? 0.3640 0.4293 0.3174 -0.1206 0.0214 -0.0030 227 TRP A CD1 1661 C CD2 . TRP A 212 ? 0.3326 0.4311 0.2278 -0.1583 0.0432 -0.1211 227 TRP A CD2 1662 N NE1 . TRP A 212 ? 0.4292 0.4664 0.2855 -0.1714 -0.0338 -0.0902 227 TRP A NE1 1663 C CE2 . TRP A 212 ? 0.4201 0.3612 0.2610 -0.1376 0.0413 -0.1022 227 TRP A CE2 1664 C CE3 . TRP A 212 ? 0.3411 0.2829 0.3013 -0.1538 0.0013 -0.0737 227 TRP A CE3 1665 C CZ2 . TRP A 212 ? 0.3521 0.5156 0.3815 -0.1597 -0.0434 -0.0585 227 TRP A CZ2 1666 C CZ3 . TRP A 212 ? 0.3142 0.3190 0.3287 -0.1394 -0.0240 -0.0281 227 TRP A CZ3 1667 C CH2 . TRP A 212 ? 0.4197 0.3753 0.3183 -0.1435 0.0977 -0.0091 227 TRP A CH2 1668 N N . GLU A 213 ? 0.5062 0.5677 0.2507 -0.1978 0.0344 -0.1199 228 GLU A N 1669 C CA . GLU A 213 ? 0.5046 0.5507 0.2158 -0.1767 0.0484 -0.0819 228 GLU A CA 1670 C C . GLU A 213 ? 0.5144 0.4646 0.3654 -0.1699 0.0308 -0.0573 228 GLU A C 1671 O O . GLU A 213 ? 0.4904 0.6000 0.5014 -0.1609 0.1645 0.0094 228 GLU A O 1672 C CB . GLU A 213 ? 0.6144 0.4207 0.3629 -0.0556 0.1125 -0.1392 228 GLU A CB 1673 C CG . GLU A 213 ? 0.7127 0.6749 0.5920 -0.1041 0.0091 -0.1038 228 GLU A CG 1674 C CD . GLU A 213 ? 0.8060 0.8868 0.8990 0.0047 -0.0009 0.0358 228 GLU A CD 1675 O OE1 . GLU A 213 ? 0.8518 0.9446 0.9711 0.0059 0.0432 0.0134 228 GLU A OE1 1676 O OE2 . GLU A 213 ? 0.8073 0.9654 1.0033 0.0481 -0.0188 0.0256 228 GLU A OE2 1677 N N . ASN A 214 ? 0.4170 0.5276 0.2165 -0.1528 -0.0299 -0.0755 229 ASN A N 1678 C CA . ASN A 214 ? 0.4365 0.2691 0.3802 -0.1186 -0.0261 -0.0421 229 ASN A CA 1679 C C . ASN A 214 ? 0.4314 0.4433 0.2701 -0.1871 0.0499 0.0259 229 ASN A C 1680 O O . ASN A 214 ? 0.5292 0.5133 0.2212 -0.2288 0.0114 0.0436 229 ASN A O 1681 C CB . ASN A 214 ? 0.4811 0.5793 0.4399 -0.1647 -0.0123 -0.1405 229 ASN A CB 1682 C CG . ASN A 214 ? 0.5339 0.6896 0.6907 -0.0830 0.0057 -0.0222 229 ASN A CG 1683 O OD1 . ASN A 214 ? 0.6267 0.8084 0.7293 -0.0104 -0.0414 0.0016 229 ASN A OD1 1684 N ND2 . ASN A 214 ? 0.5837 0.7481 0.6643 -0.0301 -0.0523 0.0011 229 ASN A ND2 1685 N N . LEU A 215 ? 0.3542 0.5042 0.2791 -0.1116 -0.0595 -0.1227 230 LEU A N 1686 C CA . LEU A 215 ? 0.2932 0.4248 0.3004 -0.1880 0.0480 -0.0471 230 LEU A CA 1687 C C . LEU A 215 ? 0.2374 0.4252 0.2289 -0.1495 0.0092 -0.0103 230 LEU A C 1688 O O . LEU A 215 ? 0.3202 0.4615 0.2863 -0.1303 -0.0638 -0.1003 230 LEU A O 1689 C CB . LEU A 215 ? 0.3150 0.3752 0.1687 -0.1889 0.0430 -0.0538 230 LEU A CB 1690 C CG . LEU A 215 ? 0.2766 0.3972 0.2089 -0.1383 0.0098 -0.0392 230 LEU A CG 1691 C CD1 . LEU A 215 ? 0.2423 0.4250 0.2623 -0.0326 0.0044 0.0370 230 LEU A CD1 1692 C CD2 . LEU A 215 ? 0.2644 0.5133 0.2173 -0.1793 0.0041 0.0202 230 LEU A CD2 1693 N N . ASN A 216 ? 0.2495 0.3974 0.1767 -0.1230 -0.0218 -0.0502 231 ASN A N 1694 C CA . ASN A 216 ? 0.2459 0.3440 0.1757 -0.1428 0.0144 0.0253 231 ASN A CA 1695 C C . ASN A 216 ? 0.2468 0.4324 0.2476 -0.0657 0.0497 0.0575 231 ASN A C 1696 O O . ASN A 216 ? 0.2459 0.4283 0.1551 -0.0914 -0.0320 -0.0275 231 ASN A O 1697 C CB . ASN A 216 ? 0.2446 0.4336 0.1488 -0.1125 -0.0106 -0.0323 231 ASN A CB 1698 C CG . ASN A 216 ? 0.1644 0.4189 0.1297 -0.0745 0.0043 -0.0309 231 ASN A CG 1699 O OD1 . ASN A 216 ? 0.2328 0.4994 0.1670 -0.1095 0.0137 0.0030 231 ASN A OD1 1700 N ND2 . ASN A 216 ? 0.2775 0.6074 0.2144 -0.0596 -0.0677 0.0397 231 ASN A ND2 1701 N N . VAL A 217 ? 0.2858 0.3404 0.1632 -0.1603 -0.0209 -0.0089 232 VAL A N 1702 C CA . VAL A 217 ? 0.2372 0.3344 0.1439 -0.1474 -0.0313 0.0346 232 VAL A CA 1703 C C . VAL A 217 ? 0.2297 0.2543 0.1932 -0.0689 -0.0492 -0.0119 232 VAL A C 1704 O O . VAL A 217 ? 0.2939 0.3354 0.1798 -0.1136 0.0255 -0.0670 232 VAL A O 1705 C CB . VAL A 217 ? 0.2127 0.3607 0.1438 -0.1204 -0.0193 -0.0058 232 VAL A CB 1706 C CG1 . VAL A 217 ? 0.2671 0.4129 0.1642 -0.1571 0.0245 0.0018 232 VAL A CG1 1707 C CG2 . VAL A 217 ? 0.3511 0.3200 0.2183 -0.1582 -0.0449 -0.0328 232 VAL A CG2 1708 N N . ILE A 218 ? 0.2113 0.2946 0.1647 -0.1168 0.0088 -0.0578 233 ILE A N 1709 C CA . ILE A 218 ? 0.1823 0.1954 0.2377 -0.0791 -0.0429 -0.0240 233 ILE A CA 1710 C C . ILE A 218 ? 0.2893 0.3586 0.1837 -0.0584 0.0186 -0.0367 233 ILE A C 1711 O O . ILE A 218 ? 0.2535 0.3596 0.1431 -0.0842 -0.0166 -0.0196 233 ILE A O 1712 C CB . ILE A 218 ? 0.2190 0.2699 0.1514 -0.1118 -0.0543 0.0268 233 ILE A CB 1713 C CG1 . ILE A 218 ? 0.2495 0.2358 0.1556 -0.0655 0.0245 0.0708 233 ILE A CG1 1714 C CG2 . ILE A 218 ? 0.2363 0.2998 0.1062 -0.0488 -0.0165 -0.0302 233 ILE A CG2 1715 C CD1 . ILE A 218 ? 0.2425 0.3286 0.1511 -0.1120 -0.0350 0.0570 233 ILE A CD1 1716 N N . ILE A 219 ? 0.2592 0.2993 0.1512 -0.1308 0.0292 -0.0084 234 ILE A N 1717 C CA . ILE A 219 ? 0.2373 0.2048 0.1476 -0.1071 -0.0413 0.0424 234 ILE A CA 1718 C C . ILE A 219 ? 0.2297 0.2472 0.1279 -0.0733 0.0368 -0.0288 234 ILE A C 1719 O O . ILE A 219 ? 0.2015 0.2707 0.1666 -0.0379 0.0266 -0.0240 234 ILE A O 1720 C CB . ILE A 219 ? 0.2325 0.2020 0.1434 -0.1074 -0.0025 -0.0269 234 ILE A CB 1721 C CG1 . ILE A 219 ? 0.2561 0.1267 0.2387 -0.0489 -0.0428 -0.0458 234 ILE A CG1 1722 C CG2 . ILE A 219 ? 0.2903 0.2726 0.1580 -0.1320 -0.0275 -0.0216 234 ILE A CG2 1723 C CD1 . ILE A 219 ? 0.3068 0.2261 0.2335 -0.1086 -0.0141 -0.0719 234 ILE A CD1 1724 N N . THR A 220 ? 0.1766 0.2287 0.1245 -0.0900 -0.0072 -0.0317 235 THR A N 1725 C CA . THR A 220 ? 0.2102 0.2870 0.1084 -0.1117 0.0032 -0.0018 235 THR A CA 1726 C C . THR A 220 ? 0.1850 0.2713 0.1415 -0.0853 0.0157 0.0458 235 THR A C 1727 O O . THR A 220 ? 0.1776 0.2625 0.1384 -0.0678 0.0120 -0.0035 235 THR A O 1728 C CB . THR A 220 ? 0.1726 0.2090 0.2217 -0.0783 -0.0032 0.0351 235 THR A CB 1729 O OG1 . THR A 220 ? 0.1542 0.2357 0.1946 -0.0522 -0.0113 -0.0113 235 THR A OG1 1730 C CG2 . THR A 220 ? 0.2521 0.1872 0.1712 -0.0602 0.0401 -0.0271 235 THR A CG2 1731 N N . SER A 221 ? 0.1469 0.1727 0.2208 -0.0479 -0.0179 -0.0270 236 SER A N 1732 C CA . SER A 221 ? 0.1740 0.1069 0.1566 -0.0479 0.0308 0.0256 236 SER A CA 1733 C C . SER A 221 ? 0.1801 0.2201 0.2085 -0.0916 0.0268 0.0335 236 SER A C 1734 O O . SER A 221 ? 0.1688 0.2206 0.1714 -0.0666 0.0084 0.0019 236 SER A O 1735 C CB . SER A 221 ? 0.1844 0.1540 0.1196 -0.0504 0.0455 0.0208 236 SER A CB 1736 O OG . SER A 221 ? 0.1842 0.2271 0.1123 -0.0235 0.0259 0.0069 236 SER A OG 1737 N N . ASP A 222 ? 0.2111 0.2463 0.1550 -0.0571 0.0087 0.0211 237 ASP A N 1738 C CA . ASP A 222 ? 0.1056 0.1670 0.1851 0.0383 -0.0169 0.0457 237 ASP A CA 1739 C C . ASP A 222 ? 0.1258 0.2174 0.1500 0.0371 0.0225 0.0894 237 ASP A C 1740 O O . ASP A 222 ? 0.1903 0.2065 0.1590 -0.0553 0.0189 0.0608 237 ASP A O 1741 C CB . ASP A 222 ? 0.1271 0.2571 0.1579 -0.0197 0.0282 0.0326 237 ASP A CB 1742 C CG . ASP A 222 ? 0.1326 0.2967 0.2998 0.0050 -0.0290 -0.0891 237 ASP A CG 1743 O OD1 . ASP A 222 ? 0.1649 0.2422 0.1281 -0.0509 -0.0040 -0.0087 237 ASP A OD1 1744 O OD2 . ASP A 222 ? 0.1474 0.1352 0.1649 -0.0208 -0.0142 0.0384 237 ASP A OD2 1745 N N . HIS A 223 ? 0.1618 0.1859 0.0835 -0.0010 -0.0327 -0.0309 238 HIS A N 1746 C CA . HIS A 223 ? 0.1481 0.2046 0.0758 -0.0500 -0.0019 -0.0123 238 HIS A CA 1747 C C . HIS A 223 ? 0.2134 0.1367 0.1586 -0.0775 0.0546 -0.0315 238 HIS A C 1748 O O . HIS A 223 ? 0.2079 0.1671 0.1241 -0.0433 0.0180 0.0085 238 HIS A O 1749 C CB . HIS A 223 ? 0.1734 0.1752 0.0838 0.0021 -0.0171 0.0083 238 HIS A CB 1750 C CG . HIS A 223 ? 0.1521 0.2163 0.1499 -0.0307 0.0706 0.0111 238 HIS A CG 1751 N ND1 . HIS A 223 ? 0.1865 0.0998 0.1188 -0.0182 0.0162 0.0236 238 HIS A ND1 1752 C CD2 . HIS A 223 ? 0.1707 0.3547 0.1724 0.0065 0.0216 -0.1045 238 HIS A CD2 1753 C CE1 . HIS A 223 ? 0.0911 0.1497 0.1983 0.0234 0.0385 -0.0144 238 HIS A CE1 1754 N NE2 . HIS A 223 ? 0.0710 0.1689 0.1800 0.0217 -0.0239 0.0037 238 HIS A NE2 1755 N N . GLY A 224 ? 0.1609 0.2523 0.1708 0.0145 0.0330 -0.0036 239 GLY A N 1756 C CA . GLY A 224 ? 0.1688 0.1607 0.1784 -0.0269 0.0048 0.0210 239 GLY A CA 1757 C C . GLY A 224 ? 0.2075 0.0872 0.1140 0.0342 0.0170 0.0194 239 GLY A C 1758 O O . GLY A 224 ? 0.1629 0.1570 0.1686 0.0099 -0.0338 0.0297 239 GLY A O 1759 N N . MET A 225 ? 0.2324 0.1073 0.0946 0.0085 0.0201 -0.0041 240 MET A N 1760 C CA . MET A 225 ? 0.1620 0.2701 0.1012 0.0306 -0.0269 0.0232 240 MET A CA 1761 C C . MET A 225 ? 0.1826 0.1939 0.1526 0.0330 0.0075 0.0139 240 MET A C 1762 O O . MET A 225 ? 0.1737 0.1974 0.1813 0.0460 0.0178 0.0282 240 MET A O 1763 C CB . MET A 225 ? 0.1782 0.2564 0.1791 -0.0724 0.0641 -0.0369 240 MET A CB 1764 C CG . MET A 225 ? 0.2271 0.1087 0.1739 -0.0309 -0.0082 0.0053 240 MET A CG 1765 S SD . MET A 225 ? 0.1700 0.1533 0.1652 -0.0103 0.0097 -0.0058 240 MET A SD 1766 C CE . MET A 225 ? 0.1335 0.1339 0.2368 -0.0063 -0.0501 0.0079 240 MET A CE 1767 N N . THR A 226 ? 0.2157 0.1177 0.1283 0.0005 -0.0221 -0.0109 241 THR A N 1768 C CA . THR A 226 ? 0.2204 0.2442 0.1039 0.0319 0.0488 -0.0146 241 THR A CA 1769 C C . THR A 226 ? 0.1621 0.1605 0.2376 0.0559 -0.0162 -0.0256 241 THR A C 1770 O O . THR A 226 ? 0.1935 0.1751 0.1863 0.0652 0.0087 0.0745 241 THR A O 1771 C CB . THR A 226 ? 0.1859 0.1511 0.3180 0.0454 0.0877 0.0795 241 THR A CB 1772 O OG1 . THR A 226 ? 0.1763 0.2000 0.2482 0.0166 0.0308 -0.0122 241 THR A OG1 1773 C CG2 . THR A 226 ? 0.1450 0.1298 0.2535 0.0322 0.0041 -0.0072 241 THR A CG2 1774 N N . GLN A 227 ? 0.2001 0.1301 0.1960 -0.0087 0.0048 0.0280 242 GLN A N 1775 C CA . GLN A 227 ? 0.2248 0.1906 0.1622 -0.0676 -0.0215 0.0761 242 GLN A CA 1776 C C . GLN A 227 ? 0.1574 0.1526 0.2196 -0.0724 -0.0245 -0.0217 242 GLN A C 1777 O O . GLN A 227 ? 0.1734 0.2013 0.1703 -0.0021 -0.0318 0.0234 242 GLN A O 1778 C CB . GLN A 227 ? 0.2835 0.2403 0.1479 0.0209 -0.0008 0.0881 242 GLN A CB 1779 C CG . GLN A 227 ? 0.2451 0.3207 0.1501 -0.0241 -0.0309 0.0449 242 GLN A CG 1780 C CD . GLN A 227 ? 0.3399 0.2659 0.1646 -0.0270 -0.0472 0.0515 242 GLN A CD 1781 O OE1 . GLN A 227 ? 0.2970 0.1878 0.2477 -0.0178 -0.0503 0.0502 242 GLN A OE1 1782 N NE2 . GLN A 227 ? 0.3631 0.2218 0.2932 -0.0194 0.0991 0.0949 242 GLN A NE2 1783 N N . CYS A 228 ? 0.2107 0.1968 0.1515 0.0698 0.0276 0.0600 243 CYS A N 1784 C CA . CYS A 228 ? 0.2037 0.2056 0.1278 0.0387 -0.0109 0.0232 243 CYS A CA 1785 C C . CYS A 228 ? 0.2096 0.2595 0.1152 0.0151 -0.0211 0.0489 243 CYS A C 1786 O O . CYS A 228 ? 0.3463 0.2393 0.1422 -0.0357 0.0128 0.0383 243 CYS A O 1787 C CB . CYS A 228 ? 0.2231 0.1985 0.1496 0.0024 -0.0323 0.0829 243 CYS A CB 1788 S SG . CYS A 228 ? 0.2274 0.2044 0.1654 0.0344 -0.0229 0.0165 243 CYS A SG 1789 N N . SER A 229 ? 0.1562 0.2721 0.1173 0.0420 -0.0249 0.0409 244 SER A N 1790 C CA . SER A 229 ? 0.1976 0.2192 0.1303 0.0262 -0.0403 0.0631 244 SER A CA 1791 C C . SER A 229 ? 0.2474 0.2974 0.1203 0.0029 -0.0167 0.0643 244 SER A C 1792 O O . SER A 229 ? 0.2160 0.1939 0.1871 0.0221 0.0015 0.0268 244 SER A O 1793 C CB . SER A 229 ? 0.2881 0.2482 0.1758 0.0823 -0.0811 0.0207 244 SER A CB 1794 O OG . SER A 229 ? 0.2340 0.3656 0.2229 0.0426 -0.0305 0.0079 244 SER A OG 1795 N N . GLN A 230 ? 0.2607 0.2630 0.1133 -0.0002 -0.0095 0.0667 245 GLN A N 1796 C CA . GLN A 230 ? 0.2525 0.3503 0.1295 -0.1007 0.0095 0.0236 245 GLN A CA 1797 C C . GLN A 230 ? 0.2435 0.2725 0.1610 -0.0565 0.0096 0.0888 245 GLN A C 1798 O O . GLN A 230 ? 0.2803 0.3073 0.1823 -0.0400 -0.0507 0.0797 245 GLN A O 1799 C CB . GLN A 230 ? 0.2948 0.2897 0.1836 -0.0870 0.0503 0.0599 245 GLN A CB 1800 C CG . GLN A 230 ? 0.3900 0.2578 0.1635 0.0096 0.0347 0.0646 245 GLN A CG 1801 C CD . GLN A 230 ? 0.4002 0.4739 0.5562 0.1456 0.0352 0.1169 245 GLN A CD 1802 O OE1 . GLN A 230 ? 0.4464 0.3932 0.5925 0.0309 0.1242 0.2094 245 GLN A OE1 1803 N NE2 . GLN A 230 ? 0.5657 0.5711 0.5230 0.0621 0.0421 0.0561 245 GLN A NE2 1804 N N . ASP A 231 ? 0.2170 0.2854 0.1976 -0.0400 0.0488 0.0173 246 ASP A N 1805 C CA . ASP A 231 ? 0.2324 0.2788 0.2311 -0.0406 0.0165 0.1251 246 ASP A CA 1806 C C . ASP A 231 ? 0.2479 0.2298 0.1824 -0.0254 -0.0027 0.0754 246 ASP A C 1807 O O . ASP A 231 ? 0.2342 0.3214 0.2359 -0.0281 -0.0251 0.0269 246 ASP A O 1808 C CB . ASP A 231 ? 0.3445 0.3052 0.3029 0.0397 0.0008 0.1244 246 ASP A CB 1809 C CG . ASP A 231 ? 0.4410 0.3784 0.4520 0.0822 0.0071 0.0179 246 ASP A CG 1810 O OD1 . ASP A 231 ? 0.4431 0.4862 0.3946 0.1147 0.0254 0.1637 246 ASP A OD1 1811 O OD2 . ASP A 231 ? 0.5226 0.4354 0.5491 0.1358 -0.0255 0.1567 246 ASP A OD2 1812 N N . ARG A 232 ? 0.2954 0.2039 0.1453 0.0366 -0.0290 0.0663 247 ARG A N 1813 C CA . ARG A 232 ? 0.2404 0.1634 0.1873 0.0865 -0.0313 0.0190 247 ARG A CA 1814 C C . ARG A 232 ? 0.2031 0.3026 0.1579 -0.0112 -0.0491 0.0757 247 ARG A C 1815 O O . ARG A 232 ? 0.1838 0.2067 0.1306 0.0194 -0.0149 -0.0008 247 ARG A O 1816 C CB . ARG A 232 ? 0.1937 0.1626 0.2244 0.0592 0.0188 -0.0580 247 ARG A CB 1817 C CG . ARG A 232 ? 0.2097 0.2467 0.1890 0.0484 0.0186 -0.0617 247 ARG A CG 1818 C CD . ARG A 232 ? 0.1706 0.2986 0.2495 -0.0179 -0.0320 -0.0156 247 ARG A CD 1819 N NE . ARG A 232 ? 0.2075 0.1784 0.1961 0.0581 0.0258 0.0865 247 ARG A NE 1820 C CZ . ARG A 232 ? 0.2272 0.2575 0.2009 0.0056 -0.0453 0.1107 247 ARG A CZ 1821 N NH1 . ARG A 232 ? 0.2847 0.2713 0.2003 -0.0189 0.0557 0.0242 247 ARG A NH1 1822 N NH2 . ARG A 232 ? 0.2177 0.2982 0.1207 0.0513 -0.0358 0.0059 247 ARG A NH2 1823 N N . LEU A 233 ? 0.2217 0.2575 0.1796 -0.0650 -0.0173 0.0329 248 LEU A N 1824 C CA . LEU A 233 ? 0.2399 0.2403 0.1466 0.0276 0.0372 0.0299 248 LEU A CA 1825 C C . LEU A 233 ? 0.2299 0.2468 0.1508 -0.0148 -0.0419 0.0617 248 LEU A C 1826 O O . LEU A 233 ? 0.2718 0.2647 0.2017 0.0324 -0.0929 0.0031 248 LEU A O 1827 C CB . LEU A 233 ? 0.2181 0.1704 0.1727 0.0147 0.0381 -0.0296 248 LEU A CB 1828 C CG . LEU A 233 ? 0.2100 0.3045 0.1410 -0.0522 0.0232 -0.0220 248 LEU A CG 1829 C CD1 . LEU A 233 ? 0.1887 0.2490 0.1359 0.0144 0.0082 0.0155 248 LEU A CD1 1830 C CD2 . LEU A 233 ? 0.1672 0.2091 0.1720 -0.0123 -0.0320 0.0056 248 LEU A CD2 1831 N N . ILE A 234 ? 0.2278 0.1531 0.1452 0.0006 -0.0071 0.0073 249 ILE A N 1832 C CA . ILE A 234 ? 0.2005 0.2004 0.1819 0.0247 -0.0276 0.0458 249 ILE A CA 1833 C C . ILE A 234 ? 0.2410 0.3302 0.1268 0.0216 -0.0620 -0.0006 249 ILE A C 1834 O O . ILE A 234 ? 0.2275 0.2815 0.1314 -0.0135 -0.0259 -0.0161 249 ILE A O 1835 C CB . ILE A 234 ? 0.2548 0.3744 0.1286 -0.0062 -0.0429 0.0032 249 ILE A CB 1836 C CG1 . ILE A 234 ? 0.2440 0.2850 0.1900 0.0460 0.0246 -0.0832 249 ILE A CG1 1837 C CG2 . ILE A 234 ? 0.3002 0.3856 0.1867 -0.0113 -0.0408 -0.0008 249 ILE A CG2 1838 C CD1 . ILE A 234 ? 0.2884 0.2933 0.1485 0.0805 0.0353 0.0093 249 ILE A CD1 1839 N N . ASN A 235 ? 0.2792 0.2056 0.1706 -0.0231 0.0266 -0.0023 250 ASN A N 1840 C CA . ASN A 235 ? 0.3041 0.1956 0.1543 0.0327 0.0236 0.0217 250 ASN A CA 1841 C C . ASN A 235 ? 0.2688 0.2062 0.1711 -0.0470 0.0309 -0.0373 250 ASN A C 1842 O O . ASN A 235 ? 0.3172 0.2554 0.2132 -0.0652 -0.0269 -0.0650 250 ASN A O 1843 C CB . ASN A 235 ? 0.3544 0.2822 0.2225 0.0330 0.0070 -0.0138 250 ASN A CB 1844 C CG . ASN A 235 ? 0.3371 0.2283 0.2251 0.0559 -0.0137 0.0224 250 ASN A CG 1845 O OD1 . ASN A 235 ? 0.3586 0.3090 0.2763 0.0540 0.1106 -0.0289 250 ASN A OD1 1846 N ND2 . ASN A 235 ? 0.4562 0.3074 0.2019 -0.0343 0.0354 0.1031 250 ASN A ND2 1847 N N . LEU A 236 ? 0.2637 0.2377 0.2121 0.0125 -0.0094 0.0554 251 LEU A N 1848 C CA . LEU A 236 ? 0.2601 0.2858 0.2188 0.0475 0.0153 0.0725 251 LEU A CA 1849 C C . LEU A 236 ? 0.3785 0.3118 0.1857 0.0017 0.0492 -0.0942 251 LEU A C 1850 O O . LEU A 236 ? 0.3821 0.3297 0.1987 -0.0219 -0.0075 -0.0364 251 LEU A O 1851 C CB . LEU A 236 ? 0.2919 0.2966 0.2179 0.0394 -0.0019 0.0385 251 LEU A CB 1852 C CG . LEU A 236 ? 0.3067 0.4172 0.1516 -0.0146 0.0224 -0.0435 251 LEU A CG 1853 C CD1 . LEU A 236 ? 0.3807 0.3058 0.2482 0.1048 -0.1231 0.0187 251 LEU A CD1 1854 C CD2 . LEU A 236 ? 0.2814 0.4738 0.2194 -0.1280 0.0722 0.0001 251 LEU A CD2 1855 N N . ASP A 237 ? 0.4123 0.3428 0.1677 0.0123 0.0311 -0.0276 252 ASP A N 1856 C CA . ASP A 237 ? 0.3837 0.3435 0.2290 0.0122 0.0456 -0.0564 252 ASP A CA 1857 C C . ASP A 237 ? 0.4405 0.3183 0.2281 0.0272 0.1223 -0.0684 252 ASP A C 1858 O O . ASP A 237 ? 0.5228 0.4679 0.2536 0.0929 0.1127 -0.0429 252 ASP A O 1859 C CB . ASP A 237 ? 0.3931 0.4190 0.1983 0.0376 0.0502 -0.1171 252 ASP A CB 1860 C CG . ASP A 237 ? 0.4160 0.3621 0.3201 0.0253 0.0223 0.0005 252 ASP A CG 1861 O OD1 . ASP A 237 ? 0.4563 0.3234 0.2780 -0.0142 0.0460 0.0045 252 ASP A OD1 1862 O OD2 . ASP A 237 ? 0.4882 0.3841 0.2522 0.0029 0.0668 -0.0389 252 ASP A OD2 1863 N N . SER A 238 ? 0.4744 0.2128 0.2322 0.0727 0.0151 -0.0133 253 SER A N 1864 C CA . SER A 238 ? 0.4136 0.3015 0.3573 0.0807 -0.0929 0.0283 253 SER A CA 1865 C C . SER A 238 ? 0.3257 0.4538 0.3428 0.1150 -0.1107 -0.0058 253 SER A C 1866 O O . SER A 238 ? 0.4059 0.5178 0.2949 0.0273 -0.0964 0.0243 253 SER A O 1867 C CB . SER A 238 ? 0.4576 0.2781 0.2605 0.0398 -0.0843 0.0226 253 SER A CB 1868 O OG . SER A 238 ? 0.5415 0.5493 0.3649 0.0036 -0.1433 -0.0768 253 SER A OG 1869 N N . CYS A 239 ? 0.3644 0.4267 0.3728 0.0363 -0.0523 -0.0589 254 CYS A N 1870 C CA . CYS A 239 ? 0.3179 0.3349 0.3543 0.0751 -0.0819 -0.0836 254 CYS A CA 1871 C C . CYS A 239 ? 0.3672 0.3338 0.4666 -0.0740 -0.0924 -0.0807 254 CYS A C 1872 O O . CYS A 239 ? 0.3829 0.3874 0.3730 0.0028 -0.1142 -0.1044 254 CYS A O 1873 C CB . CYS A 239 ? 0.3744 0.4237 0.4285 0.0948 0.0835 -0.1454 254 CYS A CB 1874 S SG . CYS A 239 ? 0.3600 0.3906 0.3600 -0.0050 -0.0258 -0.0430 254 CYS A SG 1875 N N . ILE A 240 ? 0.3918 0.2261 0.3073 -0.0052 0.0250 -0.0906 255 ILE A N 1876 C CA . ILE A 240 ? 0.4337 0.2974 0.2661 0.0171 0.0912 -0.1008 255 ILE A CA 1877 C C . ILE A 240 ? 0.4128 0.2641 0.2543 0.0015 0.0213 -0.1376 255 ILE A C 1878 O O . ILE A 240 ? 0.5667 0.2287 0.2853 0.0007 -0.0555 -0.0855 255 ILE A O 1879 C CB . ILE A 240 ? 0.4110 0.2228 0.3267 -0.0443 -0.0066 -0.1282 255 ILE A CB 1880 C CG1 . ILE A 240 ? 0.4641 0.4489 0.3311 0.0480 0.1451 -0.0631 255 ILE A CG1 1881 C CG2 . ILE A 240 ? 0.3969 0.2940 0.2617 -0.0274 -0.0133 0.0208 255 ILE A CG2 1882 C CD1 . ILE A 240 ? 0.4538 0.3219 0.4536 -0.0685 0.0162 -0.0938 255 ILE A CD1 1883 N N . ASP A 241 ? 0.4801 0.3698 0.3119 0.0454 0.0318 -0.1104 256 ASP A N 1884 C CA . ASP A 241 ? 0.5138 0.4067 0.3013 0.0249 0.0058 -0.1189 256 ASP A CA 1885 C C . ASP A 241 ? 0.5109 0.3513 0.3507 0.0588 0.0574 -0.1834 256 ASP A C 1886 O O . ASP A 241 ? 0.4954 0.3970 0.3250 0.0902 0.0004 -0.1823 256 ASP A O 1887 C CB . ASP A 241 ? 0.5015 0.4516 0.3100 0.0376 -0.0173 -0.1301 256 ASP A CB 1888 C CG . ASP A 241 ? 0.5673 0.5852 0.5384 0.1499 -0.0316 -0.0493 256 ASP A CG 1889 O OD1 . ASP A 241 ? 0.5571 0.5875 0.6014 0.0883 0.1105 0.0173 256 ASP A OD1 1890 O OD2 . ASP A 241 ? 0.6818 0.5117 0.4095 0.0517 -0.0213 -0.1846 256 ASP A OD2 1891 N N . HIS A 242 ? 0.4682 0.4954 0.3709 0.0820 0.0539 -0.0275 257 HIS A N 1892 C CA . HIS A 242 ? 0.5311 0.6158 0.3294 -0.0371 -0.0016 -0.0168 257 HIS A CA 1893 C C . HIS A 242 ? 0.5198 0.6495 0.4189 0.0428 0.0349 -0.0032 257 HIS A C 1894 O O . HIS A 242 ? 0.4510 0.6781 0.3644 0.0449 -0.0215 0.0562 257 HIS A O 1895 C CB . HIS A 242 ? 0.6125 0.6957 0.6534 -0.0323 -0.0513 -0.0630 257 HIS A CB 1896 C CG . HIS A 242 ? 0.6490 0.7174 0.7570 -0.0721 -0.0231 -0.0576 257 HIS A CG 1897 N ND1 . HIS A 242 ? 0.6582 0.8293 0.8090 0.0410 0.0555 0.0477 257 HIS A ND1 1898 C CD2 . HIS A 242 ? 0.6167 0.7678 0.7913 0.0498 0.0266 0.0335 257 HIS A CD2 1899 C CE1 . HIS A 242 ? 0.6649 0.7559 0.7521 -0.0105 0.0080 0.0636 257 HIS A CE1 1900 N NE2 . HIS A 242 ? 0.6397 0.7291 0.7773 0.0888 0.0438 0.0546 257 HIS A NE2 1901 N N . SER A 243 ? 0.5438 0.5246 0.4230 0.1182 0.1181 -0.1460 258 SER A N 1902 C CA . SER A 243 ? 0.5848 0.5698 0.5509 0.0454 0.0355 -0.1118 258 SER A CA 1903 C C . SER A 243 ? 0.6088 0.5335 0.4271 0.1696 0.0238 -0.0698 258 SER A C 1904 O O . SER A 243 ? 0.7042 0.5908 0.4389 0.2237 0.0568 -0.1906 258 SER A O 1905 C CB . SER A 243 ? 0.6227 0.6508 0.5328 0.0848 0.0273 -0.1257 258 SER A CB 1906 O OG . SER A 243 ? 0.7007 0.5424 0.5001 0.0833 -0.0331 -0.2889 258 SER A OG 1907 N N . TYR A 244 ? 0.4666 0.4046 0.2704 0.1156 0.0083 -0.1450 259 TYR A N 1908 C CA . TYR A 244 ? 0.4842 0.3106 0.3350 0.0531 0.0273 -0.1700 259 TYR A CA 1909 C C . TYR A 244 ? 0.5145 0.2758 0.2579 0.0179 -0.0764 -0.1071 259 TYR A C 1910 O O . TYR A 244 ? 0.5161 0.1713 0.3680 0.0579 -0.0189 -0.0553 259 TYR A O 1911 C CB . TYR A 244 ? 0.5061 0.4770 0.3838 0.0141 -0.1339 -0.0850 259 TYR A CB 1912 C CG . TYR A 244 ? 0.5717 0.5579 0.5351 0.0310 -0.0169 -0.0550 259 TYR A CG 1913 C CD1 . TYR A 244 ? 0.6147 0.5426 0.4852 -0.0621 -0.0648 -0.1627 259 TYR A CD1 1914 C CD2 . TYR A 244 ? 0.5982 0.6080 0.6099 0.0622 -0.0157 -0.1622 259 TYR A CD2 1915 C CE1 . TYR A 244 ? 0.6618 0.6385 0.6342 -0.0330 -0.0216 -0.0367 259 TYR A CE1 1916 C CE2 . TYR A 244 ? 0.5763 0.6485 0.6336 -0.0077 -0.1242 -0.1094 259 TYR A CE2 1917 C CZ . TYR A 244 ? 0.6539 0.6950 0.6441 -0.0302 -0.0711 -0.0729 259 TYR A CZ 1918 O OH . TYR A 244 ? 0.6276 0.7410 0.6213 -0.0174 -0.1180 -0.0770 259 TYR A OH 1919 N N . TYR A 245 ? 0.4632 0.2870 0.2639 0.0831 -0.0263 -0.1252 260 TYR A N 1920 C CA . TYR A 245 ? 0.3742 0.2528 0.2637 0.0397 -0.0192 -0.1105 260 TYR A CA 1921 C C . TYR A 245 ? 0.4161 0.3094 0.3031 0.1581 -0.0135 -0.0252 260 TYR A C 1922 O O . TYR A 245 ? 0.4988 0.2470 0.3772 0.0426 0.0362 -0.1104 260 TYR A O 1923 C CB . TYR A 245 ? 0.3964 0.2790 0.2570 -0.0650 0.0447 0.0172 260 TYR A CB 1924 C CG . TYR A 245 ? 0.3606 0.2224 0.2006 -0.0410 -0.0240 -0.0945 260 TYR A CG 1925 C CD1 . TYR A 245 ? 0.3616 0.1763 0.1901 0.0334 0.0367 -0.0508 260 TYR A CD1 1926 C CD2 . TYR A 245 ? 0.3028 0.1695 0.2260 -0.0228 0.0300 -0.0012 260 TYR A CD2 1927 C CE1 . TYR A 245 ? 0.3873 0.1692 0.2745 0.0153 -0.0605 -0.0046 260 TYR A CE1 1928 C CE2 . TYR A 245 ? 0.3486 0.2497 0.2796 0.0143 0.0362 -0.0363 260 TYR A CE2 1929 C CZ . TYR A 245 ? 0.3852 0.1947 0.3530 -0.0203 0.0280 -0.0679 260 TYR A CZ 1930 O OH . TYR A 245 ? 0.4409 0.2019 0.2413 0.0124 0.0223 -0.0554 260 TYR A OH 1931 N N . THR A 246 ? 0.3762 0.2153 0.2254 0.0427 0.0411 -0.0164 261 THR A N 1932 C CA . THR A 246 ? 0.3667 0.2645 0.2873 0.0127 0.0820 0.0257 261 THR A CA 1933 C C . THR A 246 ? 0.2686 0.2459 0.2570 0.0751 0.0353 -0.0556 261 THR A C 1934 O O . THR A 246 ? 0.2636 0.2576 0.2635 0.0231 0.0226 -0.0233 261 THR A O 1935 C CB . THR A 246 ? 0.3318 0.2083 0.3136 0.1250 -0.0469 -0.0238 261 THR A CB 1936 O OG1 . THR A 246 ? 0.3882 0.1565 0.4205 0.0576 0.0542 -0.0484 261 THR A OG1 1937 C CG2 . THR A 246 ? 0.3694 0.3271 0.3147 0.1008 -0.0432 -0.0987 261 THR A CG2 1938 N N . LEU A 247 ? 0.3497 0.1968 0.2286 -0.0105 -0.0358 -0.0233 262 LEU A N 1939 C CA . LEU A 247 ? 0.3151 0.2076 0.1683 -0.0215 0.0170 -0.0781 262 LEU A CA 1940 C C . LEU A 247 ? 0.2599 0.2441 0.1404 -0.0347 0.0234 0.0402 262 LEU A C 1941 O O . LEU A 247 ? 0.2278 0.3207 0.2280 -0.0051 0.0546 -0.0035 262 LEU A O 1942 C CB . LEU A 247 ? 0.3173 0.2232 0.2613 0.0257 0.0004 0.0680 262 LEU A CB 1943 C CG . LEU A 247 ? 0.3510 0.1739 0.3138 0.1015 -0.0123 0.0465 262 LEU A CG 1944 C CD1 . LEU A 247 ? 0.3061 0.2593 0.2776 0.0769 -0.0703 -0.0906 262 LEU A CD1 1945 C CD2 . LEU A 247 ? 0.3838 0.1390 0.2874 0.0285 0.0107 0.0645 262 LEU A CD2 1946 N N . ILE A 248 ? 0.3043 0.1715 0.1725 0.0495 -0.0243 0.0634 263 ILE A N 1947 C CA . ILE A 248 ? 0.2680 0.1708 0.2174 0.0911 0.0517 0.0643 263 ILE A CA 1948 C C . ILE A 248 ? 0.1968 0.1999 0.1697 0.0883 -0.0067 0.0162 263 ILE A C 1949 O O . ILE A 248 ? 0.2088 0.2969 0.2385 0.0180 -0.0325 0.0015 263 ILE A O 1950 C CB . ILE A 248 ? 0.2706 0.0889 0.2400 0.0052 0.0232 -0.0197 263 ILE A CB 1951 C CG1 . ILE A 248 ? 0.2695 0.2249 0.2844 0.0537 0.0336 -0.1169 263 ILE A CG1 1952 C CG2 . ILE A 248 ? 0.2873 0.2484 0.2207 0.0053 -0.0253 -0.0588 263 ILE A CG2 1953 C CD1 . ILE A 248 ? 0.3139 0.1862 0.2474 0.1057 0.0673 0.0562 263 ILE A CD1 1954 N N . ASP A 249 ? 0.2542 0.1702 0.2254 0.1052 -0.0004 0.0162 264 ASP A N 1955 C CA . ASP A 249 ? 0.1819 0.2760 0.2475 0.0462 -0.0089 0.0744 264 ASP A CA 1956 C C . ASP A 249 ? 0.2275 0.1562 0.2138 -0.0229 -0.0042 -0.0665 264 ASP A C 1957 O O . ASP A 249 ? 0.2154 0.1804 0.1977 -0.0057 -0.0015 0.0151 264 ASP A O 1958 C CB . ASP A 249 ? 0.2576 0.2472 0.1332 0.0288 0.0060 -0.0146 264 ASP A CB 1959 C CG . ASP A 249 ? 0.2242 0.2680 0.2146 0.0248 0.0732 0.1089 264 ASP A CG 1960 O OD1 . ASP A 249 ? 0.2462 0.3095 0.1953 0.0189 0.0359 -0.0217 264 ASP A OD1 1961 O OD2 . ASP A 249 ? 0.2008 0.2461 0.2012 -0.0144 0.0334 0.0652 264 ASP A OD2 1962 N N . LEU A 250 ? 0.2256 0.1621 0.1859 0.0505 -0.0006 0.0109 265 LEU A N 1963 C CA . LEU A 250 ? 0.2069 0.1721 0.1895 0.0028 0.0446 0.0146 265 LEU A CA 1964 C C . LEU A 250 ? 0.1860 0.1874 0.1704 0.0764 0.0318 0.0683 265 LEU A C 1965 O O . LEU A 250 ? 0.2030 0.1724 0.2455 0.0530 0.0023 -0.0049 265 LEU A O 1966 C CB . LEU A 250 ? 0.2255 0.2632 0.1452 0.0052 0.0081 0.0047 265 LEU A CB 1967 C CG . LEU A 250 ? 0.2529 0.2575 0.1816 -0.0564 0.0318 -0.0658 265 LEU A CG 1968 C CD1 . LEU A 250 ? 0.3107 0.2408 0.2015 0.0551 0.0395 0.0552 265 LEU A CD1 1969 C CD2 . LEU A 250 ? 0.2509 0.2208 0.2742 -0.0084 0.1037 0.0237 265 LEU A CD2 1970 N N . SER A 251 ? 0.1508 0.2198 0.2047 0.0140 0.0380 -0.0152 266 SER A N 1971 C CA . SER A 251 ? 0.1378 0.2031 0.1253 0.0339 0.0150 0.0288 266 SER A CA 1972 C C . SER A 251 ? 0.1827 0.1998 0.0907 0.0163 0.0153 0.0159 266 SER A C 1973 O O . SER A 251 ? 0.1786 0.1685 0.2014 -0.0182 -0.0129 0.0397 266 SER A O 1974 C CB . SER A 251 ? 0.1617 0.2001 0.1796 0.0185 -0.0077 0.0975 266 SER A CB 1975 O OG . SER A 251 ? 0.1844 0.2612 0.0916 0.0051 -0.0289 0.0143 266 SER A OG 1976 N N . PRO A 252 ? 0.1708 0.1019 0.1473 -0.0188 -0.0221 -0.0171 267 PRO A N 1977 C CA . PRO A 252 ? 0.1163 0.1416 0.1678 -0.0311 0.0082 -0.0485 267 PRO A CA 1978 C C . PRO A 252 ? 0.1002 0.2097 0.1677 -0.0357 0.0371 0.0090 267 PRO A C 1979 O O . PRO A 252 ? 0.1113 0.1592 0.1947 0.0115 0.0034 0.0082 267 PRO A O 1980 C CB . PRO A 252 ? 0.1171 0.2139 0.1316 0.0231 -0.0266 -0.0513 267 PRO A CB 1981 C CG . PRO A 252 ? 0.1206 0.1654 0.1543 0.0010 -0.0231 0.0133 267 PRO A CG 1982 C CD . PRO A 252 ? 0.1389 0.1456 0.1902 -0.0250 0.0196 -0.0259 267 PRO A CD 1983 N N . VAL A 253 ? 0.1843 0.1721 0.1610 0.0314 -0.0202 -0.0120 268 VAL A N 1984 C CA . VAL A 253 ? 0.1864 0.1563 0.2139 0.0628 -0.0289 0.0521 268 VAL A CA 1985 C C . VAL A 253 ? 0.1371 0.1506 0.1633 -0.0219 -0.0236 0.0486 268 VAL A C 1986 O O . VAL A 253 ? 0.1452 0.1960 0.1723 0.0057 -0.0242 -0.0148 268 VAL A O 1987 C CB . VAL A 253 ? 0.1335 0.2551 0.1323 0.0197 0.0129 0.0602 268 VAL A CB 1988 C CG1 . VAL A 253 ? 0.2356 0.1312 0.1609 -0.0352 0.0175 0.0579 268 VAL A CG1 1989 C CG2 . VAL A 253 ? 0.1879 0.1531 0.1685 0.0370 -0.0071 0.0276 268 VAL A CG2 1990 N N . ALA A 254 ? 0.2410 0.1661 0.1361 -0.0584 -0.0181 0.0156 269 ALA A N 1991 C CA . ALA A 254 ? 0.2354 0.2416 0.1165 0.0044 -0.0158 -0.0168 269 ALA A CA 1992 C C . ALA A 254 ? 0.2297 0.1071 0.1580 -0.0344 -0.0096 0.0453 269 ALA A C 1993 O O . ALA A 254 ? 0.2381 0.1515 0.2304 -0.0432 0.0053 0.0476 269 ALA A O 1994 C CB . ALA A 254 ? 0.1808 0.1963 0.2019 0.0243 0.0319 -0.0286 269 ALA A CB 1995 N N . ALA A 255 ? 0.2382 0.1168 0.1886 0.0460 -0.0430 0.0124 270 ALA A N 1996 C CA . ALA A 255 ? 0.2187 0.1573 0.1662 -0.0033 -0.0428 -0.0314 270 ALA A CA 1997 C C . ALA A 255 ? 0.2908 0.2875 0.1972 0.0245 -0.0702 0.0119 270 ALA A C 1998 O O . ALA A 255 ? 0.2706 0.1636 0.2265 0.0113 -0.0054 -0.0305 270 ALA A O 1999 C CB . ALA A 255 ? 0.2484 0.0843 0.1600 0.0155 -0.0383 -0.0127 270 ALA A CB 2000 N N . ILE A 256 ? 0.3019 0.1318 0.1873 0.0139 -0.0038 -0.0481 271 ILE A N 2001 C CA . ILE A 256 ? 0.2739 0.0970 0.2782 -0.0209 -0.0181 -0.0307 271 ILE A CA 2002 C C . ILE A 256 ? 0.2868 0.1943 0.2137 0.0396 -0.0012 -0.0772 271 ILE A C 2003 O O . ILE A 256 ? 0.2378 0.2154 0.2845 0.0508 -0.0292 -0.0476 271 ILE A O 2004 C CB . ILE A 256 ? 0.2753 0.2105 0.2528 0.0161 -0.0531 -0.0348 271 ILE A CB 2005 C CG1 . ILE A 256 ? 0.2450 0.2594 0.1976 -0.0299 -0.0042 0.0127 271 ILE A CG1 2006 C CG2 . ILE A 256 ? 0.3379 0.1902 0.1863 -0.0019 -0.0471 -0.0790 271 ILE A CG2 2007 C CD1 . ILE A 256 ? 0.3394 0.2062 0.2440 -0.0060 -0.0062 -0.0089 271 ILE A CD1 2008 N N . LEU A 257 ? 0.2809 0.1062 0.2906 0.0277 -0.0339 -0.0344 272 LEU A N 2009 C CA . LEU A 257 ? 0.2912 0.1430 0.2373 0.0530 -0.0255 -0.0702 272 LEU A CA 2010 C C . LEU A 257 ? 0.2346 0.2962 0.2874 0.0902 -0.0578 -0.1439 272 LEU A C 2011 O O . LEU A 257 ? 0.3706 0.1903 0.3567 0.0815 0.0128 -0.0810 272 LEU A O 2012 C CB . LEU A 257 ? 0.2688 0.1894 0.2283 0.0796 -0.0841 -0.0272 272 LEU A CB 2013 C CG . LEU A 257 ? 0.3865 0.1723 0.3506 0.0619 0.0636 0.0371 272 LEU A CG 2014 C CD1 . LEU A 257 ? 0.3638 0.3243 0.3105 0.0531 0.1039 -0.0241 272 LEU A CD1 2015 C CD2 . LEU A 257 ? 0.3303 0.1698 0.4822 0.0688 -0.0655 -0.0236 272 LEU A CD2 2016 N N . PRO A 258 ? 0.2928 0.1349 0.2783 -0.0041 0.0098 -0.0512 273 PRO A N 2017 C CA . PRO A 258 ? 0.3434 0.3222 0.3281 0.0225 0.0342 -0.1602 273 PRO A CA 2018 C C . PRO A 258 ? 0.4012 0.3411 0.4571 0.0279 -0.0139 0.0672 273 PRO A C 2019 O O . PRO A 258 ? 0.4083 0.2206 0.4322 -0.0019 0.0575 -0.1413 273 PRO A O 2020 C CB . PRO A 258 ? 0.3632 0.3292 0.3328 0.0547 0.0822 0.0168 273 PRO A CB 2021 C CG . PRO A 258 ? 0.2977 0.2752 0.3857 -0.0433 0.0437 -0.0745 273 PRO A CG 2022 C CD . PRO A 258 ? 0.2401 0.2849 0.3334 -0.0378 -0.0240 -0.0008 273 PRO A CD 2023 N N . LYS A 259 ? 0.4223 0.2235 0.3358 0.0153 0.0248 0.0069 274 LYS A N 2024 C CA . LYS A 259 ? 0.4300 0.2881 0.4193 0.0695 0.0992 -0.1213 274 LYS A CA 2025 C C . LYS A 259 ? 0.4386 0.4011 0.3950 0.1427 -0.0538 -0.1250 274 LYS A C 2026 O O . LYS A 259 ? 0.5294 0.3207 0.5816 0.0944 -0.0357 -0.0886 274 LYS A O 2027 C CB . LYS A 259 ? 0.4816 0.2905 0.4066 0.0892 0.0644 -0.1573 274 LYS A CB 2028 C CG . LYS A 259 ? 0.5222 0.4079 0.3834 0.1012 0.0828 -0.1214 274 LYS A CG 2029 C CD . LYS A 259 ? 0.5048 0.4730 0.5391 0.1579 0.1717 -0.0160 274 LYS A CD 2030 C CE . LYS A 259 ? 0.5038 0.5625 0.5773 -0.0654 0.0629 0.0840 274 LYS A CE 2031 N NZ . LYS A 259 ? 0.5416 0.7518 0.7960 -0.0742 -0.1041 0.0124 274 LYS A NZ 2032 N N . ILE A 260 ? 0.5434 0.4515 0.5894 -0.0028 -0.0397 -0.2037 275 ILE A N 2033 C CA . ILE A 260 ? 0.5365 0.3809 0.5290 -0.0297 -0.0297 -0.1109 275 ILE A CA 2034 C C . ILE A 260 ? 0.5748 0.4687 0.3955 -0.0699 -0.0602 -0.0686 275 ILE A C 2035 O O . ILE A 260 ? 0.6102 0.3933 0.4926 -0.0763 0.0150 -0.0289 275 ILE A O 2036 C CB . ILE A 260 ? 0.5496 0.4106 0.6460 0.0467 0.0476 -0.1832 275 ILE A CB 2037 C CG1 . ILE A 260 ? 0.5902 0.5483 0.5092 0.0714 -0.1204 0.0410 275 ILE A CG1 2038 C CG2 . ILE A 260 ? 0.5508 0.3614 0.4904 -0.0502 0.0783 -0.1607 275 ILE A CG2 2039 C CD1 . ILE A 260 ? 0.6350 0.6973 0.5887 0.0391 -0.0012 -0.0638 275 ILE A CD1 2040 N N . ASN A 261 ? 0.5683 0.2927 0.5348 0.0469 0.0224 -0.1373 276 ASN A N 2041 C CA . ASN A 261 ? 0.5800 0.4052 0.5546 0.0700 0.0006 -0.1139 276 ASN A CA 2042 C C . ASN A 261 ? 0.5471 0.2534 0.3757 0.0269 0.0073 -0.1464 276 ASN A C 2043 O O . ASN A 261 ? 0.5576 0.3180 0.3253 -0.0424 -0.0071 -0.0325 276 ASN A O 2044 C CB . ASN A 261 ? 0.6282 0.4076 0.5691 0.0957 -0.0552 -0.1057 276 ASN A CB 2045 C CG . ASN A 261 ? 0.7210 0.8754 0.8154 -0.0212 0.0575 -0.0020 276 ASN A CG 2046 O OD1 . ASN A 261 ? 0.7610 0.9266 0.9036 -0.0183 0.1205 -0.0262 276 ASN A OD1 2047 N ND2 . ASN A 261 ? 0.7172 0.9838 0.9498 -0.0245 0.0781 0.0234 276 ASN A ND2 2048 N N . ARG A 262 ? 0.4932 0.3373 0.4109 -0.0431 0.0102 -0.1754 277 ARG A N 2049 C CA . ARG A 262 ? 0.4747 0.3645 0.2743 0.0240 0.0103 -0.1271 277 ARG A CA 2050 C C . ARG A 262 ? 0.4499 0.3774 0.3336 -0.0832 -0.0467 -0.0491 277 ARG A C 2051 O O . ARG A 262 ? 0.4198 0.2487 0.4867 0.0120 -0.0991 0.0378 277 ARG A O 2052 C CB . ARG A 262 ? 0.4665 0.3344 0.2821 -0.0023 -0.0216 -0.0239 277 ARG A CB 2053 C CG . ARG A 262 ? 0.4294 0.3174 0.2636 -0.0569 -0.0002 -0.0288 277 ARG A CG 2054 C CD . ARG A 262 ? 0.4543 0.3620 0.2680 -0.0023 -0.0514 -0.0150 277 ARG A CD 2055 N NE . ARG A 262 ? 0.4420 0.4525 0.5103 -0.0180 -0.0238 -0.0498 277 ARG A NE 2056 C CZ . ARG A 262 ? 0.4821 0.5305 0.4088 -0.1287 0.0179 -0.1650 277 ARG A CZ 2057 N NH1 . ARG A 262 ? 0.5510 0.4071 0.5289 -0.2376 0.0533 -0.0206 277 ARG A NH1 2058 N NH2 . ARG A 262 ? 0.5367 0.2235 0.5024 -0.0356 0.0596 0.0094 277 ARG A NH2 2059 N N . THR A 263 ? 0.4339 0.2972 0.3267 -0.0766 -0.1114 -0.0890 278 THR A N 2060 C CA . THR A 263 ? 0.4387 0.3554 0.3663 -0.1420 -0.0728 -0.1193 278 THR A CA 2061 C C . THR A 263 ? 0.4014 0.4002 0.5064 -0.0198 -0.0891 -0.0939 278 THR A C 2062 O O . THR A 263 ? 0.3665 0.3093 0.4491 -0.0167 -0.1070 -0.0949 278 THR A O 2063 C CB . THR A 263 ? 0.4600 0.3501 0.5758 -0.0621 -0.1005 0.0455 278 THR A CB 2064 O OG1 . THR A 263 ? 0.4948 0.4661 0.6424 -0.2428 0.0256 -0.1087 278 THR A OG1 2065 C CG2 . THR A 263 ? 0.5096 0.4267 0.5706 -0.1672 -0.0998 -0.0848 278 THR A CG2 2066 N N . GLU A 264 ? 0.4353 0.4304 0.5663 -0.0213 -0.0091 -0.1549 279 GLU A N 2067 C CA . GLU A 264 ? 0.4316 0.2846 0.4998 -0.0898 -0.0295 -0.1583 279 GLU A CA 2068 C C . GLU A 264 ? 0.4093 0.2981 0.3492 -0.0164 -0.0888 -0.1570 279 GLU A C 2069 O O . GLU A 264 ? 0.3658 0.2831 0.3554 0.0326 -0.0088 -0.1263 279 GLU A O 2070 C CB . GLU A 264 ? 0.4808 0.4055 0.5411 -0.0018 0.0835 -0.2501 279 GLU A CB 2071 C CG . GLU A 264 ? 0.5360 0.6108 0.6294 0.0422 0.0661 -0.0930 279 GLU A CG 2072 C CD . GLU A 264 ? 0.6701 0.7491 0.7597 0.0787 -0.0454 0.0449 279 GLU A CD 2073 O OE1 . GLU A 264 ? 0.7206 0.7798 0.8014 0.0514 -0.0211 0.0813 279 GLU A OE1 2074 O OE2 . GLU A 264 ? 0.6894 0.8404 0.8468 -0.0121 -0.0649 -0.0476 279 GLU A OE2 2075 N N . VAL A 265 ? 0.3271 0.2611 0.3182 -0.0229 -0.0402 -0.0738 280 VAL A N 2076 C CA . VAL A 265 ? 0.3322 0.3558 0.4009 0.1224 -0.0564 -0.1410 280 VAL A CA 2077 C C . VAL A 265 ? 0.3469 0.3976 0.3013 -0.0228 -0.1188 -0.1097 280 VAL A C 2078 O O . VAL A 265 ? 0.3541 0.2563 0.2431 0.0114 -0.0212 -0.0498 280 VAL A O 2079 C CB . VAL A 265 ? 0.2949 0.3127 0.3444 0.0637 -0.0030 -0.0269 280 VAL A CB 2080 C CG1 . VAL A 265 ? 0.2334 0.3193 0.4074 -0.0228 -0.0655 -0.0954 280 VAL A CG1 2081 C CG2 . VAL A 265 ? 0.3628 0.2818 0.5000 0.0355 -0.0618 -0.0667 280 VAL A CG2 2082 N N . TYR A 266 ? 0.2993 0.2064 0.3352 0.0029 0.0271 -0.1034 281 TYR A N 2083 C CA . TYR A 266 ? 0.3247 0.3475 0.1831 0.0446 -0.0525 -0.0215 281 TYR A CA 2084 C C . TYR A 266 ? 0.3465 0.3559 0.2757 0.0586 -0.0890 -0.1551 281 TYR A C 2085 O O . TYR A 266 ? 0.3597 0.2549 0.2415 0.0084 -0.0263 -0.0511 281 TYR A O 2086 C CB . TYR A 266 ? 0.3506 0.2729 0.2328 -0.0687 -0.0008 -0.0026 281 TYR A CB 2087 C CG . TYR A 266 ? 0.3028 0.2787 0.2493 -0.0843 0.0224 0.0247 281 TYR A CG 2088 C CD1 . TYR A 266 ? 0.2918 0.1941 0.3463 -0.1135 0.0151 -0.0409 281 TYR A CD1 2089 C CD2 . TYR A 266 ? 0.3760 0.2538 0.2546 -0.1033 0.0149 -0.0427 281 TYR A CD2 2090 C CE1 . TYR A 266 ? 0.2463 0.4248 0.4152 0.0198 -0.0274 -0.0602 281 TYR A CE1 2091 C CE2 . TYR A 266 ? 0.3400 0.2794 0.2712 -0.0662 0.0081 0.0248 281 TYR A CE2 2092 C CZ . TYR A 266 ? 0.2153 0.3120 0.4999 0.0208 -0.0125 -0.1150 281 TYR A CZ 2093 O OH . TYR A 266 ? 0.2980 0.3238 0.3944 -0.0006 0.0308 0.0679 281 TYR A OH 2094 N N . ASN A 267 ? 0.2657 0.3571 0.2596 -0.0579 -0.0564 -0.1006 282 ASN A N 2095 C CA . ASN A 267 ? 0.3565 0.2649 0.3661 -0.1091 -0.0689 -0.0740 282 ASN A CA 2096 C C . ASN A 267 ? 0.3321 0.2820 0.2744 0.0236 -0.0218 -0.1273 282 ASN A C 2097 O O . ASN A 267 ? 0.3428 0.3719 0.3223 0.0297 -0.0029 -0.0472 282 ASN A O 2098 C CB . ASN A 267 ? 0.4095 0.3584 0.3308 -0.0928 -0.0743 -0.0244 282 ASN A CB 2099 C CG . ASN A 267 ? 0.4184 0.3993 0.3988 -0.0083 -0.0482 -0.0640 282 ASN A CG 2100 O OD1 . ASN A 267 ? 0.3671 0.2781 0.4584 -0.0060 -0.0296 -0.0736 282 ASN A OD1 2101 N ND2 . ASN A 267 ? 0.4513 0.2812 0.4513 -0.0534 -0.0577 -0.0637 282 ASN A ND2 2102 N N . LYS A 268 ? 0.2623 0.3756 0.2879 0.0060 0.0280 -0.1323 283 LYS A N 2103 C CA . LYS A 268 ? 0.3390 0.2851 0.2252 0.0920 -0.0639 -0.1156 283 LYS A CA 2104 C C . LYS A 268 ? 0.3124 0.3695 0.2513 0.0707 -0.1146 -0.1171 283 LYS A C 2105 O O . LYS A 268 ? 0.2881 0.3643 0.2864 0.0635 -0.0392 -0.0277 283 LYS A O 2106 C CB . LYS A 268 ? 0.3636 0.3061 0.3124 0.1396 -0.0064 -0.1116 283 LYS A CB 2107 C CG . LYS A 268 ? 0.4783 0.4275 0.3605 0.0219 0.0335 0.0131 283 LYS A CG 2108 C CD . LYS A 268 ? 0.5366 0.4558 0.3549 0.0895 0.0469 -0.0800 283 LYS A CD 2109 C CE . LYS A 268 ? 0.5785 0.6980 0.7050 0.0664 -0.0093 0.0493 283 LYS A CE 2110 N NZ . LYS A 268 ? 0.6250 0.8385 0.7510 0.0441 -0.0102 -0.0080 283 LYS A NZ 2111 N N . LEU A 269 ? 0.2392 0.3132 0.2257 -0.0013 -0.0424 -0.0055 284 LEU A N 2112 C CA . LEU A 269 ? 0.2517 0.2786 0.2952 -0.0123 -0.0173 -0.0738 284 LEU A CA 2113 C C . LEU A 269 ? 0.3173 0.2804 0.2307 -0.0062 -0.0695 -0.0587 284 LEU A C 2114 O O . LEU A 269 ? 0.2630 0.2666 0.2371 0.0745 -0.0071 -0.0124 284 LEU A O 2115 C CB . LEU A 269 ? 0.2153 0.4006 0.1692 0.0700 -0.0056 -0.0227 284 LEU A CB 2116 C CG . LEU A 269 ? 0.2484 0.2446 0.2198 0.0452 -0.0446 -0.0912 284 LEU A CG 2117 C CD1 . LEU A 269 ? 0.2276 0.2814 0.3202 0.0806 -0.1133 -0.1460 284 LEU A CD1 2118 C CD2 . LEU A 269 ? 0.2237 0.2908 0.3087 -0.0217 -0.0248 -0.0582 284 LEU A CD2 2119 N N . LYS A 270 ? 0.2778 0.2287 0.2789 0.0732 -0.0138 -0.0386 285 LYS A N 2120 C CA . LYS A 270 ? 0.2122 0.1658 0.2962 0.0044 -0.0535 0.0241 285 LYS A CA 2121 C C . LYS A 270 ? 0.2204 0.2756 0.3376 0.1157 0.0607 0.0370 285 LYS A C 2122 O O . LYS A 270 ? 0.2500 0.2071 0.2955 0.0321 0.0465 -0.0144 285 LYS A O 2123 C CB . LYS A 270 ? 0.2287 0.2838 0.3080 0.0070 0.0095 -0.0910 285 LYS A CB 2124 C CG . LYS A 270 ? 0.3148 0.2564 0.3757 -0.0826 0.0727 0.0187 285 LYS A CG 2125 C CD . LYS A 270 ? 0.2495 0.3178 0.3861 0.0336 0.0616 0.0026 285 LYS A CD 2126 C CE . LYS A 270 ? 0.2195 0.3159 0.5483 0.0148 -0.0240 0.1160 285 LYS A CE 2127 N NZ . LYS A 270 ? 0.2835 0.1727 0.4276 0.0670 0.0156 -0.0009 285 LYS A NZ 2128 N N . ASN A 271 ? 0.2176 0.2648 0.2389 -0.0077 -0.0181 0.0185 286 ASN A N 2129 C CA . ASN A 271 ? 0.2710 0.2956 0.2484 -0.0872 -0.0123 -0.0387 286 ASN A CA 2130 C C . ASN A 271 ? 0.2481 0.3084 0.2178 0.0139 -0.1022 -0.0307 286 ASN A C 2131 O O . ASN A 271 ? 0.3614 0.3978 0.2778 -0.0370 -0.1103 0.0399 286 ASN A O 2132 C CB . ASN A 271 ? 0.2342 0.2114 0.2427 -0.0307 0.0149 0.0026 286 ASN A CB 2133 C CG . ASN A 271 ? 0.2343 0.3309 0.3435 -0.0694 -0.0094 -0.0446 286 ASN A CG 2134 O OD1 . ASN A 271 ? 0.2307 0.3395 0.3569 0.0326 -0.0969 -0.0727 286 ASN A OD1 2135 N ND2 . ASN A 271 ? 0.2716 0.2806 0.3856 0.0262 -0.0342 -0.0348 286 ASN A ND2 2136 N N . CYS A 272 ? 0.2286 0.3528 0.2637 0.0145 -0.0907 -0.0474 287 CYS A N 2137 C CA . CYS A 272 ? 0.2786 0.3664 0.2354 -0.1394 -0.0319 -0.0637 287 CYS A CA 2138 C C . CYS A 272 ? 0.2300 0.3488 0.1624 -0.0329 -0.0276 -0.0718 287 CYS A C 2139 O O . CYS A 272 ? 0.3391 0.2836 0.2108 -0.0061 -0.0681 0.0527 287 CYS A O 2140 C CB . CYS A 272 ? 0.2840 0.3091 0.2782 -0.0665 -0.0923 -0.0612 287 CYS A CB 2141 S SG . CYS A 272 ? 0.2380 0.3989 0.2956 -0.0235 -0.0287 -0.0321 287 CYS A SG 2142 N N . SER A 273 ? 0.1984 0.2612 0.2408 -0.0528 -0.0506 -0.0550 288 SER A N 2143 C CA . SER A 273 ? 0.2344 0.2297 0.2756 -0.0596 -0.0650 0.0453 288 SER A CA 2144 C C . SER A 273 ? 0.1659 0.2223 0.3800 -0.0197 0.0583 -0.0083 288 SER A C 2145 O O . SER A 273 ? 0.2474 0.3376 0.2799 -0.0145 -0.0031 0.0591 288 SER A O 2146 C CB . SER A 273 ? 0.2179 0.2489 0.2441 -0.0371 -0.0184 -0.0704 288 SER A CB 2147 O OG . SER A 273 ? 0.2271 0.2872 0.2363 -0.0236 -0.0577 -0.0051 288 SER A OG 2148 N N . PRO A 274 ? 0.1787 0.4033 0.2155 -0.0068 -0.0284 -0.0303 289 PRO A N 2149 C CA . PRO A 274 ? 0.1795 0.3051 0.2466 0.0005 -0.1029 0.0397 289 PRO A CA 2150 C C . PRO A 274 ? 0.1391 0.2996 0.1994 0.0454 -0.0495 -0.0665 289 PRO A C 2151 O O . PRO A 274 ? 0.2027 0.2440 0.2903 -0.0243 -0.0071 -0.0610 289 PRO A O 2152 C CB . PRO A 274 ? 0.2523 0.4036 0.2988 0.0314 -0.1473 0.0070 289 PRO A CB 2153 C CG . PRO A 274 ? 0.2564 0.3277 0.4722 0.0490 -0.0103 0.1296 289 PRO A CG 2154 C CD . PRO A 274 ? 0.2857 0.2791 0.3539 0.0772 -0.1306 -0.0008 289 PRO A CD 2155 N N . HIS A 275 ? 0.1685 0.2191 0.2256 -0.0252 -0.0726 0.0029 290 HIS A N 2156 C CA . HIS A 275 ? 0.2729 0.1353 0.2286 -0.0556 -0.0307 0.0274 290 HIS A CA 2157 C C . HIS A 275 ? 0.1893 0.2059 0.2805 -0.0481 -0.0365 0.0310 290 HIS A C 2158 O O . HIS A 275 ? 0.1918 0.1278 0.2406 -0.0169 -0.0114 0.0464 290 HIS A O 2159 C CB . HIS A 275 ? 0.2273 0.1947 0.2533 0.0297 -0.0363 0.0813 290 HIS A CB 2160 C CG . HIS A 275 ? 0.2248 0.2634 0.3005 -0.0369 -0.0463 0.1527 290 HIS A CG 2161 N ND1 . HIS A 275 ? 0.2183 0.3963 0.5035 0.0002 -0.1300 0.0823 290 HIS A ND1 2162 C CD2 . HIS A 275 ? 0.3037 0.2691 0.3035 -0.0833 -0.0527 0.1438 290 HIS A CD2 2163 C CE1 . HIS A 275 ? 0.2618 0.3409 0.4200 -0.0493 -0.1650 0.0685 290 HIS A CE1 2164 N NE2 . HIS A 275 ? 0.2384 0.3696 0.4478 -0.0479 -0.1103 0.1388 290 HIS A NE2 2165 N N . MET A 276 ? 0.1861 0.2812 0.1624 0.0135 -0.0283 0.0605 291 MET A N 2166 C CA . MET A 276 ? 0.2067 0.1951 0.2444 -0.0676 -0.0460 0.0998 291 MET A CA 2167 C C . MET A 276 ? 0.2085 0.2580 0.1940 -0.0077 -0.0970 0.0092 291 MET A C 2168 O O . MET A 276 ? 0.2616 0.3403 0.2111 -0.0899 -0.1046 0.0338 291 MET A O 2169 C CB . MET A 276 ? 0.1684 0.3094 0.2089 -0.0299 -0.0161 0.0411 291 MET A CB 2170 C CG . MET A 276 ? 0.1891 0.2823 0.2227 -0.0315 -0.0018 -0.0665 291 MET A CG 2171 S SD . MET A 276 ? 0.2488 0.2600 0.2473 0.0077 -0.0242 0.0113 291 MET A SD 2172 C CE . MET A 276 ? 0.2855 0.2105 0.1425 -0.0325 -0.0509 -0.0570 291 MET A CE 2173 N N . ASN A 277 ? 0.2409 0.1855 0.2092 -0.0142 -0.0479 0.0707 292 ASN A N 2174 C CA . ASN A 277 ? 0.2327 0.1654 0.2488 -0.0324 -0.0674 0.0934 292 ASN A CA 2175 C C . ASN A 277 ? 0.1971 0.1932 0.1757 -0.0169 -0.0898 0.0378 292 ASN A C 2176 O O . ASN A 277 ? 0.1976 0.2563 0.3413 -0.0294 -0.1252 0.0605 292 ASN A O 2177 C CB . ASN A 277 ? 0.1773 0.3460 0.1999 -0.0656 -0.0048 0.0542 292 ASN A CB 2178 C CG . ASN A 277 ? 0.1797 0.2899 0.3502 -0.0894 0.0137 -0.0250 292 ASN A CG 2179 O OD1 . ASN A 277 ? 0.2369 0.3290 0.4045 -0.0428 -0.0160 -0.0669 292 ASN A OD1 2180 N ND2 . ASN A 277 ? 0.1701 0.3653 0.2732 -0.0424 0.0067 0.0637 292 ASN A ND2 2181 N N . VAL A 278 ? 0.2422 0.2642 0.1833 -0.0802 0.0110 -0.0550 293 VAL A N 2182 C CA . VAL A 278 ? 0.2103 0.2342 0.1178 -0.0172 -0.0163 0.0429 293 VAL A CA 2183 C C . VAL A 278 ? 0.2272 0.2506 0.1682 -0.0261 -0.0095 0.0278 293 VAL A C 2184 O O . VAL A 278 ? 0.2373 0.2449 0.2614 -0.0628 -0.0312 0.0385 293 VAL A O 2185 C CB . VAL A 278 ? 0.1860 0.3437 0.1292 -0.0615 -0.0088 -0.0076 293 VAL A CB 2186 C CG1 . VAL A 278 ? 0.2121 0.1710 0.2385 0.0172 -0.0048 -0.0557 293 VAL A CG1 2187 C CG2 . VAL A 278 ? 0.1716 0.3351 0.2251 -0.0264 0.0349 0.0310 293 VAL A CG2 2188 N N . TYR A 279 ? 0.2391 0.2265 0.1596 -0.0318 -0.0355 -0.0165 294 TYR A N 2189 C CA . TYR A 279 ? 0.2360 0.2508 0.1246 -0.0265 -0.0286 -0.0374 294 TYR A CA 2190 C C . TYR A 279 ? 0.2304 0.1268 0.2292 -0.0381 0.0716 0.0317 294 TYR A C 2191 O O . TYR A 279 ? 0.2172 0.1727 0.2321 -0.0379 0.0117 0.0201 294 TYR A O 2192 C CB . TYR A 279 ? 0.1890 0.2634 0.1357 -0.0114 -0.0282 0.0632 294 TYR A CB 2193 C CG . TYR A 279 ? 0.1885 0.2112 0.1949 0.0261 0.0054 0.0372 294 TYR A CG 2194 C CD1 . TYR A 279 ? 0.1863 0.2401 0.2131 0.0180 0.0252 0.0602 294 TYR A CD1 2195 C CD2 . TYR A 279 ? 0.2092 0.3000 0.1872 -0.0707 -0.0165 0.0353 294 TYR A CD2 2196 C CE1 . TYR A 279 ? 0.1680 0.2737 0.2359 -0.0316 -0.0411 0.0424 294 TYR A CE1 2197 C CE2 . TYR A 279 ? 0.1926 0.3074 0.1983 0.0720 0.0308 0.0488 294 TYR A CE2 2198 C CZ . TYR A 279 ? 0.1580 0.1667 0.2399 0.0661 0.0474 0.0108 294 TYR A CZ 2199 O OH . TYR A 279 ? 0.1726 0.2318 0.2399 0.0096 0.0061 0.0300 294 TYR A OH 2200 N N . LEU A 280 ? 0.2888 0.1830 0.2160 -0.0708 -0.0197 -0.0136 295 LEU A N 2201 C CA . LEU A 280 ? 0.2951 0.2214 0.1978 -0.0022 -0.0585 -0.0035 295 LEU A CA 2202 C C . LEU A 280 ? 0.2437 0.2154 0.2308 -0.0701 -0.0629 0.0705 295 LEU A C 2203 O O . LEU A 280 ? 0.3190 0.1734 0.2271 -0.0261 -0.0152 0.0361 295 LEU A O 2204 C CB . LEU A 280 ? 0.3317 0.1854 0.2386 -0.0859 -0.0630 -0.0372 295 LEU A CB 2205 C CG . LEU A 280 ? 0.3657 0.2397 0.2596 -0.0576 -0.0892 -0.0844 295 LEU A CG 2206 C CD1 . LEU A 280 ? 0.3161 0.3776 0.3470 -0.1172 -0.0892 -0.1079 295 LEU A CD1 2207 C CD2 . LEU A 280 ? 0.3129 0.2786 0.3179 0.0355 -0.0132 -0.1555 295 LEU A CD2 2208 N N . LYS A 281 ? 0.2057 0.1738 0.1746 -0.0379 -0.0370 0.0168 296 LYS A N 2209 C CA . LYS A 281 ? 0.3385 0.2080 0.1950 -0.0822 -0.0271 0.0615 296 LYS A CA 2210 C C . LYS A 281 ? 0.3737 0.1915 0.2192 -0.1121 -0.0360 0.0516 296 LYS A C 2211 O O . LYS A 281 ? 0.2659 0.2273 0.2486 -0.0494 -0.0557 -0.0259 296 LYS A O 2212 C CB . LYS A 281 ? 0.2658 0.2078 0.2709 -0.0424 -0.0442 -0.0675 296 LYS A CB 2213 C CG . LYS A 281 ? 0.2610 0.2193 0.2879 -0.0426 -0.0637 0.0344 296 LYS A CG 2214 C CD . LYS A 281 ? 0.3088 0.2658 0.2146 -0.0398 -0.0753 0.0416 296 LYS A CD 2215 C CE . LYS A 281 ? 0.4354 0.3106 0.1923 -0.1925 0.0150 0.0133 296 LYS A CE 2216 N NZ . LYS A 281 ? 0.4974 0.2309 0.4455 -0.0120 -0.0471 -0.0225 296 LYS A NZ 2217 N N . GLU A 282 ? 0.2851 0.2705 0.2624 0.0202 0.0262 0.0977 297 GLU A N 2218 C CA . GLU A 282 ? 0.3098 0.1480 0.3569 -0.0340 -0.0070 0.0399 297 GLU A CA 2219 C C . GLU A 282 ? 0.2946 0.2665 0.2558 -0.0972 0.0187 -0.0570 297 GLU A C 2220 O O . GLU A 282 ? 0.2860 0.1951 0.2956 -0.0194 0.0048 0.0570 297 GLU A O 2221 C CB . GLU A 282 ? 0.3939 0.1812 0.3709 -0.0807 0.0236 -0.0359 297 GLU A CB 2222 C CG . GLU A 282 ? 0.4394 0.3145 0.3893 -0.1632 0.0566 -0.0951 297 GLU A CG 2223 C CD . GLU A 282 ? 0.4929 0.3343 0.4602 -0.0587 -0.0130 -0.0770 297 GLU A CD 2224 O OE1 . GLU A 282 ? 0.5123 0.1636 0.4133 -0.0311 -0.0484 0.0553 297 GLU A OE1 2225 O OE2 . GLU A 282 ? 0.4852 0.3410 0.6468 -0.0661 -0.1772 -0.1487 297 GLU A OE2 2226 N N . ASP A 283 ? 0.2848 0.1555 0.3034 -0.0263 -0.0332 0.0327 298 ASP A N 2227 C CA . ASP A 283 ? 0.2777 0.2315 0.2538 -0.0742 -0.0775 0.0217 298 ASP A CA 2228 C C . ASP A 283 ? 0.1875 0.3773 0.2333 -0.0812 -0.0106 0.0376 298 ASP A C 2229 O O . ASP A 283 ? 0.2315 0.2972 0.2402 -0.0648 -0.0373 0.0051 298 ASP A O 2230 C CB . ASP A 283 ? 0.2738 0.1707 0.2530 -0.0616 -0.1022 -0.0188 298 ASP A CB 2231 C CG . ASP A 283 ? 0.3243 0.2436 0.1941 -0.1103 -0.0765 -0.0138 298 ASP A CG 2232 O OD1 . ASP A 283 ? 0.2713 0.2220 0.3515 -0.0678 -0.0258 0.0183 298 ASP A OD1 2233 O OD2 . ASP A 283 ? 0.3472 0.4443 0.2524 -0.0278 -0.0855 -0.1157 298 ASP A OD2 2234 N N . ILE A 284 ? 0.1891 0.2703 0.2124 -0.1121 -0.0181 -0.0249 299 ILE A N 2235 C CA . ILE A 284 ? 0.1654 0.2499 0.2322 -0.0543 -0.0560 -0.0422 299 ILE A CA 2236 C C . ILE A 284 ? 0.2869 0.1027 0.2793 -0.0152 -0.0484 0.0005 299 ILE A C 2237 O O . ILE A 284 ? 0.2787 0.1753 0.1898 -0.0344 -0.0105 0.0144 299 ILE A O 2238 C CB . ILE A 284 ? 0.1816 0.1327 0.1836 -0.0212 -0.0354 -0.0326 299 ILE A CB 2239 C CG1 . ILE A 284 ? 0.1420 0.2332 0.2615 -0.0648 0.0228 -0.0336 299 ILE A CG1 2240 C CG2 . ILE A 284 ? 0.2140 0.1793 0.2364 -0.0173 -0.0351 0.0227 299 ILE A CG2 2241 C CD1 . ILE A 284 ? 0.1771 0.2131 0.2063 -0.0077 -0.0026 0.0057 299 ILE A CD1 2242 N N . PRO A 285 ? 0.2417 0.1399 0.1641 -0.0505 -0.0211 0.0276 300 PRO A N 2243 C CA . PRO A 285 ? 0.3028 0.1214 0.1826 0.0050 -0.0027 0.0516 300 PRO A CA 2244 C C . PRO A 285 ? 0.2068 0.1534 0.1350 -0.0529 -0.0220 0.0599 300 PRO A C 2245 O O . PRO A 285 ? 0.1729 0.1741 0.2118 -0.0388 -0.0101 0.0073 300 PRO A O 2246 C CB . PRO A 285 ? 0.4068 0.1784 0.1875 -0.0557 -0.0619 0.0556 300 PRO A CB 2247 C CG . PRO A 285 ? 0.3624 0.2669 0.1457 0.0013 -0.0448 0.0437 300 PRO A CG 2248 C CD . PRO A 285 ? 0.2724 0.1944 0.2052 0.0558 0.0490 0.0140 300 PRO A CD 2249 N N . ASN A 286 ? 0.2552 0.1937 0.1271 0.0575 0.0176 0.0556 301 ASN A N 2250 C CA . ASN A 286 ? 0.2330 0.1831 0.1971 -0.0523 0.0210 0.0831 301 ASN A CA 2251 C C . ASN A 286 ? 0.1971 0.1774 0.1983 -0.0199 -0.0338 0.0822 301 ASN A C 2252 O O . ASN A 286 ? 0.1585 0.3048 0.1907 -0.0204 -0.0429 0.0335 301 ASN A O 2253 C CB . ASN A 286 ? 0.2566 0.2085 0.3082 -0.1115 0.0316 0.0488 301 ASN A CB 2254 C CG . ASN A 286 ? 0.2010 0.3363 0.3407 -0.0540 -0.0997 0.0543 301 ASN A CG 2255 O OD1 . ASN A 286 ? 0.4205 0.2454 0.4475 -0.0864 0.0091 0.1417 301 ASN A OD1 2256 N ND2 . ASN A 286 ? 0.2536 0.3978 0.3811 -0.1101 -0.0981 0.0633 301 ASN A ND2 2257 N N . ARG A 287 ? 0.1799 0.2176 0.1715 -0.0587 0.0300 0.0603 302 ARG A N 2258 C CA . ARG A 287 ? 0.1881 0.1656 0.2230 -0.0886 -0.0322 0.0045 302 ARG A CA 2259 C C . ARG A 287 ? 0.1523 0.1947 0.2379 -0.0585 -0.0601 0.0162 302 ARG A C 2260 O O . ARG A 287 ? 0.1917 0.2641 0.1941 -0.0342 0.0028 -0.0029 302 ARG A O 2261 C CB . ARG A 287 ? 0.2032 0.1633 0.2890 -0.0299 0.0170 -0.0261 302 ARG A CB 2262 C CG . ARG A 287 ? 0.2512 0.1866 0.1638 0.0025 -0.0025 -0.0201 302 ARG A CG 2263 C CD . ARG A 287 ? 0.1634 0.3475 0.2825 0.0316 -0.0086 0.1008 302 ARG A CD 2264 N NE . ARG A 287 ? 0.2099 0.3502 0.3302 -0.0073 -0.0710 0.0974 302 ARG A NE 2265 C CZ . ARG A 287 ? 0.2286 0.2197 0.3202 0.0298 0.0434 -0.0357 302 ARG A CZ 2266 N NH1 . ARG A 287 ? 0.1809 0.1912 0.2892 -0.0333 0.0327 0.0263 302 ARG A NH1 2267 N NH2 . ARG A 287 ? 0.2017 0.3405 0.2156 -0.0023 0.0056 -0.0164 302 ARG A NH2 2268 N N . PHE A 288 ? 0.1221 0.2071 0.2024 0.0283 -0.0076 0.0001 303 PHE A N 2269 C CA . PHE A 288 ? 0.1623 0.1223 0.2658 0.0259 0.0289 -0.0064 303 PHE A CA 2270 C C . PHE A 288 ? 0.2504 0.1836 0.1952 -0.0981 0.0437 0.0178 303 PHE A C 2271 O O . PHE A 288 ? 0.2518 0.1579 0.1402 -0.0571 -0.0065 0.0330 303 PHE A O 2272 C CB . PHE A 288 ? 0.1703 0.3031 0.1120 -0.0388 0.0237 0.0317 303 PHE A CB 2273 C CG . PHE A 288 ? 0.1427 0.2624 0.1435 -0.0354 0.0133 0.0452 303 PHE A CG 2274 C CD1 . PHE A 288 ? 0.2705 0.2780 0.1634 0.0454 -0.0332 0.0310 303 PHE A CD1 2275 C CD2 . PHE A 288 ? 0.1462 0.1614 0.2546 0.0285 0.0191 0.0167 303 PHE A CD2 2276 C CE1 . PHE A 288 ? 0.2503 0.2985 0.2031 0.1438 -0.0200 0.0171 303 PHE A CE1 2277 C CE2 . PHE A 288 ? 0.1875 0.1264 0.3263 -0.0346 0.0095 0.0498 303 PHE A CE2 2278 C CZ . PHE A 288 ? 0.1792 0.1713 0.3015 0.0301 0.0312 0.0915 303 PHE A CZ 2279 N N . TYR A 289 ? 0.1720 0.2325 0.1670 0.0022 -0.0104 0.0701 304 TYR A N 2280 C CA . TYR A 289 ? 0.2068 0.1920 0.1038 -0.0486 0.0104 -0.0201 304 TYR A CA 2281 C C . TYR A 289 ? 0.2063 0.2056 0.1870 -0.0586 0.0059 0.0873 304 TYR A C 2282 O O . TYR A 289 ? 0.1955 0.1541 0.1758 -0.0294 -0.0119 0.0427 304 TYR A O 2283 C CB . TYR A 289 ? 0.2636 0.1293 0.1728 0.0247 0.0508 0.0124 304 TYR A CB 2284 C CG . TYR A 289 ? 0.1825 0.3085 0.1505 0.0414 -0.0313 -0.0430 304 TYR A CG 2285 C CD1 . TYR A 289 ? 0.2564 0.2187 0.2076 -0.0207 -0.0034 0.0191 304 TYR A CD1 2286 C CD2 . TYR A 289 ? 0.1833 0.3213 0.2172 0.0107 -0.0571 -0.0215 304 TYR A CD2 2287 C CE1 . TYR A 289 ? 0.2922 0.3340 0.1469 0.0364 0.0427 -0.0218 304 TYR A CE1 2288 C CE2 . TYR A 289 ? 0.2608 0.3451 0.2276 -0.0165 0.0300 0.0807 304 TYR A CE2 2289 C CZ . TYR A 289 ? 0.1917 0.3232 0.2653 0.0371 0.0014 -0.0502 304 TYR A CZ 2290 O OH . TYR A 289 ? 0.2520 0.4223 0.3709 0.0347 0.0886 -0.0047 304 TYR A OH 2291 N N . TYR A 290 ? 0.2401 0.1665 0.1777 0.0466 -0.0102 0.0270 305 TYR A N 2292 C CA . TYR A 290 ? 0.2698 0.2143 0.2057 -0.0429 0.0467 -0.0246 305 TYR A CA 2293 C C . TYR A 290 ? 0.2451 0.2347 0.2049 0.0418 0.0511 0.1044 305 TYR A C 2294 O O . TYR A 290 ? 0.2275 0.3429 0.1712 -0.0362 -0.0076 0.0582 305 TYR A O 2295 C CB . TYR A 290 ? 0.1707 0.1924 0.1879 0.0143 0.0084 0.0235 305 TYR A CB 2296 C CG . TYR A 290 ? 0.1829 0.2246 0.1759 0.0010 -0.0215 -0.0228 305 TYR A CG 2297 C CD1 . TYR A 290 ? 0.1939 0.1878 0.1949 0.0268 -0.0064 -0.0079 305 TYR A CD1 2298 C CD2 . TYR A 290 ? 0.1921 0.2377 0.1297 0.0369 -0.0310 0.0612 305 TYR A CD2 2299 C CE1 . TYR A 290 ? 0.1225 0.2083 0.2906 0.0212 -0.0070 0.0060 305 TYR A CE1 2300 C CE2 . TYR A 290 ? 0.2091 0.1556 0.1357 -0.0097 0.0398 0.0228 305 TYR A CE2 2301 C CZ . TYR A 290 ? 0.1432 0.2358 0.2458 0.0042 0.0386 0.1135 305 TYR A CZ 2302 O OH . TYR A 290 ? 0.2085 0.1537 0.1655 0.0091 0.0059 -0.0118 305 TYR A OH 2303 N N . GLN A 291 ? 0.2057 0.1474 0.2578 -0.0079 -0.0116 -0.0040 306 GLN A N 2304 C CA . GLN A 291 ? 0.1812 0.2988 0.3278 0.0241 -0.0170 -0.0835 306 GLN A CA 2305 C C . GLN A 291 ? 0.2120 0.3431 0.2677 0.0215 0.0460 -0.1283 306 GLN A C 2306 O O . GLN A 291 ? 0.2533 0.2518 0.2539 0.0383 0.0192 -0.0206 306 GLN A O 2307 C CB . GLN A 291 ? 0.2168 0.4392 0.4326 -0.0220 -0.0063 0.0147 306 GLN A CB 2308 C CG . GLN A 291 ? 0.3184 0.4718 0.5068 0.0522 0.0550 0.0874 306 GLN A CG 2309 C CD . GLN A 291 ? 0.2688 0.3464 0.4158 0.0017 0.0624 0.1339 306 GLN A CD 2310 O OE1 . GLN A 291 ? 0.3147 0.4361 0.3908 -0.0832 -0.0674 0.1843 306 GLN A OE1 2311 N NE2 . GLN A 291 ? 0.2985 0.4872 0.3735 -0.0105 -0.0364 0.0482 306 GLN A NE2 2312 N N . HIS A 292 ? 0.2705 0.2441 0.2123 -0.0541 0.0002 0.0141 307 HIS A N 2313 C CA . HIS A 292 ? 0.3190 0.2157 0.2785 -0.0778 0.0199 0.1030 307 HIS A CA 2314 C C . HIS A 292 ? 0.3644 0.1427 0.2904 -0.0360 0.1172 0.0107 307 HIS A C 2315 O O . HIS A 292 ? 0.3925 0.1539 0.3004 -0.0359 0.0082 0.0482 307 HIS A O 2316 C CB . HIS A 292 ? 0.2849 0.3080 0.3394 -0.0604 0.0250 0.1601 307 HIS A CB 2317 C CG . HIS A 292 ? 0.3422 0.3762 0.4774 -0.0709 0.1492 0.1240 307 HIS A CG 2318 N ND1 . HIS A 292 ? 0.3609 0.4596 0.6303 0.0149 0.1221 0.0996 307 HIS A ND1 2319 C CD2 . HIS A 292 ? 0.3351 0.5032 0.5251 -0.0731 0.2023 0.0589 307 HIS A CD2 2320 C CE1 . HIS A 292 ? 0.2606 0.3140 0.5744 -0.0393 0.0656 0.0011 307 HIS A CE1 2321 N NE2 . HIS A 292 ? 0.2893 0.6519 0.6660 -0.1026 0.0530 -0.0103 307 HIS A NE2 2322 N N . ASN A 293 ? 0.3108 0.1278 0.2420 -0.0164 0.0366 -0.0296 308 ASN A N 2323 C CA . ASN A 293 ? 0.2426 0.1972 0.2735 -0.0563 -0.0120 -0.0144 308 ASN A CA 2324 C C . ASN A 293 ? 0.3268 0.2045 0.2608 0.0846 -0.1420 -0.0392 308 ASN A C 2325 O O . ASN A 293 ? 0.2547 0.1638 0.2412 0.0196 -0.0257 0.0215 308 ASN A O 2326 C CB . ASN A 293 ? 0.2221 0.1534 0.3016 -0.0420 -0.0629 0.0859 308 ASN A CB 2327 C CG . ASN A 293 ? 0.1949 0.1792 0.2420 0.0129 0.0079 0.0554 308 ASN A CG 2328 O OD1 . ASN A 293 ? 0.2747 0.1338 0.2800 -0.0232 0.0302 0.0355 308 ASN A OD1 2329 N ND2 . ASN A 293 ? 0.3001 0.2150 0.2018 -0.0140 -0.0263 0.0492 308 ASN A ND2 2330 N N . ASP A 294 ? 0.2283 0.2149 0.2878 0.0134 -0.0080 0.0244 309 ASP A N 2331 C CA . ASP A 294 ? 0.3339 0.1391 0.3000 0.0742 0.0128 -0.0402 309 ASP A CA 2332 C C . ASP A 294 ? 0.3381 0.2041 0.2627 -0.0042 -0.0883 0.0179 309 ASP A C 2333 O O . ASP A 294 ? 0.3836 0.2009 0.2749 -0.0313 -0.0430 -0.0351 309 ASP A O 2334 C CB . ASP A 294 ? 0.4450 0.2940 0.4200 0.1087 0.0551 0.1168 309 ASP A CB 2335 C CG . ASP A 294 ? 0.4855 0.5939 0.5180 0.1324 -0.0216 0.1103 309 ASP A CG 2336 O OD1 . ASP A 294 ? 0.5556 0.3849 0.6066 -0.0648 0.1023 0.2115 309 ASP A OD1 2337 O OD2 . ASP A 294 ? 0.6076 0.6607 0.7550 0.1402 0.0793 0.0548 309 ASP A OD2 2338 N N . ARG A 295 ? 0.3321 0.2459 0.2302 0.0444 -0.0246 0.0567 310 ARG A N 2339 C CA . ARG A 295 ? 0.3194 0.1966 0.2110 -0.0246 -0.0493 0.0301 310 ARG A CA 2340 C C . ARG A 295 ? 0.3010 0.1438 0.3902 -0.0147 -0.0098 -0.0779 310 ARG A C 2341 O O . ARG A 295 ? 0.2925 0.2143 0.2701 0.0099 -0.0473 -0.0029 310 ARG A O 2342 C CB . ARG A 295 ? 0.3052 0.2008 0.1825 0.0044 -0.0360 0.0193 310 ARG A CB 2343 C CG . ARG A 295 ? 0.2508 0.2210 0.2196 0.0860 -0.0428 0.0422 310 ARG A CG 2344 C CD . ARG A 295 ? 0.2949 0.2825 0.2258 0.0224 -0.0218 -0.0116 310 ARG A CD 2345 N NE . ARG A 295 ? 0.2456 0.2941 0.2224 -0.0091 0.0455 0.0139 310 ARG A NE 2346 C CZ . ARG A 295 ? 0.2615 0.1326 0.2101 0.0671 0.0099 -0.0374 310 ARG A CZ 2347 N NH1 . ARG A 295 ? 0.2514 0.1421 0.2631 0.0484 -0.0009 -0.0310 310 ARG A NH1 2348 N NH2 . ARG A 295 ? 0.2671 0.2330 0.3012 0.0424 -0.0628 0.0811 310 ARG A NH2 2349 N N . ILE A 296 ? 0.2771 0.1268 0.2182 -0.0372 -0.0601 -0.0019 311 ILE A N 2350 C CA . ILE A 296 ? 0.2391 0.1806 0.1991 0.0217 -0.0325 -0.0804 311 ILE A CA 2351 C C . ILE A 296 ? 0.2515 0.1135 0.2187 -0.0006 -0.0066 0.0684 311 ILE A C 2352 O O . ILE A 296 ? 0.2474 0.1510 0.2791 -0.0023 -0.0245 0.0421 311 ILE A O 2353 C CB . ILE A 296 ? 0.2129 0.2035 0.1970 -0.0003 -0.0351 -0.0192 311 ILE A CB 2354 C CG1 . ILE A 296 ? 0.2035 0.3133 0.1540 0.0262 0.0284 -0.0106 311 ILE A CG1 2355 C CG2 . ILE A 296 ? 0.2398 0.1938 0.2361 0.0066 -0.0496 0.0014 311 ILE A CG2 2356 C CD1 . ILE A 296 ? 0.2081 0.2731 0.2263 -0.0133 0.0097 0.0199 311 ILE A CD1 2357 N N . GLN A 297 ? 0.2821 0.2098 0.1455 0.0566 0.0120 0.0434 312 GLN A N 2358 C CA . GLN A 297 ? 0.2731 0.0887 0.1744 0.0002 -0.0396 -0.0018 312 GLN A CA 2359 C C . GLN A 297 ? 0.2449 0.0953 0.2388 -0.0124 -0.0072 -0.0490 312 GLN A C 2360 O O . GLN A 297 ? 0.2828 0.1770 0.2025 0.0513 -0.0083 0.0095 312 GLN A O 2361 C CB . GLN A 297 ? 0.1947 0.2051 0.2875 -0.0004 0.0072 0.0386 312 GLN A CB 2362 C CG . GLN A 297 ? 0.2542 0.1427 0.2944 0.0569 0.0340 0.0077 312 GLN A CG 2363 C CD . GLN A 297 ? 0.2727 0.2238 0.2162 0.0105 0.0095 -0.1188 312 GLN A CD 2364 O OE1 . GLN A 297 ? 0.2811 0.1881 0.2492 0.0430 -0.0251 -0.0714 312 GLN A OE1 2365 N NE2 . GLN A 297 ? 0.2425 0.2350 0.2169 -0.0010 -0.0534 0.0429 312 GLN A NE2 2366 N N . PRO A 298 ? 0.2786 0.1211 0.2352 -0.0486 -0.0481 -0.0174 313 PRO A N 2367 C CA . PRO A 298 ? 0.3169 0.1692 0.3072 -0.0794 -0.0883 -0.0194 313 PRO A CA 2368 C C . PRO A 298 ? 0.2991 0.1692 0.1985 -0.0829 0.0478 0.0252 313 PRO A C 2369 O O . PRO A 298 ? 0.2753 0.1096 0.2354 -0.0443 0.0279 -0.0099 313 PRO A O 2370 C CB . PRO A 298 ? 0.2984 0.2034 0.4306 0.0367 -0.0150 -0.0729 313 PRO A CB 2371 C CG . PRO A 298 ? 0.2978 0.1226 0.3596 0.0287 -0.0538 0.0261 313 PRO A CG 2372 C CD . PRO A 298 ? 0.3374 0.2030 0.4423 0.0887 0.0679 -0.0296 313 PRO A CD 2373 N N . ILE A 299 ? 0.2596 0.1784 0.1503 -0.0001 -0.0232 0.0127 314 ILE A N 2374 C CA . ILE A 299 ? 0.3417 0.1875 0.1484 -0.0515 -0.0661 -0.0099 314 ILE A CA 2375 C C . ILE A 299 ? 0.2262 0.1798 0.2339 0.0023 0.0641 -0.0225 314 ILE A C 2376 O O . ILE A 299 ? 0.2283 0.1776 0.2175 -0.0083 0.0080 -0.0194 314 ILE A O 2377 C CB . ILE A 299 ? 0.3183 0.1096 0.1919 0.0112 -0.0566 -0.0226 314 ILE A CB 2378 C CG1 . ILE A 299 ? 0.3179 0.2216 0.2501 0.0001 -0.0579 -0.1163 314 ILE A CG1 2379 C CG2 . ILE A 299 ? 0.2487 0.1723 0.2510 -0.0267 -0.0180 0.0221 314 ILE A CG2 2380 C CD1 . ILE A 299 ? 0.3365 0.2272 0.2402 -0.0106 -0.0419 -0.1181 314 ILE A CD1 2381 N N . ILE A 300 ? 0.2289 0.1640 0.1586 -0.0055 -0.0218 0.0083 315 ILE A N 2382 C CA . ILE A 300 ? 0.2124 0.1580 0.1830 -0.0413 -0.0332 0.0539 315 ILE A CA 2383 C C . ILE A 300 ? 0.1764 0.2184 0.1858 0.0526 0.0018 0.0043 315 ILE A C 2384 O O . ILE A 300 ? 0.1980 0.1466 0.2745 -0.0062 -0.0246 -0.0053 315 ILE A O 2385 C CB . ILE A 300 ? 0.2130 0.3450 0.2338 0.0257 -0.0248 0.0335 315 ILE A CB 2386 C CG1 . ILE A 300 ? 0.2810 0.1831 0.2608 0.0535 -0.1042 0.0323 315 ILE A CG1 2387 C CG2 . ILE A 300 ? 0.3505 0.1866 0.1707 -0.0005 -0.0666 -0.0560 315 ILE A CG2 2388 C CD1 . ILE A 300 ? 0.2827 0.2503 0.2448 -0.0499 -0.0471 -0.1150 315 ILE A CD1 2389 N N . LEU A 301 ? 0.2416 0.2125 0.1589 -0.0153 0.0084 0.0171 316 LEU A N 2390 C CA . LEU A 301 ? 0.2394 0.1321 0.1501 0.0122 0.0084 -0.0637 316 LEU A CA 2391 C C . LEU A 301 ? 0.2142 0.0963 0.1233 0.0370 -0.0303 -0.0303 316 LEU A C 2392 O O . LEU A 301 ? 0.2128 0.2321 0.2508 -0.0611 -0.0433 -0.0542 316 LEU A O 2393 C CB . LEU A 301 ? 0.1968 0.2237 0.1412 -0.0202 0.0080 -0.0420 316 LEU A CB 2394 C CG . LEU A 301 ? 0.2736 0.1329 0.1056 -0.0199 0.0138 -0.0313 316 LEU A CG 2395 C CD1 . LEU A 301 ? 0.2295 0.2334 0.1581 -0.0296 -0.0029 0.0083 316 LEU A CD1 2396 C CD2 . LEU A 301 ? 0.2391 0.2764 0.2731 -0.0843 -0.0795 -0.0546 316 LEU A CD2 2397 N N . VAL A 302 ? 0.1767 0.0981 0.2217 0.0108 -0.0249 -0.0117 317 VAL A N 2398 C CA . VAL A 302 ? 0.1840 0.1534 0.2050 -0.0064 0.0248 0.0878 317 VAL A CA 2399 C C . VAL A 302 ? 0.1297 0.0959 0.1859 -0.0116 -0.0220 0.0352 317 VAL A C 2400 O O . VAL A 302 ? 0.1185 0.2194 0.1695 0.0024 -0.0412 0.0400 317 VAL A O 2401 C CB . VAL A 302 ? 0.1675 0.1429 0.1515 -0.0150 0.0003 0.0684 317 VAL A CB 2402 C CG1 . VAL A 302 ? 0.2058 0.1609 0.1940 -0.0133 -0.0533 -0.0293 317 VAL A CG1 2403 C CG2 . VAL A 302 ? 0.2061 0.2008 0.1799 -0.0234 -0.0222 0.0680 317 VAL A CG2 2404 N N . ALA A 303 ? 0.1772 0.1644 0.1479 -0.0217 -0.0186 0.0046 318 ALA A N 2405 C CA . ALA A 303 ? 0.1787 0.1317 0.1630 -0.0220 0.0142 0.0694 318 ALA A CA 2406 C C . ALA A 303 ? 0.1335 0.2943 0.1534 -0.0473 -0.0361 -0.0243 318 ALA A C 2407 O O . ALA A 303 ? 0.1178 0.2133 0.1686 -0.0174 -0.0264 0.0005 318 ALA A O 2408 C CB . ALA A 303 ? 0.1714 0.2145 0.1702 -0.0176 0.0022 -0.0201 318 ALA A CB 2409 N N . ASP A 304 ? 0.1033 0.2783 0.1880 0.0159 -0.0055 -0.0158 319 ASP A N 2410 C CA . ASP A 304 ? 0.1550 0.1650 0.1854 -0.0191 -0.0458 -0.0126 319 ASP A CA 2411 C C . ASP A 304 ? 0.1401 0.2221 0.1262 -0.0129 0.0018 -0.0165 319 ASP A C 2412 O O . ASP A 304 ? 0.1606 0.2166 0.1602 -0.0048 0.0456 0.0354 319 ASP A O 2413 C CB . ASP A 304 ? 0.1643 0.2441 0.1726 -0.0546 -0.0667 0.0789 319 ASP A CB 2414 C CG . ASP A 304 ? 0.1324 0.2421 0.2086 0.0560 -0.0537 -0.0054 319 ASP A CG 2415 O OD1 . ASP A 304 ? 0.1665 0.2192 0.3781 -0.0124 -0.0791 0.0933 319 ASP A OD1 2416 O OD2 . ASP A 304 ? 0.1527 0.3071 0.2729 0.0096 -0.0696 0.0207 319 ASP A OD2 2417 N N . GLU A 305 ? 0.1266 0.2389 0.1850 -0.0055 -0.0248 0.0377 320 GLU A N 2418 C CA . GLU A 305 ? 0.1585 0.2069 0.1322 -0.0094 0.0571 0.0110 320 GLU A CA 2419 C C . GLU A 305 ? 0.1395 0.1640 0.1442 -0.0151 0.0646 -0.0052 320 GLU A C 2420 O O . GLU A 305 ? 0.1886 0.2168 0.1818 0.0231 -0.0170 -0.0103 320 GLU A O 2421 C CB . GLU A 305 ? 0.1646 0.1285 0.1562 0.0178 0.0164 0.0613 320 GLU A CB 2422 C CG . GLU A 305 ? 0.2210 0.1985 0.2483 -0.0485 0.0823 -0.0030 320 GLU A CG 2423 C CD . GLU A 305 ? 0.1513 0.2806 0.2134 0.0440 -0.0272 0.0520 320 GLU A CD 2424 O OE1 . GLU A 305 ? 0.1928 0.3109 0.2850 0.0745 -0.0573 -0.0498 320 GLU A OE1 2425 O OE2 . GLU A 305 ? 0.2455 0.2752 0.2605 0.0247 -0.0471 -0.0240 320 GLU A OE2 2426 N N . GLY A 306 ? 0.1616 0.1508 0.1813 -0.0337 0.0359 -0.0061 321 GLY A N 2427 C CA . GLY A 306 ? 0.2313 0.1932 0.1308 -0.0215 0.0701 0.0309 321 GLY A CA 2428 C C . GLY A 306 ? 0.1591 0.1873 0.2095 0.0023 0.0392 -0.0252 321 GLY A C 2429 O O . GLY A 306 ? 0.1710 0.2418 0.1674 -0.0118 -0.0013 0.0186 321 GLY A O 2430 N N . TRP A 307 ? 0.1350 0.1293 0.1267 0.0185 0.0044 0.0380 322 TRP A N 2431 C CA . TRP A 307 ? 0.1399 0.3311 0.1531 0.0065 0.0096 -0.0402 322 TRP A CA 2432 C C . TRP A 307 ? 0.1439 0.2196 0.1891 -0.0024 0.0367 0.0600 322 TRP A C 2433 O O . TRP A 307 ? 0.1964 0.1996 0.1364 0.0265 0.0094 0.0481 322 TRP A O 2434 C CB . TRP A 307 ? 0.1954 0.1981 0.1385 0.0342 -0.0670 0.0283 322 TRP A CB 2435 C CG . TRP A 307 ? 0.1742 0.2179 0.1321 0.0143 -0.0259 0.0738 322 TRP A CG 2436 C CD1 . TRP A 307 ? 0.1233 0.2677 0.2790 0.0357 -0.0327 0.0038 322 TRP A CD1 2437 C CD2 . TRP A 307 ? 0.1753 0.3127 0.1610 -0.0119 0.0224 0.0957 322 TRP A CD2 2438 N NE1 . TRP A 307 ? 0.1600 0.2913 0.2489 -0.0417 -0.0363 0.0622 322 TRP A NE1 2439 C CE2 . TRP A 307 ? 0.1728 0.3578 0.2099 -0.0298 -0.0039 0.0246 322 TRP A CE2 2440 C CE3 . TRP A 307 ? 0.2232 0.2401 0.1173 -0.0393 -0.0122 0.0245 322 TRP A CE3 2441 C CZ2 . TRP A 307 ? 0.2200 0.2559 0.2354 -0.0503 -0.0516 -0.0561 322 TRP A CZ2 2442 C CZ3 . TRP A 307 ? 0.1900 0.3396 0.2139 0.0202 0.0144 -0.0627 322 TRP A CZ3 2443 C CH2 . TRP A 307 ? 0.1780 0.1875 0.2612 -0.0111 0.0110 0.0660 322 TRP A CH2 2444 N N . THR A 308 ? 0.1227 0.2078 0.2307 -0.0408 0.0098 -0.0078 323 THR A N 2445 C CA . THR A 308 ? 0.1641 0.2615 0.1188 -0.0059 0.0004 -0.0047 323 THR A CA 2446 C C . THR A 308 ? 0.1652 0.2275 0.1031 -0.0247 0.0223 0.0198 323 THR A C 2447 O O . THR A 308 ? 0.2241 0.1712 0.1278 0.0005 -0.0234 -0.0061 323 THR A O 2448 C CB . THR A 308 ? 0.1391 0.0914 0.2443 -0.0129 0.0315 -0.0363 323 THR A CB 2449 O OG1 . THR A 308 ? 0.1920 0.1611 0.1702 -0.0354 -0.0032 0.0135 323 THR A OG1 2450 C CG2 . THR A 308 ? 0.1241 0.2854 0.1192 0.0019 0.0210 0.0552 323 THR A CG2 2451 N N . ILE A 309 ? 0.2159 0.1524 0.1228 -0.0535 -0.0361 0.0145 324 ILE A N 2452 C CA . ILE A 309 ? 0.1763 0.1167 0.1843 -0.0069 -0.0298 0.0557 324 ILE A CA 2453 C C . ILE A 309 ? 0.1795 0.2545 0.1708 0.0025 -0.0345 -0.0795 324 ILE A C 2454 O O . ILE A 309 ? 0.2080 0.1710 0.1640 -0.0255 -0.0087 0.0350 324 ILE A O 2455 C CB . ILE A 309 ? 0.1792 0.0679 0.1441 0.0262 0.0022 -0.0063 324 ILE A CB 2456 C CG1 . ILE A 309 ? 0.1594 0.2490 0.1628 -0.0140 0.0220 0.0477 324 ILE A CG1 2457 C CG2 . ILE A 309 ? 0.2217 0.1728 0.1666 -0.0199 0.0493 -0.0533 324 ILE A CG2 2458 C CD1 . ILE A 309 ? 0.2462 0.2072 0.1182 -0.0224 0.0149 0.0335 324 ILE A CD1 2459 N N . VAL A 310 ? 0.2032 0.1498 0.2043 0.0047 0.0455 -0.0404 325 VAL A N 2460 C CA . VAL A 310 ? 0.2277 0.1642 0.2507 0.0498 0.0019 -0.0893 325 VAL A CA 2461 C C . VAL A 310 ? 0.2471 0.1469 0.1232 -0.0850 0.0315 -0.0070 325 VAL A C 2462 O O . VAL A 310 ? 0.2311 0.2360 0.1923 -0.0362 0.0138 -0.0317 325 VAL A O 2463 C CB . VAL A 310 ? 0.2727 0.1718 0.1902 0.0670 -0.0271 0.0067 325 VAL A CB 2464 C CG1 . VAL A 310 ? 0.2160 0.2057 0.1973 -0.0143 0.0381 0.0531 325 VAL A CG1 2465 C CG2 . VAL A 310 ? 0.2278 0.2797 0.1771 -0.0008 -0.0348 -0.0118 325 VAL A CG2 2466 N N . LEU A 311 ? 0.2243 0.2553 0.1767 -0.0204 0.0889 0.0103 326 LEU A N 2467 C CA . LEU A 311 ? 0.2944 0.3382 0.1372 0.0225 0.0775 0.0167 326 LEU A CA 2468 C C . LEU A 311 ? 0.2528 0.2851 0.2042 0.0867 0.0685 -0.0515 326 LEU A C 2469 O O . LEU A 311 ? 0.2971 0.2864 0.1615 0.0224 0.0766 -0.0133 326 LEU A O 2470 C CB . LEU A 311 ? 0.3105 0.3386 0.2206 0.0693 0.0048 -0.0299 326 LEU A CB 2471 C CG . LEU A 311 ? 0.2838 0.2795 0.2722 0.0701 -0.0182 0.0920 326 LEU A CG 2472 C CD1 . LEU A 311 ? 0.3399 0.4253 0.4084 0.0995 -0.0264 -0.0049 326 LEU A CD1 2473 C CD2 . LEU A 311 ? 0.3688 0.2456 0.3354 -0.1232 0.0263 0.0503 326 LEU A CD2 2474 N N . ASN A 312 ? 0.2348 0.3278 0.2131 0.0033 0.0769 -0.0176 327 ASN A N 2475 C CA . ASN A 312 ? 0.3800 0.2511 0.1801 -0.0476 0.0768 0.0070 327 ASN A CA 2476 C C . ASN A 312 ? 0.3486 0.3578 0.1975 -0.0508 0.0759 0.0377 327 ASN A C 2477 O O . ASN A 312 ? 0.3578 0.4415 0.2331 -0.0712 0.0762 0.0782 327 ASN A O 2478 C CB . ASN A 312 ? 0.4002 0.3884 0.1679 -0.0469 0.0521 -0.0714 327 ASN A CB 2479 C CG . ASN A 312 ? 0.4178 0.3739 0.3968 0.0193 0.0661 -0.0185 327 ASN A CG 2480 O OD1 . ASN A 312 ? 0.4353 0.5021 0.1871 -0.0176 0.0521 -0.0667 327 ASN A OD1 2481 N ND2 . ASN A 312 ? 0.4701 0.3634 0.3272 0.0569 0.0879 0.0976 327 ASN A ND2 2482 N N . GLU A 313 ? 0.2922 0.2872 0.2184 -0.0347 0.0894 -0.0682 328 GLU A N 2483 C CA . GLU A 313 ? 0.3745 0.3348 0.2957 -0.0891 0.0538 -0.0588 328 GLU A CA 2484 C C . GLU A 313 ? 0.3114 0.3202 0.2451 -0.0449 0.0349 -0.0408 328 GLU A C 2485 O O . GLU A 313 ? 0.2532 0.4276 0.2744 -0.0419 0.0660 -0.0268 328 GLU A O 2486 C CB . GLU A 313 ? 0.4460 0.3579 0.2377 -0.0709 0.0379 -0.1289 328 GLU A CB 2487 C CG . GLU A 313 ? 0.3367 0.4232 0.3205 -0.0881 0.1258 -0.1005 328 GLU A CG 2488 C CD . GLU A 313 ? 0.5375 0.6289 0.5927 -0.0039 0.1029 -0.0371 328 GLU A CD 2489 O OE1 . GLU A 313 ? 0.5429 0.6557 0.5695 0.0289 0.0482 -0.2354 328 GLU A OE1 2490 O OE2 . GLU A 313 ? 0.6064 0.7003 0.6293 -0.0051 0.0762 -0.0423 328 GLU A OE2 2491 N N . SER A 314 ? 0.3089 0.3117 0.1748 0.0318 0.1004 0.0205 329 SER A N 2492 C CA . SER A 314 ? 0.2539 0.2787 0.1520 -0.0366 0.0639 0.0304 329 SER A CA 2493 C C . SER A 314 ? 0.2467 0.2919 0.2285 -0.0589 0.0724 -0.0204 329 SER A C 2494 O O . SER A 314 ? 0.2929 0.4230 0.2776 -0.0399 0.0391 -0.0025 329 SER A O 2495 C CB . SER A 314 ? 0.3277 0.1884 0.1875 -0.0245 0.1174 0.0116 329 SER A CB 2496 O OG . SER A 314 ? 0.3554 0.3238 0.1748 -0.0737 0.0469 -0.0332 329 SER A OG 2497 N N . SER A 315 ? 0.2690 0.2809 0.2915 -0.0535 0.0749 -0.0771 330 SER A N 2498 C CA . SER A 315 ? 0.2510 0.3657 0.2786 0.0476 0.1189 -0.0496 330 SER A CA 2499 C C . SER A 315 ? 0.1921 0.2774 0.2465 -0.0739 0.0854 -0.0040 330 SER A C 2500 O O . SER A 315 ? 0.2564 0.3522 0.2136 -0.0563 0.0826 0.0023 330 SER A O 2501 C CB . SER A 315 ? 0.4108 0.3780 0.4703 -0.0278 -0.1831 0.0629 330 SER A CB 2502 O OG . SER A 315 ? 0.4802 0.6056 0.5503 0.0075 -0.1703 0.0420 330 SER A OG 2503 N N . GLN A 316 ? 0.2642 0.2477 0.2554 -0.0597 0.0897 -0.0369 331 GLN A N 2504 C CA . GLN A 316 ? 0.2650 0.3218 0.2212 0.0040 0.0111 -0.1413 331 GLN A CA 2505 C C . GLN A 316 ? 0.1904 0.2748 0.2508 -0.0147 0.1029 -0.0307 331 GLN A C 2506 O O . GLN A 316 ? 0.2078 0.3252 0.2690 -0.0216 0.0275 -0.0378 331 GLN A O 2507 C CB . GLN A 316 ? 0.3019 0.3188 0.2188 0.0849 0.0531 0.0059 331 GLN A CB 2508 C CG . GLN A 316 ? 0.3145 0.3152 0.2991 0.0403 -0.0202 -0.0512 331 GLN A CG 2509 C CD . GLN A 316 ? 0.3750 0.4669 0.3374 -0.0762 0.0198 -0.0662 331 GLN A CD 2510 O OE1 . GLN A 316 ? 0.5392 0.5509 0.2919 -0.0297 0.0209 0.0215 331 GLN A OE1 2511 N NE2 . GLN A 316 ? 0.3151 0.5792 0.3389 -0.0695 -0.0805 0.0787 331 GLN A NE2 2512 N N . LYS A 317 ? 0.2233 0.2654 0.1494 0.0029 0.0105 -0.0353 332 LYS A N 2513 C CA . LYS A 317 ? 0.2673 0.2050 0.1003 -0.0113 0.0399 0.0248 332 LYS A CA 2514 C C . LYS A 317 ? 0.3035 0.1898 0.1529 -0.1052 0.0764 -0.0448 332 LYS A C 2515 O O . LYS A 317 ? 0.2723 0.1297 0.1580 -0.0372 0.0057 0.0174 332 LYS A O 2516 C CB . LYS A 317 ? 0.2349 0.2776 0.2763 -0.0565 0.0218 0.0417 332 LYS A CB 2517 C CG . LYS A 317 ? 0.3377 0.2491 0.2734 -0.0971 -0.0079 0.0684 332 LYS A CG 2518 C CD . LYS A 317 ? 0.3870 0.2667 0.3329 0.0050 0.0219 0.1026 332 LYS A CD 2519 C CE . LYS A 317 ? 0.3923 0.4143 0.2331 0.0036 -0.0663 0.0571 332 LYS A CE 2520 N NZ . LYS A 317 ? 0.3865 0.4321 0.3685 -0.0106 -0.1127 0.0388 332 LYS A NZ 2521 N N . LEU A 318 ? 0.2856 0.2010 0.1375 0.0293 0.0441 -0.0116 333 LEU A N 2522 C CA . LEU A 318 ? 0.2794 0.1261 0.1396 0.0356 0.0782 0.0092 333 LEU A CA 2523 C C . LEU A 318 ? 0.2860 0.1170 0.1341 0.0466 0.0489 0.0145 333 LEU A C 2524 O O . LEU A 318 ? 0.2582 0.1166 0.2063 0.0369 -0.0051 0.0561 333 LEU A O 2525 C CB . LEU A 318 ? 0.2975 0.1502 0.1851 -0.0232 -0.0194 0.0619 333 LEU A CB 2526 C CG . LEU A 318 ? 0.2982 0.2825 0.2224 -0.0001 0.0192 0.1347 333 LEU A CG 2527 C CD1 . LEU A 318 ? 0.3618 0.2867 0.1974 -0.0440 0.0178 0.0878 333 LEU A CD1 2528 C CD2 . LEU A 318 ? 0.4467 0.3176 0.2002 -0.0430 -0.0238 0.1081 333 LEU A CD2 2529 N N . GLY A 319 ? 0.2423 0.2171 0.1064 -0.0690 0.0300 0.0175 334 GLY A N 2530 C CA . GLY A 319 ? 0.1952 0.1720 0.1411 -0.0360 -0.0041 0.0739 334 GLY A CA 2531 C C . GLY A 319 ? 0.1998 0.1626 0.1148 -0.0555 0.0114 0.0435 334 GLY A C 2532 O O . GLY A 319 ? 0.1988 0.1726 0.2141 0.0121 0.0228 0.0469 334 GLY A O 2533 N N . ASP A 320 ? 0.1611 0.1305 0.1280 -0.0317 0.0397 0.0378 335 ASP A N 2534 C CA . ASP A 320 ? 0.2105 0.1466 0.1747 -0.0372 0.0310 0.0691 335 ASP A CA 2535 C C . ASP A 320 ? 0.1501 0.2017 0.1757 -0.0015 0.0104 0.0212 335 ASP A C 2536 O O . ASP A 320 ? 0.1645 0.1522 0.1307 0.0047 0.0178 0.0268 335 ASP A O 2537 C CB . ASP A 320 ? 0.2116 0.1248 0.1744 -0.0073 -0.0101 -0.0209 335 ASP A CB 2538 C CG . ASP A 320 ? 0.2186 0.3142 0.1274 -0.0017 0.0451 -0.0484 335 ASP A CG 2539 O OD1 . ASP A 320 ? 0.2108 0.1810 0.1598 0.0008 0.0128 -0.0157 335 ASP A OD1 2540 O OD2 . ASP A 320 ? 0.1997 0.2632 0.1913 0.0326 -0.0348 -0.0167 335 ASP A OD2 2541 N N . HIS A 321 ? 0.1888 0.2652 0.1147 0.0401 0.0230 -0.0139 336 HIS A N 2542 C CA . HIS A 321 ? 0.1623 0.0930 0.0922 -0.0082 0.0337 -0.0014 336 HIS A CA 2543 C C . HIS A 321 ? 0.1434 0.0764 0.1967 -0.0124 -0.0336 -0.0196 336 HIS A C 2544 O O . HIS A 321 ? 0.2283 0.1188 0.1491 0.0216 0.0093 0.0110 336 HIS A O 2545 C CB . HIS A 321 ? 0.1485 0.1297 0.1107 0.0064 -0.0099 -0.0294 336 HIS A CB 2546 C CG . HIS A 321 ? 0.1435 0.0657 0.1201 -0.0060 0.0031 0.0308 336 HIS A CG 2547 N ND1 . HIS A 321 ? 0.1615 0.0959 0.1366 -0.0141 -0.0267 0.0216 336 HIS A ND1 2548 C CD2 . HIS A 321 ? 0.2229 0.1576 0.1294 -0.0756 0.0182 0.0262 336 HIS A CD2 2549 C CE1 . HIS A 321 ? 0.0993 0.1902 0.1728 -0.0389 0.0199 0.0437 336 HIS A CE1 2550 N NE2 . HIS A 321 ? 0.1649 0.2167 0.1119 -0.0499 0.0131 -0.0034 336 HIS A NE2 2551 N N . GLY A 322 ? 0.1493 0.1191 0.1816 -0.0406 0.0119 0.0521 337 GLY A N 2552 C CA . GLY A 322 ? 0.0783 0.1778 0.1817 -0.0334 0.0236 0.0051 337 GLY A CA 2553 C C . GLY A 322 ? 0.0993 0.2084 0.1081 -0.0036 0.0119 -0.0281 337 GLY A C 2554 O O . GLY A 322 ? 0.1654 0.1772 0.1978 -0.0168 -0.0273 0.0292 337 GLY A O 2555 N N . TYR A 323 ? 0.0934 0.1898 0.1827 0.0115 -0.0022 -0.0239 338 TYR A N 2556 C CA . TYR A 323 ? 0.1173 0.1698 0.1782 -0.0020 0.0164 0.0883 338 TYR A CA 2557 C C . TYR A 323 ? 0.0985 0.2040 0.2152 -0.0325 0.0334 0.0239 338 TYR A C 2558 O O . TYR A 323 ? 0.1244 0.2637 0.1697 -0.0203 -0.0139 0.0429 338 TYR A O 2559 C CB . TYR A 323 ? 0.1815 0.1594 0.1169 -0.0060 -0.0091 0.0448 338 TYR A CB 2560 C CG . TYR A 323 ? 0.1498 0.1394 0.0973 -0.0105 0.0113 0.0442 338 TYR A CG 2561 C CD1 . TYR A 323 ? 0.1530 0.2622 0.0914 0.0074 -0.0214 -0.0255 338 TYR A CD1 2562 C CD2 . TYR A 323 ? 0.1300 0.2669 0.1641 -0.0363 0.0340 0.0529 338 TYR A CD2 2563 C CE1 . TYR A 323 ? 0.1541 0.2666 0.1482 -0.0245 0.0377 -0.0191 338 TYR A CE1 2564 C CE2 . TYR A 323 ? 0.1520 0.2250 0.1198 0.0194 -0.0158 0.0173 338 TYR A CE2 2565 C CZ . TYR A 323 ? 0.1889 0.2290 0.0965 0.0331 -0.0333 0.0251 338 TYR A CZ 2566 O OH . TYR A 323 ? 0.2359 0.2360 0.1312 0.0217 -0.0012 0.0362 338 TYR A OH 2567 N N . ASP A 324 ? 0.1018 0.1870 0.1599 -0.0049 0.0563 0.0168 339 ASP A N 2568 C CA . ASP A 324 ? 0.1031 0.2581 0.1206 0.0036 -0.0260 -0.0367 339 ASP A CA 2569 C C . ASP A 324 ? 0.1148 0.2494 0.2007 -0.0453 -0.0327 0.0729 339 ASP A C 2570 O O . ASP A 324 ? 0.1439 0.2312 0.1542 -0.0264 0.0306 0.0084 339 ASP A O 2571 C CB . ASP A 324 ? 0.1198 0.2752 0.1405 -0.0652 -0.0258 0.0516 339 ASP A CB 2572 C CG . ASP A 324 ? 0.1451 0.2933 0.2969 -0.0621 -0.0506 0.0837 339 ASP A CG 2573 O OD1 . ASP A 324 ? 0.1611 0.2022 0.2100 -0.0063 0.0004 0.0441 339 ASP A OD1 2574 O OD2 . ASP A 324 ? 0.1780 0.4426 0.1871 -0.0293 0.0319 0.0241 339 ASP A OD2 2575 N N . ASN A 325 ? 0.1639 0.2073 0.1200 0.0149 0.0043 0.0471 340 ASN A N 2576 C CA . ASN A 325 ? 0.1926 0.2132 0.1211 0.0021 0.0574 0.0173 340 ASN A CA 2577 C C . ASN A 325 ? 0.0964 0.2270 0.0985 -0.0377 0.0026 0.0036 340 ASN A C 2578 O O . ASN A 325 ? 0.1517 0.2656 0.1360 0.0103 -0.0117 -0.0515 340 ASN A O 2579 C CB . ASN A 325 ? 0.1940 0.1787 0.1324 -0.0425 -0.0215 0.0467 340 ASN A CB 2580 C CG . ASN A 325 ? 0.1895 0.1420 0.1289 -0.0450 -0.0152 0.0573 340 ASN A CG 2581 O OD1 . ASN A 325 ? 0.1923 0.2470 0.1533 -0.0396 0.0029 0.0032 340 ASN A OD1 2582 N ND2 . ASN A 325 ? 0.1391 0.2270 0.1449 -0.0133 -0.0317 0.0437 340 ASN A ND2 2583 N N . SER A 326 ? 0.1030 0.1769 0.2312 -0.0142 0.0036 0.0868 341 SER A N 2584 C CA . SER A 326 ? 0.1114 0.2164 0.2982 -0.0234 0.0093 0.0670 341 SER A CA 2585 C C . SER A 326 ? 0.1781 0.2870 0.2393 -0.0647 0.0096 -0.0054 341 SER A C 2586 O O . SER A 326 ? 0.2423 0.2654 0.2094 -0.0090 0.0598 -0.0074 341 SER A O 2587 C CB . SER A 326 ? 0.1835 0.1553 0.2966 -0.0306 0.0786 0.0440 341 SER A CB 2588 O OG . SER A 326 ? 0.2056 0.2268 0.3861 -0.0442 0.1245 -0.0066 341 SER A OG 2589 N N . LEU A 327 ? 0.1309 0.2785 0.1954 -0.0201 -0.0195 0.0457 342 LEU A N 2590 C CA . LEU A 327 ? 0.2001 0.1276 0.1655 0.0220 0.0512 0.0069 342 LEU A CA 2591 C C . LEU A 327 ? 0.1792 0.1651 0.1354 0.0327 0.0502 -0.0427 342 LEU A C 2592 O O . LEU A 327 ? 0.1634 0.1330 0.2087 0.0359 0.0066 -0.0117 342 LEU A O 2593 C CB . LEU A 327 ? 0.1976 0.1136 0.1668 -0.0040 0.0180 0.0099 342 LEU A CB 2594 C CG . LEU A 327 ? 0.1348 0.2016 0.2170 -0.0059 0.0043 -0.0484 342 LEU A CG 2595 C CD1 . LEU A 327 ? 0.1644 0.2644 0.1472 0.0087 0.0185 0.0341 342 LEU A CD1 2596 C CD2 . LEU A 327 ? 0.1053 0.3164 0.2648 0.0403 -0.0048 0.0078 342 LEU A CD2 2597 N N . PRO A 328 ? 0.1452 0.2417 0.2324 0.0452 0.0779 -0.0056 343 PRO A N 2598 C CA . PRO A 328 ? 0.1938 0.2317 0.2869 0.0233 0.0965 -0.0557 343 PRO A CA 2599 C C . PRO A 328 ? 0.2090 0.1978 0.0985 0.0122 -0.0009 0.0308 343 PRO A C 2600 O O . PRO A 328 ? 0.1885 0.2049 0.1587 0.0089 -0.0023 -0.0275 343 PRO A O 2601 C CB . PRO A 328 ? 0.1686 0.2146 0.3436 0.0050 0.0929 -0.0690 343 PRO A CB 2602 C CG . PRO A 328 ? 0.1446 0.2594 0.4033 0.0233 0.0165 0.0590 343 PRO A CG 2603 C CD . PRO A 328 ? 0.1734 0.1944 0.3057 0.0617 0.0727 -0.0144 343 PRO A CD 2604 N N . SER A 329 ? 0.1660 0.1350 0.1450 0.0024 0.0648 0.0346 344 SER A N 2605 C CA . SER A 329 ? 0.2007 0.1680 0.1152 0.0092 0.0268 -0.0105 344 SER A CA 2606 C C . SER A 329 ? 0.2605 0.2056 0.1217 -0.0692 -0.0012 0.0412 344 SER A C 2607 O O . SER A 329 ? 0.2074 0.1554 0.1577 -0.0234 0.0009 0.0158 344 SER A O 2608 C CB . SER A 329 ? 0.2207 0.1095 0.2567 0.0383 0.0123 -0.0412 344 SER A CB 2609 O OG . SER A 329 ? 0.1949 0.1871 0.1806 0.0471 0.0263 0.0042 344 SER A OG 2610 N N . MET A 330 ? 0.1460 0.1552 0.1716 0.0338 0.0020 0.0129 345 MET A N 2611 C CA . MET A 330 ? 0.1914 0.1478 0.1154 0.0116 0.0143 -0.0625 345 MET A CA 2612 C C . MET A 330 ? 0.1523 0.1677 0.0910 -0.0165 0.0145 -0.0159 345 MET A C 2613 O O . MET A 330 ? 0.1288 0.1976 0.1763 -0.0034 0.0126 0.0076 345 MET A O 2614 C CB . MET A 330 ? 0.2059 0.1272 0.0918 0.0237 0.0259 0.0084 345 MET A CB 2615 C CG . MET A 330 ? 0.1335 0.1414 0.1873 -0.0018 0.0442 0.0238 345 MET A CG 2616 S SD . MET A 330 ? 0.1520 0.1519 0.1448 0.0020 0.0179 0.0198 345 MET A SD 2617 C CE . MET A 330 ? 0.1582 0.1750 0.1819 -0.0191 0.0220 -0.0235 345 MET A CE 2618 N N . HIS A 331 ? 0.1808 0.2036 0.1120 -0.0608 0.0493 -0.0426 346 HIS A N 2619 C CA . HIS A 331 ? 0.1623 0.1642 0.1907 -0.0493 0.0678 -0.0143 346 HIS A CA 2620 C C . HIS A 331 ? 0.1489 0.2510 0.1238 -0.0516 0.0340 0.0089 346 HIS A C 2621 O O . HIS A 331 ? 0.1950 0.2147 0.1622 -0.0479 0.0264 -0.0082 346 HIS A O 2622 C CB . HIS A 331 ? 0.1562 0.2120 0.2074 -0.0226 0.0836 -0.0236 346 HIS A CB 2623 C CG . HIS A 331 ? 0.1264 0.1663 0.1962 -0.0380 0.0422 0.0466 346 HIS A CG 2624 N ND1 . HIS A 331 ? 0.2000 0.3107 0.2610 -0.0202 0.0754 -0.0763 346 HIS A ND1 2625 C CD2 . HIS A 331 ? 0.1185 0.1509 0.2032 -0.0554 -0.0124 0.0339 346 HIS A CD2 2626 C CE1 . HIS A 331 ? 0.3270 0.1345 0.2400 -0.0282 -0.0021 -0.0626 346 HIS A CE1 2627 N NE2 . HIS A 331 ? 0.1379 0.3151 0.2100 -0.0406 0.0159 0.0695 346 HIS A NE2 2628 N N . PRO A 332 ? 0.1982 0.1317 0.1011 -0.0501 0.0083 0.0157 347 PRO A N 2629 C CA . PRO A 332 ? 0.2090 0.1175 0.1393 0.0054 0.0002 -0.0594 347 PRO A CA 2630 C C . PRO A 332 ? 0.1950 0.1260 0.2417 0.0304 0.0214 -0.0638 347 PRO A C 2631 O O . PRO A 332 ? 0.1910 0.2876 0.1617 -0.0447 0.0026 -0.0103 347 PRO A O 2632 C CB . PRO A 332 ? 0.2243 0.2073 0.1992 0.0244 0.0235 0.0692 347 PRO A CB 2633 C CG . PRO A 332 ? 0.1759 0.1186 0.1636 -0.0216 0.0004 -0.0277 347 PRO A CG 2634 C CD . PRO A 332 ? 0.1213 0.1987 0.1431 -0.0243 -0.0266 0.0334 347 PRO A CD 2635 N N . PHE A 333 ? 0.2349 0.2331 0.1715 -0.0723 0.0447 -0.0529 348 PHE A N 2636 C CA . PHE A 333 ? 0.2024 0.1349 0.2344 -0.0301 -0.0115 -0.0770 348 PHE A CA 2637 C C . PHE A 333 ? 0.2368 0.2666 0.1891 0.0281 0.0642 -0.0886 348 PHE A C 2638 O O . PHE A 333 ? 0.2078 0.2239 0.1781 -0.0452 0.0400 -0.0652 348 PHE A O 2639 C CB . PHE A 333 ? 0.2062 0.1924 0.1961 -0.0503 0.0153 -0.0480 348 PHE A CB 2640 C CG . PHE A 333 ? 0.2276 0.2227 0.1761 -0.0547 0.0108 -0.0216 348 PHE A CG 2641 C CD1 . PHE A 333 ? 0.3157 0.2179 0.2467 -0.0509 0.0991 -0.0817 348 PHE A CD1 2642 C CD2 . PHE A 333 ? 0.2851 0.2865 0.1484 -0.1497 -0.0352 0.0149 348 PHE A CD2 2643 C CE1 . PHE A 333 ? 0.2976 0.3851 0.1771 -0.1212 0.0085 -0.0847 348 PHE A CE1 2644 C CE2 . PHE A 333 ? 0.3305 0.2360 0.1720 -0.1131 -0.0138 -0.0225 348 PHE A CE2 2645 C CZ . PHE A 333 ? 0.3069 0.3888 0.1930 -0.1233 0.0406 -0.1071 348 PHE A CZ 2646 N N . LEU A 334 ? 0.1637 0.3305 0.1507 -0.0722 -0.0058 -0.0316 349 LEU A N 2647 C CA . LEU A 334 ? 0.1760 0.1903 0.1885 -0.0698 -0.0240 -0.0561 349 LEU A CA 2648 C C . LEU A 334 ? 0.2348 0.2258 0.1896 -0.1140 0.0332 -0.0636 349 LEU A C 2649 O O . LEU A 334 ? 0.2509 0.3278 0.2090 -0.0819 0.0548 -0.1010 349 LEU A O 2650 C CB . LEU A 334 ? 0.1760 0.1758 0.2602 -0.0501 0.0193 -0.0001 349 LEU A CB 2651 C CG . LEU A 334 ? 0.1697 0.2794 0.2297 -0.0048 -0.0064 -0.0677 349 LEU A CG 2652 C CD1 . LEU A 334 ? 0.1784 0.2421 0.2304 -0.0300 0.0032 0.0641 349 LEU A CD1 2653 C CD2 . LEU A 334 ? 0.1973 0.2052 0.2066 -0.0355 0.0206 -0.1052 349 LEU A CD2 2654 N N . ALA A 335 ? 0.2520 0.2026 0.1545 -0.0955 0.0458 -0.0660 350 ALA A N 2655 C CA . ALA A 335 ? 0.2629 0.2046 0.1286 -0.0243 0.0232 -0.0037 350 ALA A CA 2656 C C . ALA A 335 ? 0.2352 0.3053 0.1539 -0.0389 0.0656 -0.0712 350 ALA A C 2657 O O . ALA A 335 ? 0.2172 0.4084 0.1632 -0.1131 0.0343 -0.0845 350 ALA A O 2658 C CB . ALA A 335 ? 0.3851 0.1292 0.2179 -0.0475 0.0621 -0.0172 350 ALA A CB 2659 N N . ALA A 336 ? 0.2031 0.2705 0.1730 -0.0577 0.0182 -0.0397 351 ALA A N 2660 C CA . ALA A 336 ? 0.2349 0.1743 0.2039 -0.0342 0.0095 -0.0951 351 ALA A CA 2661 C C . ALA A 336 ? 0.2240 0.2202 0.1940 -0.0463 0.0365 -0.0533 351 ALA A C 2662 O O . ALA A 336 ? 0.3048 0.2912 0.1858 -0.0738 0.0251 -0.0818 351 ALA A O 2663 C CB . ALA A 336 ? 0.2657 0.1845 0.2652 -0.1132 0.0179 0.0053 351 ALA A CB 2664 N N . HIS A 337 ? 0.2209 0.3116 0.1934 -0.1248 0.0015 -0.0586 352 HIS A N 2665 C CA . HIS A 337 ? 0.2722 0.3533 0.2081 -0.1460 0.0213 -0.0856 352 HIS A CA 2666 C C . HIS A 337 ? 0.3184 0.3613 0.1797 -0.1510 0.0759 -0.0534 352 HIS A C 2667 O O . HIS A 337 ? 0.2441 0.4445 0.1831 -0.1094 0.0035 -0.0884 352 HIS A O 2668 C CB . HIS A 337 ? 0.3219 0.3166 0.2593 -0.1519 0.0139 -0.0900 352 HIS A CB 2669 C CG . HIS A 337 ? 0.3200 0.3351 0.2223 -0.1714 -0.0241 -0.0233 352 HIS A CG 2670 N ND1 . HIS A 337 ? 0.3147 0.4220 0.2576 -0.1864 0.0040 -0.0687 352 HIS A ND1 2671 C CD2 . HIS A 337 ? 0.3505 0.4432 0.3628 -0.1735 0.0069 -0.1444 352 HIS A CD2 2672 C CE1 . HIS A 337 ? 0.3313 0.1597 0.3241 -0.0306 -0.0109 -0.0789 352 HIS A CE1 2673 N NE2 . HIS A 337 ? 0.3383 0.4596 0.3225 -0.1529 0.0131 -0.1280 352 HIS A NE2 2674 N N . GLY A 338 ? 0.3236 0.4806 0.1764 -0.2110 0.0069 -0.0125 353 GLY A N 2675 C CA . GLY A 338 ? 0.3391 0.4146 0.1364 -0.0744 -0.0242 -0.0205 353 GLY A CA 2676 C C . GLY A 338 ? 0.2351 0.2359 0.1473 -0.0278 -0.0323 -0.0817 353 GLY A C 2677 O O . GLY A 338 ? 0.2221 0.3732 0.2274 -0.0926 0.0015 -0.0704 353 GLY A O 2678 N N . PRO A 339 ? 0.3169 0.3736 0.2008 -0.1541 -0.0507 -0.0198 354 PRO A N 2679 C CA . PRO A 339 ? 0.3846 0.3926 0.1711 -0.1611 0.0518 -0.0557 354 PRO A CA 2680 C C . PRO A 339 ? 0.3313 0.4948 0.2438 -0.1562 0.0597 -0.1429 354 PRO A C 2681 O O . PRO A 339 ? 0.3319 0.5119 0.2260 -0.1244 0.0350 -0.1349 354 PRO A O 2682 C CB . PRO A 339 ? 0.3572 0.4460 0.2548 -0.0689 -0.0328 -0.0562 354 PRO A CB 2683 C CG . PRO A 339 ? 0.4358 0.5106 0.3419 -0.1440 0.0173 0.0397 354 PRO A CG 2684 C CD . PRO A 339 ? 0.3441 0.3233 0.2898 -0.1352 -0.0765 0.0260 354 PRO A CD 2685 N N . ALA A 340 ? 0.2956 0.4394 0.2406 -0.1821 0.0039 -0.0623 355 ALA A N 2686 C CA . ALA A 340 ? 0.3407 0.3135 0.1940 -0.1216 -0.0370 -0.0326 355 ALA A CA 2687 C C . ALA A 340 ? 0.3406 0.4923 0.2221 -0.1551 -0.0087 -0.0942 355 ALA A C 2688 O O . ALA A 340 ? 0.2920 0.4388 0.1944 -0.1237 -0.0079 -0.0599 355 ALA A O 2689 C CB . ALA A 340 ? 0.3518 0.3084 0.2401 -0.1366 -0.0090 -0.0269 355 ALA A CB 2690 N N . PHE A 341 ? 0.3294 0.3944 0.2021 -0.1337 0.0553 -0.1071 356 PHE A N 2691 C CA . PHE A 341 ? 0.2883 0.3964 0.2268 -0.1288 0.0505 0.0140 356 PHE A CA 2692 C C . PHE A 341 ? 0.3463 0.4972 0.2895 -0.0855 0.0260 0.0308 356 PHE A C 2693 O O . PHE A 341 ? 0.2977 0.5728 0.2549 -0.1938 0.0670 -0.1150 356 PHE A O 2694 C CB . PHE A 341 ? 0.2519 0.3898 0.1577 -0.0524 0.0655 -0.0442 356 PHE A CB 2695 C CG . PHE A 341 ? 0.2532 0.2803 0.1612 -0.0446 0.0644 -0.0837 356 PHE A CG 2696 C CD1 . PHE A 341 ? 0.2388 0.2881 0.2055 -0.0143 0.0840 -0.0465 356 PHE A CD1 2697 C CD2 . PHE A 341 ? 0.3074 0.2717 0.1637 -0.1326 0.0116 -0.0484 356 PHE A CD2 2698 C CE1 . PHE A 341 ? 0.2894 0.4037 0.1895 -0.0354 0.0849 0.0099 356 PHE A CE1 2699 C CE2 . PHE A 341 ? 0.3109 0.2826 0.1521 -0.0511 0.0205 -0.0867 356 PHE A CE2 2700 C CZ . PHE A 341 ? 0.3292 0.3734 0.2302 -0.1082 0.0709 0.0718 356 PHE A CZ 2701 N N . HIS A 342 ? 0.3366 0.4074 0.2031 -0.0980 0.1021 -0.0653 357 HIS A N 2702 C CA . HIS A 342 ? 0.3530 0.3765 0.2571 -0.0173 -0.0004 -0.0594 357 HIS A CA 2703 C C . HIS A 342 ? 0.4074 0.2988 0.2957 -0.1045 0.0870 -0.0294 357 HIS A C 2704 O O . HIS A 342 ? 0.4276 0.4183 0.2678 -0.1168 0.1165 -0.1349 357 HIS A O 2705 C CB . HIS A 342 ? 0.4002 0.3516 0.1675 -0.0992 0.0555 0.0360 357 HIS A CB 2706 C CG . HIS A 342 ? 0.3858 0.3583 0.1777 -0.0706 0.0980 -0.0529 357 HIS A CG 2707 N ND1 . HIS A 342 ? 0.5214 0.2584 0.2190 -0.1486 0.1244 -0.0472 357 HIS A ND1 2708 C CD2 . HIS A 342 ? 0.3637 0.3257 0.2361 -0.1127 0.0435 0.0015 357 HIS A CD2 2709 C CE1 . HIS A 342 ? 0.4323 0.4082 0.3121 -0.1516 0.0700 0.0056 357 HIS A CE1 2710 N NE2 . HIS A 342 ? 0.3008 0.4699 0.3428 -0.1090 0.0999 -0.0359 357 HIS A NE2 2711 N N . LYS A 343 ? 0.4201 0.3048 0.3876 -0.1607 0.1013 -0.1320 358 LYS A N 2712 C CA . LYS A 343 ? 0.4448 0.2657 0.3818 -0.1681 0.0057 -0.0375 358 LYS A CA 2713 C C . LYS A 343 ? 0.4382 0.3527 0.4393 -0.1296 0.1850 -0.0375 358 LYS A C 2714 O O . LYS A 343 ? 0.4674 0.4879 0.4678 -0.0011 0.2081 -0.0917 358 LYS A O 2715 C CB . LYS A 343 ? 0.5336 0.3915 0.4647 -0.1631 0.1495 -0.0545 358 LYS A CB 2716 C CG . LYS A 343 ? 0.5885 0.6644 0.7317 -0.0741 0.0326 -0.0639 358 LYS A CG 2717 C CD . LYS A 343 ? 0.6228 0.7859 0.8315 -0.0760 0.0434 -0.0021 358 LYS A CD 2718 C CE . LYS A 343 ? 0.6222 0.7489 0.7363 -0.0932 0.1688 0.0176 358 LYS A CE 2719 N NZ . LYS A 343 ? 0.5627 0.5372 0.4558 -0.1549 0.2049 -0.1895 358 LYS A NZ 2720 N N . GLY A 344 ? 0.4572 0.2785 0.2620 -0.1030 0.0815 -0.0888 359 GLY A N 2721 C CA . GLY A 344 ? 0.4523 0.3899 0.3440 -0.0259 0.1487 -0.0698 359 GLY A CA 2722 C C . GLY A 344 ? 0.4304 0.3038 0.3607 0.0229 0.1708 0.0709 359 GLY A C 2723 O O . GLY A 344 ? 0.5439 0.3740 0.5702 0.0052 0.0724 -0.0717 359 GLY A O 2724 N N . TYR A 345 ? 0.4047 0.4154 0.2982 -0.0993 0.0987 -0.1038 360 TYR A N 2725 C CA . TYR A 345 ? 0.4180 0.3469 0.1917 -0.0800 0.0651 -0.0976 360 TYR A CA 2726 C C . TYR A 345 ? 0.4118 0.3008 0.2717 -0.1018 -0.0695 -0.0861 360 TYR A C 2727 O O . TYR A 345 ? 0.3908 0.3672 0.3392 -0.0591 0.0852 -0.0916 360 TYR A O 2728 C CB . TYR A 345 ? 0.4626 0.3615 0.1908 -0.0323 0.1194 -0.0103 360 TYR A CB 2729 C CG . TYR A 345 ? 0.3874 0.3818 0.2371 -0.0822 0.0784 -0.1372 360 TYR A CG 2730 C CD1 . TYR A 345 ? 0.4093 0.4814 0.3518 -0.0794 0.1481 -0.0111 360 TYR A CD1 2731 C CD2 . TYR A 345 ? 0.3916 0.3114 0.2241 -0.0410 0.0717 -0.1220 360 TYR A CD2 2732 C CE1 . TYR A 345 ? 0.4334 0.5409 0.3814 -0.0760 0.0980 -0.0742 360 TYR A CE1 2733 C CE2 . TYR A 345 ? 0.3668 0.4212 0.2867 -0.0317 0.1129 -0.0815 360 TYR A CE2 2734 C CZ . TYR A 345 ? 0.3957 0.3747 0.3207 -0.0392 0.1787 0.0158 360 TYR A CZ 2735 O OH . TYR A 345 ? 0.3531 0.4243 0.4468 -0.0555 0.1130 0.0127 360 TYR A OH 2736 N N . LYS A 346 ? 0.3753 0.3148 0.2464 -0.1355 0.0173 -0.1076 361 LYS A N 2737 C CA . LYS A 346 ? 0.3657 0.4144 0.2248 -0.1320 0.0075 -0.1145 361 LYS A CA 2738 C C . LYS A 346 ? 0.3345 0.3412 0.2535 0.0174 0.0056 -0.1592 361 LYS A C 2739 O O . LYS A 346 ? 0.3402 0.4489 0.3587 -0.0103 0.0930 -0.1997 361 LYS A O 2740 C CB . LYS A 346 ? 0.4570 0.4955 0.3053 0.0337 0.0428 -0.1114 361 LYS A CB 2741 C CG . LYS A 346 ? 0.5981 0.6774 0.5727 -0.0190 -0.0471 -0.0568 361 LYS A CG 2742 C CD . LYS A 346 ? 0.6212 0.7823 0.8158 0.0462 -0.0258 -0.0396 361 LYS A CD 2743 C CE . LYS A 346 ? 0.6100 0.8160 0.8860 0.0823 -0.0424 0.0618 361 LYS A CE 2744 N NZ . LYS A 346 ? 0.6228 0.8177 0.9124 0.0345 -0.0027 0.0568 361 LYS A NZ 2745 N N . HIS A 347 ? 0.3140 0.3025 0.2836 -0.0616 0.0763 -0.0585 362 HIS A N 2746 C CA . HIS A 347 ? 0.3725 0.3584 0.3421 0.0095 0.1285 -0.0946 362 HIS A CA 2747 C C . HIS A 347 ? 0.2892 0.3003 0.2754 -0.0590 0.1225 -0.0761 362 HIS A C 2748 O O . HIS A 347 ? 0.2531 0.3492 0.2319 0.0056 0.0796 -0.0080 362 HIS A O 2749 C CB . HIS A 347 ? 0.3181 0.5215 0.2132 0.0309 0.0311 -0.0672 362 HIS A CB 2750 C CG . HIS A 347 ? 0.4446 0.4592 0.3506 -0.0231 0.1637 -0.0677 362 HIS A CG 2751 N ND1 . HIS A 347 ? 0.3925 0.6259 0.3331 -0.0181 0.0138 -0.0435 362 HIS A ND1 2752 C CD2 . HIS A 347 ? 0.4370 0.2600 0.3683 -0.1372 0.0179 -0.1011 362 HIS A CD2 2753 C CE1 . HIS A 347 ? 0.4668 0.3288 0.3883 0.0299 0.0227 -0.0315 362 HIS A CE1 2754 N NE2 . HIS A 347 ? 0.4450 0.2970 0.4479 -0.0990 -0.0008 -0.0366 362 HIS A NE2 2755 N N . SER A 348 ? 0.3014 0.3102 0.3027 -0.0591 0.0675 -0.0869 363 SER A N 2756 C CA . SER A 348 ? 0.2243 0.3175 0.2430 -0.0124 0.0144 -0.0737 363 SER A CA 2757 C C . SER A 348 ? 0.2509 0.2526 0.2541 -0.0653 0.1297 -0.0577 363 SER A C 2758 O O . SER A 348 ? 0.2068 0.2781 0.2447 -0.0168 0.0696 -0.0268 363 SER A O 2759 C CB . SER A 348 ? 0.2620 0.4814 0.4256 -0.0226 -0.0632 -0.1148 363 SER A CB 2760 O OG . SER A 348 ? 0.3672 0.6074 0.6069 0.0108 -0.0619 0.0079 363 SER A OG 2761 N N . THR A 349 ? 0.2100 0.2782 0.2935 -0.0637 0.0583 -0.1099 364 THR A N 2762 C CA . THR A 349 ? 0.2871 0.1498 0.1929 -0.0289 0.0068 -0.0072 364 THR A CA 2763 C C . THR A 349 ? 0.1842 0.2526 0.3221 -0.0083 0.0809 0.0924 364 THR A C 2764 O O . THR A 349 ? 0.2061 0.3876 0.2305 -0.0669 0.0864 -0.0221 364 THR A O 2765 C CB . THR A 349 ? 0.2575 0.3364 0.1911 -0.0304 0.0495 -0.0893 364 THR A CB 2766 O OG1 . THR A 349 ? 0.2461 0.3881 0.2065 -0.0252 0.0220 0.0039 364 THR A OG1 2767 C CG2 . THR A 349 ? 0.2404 0.3690 0.3282 -0.0069 0.0451 0.0410 364 THR A CG2 2768 N N . ILE A 350 ? 0.1670 0.3014 0.1717 -0.0200 0.0042 0.0323 365 ILE A N 2769 C CA . ILE A 350 ? 0.1734 0.2469 0.1618 -0.0508 0.0040 0.0146 365 ILE A CA 2770 C C . ILE A 350 ? 0.1945 0.1326 0.1666 -0.0328 0.0253 0.0075 365 ILE A C 2771 O O . ILE A 350 ? 0.2015 0.1802 0.1677 -0.0579 0.0409 0.0130 365 ILE A O 2772 C CB . ILE A 350 ? 0.1912 0.3156 0.1294 -0.0254 0.0414 -0.0159 365 ILE A CB 2773 C CG1 . ILE A 350 ? 0.2077 0.2593 0.1847 -0.0095 -0.0030 0.0302 365 ILE A CG1 2774 C CG2 . ILE A 350 ? 0.2242 0.3266 0.1578 -0.0427 0.0079 0.0008 365 ILE A CG2 2775 C CD1 . ILE A 350 ? 0.2313 0.2318 0.2003 -0.0252 -0.0322 0.0250 365 ILE A CD1 2776 N N . ASN A 351 ? 0.1647 0.2089 0.2118 -0.0035 0.0108 -0.1048 366 ASN A N 2777 C CA . ASN A 351 ? 0.1476 0.1180 0.2125 -0.0618 0.0013 0.0011 366 ASN A CA 2778 C C . ASN A 351 ? 0.1171 0.2377 0.1157 -0.0503 0.0148 0.0259 366 ASN A C 2779 O O . ASN A 351 ? 0.1837 0.2929 0.1050 -0.0532 -0.0054 -0.0100 366 ASN A O 2780 C CB . ASN A 351 ? 0.1492 0.2997 0.1855 -0.0906 -0.0300 0.0226 366 ASN A CB 2781 C CG . ASN A 351 ? 0.2044 0.4577 0.2551 -0.0733 -0.0197 -0.1052 366 ASN A CG 2782 O OD1 . ASN A 351 ? 0.2825 0.5471 0.3035 -0.0502 0.0175 0.0910 366 ASN A OD1 2783 N ND2 . ASN A 351 ? 0.3485 0.3514 0.3213 -0.0795 0.0854 0.0156 366 ASN A ND2 2784 N N . ILE A 352 ? 0.1351 0.1961 0.1683 -0.0292 0.0548 0.0457 367 ILE A N 2785 C CA . ILE A 352 ? 0.1714 0.1900 0.1188 -0.0163 0.0624 0.0253 367 ILE A CA 2786 C C . ILE A 352 ? 0.1610 0.2349 0.0956 -0.0601 0.0100 0.0271 367 ILE A C 2787 O O . ILE A 352 ? 0.1437 0.2006 0.1641 -0.0375 -0.0085 0.0162 367 ILE A O 2788 C CB . ILE A 352 ? 0.1204 0.1695 0.1507 -0.0601 -0.0290 0.0199 367 ILE A CB 2789 C CG1 . ILE A 352 ? 0.1304 0.3026 0.1160 -0.0717 -0.0064 0.0393 367 ILE A CG1 2790 C CG2 . ILE A 352 ? 0.1791 0.1457 0.1034 -0.0813 0.0008 0.0105 367 ILE A CG2 2791 C CD1 . ILE A 352 ? 0.1512 0.3582 0.1361 -0.0360 0.0307 0.0188 367 ILE A CD1 2792 N N . VAL A 353 ? 0.1909 0.1761 0.1566 -0.0045 0.0319 0.0267 368 VAL A N 2793 C CA . VAL A 353 ? 0.1769 0.2356 0.1931 -0.0773 0.0428 0.0451 368 VAL A CA 2794 C C . VAL A 353 ? 0.1705 0.2396 0.1259 -0.0290 0.0596 -0.0070 368 VAL A C 2795 O O . VAL A 353 ? 0.2646 0.2278 0.1520 -0.0471 -0.0080 0.0404 368 VAL A O 2796 C CB . VAL A 353 ? 0.1324 0.2534 0.1896 -0.0297 0.0469 0.0389 368 VAL A CB 2797 C CG1 . VAL A 353 ? 0.1670 0.2352 0.1430 -0.0035 0.0323 0.0321 368 VAL A CG1 2798 C CG2 . VAL A 353 ? 0.1891 0.1796 0.2184 -0.0086 0.0212 0.0308 368 VAL A CG2 2799 N N . ASP A 354 ? 0.1886 0.2795 0.1042 -0.0538 0.0074 -0.0361 369 ASP A N 2800 C CA . ASP A 354 ? 0.1518 0.3073 0.1303 -0.0490 0.0238 -0.0509 369 ASP A CA 2801 C C . ASP A 354 ? 0.1650 0.3190 0.1485 -0.0476 0.0386 0.0013 369 ASP A C 2802 O O . ASP A 354 ? 0.2096 0.3323 0.1449 -0.0721 0.0100 0.0050 369 ASP A O 2803 C CB . ASP A 354 ? 0.1529 0.3081 0.1512 -0.0269 0.0266 -0.0453 369 ASP A CB 2804 C CG . ASP A 354 ? 0.1923 0.2792 0.1868 -0.0867 0.0358 -0.0690 369 ASP A CG 2805 O OD1 . ASP A 354 ? 0.2147 0.2684 0.1858 -0.0833 0.0044 -0.0048 369 ASP A OD1 2806 O OD2 . ASP A 354 ? 0.1875 0.3351 0.1647 -0.0614 0.0225 -0.0253 369 ASP A OD2 2807 N N . ILE A 355 ? 0.1383 0.2827 0.1833 -0.0685 0.0432 -0.0015 370 ILE A N 2808 C CA . ILE A 355 ? 0.1800 0.3130 0.1658 -0.0953 0.0117 0.0511 370 ILE A CA 2809 C C . ILE A 355 ? 0.2017 0.2728 0.2560 -0.1021 0.0557 0.0342 370 ILE A C 2810 O O . ILE A 355 ? 0.2226 0.2394 0.1866 -0.0613 0.0121 0.0064 370 ILE A O 2811 C CB . ILE A 355 ? 0.1637 0.1501 0.2072 -0.0477 0.0208 0.0111 370 ILE A CB 2812 C CG1 . ILE A 355 ? 0.2101 0.2417 0.1632 -0.0494 0.0645 0.0533 370 ILE A CG1 2813 C CG2 . ILE A 355 ? 0.1728 0.2877 0.1914 -0.0808 0.0164 0.0508 370 ILE A CG2 2814 C CD1 . ILE A 355 ? 0.1803 0.1889 0.2165 -0.0468 0.0461 0.0391 370 ILE A CD1 2815 N N . TYR A 356 ? 0.1889 0.3453 0.1555 -0.0914 -0.0368 0.0883 371 TYR A N 2816 C CA . TYR A 356 ? 0.2328 0.3332 0.1545 -0.0869 -0.0300 0.0418 371 TYR A CA 2817 C C . TYR A 356 ? 0.1925 0.3727 0.2044 -0.0548 -0.0175 0.0138 371 TYR A C 2818 O O . TYR A 356 ? 0.1939 0.4143 0.1831 -0.0718 0.0221 0.0634 371 TYR A O 2819 C CB . TYR A 356 ? 0.1653 0.2470 0.2380 -0.0501 -0.0243 0.0016 371 TYR A CB 2820 C CG . TYR A 356 ? 0.1765 0.2445 0.1856 -0.0126 -0.0022 -0.0031 371 TYR A CG 2821 C CD1 . TYR A 356 ? 0.2098 0.2403 0.1308 -0.0200 0.0343 0.0001 371 TYR A CD1 2822 C CD2 . TYR A 356 ? 0.2112 0.3613 0.1299 -0.0748 -0.0165 0.0470 371 TYR A CD2 2823 C CE1 . TYR A 356 ? 0.2369 0.3082 0.1806 -0.0510 0.0342 0.0168 371 TYR A CE1 2824 C CE2 . TYR A 356 ? 0.2343 0.3022 0.1828 0.0042 -0.0126 0.0425 371 TYR A CE2 2825 C CZ . TYR A 356 ? 0.2089 0.2425 0.1594 -0.0160 -0.0399 0.0923 371 TYR A CZ 2826 O OH . TYR A 356 ? 0.2374 0.3030 0.1935 -0.0584 -0.0243 0.1192 371 TYR A OH 2827 N N . PRO A 357 ? 0.1956 0.2745 0.0984 -0.0421 -0.0314 0.0125 372 PRO A N 2828 C CA . PRO A 357 ? 0.1755 0.3158 0.1948 -0.0380 0.0148 0.0005 372 PRO A CA 2829 C C . PRO A 357 ? 0.1965 0.2414 0.1582 -0.0340 0.0155 0.0901 372 PRO A C 2830 O O . PRO A 357 ? 0.2258 0.3526 0.1532 -0.0520 -0.0058 0.0913 372 PRO A O 2831 C CB . PRO A 357 ? 0.1944 0.3982 0.1701 -0.1003 0.0002 0.0128 372 PRO A CB 2832 C CG . PRO A 357 ? 0.2352 0.4662 0.1356 -0.0008 0.0054 0.0307 372 PRO A CG 2833 C CD . PRO A 357 ? 0.1534 0.3452 0.1126 -0.0159 -0.0074 -0.0301 372 PRO A CD 2834 N N . MET A 358 ? 0.2223 0.1914 0.1838 -0.0478 0.0181 0.0278 373 MET A N 2835 C CA . MET A 358 ? 0.1693 0.2524 0.2881 -0.0224 0.0118 -0.0487 373 MET A CA 2836 C C . MET A 358 ? 0.1738 0.2492 0.1422 -0.0582 0.0337 -0.0165 373 MET A C 2837 O O . MET A 358 ? 0.2308 0.3479 0.1574 -0.0363 0.0028 -0.0478 373 MET A O 2838 C CB . MET A 358 ? 0.2121 0.4525 0.2476 -0.0463 0.0456 -0.1222 373 MET A CB 2839 C CG . MET A 358 ? 0.2955 0.3020 0.1710 -0.0604 0.0123 0.0341 373 MET A CG 2840 S SD . MET A 358 ? 0.2536 0.3471 0.2094 -0.0943 0.0268 0.0105 373 MET A SD 2841 C CE . MET A 358 ? 0.3478 0.3466 0.2947 -0.0290 0.1464 0.0250 373 MET A CE 2842 N N . MET A 359 ? 0.1519 0.3585 0.1688 -0.0610 0.0441 -0.0211 374 MET A N 2843 C CA . MET A 359 ? 0.1599 0.2697 0.1406 -0.0069 0.0539 0.0228 374 MET A CA 2844 C C . MET A 359 ? 0.2298 0.3758 0.1441 -0.1172 0.0088 -0.0512 374 MET A C 2845 O O . MET A 359 ? 0.2546 0.4178 0.1570 -0.1196 -0.0237 -0.0280 374 MET A O 2846 C CB . MET A 359 ? 0.1695 0.3178 0.1959 -0.0791 0.0083 -0.0092 374 MET A CB 2847 C CG . MET A 359 ? 0.1931 0.3666 0.1207 -0.0736 -0.0222 0.0224 374 MET A CG 2848 S SD . MET A 359 ? 0.2137 0.3803 0.1599 -0.1005 0.0062 -0.0191 374 MET A SD 2849 C CE . MET A 359 ? 0.2440 0.2699 0.1384 -0.0367 0.0041 0.0309 374 MET A CE 2850 N N . CYS A 360 ? 0.1811 0.3629 0.2116 -0.0964 -0.0081 0.0033 375 CYS A N 2851 C CA . CYS A 360 ? 0.2679 0.4505 0.1617 -0.0480 -0.0318 0.0429 375 CYS A CA 2852 C C . CYS A 360 ? 0.2282 0.3161 0.1397 -0.0829 -0.0527 0.0126 375 CYS A C 2853 O O . CYS A 360 ? 0.2197 0.4532 0.1655 -0.1127 -0.0407 0.0411 375 CYS A O 2854 C CB . CYS A 360 ? 0.3073 0.2854 0.1525 -0.0837 -0.0003 0.0632 375 CYS A CB 2855 S SG . CYS A 360 ? 0.2313 0.3777 0.1660 -0.0664 -0.0244 0.0343 375 CYS A SG 2856 N N . HIS A 361 ? 0.2295 0.3949 0.1643 -0.0499 -0.0176 0.0121 376 HIS A N 2857 C CA . HIS A 361 ? 0.2224 0.4741 0.1501 -0.0987 0.0070 -0.0359 376 HIS A CA 2858 C C . HIS A 361 ? 0.3026 0.4297 0.1686 0.0332 -0.0283 0.0927 376 HIS A C 2859 O O . HIS A 361 ? 0.2861 0.4983 0.1767 -0.1318 -0.0307 0.0748 376 HIS A O 2860 C CB . HIS A 361 ? 0.2281 0.4583 0.1766 -0.0427 0.0625 -0.0185 376 HIS A CB 2861 C CG . HIS A 361 ? 0.2852 0.3777 0.1277 -0.0510 0.0021 -0.0289 376 HIS A CG 2862 N ND1 . HIS A 361 ? 0.3255 0.4803 0.2018 -0.0524 0.0256 0.0263 376 HIS A ND1 2863 C CD2 . HIS A 361 ? 0.2791 0.3152 0.2837 -0.0372 0.0236 -0.1065 376 HIS A CD2 2864 C CE1 . HIS A 361 ? 0.3525 0.5538 0.3734 -0.0551 -0.0528 -0.0484 376 HIS A CE1 2865 N NE2 . HIS A 361 ? 0.2910 0.4934 0.2366 0.0258 0.0000 -0.0637 376 HIS A NE2 2866 N N . ILE A 362 ? 0.3323 0.3529 0.1749 -0.0770 -0.0255 0.0232 377 ILE A N 2867 C CA . ILE A 362 ? 0.3115 0.2831 0.2241 -0.1230 0.0189 0.0505 377 ILE A CA 2868 C C . ILE A 362 ? 0.2769 0.3842 0.2445 -0.0395 -0.0251 0.0435 377 ILE A C 2869 O O . ILE A 362 ? 0.3109 0.5627 0.2097 -0.1230 -0.0571 -0.0236 377 ILE A O 2870 C CB . ILE A 362 ? 0.2736 0.2744 0.2881 -0.1272 -0.0535 0.0426 377 ILE A CB 2871 C CG1 . ILE A 362 ? 0.3154 0.3926 0.1999 -0.0173 0.0050 0.0034 377 ILE A CG1 2872 C CG2 . ILE A 362 ? 0.2459 0.4656 0.2638 -0.1417 0.0017 0.0313 377 ILE A CG2 2873 C CD1 . ILE A 362 ? 0.3383 0.2811 0.2587 -0.0819 0.0336 0.0131 377 ILE A CD1 2874 N N . LEU A 363 ? 0.2865 0.3335 0.2030 -0.0158 0.0293 -0.0077 378 LEU A N 2875 C CA . LEU A 363 ? 0.2472 0.4806 0.2061 -0.0124 -0.0335 0.0854 378 LEU A CA 2876 C C . LEU A 363 ? 0.2577 0.4269 0.1972 -0.1008 -0.0736 0.0956 378 LEU A C 2877 O O . LEU A 363 ? 0.2314 0.6302 0.2919 -0.0709 -0.0584 0.1480 378 LEU A O 2878 C CB . LEU A 363 ? 0.2711 0.5330 0.2110 -0.1799 0.0147 0.0062 378 LEU A CB 2879 C CG . LEU A 363 ? 0.2580 0.4126 0.2123 -0.1600 0.0148 -0.0138 378 LEU A CG 2880 C CD1 . LEU A 363 ? 0.2715 0.4470 0.1644 -0.0003 0.0410 -0.0206 378 LEU A CD1 2881 C CD2 . LEU A 363 ? 0.3115 0.4513 0.4031 -0.1690 -0.0119 0.1412 378 LEU A CD2 2882 N N . GLY A 364 ? 0.2973 0.4563 0.1931 -0.1386 -0.0708 0.0710 379 GLY A N 2883 C CA . GLY A 364 ? 0.2676 0.4892 0.2413 -0.1417 -0.0855 0.1008 379 GLY A CA 2884 C C . GLY A 364 ? 0.2935 0.4324 0.2841 -0.1431 -0.1046 0.0963 379 GLY A C 2885 O O . GLY A 364 ? 0.4021 0.5286 0.1955 0.0023 -0.0960 0.0569 379 GLY A O 2886 N N . LEU A 365 ? 0.2832 0.4704 0.2055 -0.1055 -0.0852 0.0465 380 LEU A N 2887 C CA . LEU A 365 ? 0.3219 0.3229 0.2195 -0.0244 -0.0389 0.0575 380 LEU A CA 2888 C C . LEU A 365 ? 0.4342 0.3866 0.3009 -0.0170 -0.0568 0.1282 380 LEU A C 2889 O O . LEU A 365 ? 0.3812 0.3715 0.2345 -0.1249 -0.0413 0.0943 380 LEU A O 2890 C CB . LEU A 365 ? 0.3742 0.3844 0.1867 -0.1192 0.0499 0.0548 380 LEU A CB 2891 C CG . LEU A 365 ? 0.3451 0.3997 0.2166 -0.0726 -0.0106 0.1361 380 LEU A CG 2892 C CD1 . LEU A 365 ? 0.3351 0.5285 0.2377 0.0043 0.0239 0.1593 380 LEU A CD1 2893 C CD2 . LEU A 365 ? 0.3501 0.5042 0.2731 -0.0297 -0.1067 0.0379 380 LEU A CD2 2894 N N . LYS A 366 ? 0.4809 0.4747 0.2280 -0.0646 -0.1366 0.0626 381 LYS A N 2895 C CA . LYS A 366 ? 0.4332 0.4094 0.2889 -0.1461 -0.1610 0.0639 381 LYS A CA 2896 C C . LYS A 366 ? 0.3820 0.3791 0.1581 -0.0933 -0.0708 0.0288 381 LYS A C 2897 O O . LYS A 366 ? 0.3923 0.5733 0.2305 -0.1079 -0.0688 0.1269 381 LYS A O 2898 C CB . LYS A 366 ? 0.5708 0.5336 0.2705 -0.0181 -0.0517 0.1158 381 LYS A CB 2899 C CG . LYS A 366 ? 0.6439 0.6644 0.7474 -0.0033 0.0031 0.0922 381 LYS A CG 2900 C CD . LYS A 366 ? 0.6349 0.7418 0.7643 -0.0404 -0.0021 0.0332 381 LYS A CD 2901 C CE . LYS A 366 ? 0.6616 0.7959 0.7384 -0.0115 0.0367 -0.0628 381 LYS A CE 2902 N NZ . LYS A 366 ? 0.6560 0.7518 0.7717 -0.0222 0.0329 0.0859 381 LYS A NZ 2903 N N . PRO A 367 ? 0.3189 0.4102 0.2019 -0.0791 -0.0959 0.0796 382 PRO A N 2904 C CA . PRO A 367 ? 0.2858 0.4381 0.2394 -0.0922 -0.0804 0.1414 382 PRO A CA 2905 C C . PRO A 367 ? 0.3360 0.2645 0.2169 -0.0584 0.0098 0.1161 382 PRO A C 2906 O O . PRO A 367 ? 0.4250 0.2326 0.2207 -0.1188 -0.0316 0.0647 382 PRO A O 2907 C CB . PRO A 367 ? 0.3412 0.3869 0.2161 -0.0657 -0.0281 0.1376 382 PRO A CB 2908 C CG . PRO A 367 ? 0.3801 0.5378 0.3050 -0.0912 0.0500 0.0374 382 PRO A CG 2909 C CD . PRO A 367 ? 0.3581 0.3917 0.2638 -0.0404 -0.0231 0.0019 382 PRO A CD 2910 N N . HIS A 368 ? 0.3014 0.3274 0.2025 -0.0606 -0.0121 0.0772 383 HIS A N 2911 C CA . HIS A 368 ? 0.2606 0.3035 0.2421 0.0008 0.0148 0.0841 383 HIS A CA 2912 C C . HIS A 368 ? 0.3011 0.3311 0.2375 -0.0899 -0.0119 0.1203 383 HIS A C 2913 O O . HIS A 368 ? 0.2558 0.4036 0.2681 -0.0995 -0.0469 0.0994 383 HIS A O 2914 C CB . HIS A 368 ? 0.2992 0.4117 0.3013 -0.0979 0.0197 0.1429 383 HIS A CB 2915 C CG . HIS A 368 ? 0.3341 0.4695 0.4233 -0.0404 0.0003 0.1371 383 HIS A CG 2916 N ND1 . HIS A 368 ? 0.3305 0.4975 0.4364 0.0355 -0.0442 0.1562 383 HIS A ND1 2917 C CD2 . HIS A 368 ? 0.3994 0.5157 0.4608 -0.0809 -0.0220 0.0123 383 HIS A CD2 2918 C CE1 . HIS A 368 ? 0.4344 0.3999 0.4843 0.0785 0.0045 0.0178 383 HIS A CE1 2919 N NE2 . HIS A 368 ? 0.4141 0.4467 0.4913 -0.0218 0.0033 0.1667 383 HIS A NE2 2920 N N . PRO A 369 ? 0.3454 0.3054 0.2334 -0.1548 -0.0976 0.1085 384 PRO A N 2921 C CA . PRO A 369 ? 0.2982 0.2598 0.2785 -0.0816 -0.1136 0.1263 384 PRO A CA 2922 C C . PRO A 369 ? 0.3312 0.3028 0.2150 -0.0728 -0.0916 0.0897 384 PRO A C 2923 O O . PRO A 369 ? 0.3122 0.2891 0.2137 -0.0175 -0.0603 0.0678 384 PRO A O 2924 C CB . PRO A 369 ? 0.3333 0.3807 0.2654 -0.0990 -0.0613 0.1589 384 PRO A CB 2925 C CG . PRO A 369 ? 0.3710 0.4067 0.2830 -0.0955 -0.1309 0.1403 384 PRO A CG 2926 C CD . PRO A 369 ? 0.3710 0.4633 0.3267 -0.0953 -0.0179 0.0984 384 PRO A CD 2927 N N . ASN A 370 ? 0.3064 0.2980 0.1873 -0.0569 -0.0330 0.1121 385 ASN A N 2928 C CA . ASN A 370 ? 0.2346 0.2438 0.1873 -0.0301 -0.0588 0.0570 385 ASN A CA 2929 C C . ASN A 370 ? 0.1962 0.1771 0.1774 -0.0592 0.0186 0.0687 385 ASN A C 2930 O O . ASN A 370 ? 0.2583 0.3253 0.2096 -0.1167 -0.0082 0.0966 385 ASN A O 2931 C CB . ASN A 370 ? 0.3234 0.3399 0.1190 -0.0531 -0.0144 -0.0304 385 ASN A CB 2932 C CG . ASN A 370 ? 0.2380 0.2188 0.1680 -0.0845 -0.0834 0.0719 385 ASN A CG 2933 O OD1 . ASN A 370 ? 0.3420 0.2812 0.2173 -0.0080 -0.0728 0.0789 385 ASN A OD1 2934 N ND2 . ASN A 370 ? 0.2436 0.3268 0.1404 -0.1078 -0.0505 0.0481 385 ASN A ND2 2935 N N . ASN A 371 ? 0.2452 0.1796 0.2068 -0.0411 0.0210 0.0907 386 ASN A N 2936 C CA . ASN A 371 ? 0.2379 0.2222 0.1843 0.0226 -0.0368 0.0215 386 ASN A CA 2937 C C . ASN A 371 ? 0.2273 0.1317 0.2158 -0.0626 0.0285 0.0449 386 ASN A C 2938 O O . ASN A 371 ? 0.2327 0.3030 0.2391 -0.0436 -0.0005 0.0096 386 ASN A O 2939 C CB . ASN A 371 ? 0.2366 0.2713 0.1524 -0.1145 0.0056 0.0169 386 ASN A CB 2940 C CG . ASN A 371 ? 0.2290 0.3088 0.1005 -0.0116 0.0129 0.0033 386 ASN A CG 2941 O OD1 . ASN A 371 ? 0.2066 0.2420 0.1453 -0.0469 0.0102 0.0519 386 ASN A OD1 2942 N ND2 . ASN A 371 ? 0.2571 0.3729 0.1908 -0.0743 -0.0194 0.0910 386 ASN A ND2 2943 N N . GLY A 372 ? 0.2933 0.1757 0.1998 -0.0928 0.0209 0.0128 387 GLY A N 2944 C CA . GLY A 372 ? 0.2765 0.3063 0.1740 -0.0459 0.0230 0.1017 387 GLY A CA 2945 C C . GLY A 372 ? 0.2652 0.3208 0.1435 -0.0250 -0.0401 0.0778 387 GLY A C 2946 O O . GLY A 372 ? 0.3402 0.2786 0.1705 -0.0846 0.0550 0.0283 387 GLY A O 2947 N N . THR A 373 ? 0.2856 0.2837 0.2119 -0.0553 0.0965 0.0246 388 THR A N 2948 C CA . THR A 373 ? 0.2597 0.2648 0.2226 -0.0437 0.0481 -0.0834 388 THR A CA 2949 C C . THR A 373 ? 0.2983 0.2115 0.1287 -0.0367 0.0473 0.0347 388 THR A C 2950 O O . THR A 373 ? 0.3256 0.3139 0.1459 -0.0742 0.0269 0.0531 388 THR A O 2951 C CB . THR A 373 ? 0.2428 0.4088 0.1948 -0.0908 0.0339 -0.0264 388 THR A CB 2952 O OG1 . THR A 373 ? 0.3321 0.4488 0.2935 -0.0994 0.0030 -0.1199 388 THR A OG1 2953 C CG2 . THR A 373 ? 0.2303 0.4018 0.2893 -0.1058 0.0795 -0.0462 388 THR A CG2 2954 N N . PHE A 374 ? 0.2545 0.4544 0.1683 -0.0724 0.0555 0.0131 389 PHE A N 2955 C CA . PHE A 374 ? 0.2947 0.3414 0.1699 -0.0297 -0.0144 0.0603 389 PHE A CA 2956 C C . PHE A 374 ? 0.2992 0.2404 0.1895 -0.1443 0.0252 -0.0282 389 PHE A C 2957 O O . PHE A 374 ? 0.2953 0.3580 0.1896 -0.1214 0.0241 0.0062 389 PHE A O 2958 C CB . PHE A 374 ? 0.2484 0.3520 0.1817 -0.0449 0.0110 -0.0121 389 PHE A CB 2959 C CG . PHE A 374 ? 0.2393 0.2984 0.1932 -0.0882 0.0205 -0.0643 389 PHE A CG 2960 C CD1 . PHE A 374 ? 0.2478 0.4572 0.1969 -0.0604 0.0784 -0.0281 389 PHE A CD1 2961 C CD2 . PHE A 374 ? 0.2327 0.3964 0.2800 -0.1235 -0.0033 -0.0484 389 PHE A CD2 2962 C CE1 . PHE A 374 ? 0.2948 0.4443 0.2145 -0.1154 0.0017 -0.0489 389 PHE A CE1 2963 C CE2 . PHE A 374 ? 0.2157 0.4564 0.2453 -0.1162 0.0416 0.0000 389 PHE A CE2 2964 C CZ . PHE A 374 ? 0.1744 0.4427 0.2477 -0.0721 0.0122 -0.0265 389 PHE A CZ 2965 N N . GLY A 375 ? 0.2401 0.3737 0.2424 -0.1399 0.0218 0.0459 390 GLY A N 2966 C CA . GLY A 375 ? 0.3016 0.4289 0.1836 -0.1449 0.0548 -0.0007 390 GLY A CA 2967 C C . GLY A 375 ? 0.2605 0.4025 0.2472 -0.0987 0.0788 0.0102 390 GLY A C 2968 O O . GLY A 375 ? 0.2964 0.3819 0.1752 -0.1176 0.0240 0.0185 390 GLY A O 2969 N N . HIS A 376 ? 0.2314 0.3029 0.1980 -0.0901 0.0676 0.0365 391 HIS A N 2970 C CA . HIS A 376 ? 0.2604 0.2606 0.1921 -0.0972 0.0515 -0.0132 391 HIS A CA 2971 C C . HIS A 376 ? 0.2401 0.3060 0.1455 0.0168 0.0074 -0.0106 391 HIS A C 2972 O O . HIS A 376 ? 0.2355 0.3863 0.1896 -0.0829 0.0106 0.0215 391 HIS A O 2973 C CB . HIS A 376 ? 0.2754 0.4439 0.1726 -0.0787 0.0598 -0.0737 391 HIS A CB 2974 C CG . HIS A 376 ? 0.2360 0.3516 0.2268 -0.1275 -0.0284 0.0069 391 HIS A CG 2975 N ND1 . HIS A 376 ? 0.2626 0.3383 0.1389 -0.0905 0.0208 -0.0217 391 HIS A ND1 2976 C CD2 . HIS A 376 ? 0.2860 0.4474 0.2164 -0.1769 0.0493 -0.0609 391 HIS A CD2 2977 C CE1 . HIS A 376 ? 0.2034 0.3556 0.2534 -0.0178 0.0221 -0.0930 391 HIS A CE1 2978 N NE2 . HIS A 376 ? 0.2514 0.4406 0.2634 -0.1068 0.0615 -0.1679 391 HIS A NE2 2979 N N . THR A 377 ? 0.2208 0.3008 0.1368 -0.1006 0.0519 -0.0464 392 THR A N 2980 C CA . THR A 377 ? 0.2058 0.3377 0.2284 -0.0443 0.0971 -0.0299 392 THR A CA 2981 C C . THR A 377 ? 0.2121 0.3688 0.1671 -0.0289 0.0590 -0.0714 392 THR A C 2982 O O . THR A 377 ? 0.2613 0.4387 0.1660 -0.1128 0.0518 -0.0200 392 THR A O 2983 C CB . THR A 377 ? 0.2957 0.2806 0.1219 -0.0612 0.0376 0.0313 392 THR A CB 2984 O OG1 . THR A 377 ? 0.2287 0.3383 0.1906 -0.0725 -0.0100 0.0076 392 THR A OG1 2985 C CG2 . THR A 377 ? 0.2087 0.4626 0.1888 -0.1013 0.0322 -0.1106 392 THR A CG2 2986 N N . LYS A 378 ? 0.2330 0.3775 0.1259 -0.0203 0.0432 -0.0110 393 LYS A N 2987 C CA . LYS A 378 ? 0.2566 0.3662 0.1493 -0.1126 0.0343 0.0191 393 LYS A CA 2988 C C . LYS A 378 ? 0.2592 0.3555 0.1404 -0.0868 0.0354 -0.0237 393 LYS A C 2989 O O . LYS A 378 ? 0.2899 0.3868 0.1414 -0.1267 0.0210 -0.0395 393 LYS A O 2990 C CB . LYS A 378 ? 0.3012 0.3911 0.2113 -0.1288 0.0608 0.0433 393 LYS A CB 2991 C CG . LYS A 378 ? 0.3591 0.4529 0.2572 -0.0974 0.1318 -0.0637 393 LYS A CG 2992 C CD . LYS A 378 ? 0.3202 0.4769 0.2682 -0.1017 0.1171 0.0005 393 LYS A CD 2993 C CE . LYS A 378 ? 0.3328 0.4514 0.5012 -0.0114 0.1799 -0.0058 393 LYS A CE 2994 N NZ . LYS A 378 ? 0.4017 0.5632 0.3486 -0.0424 0.1812 0.0952 393 LYS A NZ 2995 N N . CYS A 379 ? 0.2602 0.2670 0.1862 -0.0887 0.0933 -0.0422 394 CYS A N 2996 C CA . CYS A 379 ? 0.2963 0.2337 0.1983 -0.1136 0.0406 -0.0618 394 CYS A CA 2997 C C . CYS A 379 ? 0.2742 0.3849 0.1937 -0.0629 0.0000 -0.0338 394 CYS A C 2998 O O . CYS A 379 ? 0.3010 0.3669 0.2174 -0.0846 0.0492 0.0040 394 CYS A O 2999 C CB . CYS A 379 ? 0.2252 0.4059 0.2134 -0.0380 -0.0108 0.0052 394 CYS A CB 3000 S SG . CYS A 379 ? 0.2780 0.5783 0.2415 -0.0653 0.0189 0.0246 394 CYS A SG 3001 N N . LEU A 380 ? 0.2300 0.4140 0.1642 -0.0858 0.0335 -0.0721 395 LEU A N 3002 C CA . LEU A 380 ? 0.2492 0.4482 0.1724 -0.0791 0.0105 -0.0950 395 LEU A CA 3003 C C . LEU A 380 ? 0.2417 0.2854 0.1779 -0.1338 0.0070 0.0228 395 LEU A C 3004 O O . LEU A 380 ? 0.2827 0.3075 0.1977 -0.1578 0.0672 -0.0699 395 LEU A O 3005 C CB . LEU A 380 ? 0.2915 0.3434 0.1169 -0.0487 0.0283 -0.0308 395 LEU A CB 3006 C CG . LEU A 380 ? 0.2810 0.3139 0.1112 -0.0678 -0.0225 0.0007 395 LEU A CG 3007 C CD1 . LEU A 380 ? 0.2947 0.4307 0.1455 -0.0726 0.0353 -0.0495 395 LEU A CD1 3008 C CD2 . LEU A 380 ? 0.2939 0.4661 0.2003 -0.0342 0.0538 0.0175 395 LEU A CD2 3009 N N . LEU A 381 ? 0.3198 0.3124 0.1433 -0.0595 0.0588 0.0402 396 LEU A N 3010 C CA . LEU A 381 ? 0.3076 0.3865 0.1244 -0.0710 0.0110 -0.0195 396 LEU A CA 3011 C C . LEU A 381 ? 0.3375 0.3275 0.1926 -0.0830 -0.0112 -0.1035 396 LEU A C 3012 O O . LEU A 381 ? 0.3164 0.3514 0.2023 -0.0644 0.0345 -0.0347 396 LEU A O 3013 C CB . LEU A 381 ? 0.2755 0.2443 0.1989 -0.0140 0.0545 -0.0613 396 LEU A CB 3014 C CG . LEU A 381 ? 0.2132 0.3138 0.1714 -0.0957 0.0583 -0.0319 396 LEU A CG 3015 C CD1 . LEU A 381 ? 0.2783 0.3705 0.2611 -0.1039 0.0006 -0.0138 396 LEU A CD1 3016 C CD2 . LEU A 381 ? 0.2309 0.3993 0.2248 -0.1207 0.0609 0.0090 396 LEU A CD2 3017 N N . VAL A 382 ? 0.3180 0.4356 0.1617 -0.1619 0.0121 -0.0416 397 VAL A N 3018 C CA . VAL A 382 ? 0.3587 0.4262 0.1805 -0.2035 0.0425 -0.0561 397 VAL A CA 3019 C C . VAL A 382 ? 0.3984 0.3948 0.2631 -0.1901 -0.0445 0.0378 397 VAL A C 3020 O O . VAL A 382 ? 0.4094 0.6448 0.3256 -0.1385 0.0373 -0.1341 397 VAL A O 3021 C CB . VAL A 382 ? 0.4212 0.4298 0.3523 -0.1013 0.1219 -0.0221 397 VAL A CB 3022 C CG1 . VAL A 382 ? 0.4550 0.4658 0.2809 -0.1404 0.0729 -0.1045 397 VAL A CG1 3023 C CG2 . VAL A 382 ? 0.4272 0.4075 0.4170 -0.1349 0.0613 -0.1676 397 VAL A CG2 3024 N N . ASP A 383 ? 0.3935 0.3711 0.2552 -0.2021 -0.1193 0.1047 398 ASP A N 3025 C CA . ASP A 383 ? 0.3685 0.5085 0.4312 -0.1311 0.0833 0.1671 398 ASP A CA 3026 C C . ASP A 383 ? 0.2412 0.4571 0.1839 -0.0687 0.0127 0.0968 398 ASP A C 3027 O O . ASP A 383 ? 0.2160 0.3507 0.2755 -0.0421 0.0570 0.0278 398 ASP A O 3028 C CB . ASP A 383 ? 0.3600 0.4344 0.4146 0.0936 0.1045 -0.0179 398 ASP A CB 3029 C CG . ASP A 383 ? 0.4195 0.4902 0.3279 0.0080 0.1082 0.0250 398 ASP A CG 3030 O OD1 . ASP A 383 ? 0.4919 0.7095 0.4992 0.0749 0.0679 0.0401 398 ASP A OD1 3031 O OD2 . ASP A 383 ? 0.5011 0.5970 0.3833 0.0116 0.0021 -0.0554 398 ASP A OD2 3032 N N . GLN A 384 ? 0.2113 0.3968 0.2095 -0.0987 -0.0046 -0.0103 399 GLN A N 3033 C CA . GLN A 384 ? 0.2986 0.2999 0.1223 -0.0377 0.0529 -0.0376 399 GLN A CA 3034 C C . GLN A 384 ? 0.2925 0.3561 0.1548 -0.0359 0.0630 -0.0325 399 GLN A C 3035 O O . GLN A 384 ? 0.2219 0.4381 0.1930 -0.0431 0.0531 -0.0532 399 GLN A O 3036 C CB . GLN A 384 ? 0.3200 0.2966 0.2292 -0.0602 0.1077 -0.0848 399 GLN A CB 3037 C CG . GLN A 384 ? 0.3252 0.2929 0.3195 -0.0752 0.1646 -0.1042 399 GLN A CG 3038 C CD . GLN A 384 ? 0.2973 0.3139 0.3050 0.0601 0.1336 -0.0229 399 GLN A CD 3039 O OE1 . GLN A 384 ? 0.4335 0.4078 0.1752 -0.0674 0.0953 -0.0266 399 GLN A OE1 3040 N NE2 . GLN A 384 ? 0.3705 0.2967 0.2911 0.0138 0.1019 0.0123 399 GLN A NE2 3041 N N . TRP A 385 ? 0.2453 0.4162 0.1260 -0.0593 0.0140 0.0046 400 TRP A N 3042 C CA . TRP A 385 ? 0.2525 0.4165 0.1265 -0.0487 0.0076 0.0150 400 TRP A CA 3043 C C . TRP A 385 ? 0.3182 0.2685 0.2874 -0.0692 0.0744 0.0545 400 TRP A C 3044 O O . TRP A 385 ? 0.3262 0.3202 0.2178 -0.0315 -0.0082 -0.0118 400 TRP A O 3045 C CB . TRP A 385 ? 0.2315 0.3587 0.1744 -0.0749 0.0423 -0.0621 400 TRP A CB 3046 C CG . TRP A 385 ? 0.2177 0.3234 0.1098 -0.0461 -0.0055 0.0270 400 TRP A CG 3047 C CD1 . TRP A 385 ? 0.2882 0.3516 0.1852 -0.0549 -0.0150 0.1173 400 TRP A CD1 3048 C CD2 . TRP A 385 ? 0.1863 0.3527 0.1970 -0.0379 0.0365 -0.0378 400 TRP A CD2 3049 N NE1 . TRP A 385 ? 0.2289 0.3525 0.1766 -0.0654 0.0127 0.0531 400 TRP A NE1 3050 C CE2 . TRP A 385 ? 0.1737 0.3382 0.1957 0.0175 0.0344 0.0041 400 TRP A CE2 3051 C CE3 . TRP A 385 ? 0.1728 0.2958 0.2440 0.0036 -0.0343 -0.0152 400 TRP A CE3 3052 C CZ2 . TRP A 385 ? 0.2080 0.4774 0.2751 -0.0509 0.0810 -0.0421 400 TRP A CZ2 3053 C CZ3 . TRP A 385 ? 0.2184 0.3976 0.1883 -0.0478 -0.0165 0.1084 400 TRP A CZ3 3054 C CH2 . TRP A 385 ? 0.1902 0.3958 0.1850 -0.0332 -0.0221 -0.0097 400 TRP A CH2 3055 N N . CYS A 386 ? 0.3041 0.3706 0.1592 -0.1076 0.0259 0.0531 401 CYS A N 3056 C CA . CYS A 386 ? 0.2493 0.3911 0.2659 -0.0612 0.0269 0.1292 401 CYS A CA 3057 C C . CYS A 386 ? 0.3181 0.4504 0.1788 -0.0569 0.0017 0.0051 401 CYS A C 3058 O O . CYS A 386 ? 0.3477 0.4695 0.2661 -0.0683 0.0864 0.0102 401 CYS A O 3059 C CB . CYS A 386 ? 0.3676 0.3630 0.1284 0.0170 0.0350 0.0021 401 CYS A CB 3060 S SG . CYS A 386 ? 0.3652 0.4127 0.2325 -0.0185 0.0682 0.0304 401 CYS A SG 3061 N N . ILE A 387 ? 0.3431 0.2902 0.3451 -0.0668 -0.0353 -0.0010 402 ILE A N 3062 C CA . ILE A 387 ? 0.4131 0.4558 0.4509 -0.1031 -0.0290 -0.1590 402 ILE A CA 3063 C C . ILE A 387 ? 0.4798 0.5445 0.6181 -0.0332 -0.1741 -0.0866 402 ILE A C 3064 O O . ILE A 387 ? 0.5385 0.6878 0.7421 -0.0095 -0.0758 -0.0339 402 ILE A O 3065 C CB . ILE A 387 ? 0.3870 0.5350 0.5596 -0.0390 -0.0075 0.0411 402 ILE A CB 3066 C CG1 . ILE A 387 ? 0.5065 0.5083 0.4831 -0.0710 0.0560 -0.0435 402 ILE A CG1 3067 C CG2 . ILE A 387 ? 0.4909 0.6046 0.7695 -0.0341 0.0286 -0.0275 402 ILE A CG2 3068 C CD1 . ILE A 387 ? 0.5149 0.5218 0.5122 -0.0636 0.0315 -0.1109 402 ILE A CD1 3069 C C1 . NAG B . ? 0.1833 0.3756 0.2351 -0.0208 -0.0043 0.0981 501 NAG A C1 3070 C C2 . NAG B . ? 0.2587 0.3335 0.2115 -0.1161 0.0465 0.0139 501 NAG A C2 3071 C C3 . NAG B . ? 0.3252 0.2968 0.2574 -0.1611 -0.0674 0.0659 501 NAG A C3 3072 C C4 . NAG B . ? 0.3509 0.3390 0.2525 0.0558 -0.1060 0.1036 501 NAG A C4 3073 C C5 . NAG B . ? 0.2950 0.3344 0.3050 -0.0564 0.0036 0.1151 501 NAG A C5 3074 C C6 . NAG B . ? 0.3374 0.4459 0.2412 -0.0895 -0.0071 0.1122 501 NAG A C6 3075 C C7 . NAG B . ? 0.2442 0.2568 0.2330 -0.0260 -0.0065 0.0747 501 NAG A C7 3076 C C8 . NAG B . ? 0.1809 0.3985 0.2799 0.0021 -0.0506 -0.0004 501 NAG A C8 3077 N N2 . NAG B . ? 0.2345 0.2688 0.2198 -0.0241 -0.0352 0.0758 501 NAG A N2 3078 O O3 . NAG B . ? 0.3549 0.2297 0.2943 -0.1248 -0.0388 0.0455 501 NAG A O3 3079 O O4 . NAG B . ? 0.4521 0.3367 0.3862 -0.0571 -0.0964 0.0509 501 NAG A O4 3080 O O5 . NAG B . ? 0.2743 0.3001 0.2206 -0.0568 -0.0445 0.0626 501 NAG A O5 3081 O O6 . NAG B . ? 0.3516 0.3039 0.3202 -0.1159 -0.1160 0.1512 501 NAG A O6 3082 O O7 . NAG B . ? 0.2586 0.4880 0.2488 -0.0446 0.0178 0.0694 501 NAG A O7 3083 C C1 . NAG C . ? 0.5322 0.5404 0.5693 0.0043 -0.1291 0.1056 502 NAG A C1 3084 C C2 . NAG C . ? 0.5974 0.6192 0.6810 -0.0492 -0.0997 -0.0237 502 NAG A C2 3085 C C3 . NAG C . ? 0.6436 0.7643 0.7759 0.0146 -0.0654 0.0607 502 NAG A C3 3086 C C4 . NAG C . ? 0.6845 0.8566 0.9525 0.0069 0.0244 0.1229 502 NAG A C4 3087 C C5 . NAG C . ? 0.6844 0.7861 0.9260 0.0093 0.0058 0.1053 502 NAG A C5 3088 C C6 . NAG C . ? 0.6707 0.7524 0.8315 -0.0747 -0.0441 -0.0534 502 NAG A C6 3089 C C7 . NAG C . ? 0.6254 0.6741 0.7330 0.0254 -0.0159 0.0120 502 NAG A C7 3090 C C8 . NAG C . ? 0.6279 0.6498 0.7755 0.0225 -0.0111 0.1080 502 NAG A C8 3091 N N2 . NAG C . ? 0.6215 0.7024 0.7481 0.0015 -0.0697 -0.0027 502 NAG A N2 3092 O O3 . NAG C . ? 0.6494 0.7699 0.7713 0.1239 -0.0257 0.0441 502 NAG A O3 3093 O O4 . NAG C . ? 0.7314 1.0491 1.0923 -0.0414 -0.0054 0.0615 502 NAG A O4 3094 O O5 . NAG C . ? 0.6517 0.5893 0.7632 -0.0907 0.0780 0.2049 502 NAG A O5 3095 O O6 . NAG C . ? 0.7185 0.7619 0.9109 0.0069 -0.0355 -0.0499 502 NAG A O6 3096 O O7 . NAG C . ? 0.5486 0.6351 0.7829 0.1129 -0.1343 -0.1985 502 NAG A O7 3097 C C1 . NAG D . ? 0.4540 0.4787 0.4941 -0.1027 0.1143 0.0320 503 NAG A C1 3098 C C2 . NAG D . ? 0.5095 0.4509 0.5994 -0.0530 0.0811 0.0536 503 NAG A C2 3099 C C3 . NAG D . ? 0.5448 0.6538 0.7361 0.0102 0.0676 0.0188 503 NAG A C3 3100 C C4 . NAG D . ? 0.5687 0.7348 0.7574 -0.0013 0.0773 0.0408 503 NAG A C4 3101 C C5 . NAG D . ? 0.6027 0.7133 0.6748 -0.0720 0.1292 -0.0014 503 NAG A C5 3102 C C6 . NAG D . ? 0.6454 0.7210 0.7335 -0.0667 0.0261 0.0111 503 NAG A C6 3103 C C7 . NAG D . ? 0.5970 0.7195 0.6395 0.0288 0.1172 0.0260 503 NAG A C7 3104 C C8 . NAG D . ? 0.6042 0.5365 0.5977 -0.0507 0.1249 -0.1264 503 NAG A C8 3105 N N2 . NAG D . ? 0.5373 0.6197 0.6010 0.1028 0.2267 0.1094 503 NAG A N2 3106 O O3 . NAG D . ? 0.6141 0.6300 0.8233 0.0195 0.0052 0.0424 503 NAG A O3 3107 O O4 . NAG D . ? 0.6520 0.8470 0.9057 -0.0161 -0.0282 0.0570 503 NAG A O4 3108 O O5 . NAG D . ? 0.4710 0.6085 0.6409 -0.1387 0.2399 0.0878 503 NAG A O5 3109 O O6 . NAG D . ? 0.6086 0.8284 0.8421 -0.1348 -0.0740 -0.0202 503 NAG A O6 3110 O O7 . NAG D . ? 0.6219 0.8395 0.7872 -0.0474 0.0784 0.0674 503 NAG A O7 3111 C C1 . NAG E . ? 0.4232 0.6787 0.5967 0.0955 -0.0344 -0.0632 504 NAG A C1 3112 C C2 . NAG E . ? 0.4282 0.6189 0.5626 -0.0178 0.0304 -0.1701 504 NAG A C2 3113 C C3 . NAG E . ? 0.5003 0.6850 0.7546 0.0125 0.0108 -0.0920 504 NAG A C3 3114 C C4 . NAG E . ? 0.5242 0.7134 0.7193 0.0401 0.0144 -0.0943 504 NAG A C4 3115 C C5 . NAG E . ? 0.5412 0.7644 0.6941 -0.0445 0.0719 -0.0725 504 NAG A C5 3116 C C6 . NAG E . ? 0.5679 0.7396 0.7280 -0.0370 0.0095 -0.1077 504 NAG A C6 3117 C C7 . NAG E . ? 0.4490 0.7078 0.6125 -0.0002 -0.0699 0.0602 504 NAG A C7 3118 C C8 . NAG E . ? 0.3500 0.5444 0.6220 0.0039 -0.0740 0.0628 504 NAG A C8 3119 N N2 . NAG E . ? 0.3901 0.7179 0.4863 -0.0754 -0.1867 -0.0164 504 NAG A N2 3120 O O3 . NAG E . ? 0.4177 0.7232 0.6850 -0.0756 0.0005 -0.1823 504 NAG A O3 3121 O O4 . NAG E . ? 0.5815 0.8239 0.6906 0.0213 -0.1633 -0.0451 504 NAG A O4 3122 O O5 . NAG E . ? 0.4147 0.8405 0.7591 0.1006 0.0829 -0.0510 504 NAG A O5 3123 O O6 . NAG E . ? 0.7146 0.7079 0.7256 -0.1194 0.0117 -0.2553 504 NAG A O6 3124 O O7 . NAG E . ? 0.5182 0.7432 0.5698 -0.0442 0.0313 -0.0567 504 NAG A O7 3125 P P . AMP F . ? 0.2360 0.4297 0.1781 -0.0204 0.0216 -0.0028 505 AMP A P 3126 O O1P . AMP F . ? 0.4001 0.6040 0.2092 -0.0660 -0.0202 -0.0907 505 AMP A O1P 3127 O O2P . AMP F . ? 0.2684 0.4865 0.2876 -0.0062 -0.0028 -0.1441 505 AMP A O2P 3128 O O3P . AMP F . ? 0.2275 0.3327 0.1204 0.0733 0.0367 0.0200 505 AMP A O3P 3129 O "O5'" . AMP F . ? 0.2978 0.3231 0.5051 0.0452 0.1863 0.1271 505 AMP A "O5'" 3130 C "C5'" . AMP F . ? 0.3304 0.5750 0.5159 -0.0364 -0.0119 0.2592 505 AMP A "C5'" 3131 C "C4'" . AMP F . ? 0.4586 0.6761 0.6758 -0.0171 -0.0405 -0.1119 505 AMP A "C4'" 3132 O "O4'" . AMP F . ? 0.3418 0.5184 0.5355 -0.0244 0.1424 0.0848 505 AMP A "O4'" 3133 C "C3'" . AMP F . ? 0.5322 0.5902 0.7087 0.0775 -0.0490 -0.0434 505 AMP A "C3'" 3134 O "O3'" . AMP F . ? 0.4737 0.4634 0.5129 0.1610 0.0348 0.0160 505 AMP A "O3'" 3135 C "C2'" . AMP F . ? 0.4362 0.5139 0.5648 0.1195 0.0592 -0.1186 505 AMP A "C2'" 3136 O "O2'" . AMP F . ? 0.3214 0.4892 0.6580 0.0681 0.0198 0.0770 505 AMP A "O2'" 3137 C "C1'" . AMP F . ? 0.3372 0.4915 0.2856 -0.1843 0.0541 -0.0948 505 AMP A "C1'" 3138 N N9 . AMP F . ? 0.2468 0.4640 0.3884 0.0413 0.1065 0.1179 505 AMP A N9 3139 C C8 . AMP F . ? 0.2984 0.4527 0.2120 -0.0289 0.0547 0.1082 505 AMP A C8 3140 N N7 . AMP F . ? 0.4182 0.5155 0.3142 -0.0848 0.0974 -0.0267 505 AMP A N7 3141 C C5 . AMP F . ? 0.3630 0.3540 0.5247 -0.0704 0.1012 0.0414 505 AMP A C5 3142 C C6 . AMP F . ? 0.3676 0.5225 0.5830 -0.0109 -0.0049 -0.0867 505 AMP A C6 3143 N N6 . AMP F . ? 0.2734 0.3636 0.5679 -0.0478 -0.0954 0.2012 505 AMP A N6 3144 N N1 . AMP F . ? 0.4348 0.4424 0.6110 0.0255 -0.0003 -0.1656 505 AMP A N1 3145 C C2 . AMP F . ? 0.3649 0.3883 0.6869 0.1646 -0.0421 0.0615 505 AMP A C2 3146 N N3 . AMP F . ? 0.2335 0.5139 0.6154 0.0229 -0.0296 -0.0048 505 AMP A N3 3147 C C4 . AMP F . ? 0.3320 0.4650 0.4774 -0.0961 0.1479 -0.0666 505 AMP A C4 3148 ZN ZN . ZN G . ? 0.2011 0.2318 0.1906 -0.0320 -0.0021 0.0224 506 ZN A ZN 3149 ZN ZN . ZN H . ? 0.1813 0.2218 0.1818 -0.0545 -0.0084 0.0504 507 ZN A ZN # 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 PHE 1 16 ? ? ? A . n A 1 2 ARG 2 17 ? ? ? A . n A 1 3 SER 3 18 ? ? ? A . n A 1 4 ASP 4 19 ? ? ? A . n A 1 5 SER 5 20 ? ? ? A . n A 1 6 SER 6 21 ? ? ? A . n A 1 7 SER 7 22 ? ? ? A . n A 1 8 SER 8 23 ? ? ? A . n A 1 9 LEU 9 24 24 LEU ALA A . n A 1 10 PRO 10 25 25 PRO PRO A . n A 1 11 PRO 11 26 26 PRO PRO A . n A 1 12 LYS 12 27 27 LYS LYS A . n A 1 13 LEU 13 28 28 LEU LEU A . n A 1 14 LEU 14 29 29 LEU LEU A . n A 1 15 LEU 15 30 30 LEU LEU A . n A 1 16 VAL 16 31 31 VAL VAL A . n A 1 17 SER 17 32 32 SER SER A . n A 1 18 PHE 18 33 33 PHE PHE A . n A 1 19 ASP 19 34 34 ASP ASP A . n A 1 20 GLY 20 35 35 GLY GLY A . n A 1 21 PHE 21 36 36 PHE PHE A . n A 1 22 ARG 22 37 37 ARG ARG A . n A 1 23 ALA 23 38 38 ALA ALA A . n A 1 24 ASP 24 39 39 ASP ASP A . n A 1 25 TYR 25 40 40 TYR TYR A . n A 1 26 LEU 26 41 41 LEU LEU A . n A 1 27 LYS 27 42 42 LYS LYS A . n A 1 28 ASN 28 43 43 ASN ASN A . n A 1 29 TYR 29 44 44 TYR TYR A . n A 1 30 GLU 30 45 45 GLU GLU A . n A 1 31 PHE 31 46 46 PHE PHE A . n A 1 32 PRO 32 47 47 PRO PRO A . n A 1 33 HIS 33 48 48 HIS HIS A . n A 1 34 LEU 34 49 49 LEU LEU A . n A 1 35 GLN 35 50 50 GLN GLN A . n A 1 36 ASN 36 51 51 ASN ASN A . n A 1 37 PHE 37 52 52 PHE PHE A . n A 1 38 ILE 38 53 53 ILE ILE A . n A 1 39 LYS 39 54 54 LYS LYS A . n A 1 40 GLU 40 55 55 GLU GLU A . n A 1 41 GLY 41 56 56 GLY GLY A . n A 1 42 VAL 42 57 57 VAL VAL A . n A 1 43 LEU 43 58 58 LEU LEU A . n A 1 44 VAL 44 59 59 VAL VAL A . n A 1 45 GLU 45 60 60 GLU GLU A . n A 1 46 HIS 46 61 61 HIS HIS A . n A 1 47 VAL 47 62 62 VAL VAL A . n A 1 48 LYS 48 63 63 LYS LYS A . n A 1 49 ASN 49 64 64 ASN ASN A . n A 1 50 VAL 50 65 65 VAL VAL A . n A 1 51 PHE 51 66 66 PHE PHE A . n A 1 52 ILE 52 67 67 ILE ILE A . n A 1 53 THR 53 68 68 THR THR A . n A 1 54 LYS 54 69 69 LYS LYS A . n A 1 55 THR 55 70 70 THR THR A . n A 1 56 PHE 56 71 71 PHE PHE A . n A 1 57 PRO 57 72 72 PRO PRO A . n A 1 58 ASN 58 73 73 ASN ASN A . n A 1 59 HIS 59 74 74 HIS HIS A . n A 1 60 TYR 60 75 75 TYR TYR A . n A 1 61 SER 61 76 76 SER SER A . n A 1 62 ILE 62 77 77 ILE ILE A . n A 1 63 VAL 63 78 78 VAL VAL A . n A 1 64 THR 64 79 79 THR THR A . n A 1 65 GLY 65 80 80 GLY GLY A . n A 1 66 LEU 66 81 81 LEU LEU A . n A 1 67 TYR 67 82 82 TYR TYR A . n A 1 68 GLU 68 83 83 GLU GLU A . n A 1 69 GLU 69 84 84 GLU GLU A . n A 1 70 SER 70 85 85 SER SER A . n A 1 71 HIS 71 86 86 HIS HIS A . n A 1 72 GLY 72 87 87 GLY GLY A . n A 1 73 ILE 73 88 88 ILE ILE A . n A 1 74 VAL 74 89 89 VAL VAL A . n A 1 75 ALA 75 90 90 ALA ALA A . n A 1 76 ASN 76 91 91 ASN ASN A . n A 1 77 SER 77 92 92 SER SER A . n A 1 78 MET 78 93 93 MET MET A . n A 1 79 TYR 79 94 94 TYR TYR A . n A 1 80 ASP 80 95 95 ASP ASP A . n A 1 81 ALA 81 96 96 ALA ALA A . n A 1 82 VAL 82 97 97 VAL VAL A . n A 1 83 THR 83 98 98 THR THR A . n A 1 84 LYS 84 99 99 LYS LYS A . n A 1 85 LYS 85 100 100 LYS LYS A . n A 1 86 HIS 86 101 101 HIS HIS A . n A 1 87 PHE 87 102 102 PHE PHE A . n A 1 88 SER 88 103 103 SER SER A . n A 1 89 ASP 89 104 104 ASP ASP A . n A 1 90 SER 90 105 105 SER SER A . n A 1 91 ASN 91 106 106 ASN ASN A . n A 1 92 ASP 92 107 107 ASP ASP A . n A 1 93 LYS 93 108 108 LYS LYS A . n A 1 94 ASP 94 109 109 ASP ASP A . n A 1 95 PRO 95 110 110 PRO PRO A . n A 1 96 PHE 96 111 111 PHE PHE A . n A 1 97 TRP 97 112 112 TRP TRP A . n A 1 98 TRP 98 113 113 TRP TRP A . n A 1 99 ASN 99 114 114 ASN ASN A . n A 1 100 GLU 100 115 115 GLU GLU A . n A 1 101 ALA 101 116 116 ALA ALA A . n A 1 102 VAL 102 117 117 VAL VAL A . n A 1 103 PRO 103 118 118 PRO PRO A . n A 1 104 ILE 104 119 119 ILE ILE A . n A 1 105 TRP 105 120 120 TRP TRP A . n A 1 106 VAL 106 121 121 VAL VAL A . n A 1 107 THR 107 122 122 THR THR A . n A 1 108 ASN 108 123 123 ASN ASN A . n A 1 109 GLN 109 124 124 GLN GLN A . n A 1 110 LEU 110 125 125 LEU LEU A . n A 1 111 GLN 111 126 126 GLN GLN A . n A 1 112 GLU 112 127 127 GLU GLU A . n A 1 113 ASN 113 128 128 ASN ASN A . n A 1 114 ARG 114 129 129 ARG ARG A . n A 1 115 SER 115 130 130 SER SER A . n A 1 116 SER 116 131 131 SER SER A . n A 1 117 ALA 117 132 132 ALA ALA A . n A 1 118 ALA 118 133 133 ALA ALA A . n A 1 119 ALA 119 134 134 ALA ALA A . n A 1 120 MET 120 135 135 MET MET A . n A 1 121 TRP 121 136 136 TRP TRP A . n A 1 122 PRO 122 137 137 PRO PRO A . n A 1 123 GLY 123 138 138 GLY GLY A . n A 1 124 THR 124 139 139 THR THR A . n A 1 125 ASP 125 140 140 ASP ASP A . n A 1 126 VAL 126 141 141 VAL VAL A . n A 1 127 PRO 127 142 142 PRO PRO A . n A 1 128 ILE 128 143 143 ILE ILE A . n A 1 129 HIS 129 144 144 HIS HIS A . n A 1 130 ASP 130 145 145 ASP ASP A . n A 1 131 THR 131 146 146 THR THR A . n A 1 132 ILE 132 147 147 ILE ILE A . n A 1 133 SER 133 148 148 SER SER A . n A 1 134 SER 134 149 149 SER SER A . n A 1 135 TYR 135 150 150 TYR TYR A . n A 1 136 PHE 136 151 151 PHE PHE A . n A 1 137 MET 137 152 152 MET MET A . n A 1 138 ASN 138 153 153 ASN ASN A . n A 1 139 TYR 139 154 154 TYR TYR A . n A 1 140 ASN 140 155 155 ASN ASN A . n A 1 141 SER 141 156 156 SER SER A . n A 1 142 SER 142 157 157 SER SER A . n A 1 143 VAL 143 158 158 VAL VAL A . n A 1 144 SER 144 159 159 SER SER A . n A 1 145 PHE 145 160 160 PHE PHE A . n A 1 146 GLU 146 161 161 GLU GLU A . n A 1 147 GLU 147 162 162 GLU GLU A . n A 1 148 ARG 148 163 163 ARG ARG A . n A 1 149 LEU 149 164 164 LEU LEU A . n A 1 150 ASN 150 165 165 ASN ASN A . n A 1 151 ASN 151 166 166 ASN ASN A . n A 1 152 ILE 152 167 167 ILE ILE A . n A 1 153 THR 153 168 168 THR THR A . n A 1 154 MET 154 169 169 MET MET A . n A 1 155 TRP 155 170 170 TRP TRP A . n A 1 156 LEU 156 171 171 LEU LEU A . n A 1 157 ASN 157 172 172 ASN ASN A . n A 1 158 ASN 158 173 173 ASN ASN A . n A 1 159 SER 159 174 174 SER SER A . n A 1 160 ASN 160 175 175 ASN ASN A . n A 1 161 PRO 161 176 176 PRO PRO A . n A 1 162 PRO 162 177 177 PRO PRO A . n A 1 163 VAL 163 178 178 VAL VAL A . n A 1 164 THR 164 179 179 THR THR A . n A 1 165 PHE 165 180 180 PHE PHE A . n A 1 166 ALA 166 181 181 ALA ALA A . n A 1 167 THR 167 182 182 THR THR A . n A 1 168 LEU 168 183 183 LEU LEU A . n A 1 169 TYR 169 184 184 TYR TYR A . n A 1 170 TRP 170 185 185 TRP TRP A . n A 1 171 GLU 171 186 186 GLU GLU A . n A 1 172 GLU 172 187 187 GLU GLU A . n A 1 173 PRO 173 188 188 PRO PRO A . n A 1 174 ASP 174 189 189 ASP ASP A . n A 1 175 ALA 175 190 190 ALA ALA A . n A 1 176 SER 176 191 191 SER SER A . n A 1 177 GLY 177 192 192 GLY GLY A . n A 1 178 HIS 178 193 193 HIS HIS A . n A 1 179 LYS 179 194 194 LYS LYS A . n A 1 180 TYR 180 195 195 TYR TYR A . n A 1 181 GLY 181 196 196 GLY GLY A . n A 1 182 PRO 182 197 197 PRO PRO A . n A 1 183 GLU 183 198 198 GLU GLU A . n A 1 184 ASP 184 199 199 ASP ASP A . n A 1 185 LYS 185 200 200 LYS LYS A . n A 1 186 GLU 186 201 201 GLU GLU A . n A 1 187 ASN 187 202 202 ASN ASN A . n A 1 188 MET 188 203 203 MET MET A . n A 1 189 SER 189 204 204 SER SER A . n A 1 190 ARG 190 205 205 ARG ARG A . n A 1 191 VAL 191 206 206 VAL VAL A . n A 1 192 LEU 192 207 207 LEU LEU A . n A 1 193 LYS 193 208 208 LYS LYS A . n A 1 194 LYS 194 209 209 LYS LYS A . n A 1 195 ILE 195 210 210 ILE ILE A . n A 1 196 ASP 196 211 211 ASP ASP A . n A 1 197 ASP 197 212 212 ASP ASP A . n A 1 198 LEU 198 213 213 LEU LEU A . n A 1 199 ILE 199 214 214 ILE ILE A . n A 1 200 GLY 200 215 215 GLY GLY A . n A 1 201 ASP 201 216 216 ASP ASP A . n A 1 202 LEU 202 217 217 LEU LEU A . n A 1 203 VAL 203 218 218 VAL VAL A . n A 1 204 GLN 204 219 219 GLN GLN A . n A 1 205 ARG 205 220 220 ARG ARG A . n A 1 206 LEU 206 221 221 LEU LEU A . n A 1 207 LYS 207 222 222 LYS LYS A . n A 1 208 MET 208 223 223 MET MET A . n A 1 209 LEU 209 224 224 LEU LEU A . n A 1 210 GLY 210 225 225 GLY GLY A . n A 1 211 LEU 211 226 226 LEU LEU A . n A 1 212 TRP 212 227 227 TRP TRP A . n A 1 213 GLU 213 228 228 GLU GLU A . n A 1 214 ASN 214 229 229 ASN ASN A . n A 1 215 LEU 215 230 230 LEU LEU A . n A 1 216 ASN 216 231 231 ASN ASN A . n A 1 217 VAL 217 232 232 VAL VAL A . n A 1 218 ILE 218 233 233 ILE ILE A . n A 1 219 ILE 219 234 234 ILE ILE A . n A 1 220 THR 220 235 235 THR THR A . n A 1 221 SER 221 236 236 SER SER A . n A 1 222 ASP 222 237 237 ASP ASP A . n A 1 223 HIS 223 238 238 HIS HIS A . n A 1 224 GLY 224 239 239 GLY GLY A . n A 1 225 MET 225 240 240 MET MET A . n A 1 226 THR 226 241 241 THR THR A . n A 1 227 GLN 227 242 242 GLN GLN A . n A 1 228 CYS 228 243 243 CYS CYS A . n A 1 229 SER 229 244 244 SER SER A . n A 1 230 GLN 230 245 245 GLN GLN A . n A 1 231 ASP 231 246 246 ASP ASP A . n A 1 232 ARG 232 247 247 ARG ARG A . n A 1 233 LEU 233 248 248 LEU LEU A . n A 1 234 ILE 234 249 249 ILE ILE A . n A 1 235 ASN 235 250 250 ASN ASN A . n A 1 236 LEU 236 251 251 LEU LEU A . n A 1 237 ASP 237 252 252 ASP ASP A . n A 1 238 SER 238 253 253 SER SER A . n A 1 239 CYS 239 254 254 CYS CYS A . n A 1 240 ILE 240 255 255 ILE ILE A . n A 1 241 ASP 241 256 256 ASP ASP A . n A 1 242 HIS 242 257 257 HIS HIS A . n A 1 243 SER 243 258 258 SER SER A . n A 1 244 TYR 244 259 259 TYR TYR A . n A 1 245 TYR 245 260 260 TYR TYR A . n A 1 246 THR 246 261 261 THR THR A . n A 1 247 LEU 247 262 262 LEU LEU A . n A 1 248 ILE 248 263 263 ILE ILE A . n A 1 249 ASP 249 264 264 ASP ASP A . n A 1 250 LEU 250 265 265 LEU LEU A . n A 1 251 SER 251 266 266 SER SER A . n A 1 252 PRO 252 267 267 PRO PRO A . n A 1 253 VAL 253 268 268 VAL VAL A . n A 1 254 ALA 254 269 269 ALA ALA A . n A 1 255 ALA 255 270 270 ALA ALA A . n A 1 256 ILE 256 271 271 ILE ILE A . n A 1 257 LEU 257 272 272 LEU LEU A . n A 1 258 PRO 258 273 273 PRO PRO A . n A 1 259 LYS 259 274 274 LYS LYS A . n A 1 260 ILE 260 275 275 ILE ILE A . n A 1 261 ASN 261 276 276 ASN ASN A . n A 1 262 ARG 262 277 277 ARG ARG A . n A 1 263 THR 263 278 278 THR THR A . n A 1 264 GLU 264 279 279 GLU GLU A . n A 1 265 VAL 265 280 280 VAL VAL A . n A 1 266 TYR 266 281 281 TYR TYR A . n A 1 267 ASN 267 282 282 ASN ASN A . n A 1 268 LYS 268 283 283 LYS LYS A . n A 1 269 LEU 269 284 284 LEU LEU A . n A 1 270 LYS 270 285 285 LYS LYS A . n A 1 271 ASN 271 286 286 ASN ASN A . n A 1 272 CYS 272 287 287 CYS CYS A . n A 1 273 SER 273 288 288 SER SER A . n A 1 274 PRO 274 289 289 PRO PRO A . n A 1 275 HIS 275 290 290 HIS HIS A . n A 1 276 MET 276 291 291 MET MET A . n A 1 277 ASN 277 292 292 ASN ASN A . n A 1 278 VAL 278 293 293 VAL VAL A . n A 1 279 TYR 279 294 294 TYR TYR A . n A 1 280 LEU 280 295 295 LEU LEU A . n A 1 281 LYS 281 296 296 LYS LYS A . n A 1 282 GLU 282 297 297 GLU GLU A . n A 1 283 ASP 283 298 298 ASP ASP A . n A 1 284 ILE 284 299 299 ILE ILE A . n A 1 285 PRO 285 300 300 PRO PRO A . n A 1 286 ASN 286 301 301 ASN ASN A . n A 1 287 ARG 287 302 302 ARG ARG A . n A 1 288 PHE 288 303 303 PHE PHE A . n A 1 289 TYR 289 304 304 TYR TYR A . n A 1 290 TYR 290 305 305 TYR TYR A . n A 1 291 GLN 291 306 306 GLN GLN A . n A 1 292 HIS 292 307 307 HIS HIS A . n A 1 293 ASN 293 308 308 ASN ASN A . n A 1 294 ASP 294 309 309 ASP ASP A . n A 1 295 ARG 295 310 310 ARG ARG A . n A 1 296 ILE 296 311 311 ILE ILE A . n A 1 297 GLN 297 312 312 GLN GLN A . n A 1 298 PRO 298 313 313 PRO PRO A . n A 1 299 ILE 299 314 314 ILE ILE A . n A 1 300 ILE 300 315 315 ILE ILE A . n A 1 301 LEU 301 316 316 LEU LEU A . n A 1 302 VAL 302 317 317 VAL VAL A . n A 1 303 ALA 303 318 318 ALA ALA A . n A 1 304 ASP 304 319 319 ASP ASP A . n A 1 305 GLU 305 320 320 GLU GLU A . n A 1 306 GLY 306 321 321 GLY GLY A . n A 1 307 TRP 307 322 322 TRP TRP A . n A 1 308 THR 308 323 323 THR THR A . n A 1 309 ILE 309 324 324 ILE ILE A . n A 1 310 VAL 310 325 325 VAL VAL A . n A 1 311 LEU 311 326 326 LEU LEU A . n A 1 312 ASN 312 327 327 ASN ASN A . n A 1 313 GLU 313 328 328 GLU GLU A . n A 1 314 SER 314 329 329 SER SER A . n A 1 315 SER 315 330 330 SER SER A . n A 1 316 GLN 316 331 331 GLN GLN A . n A 1 317 LYS 317 332 332 LYS LYS A . n A 1 318 LEU 318 333 333 LEU LEU A . n A 1 319 GLY 319 334 334 GLY GLY A . n A 1 320 ASP 320 335 335 ASP ASP A . n A 1 321 HIS 321 336 336 HIS HIS A . n A 1 322 GLY 322 337 337 GLY GLY A . n A 1 323 TYR 323 338 338 TYR TYR A . n A 1 324 ASP 324 339 339 ASP ASP A . n A 1 325 ASN 325 340 340 ASN ASN A . n A 1 326 SER 326 341 341 SER SER A . n A 1 327 LEU 327 342 342 LEU LEU A . n A 1 328 PRO 328 343 343 PRO PRO A . n A 1 329 SER 329 344 344 SER SER A . n A 1 330 MET 330 345 345 MET MET A . n A 1 331 HIS 331 346 346 HIS HIS A . n A 1 332 PRO 332 347 347 PRO PRO A . n A 1 333 PHE 333 348 348 PHE PHE A . n A 1 334 LEU 334 349 349 LEU LEU A . n A 1 335 ALA 335 350 350 ALA ALA A . n A 1 336 ALA 336 351 351 ALA ALA A . n A 1 337 HIS 337 352 352 HIS HIS A . n A 1 338 GLY 338 353 353 GLY GLY A . n A 1 339 PRO 339 354 354 PRO PRO A . n A 1 340 ALA 340 355 355 ALA ALA A . n A 1 341 PHE 341 356 356 PHE PHE A . n A 1 342 HIS 342 357 357 HIS HIS A . n A 1 343 LYS 343 358 358 LYS LYS A . n A 1 344 GLY 344 359 359 GLY GLY A . n A 1 345 TYR 345 360 360 TYR TYR A . n A 1 346 LYS 346 361 361 LYS LYS A . n A 1 347 HIS 347 362 362 HIS HIS A . n A 1 348 SER 348 363 363 SER SER A . n A 1 349 THR 349 364 364 THR THR A . n A 1 350 ILE 350 365 365 ILE ILE A . n A 1 351 ASN 351 366 366 ASN ASN A . n A 1 352 ILE 352 367 367 ILE ILE A . n A 1 353 VAL 353 368 368 VAL VAL A . n A 1 354 ASP 354 369 369 ASP ASP A . n A 1 355 ILE 355 370 370 ILE ILE A . n A 1 356 TYR 356 371 371 TYR TYR A . n A 1 357 PRO 357 372 372 PRO PRO A . n A 1 358 MET 358 373 373 MET MET A . n A 1 359 MET 359 374 374 MET MET A . n A 1 360 CYS 360 375 375 CYS CYS A . n A 1 361 HIS 361 376 376 HIS HIS A . n A 1 362 ILE 362 377 377 ILE ILE A . n A 1 363 LEU 363 378 378 LEU LEU A . n A 1 364 GLY 364 379 379 GLY GLY A . n A 1 365 LEU 365 380 380 LEU LEU A . n A 1 366 LYS 366 381 381 LYS LYS A . n A 1 367 PRO 367 382 382 PRO PRO A . n A 1 368 HIS 368 383 383 HIS HIS A . n A 1 369 PRO 369 384 384 PRO PRO A . n A 1 370 ASN 370 385 385 ASN ASN A . n A 1 371 ASN 371 386 386 ASN ASN A . n A 1 372 GLY 372 387 387 GLY GLY A . n A 1 373 THR 373 388 388 THR THR A . n A 1 374 PHE 374 389 389 PHE PHE A . n A 1 375 GLY 375 390 390 GLY GLY A . n A 1 376 HIS 376 391 391 HIS HIS A . n A 1 377 THR 377 392 392 THR THR A . n A 1 378 LYS 378 393 393 LYS LYS A . n A 1 379 CYS 379 394 394 CYS CYS A . n A 1 380 LEU 380 395 395 LEU LEU A . n A 1 381 LEU 381 396 396 LEU LEU A . n A 1 382 VAL 382 397 397 VAL VAL A . n A 1 383 ASP 383 398 398 ASP ASP A . n A 1 384 GLN 384 399 399 GLN GLN A . n A 1 385 TRP 385 400 400 TRP TRP A . n A 1 386 CYS 386 401 401 CYS CYS A . n A 1 387 ILE 387 402 402 ILE ILE A . n A 1 388 ASN 388 403 ? ? ? A . n A 1 389 LEU 389 404 ? ? ? A . n A 1 390 PRO 390 405 ? ? ? A . n A 1 391 GLU 391 406 ? ? ? A . n A 1 392 ALA 392 407 ? ? ? A . n A 1 393 LEU 393 408 ? ? ? A . n A 1 394 ILE 394 409 ? ? ? A . n A 1 395 ASN 395 410 ? ? ? A . n A 1 396 GLU 396 411 ? ? ? A . n A 1 397 ASN 397 412 ? ? ? A . n A 1 398 LEU 398 413 ? ? ? A . n A 1 399 TYR 399 414 ? ? ? A . n A 1 400 PHE 400 415 ? ? ? A . n A 1 401 GLN 401 416 ? ? ? 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 1860 NAG NAG A . C 2 NAG 2 502 1861 NAG NAG A . D 2 NAG 1 503 1970 NAG NAG A . E 2 NAG 1 504 1980 NAG NAG A . F 3 AMP 1 505 1004 AMP AMP A . G 4 ZN 1 506 1001 ZN ZN A . H 4 ZN 1 507 1002 ZN ZN A . I 5 HOH 1 601 1 HOH HOH A . I 5 HOH 2 602 2 HOH HOH A . I 5 HOH 3 603 3 HOH HOH A . I 5 HOH 4 604 4 HOH HOH A . I 5 HOH 5 605 5 HOH HOH A . I 5 HOH 6 606 6 HOH HOH A . I 5 HOH 7 607 7 HOH HOH A . I 5 HOH 8 608 8 HOH HOH A . I 5 HOH 9 609 9 HOH HOH A . I 5 HOH 10 610 10 HOH HOH A . I 5 HOH 11 611 11 HOH HOH A . I 5 HOH 12 612 12 HOH HOH A . I 5 HOH 13 613 13 HOH HOH A . I 5 HOH 14 614 14 HOH HOH A . I 5 HOH 15 615 15 HOH HOH A . I 5 HOH 16 616 16 HOH HOH A . I 5 HOH 17 617 17 HOH HOH A . I 5 HOH 18 618 18 HOH HOH A . I 5 HOH 19 619 19 HOH HOH A . I 5 HOH 20 620 20 HOH HOH A . I 5 HOH 21 621 21 HOH HOH A . I 5 HOH 22 622 22 HOH HOH A . I 5 HOH 23 623 23 HOH HOH A . I 5 HOH 24 624 24 HOH HOH A . I 5 HOH 25 625 25 HOH HOH A . I 5 HOH 26 626 26 HOH HOH A . I 5 HOH 27 627 27 HOH HOH A . I 5 HOH 28 628 28 HOH HOH A . I 5 HOH 29 629 29 HOH HOH A . I 5 HOH 30 630 30 HOH HOH A . I 5 HOH 31 631 31 HOH HOH A . I 5 HOH 32 632 32 HOH HOH A . I 5 HOH 33 633 33 HOH HOH A . I 5 HOH 34 634 34 HOH HOH A . I 5 HOH 35 635 35 HOH HOH A . I 5 HOH 36 636 36 HOH HOH A . I 5 HOH 37 637 37 HOH HOH A . I 5 HOH 38 638 38 HOH HOH A . I 5 HOH 39 639 39 HOH HOH A . I 5 HOH 40 640 40 HOH HOH A . I 5 HOH 41 641 41 HOH HOH A . I 5 HOH 42 642 42 HOH HOH A . I 5 HOH 43 643 43 HOH HOH A . I 5 HOH 44 644 44 HOH HOH A . I 5 HOH 45 645 45 HOH HOH A . I 5 HOH 46 646 46 HOH HOH A . I 5 HOH 47 647 47 HOH HOH A . I 5 HOH 48 648 48 HOH HOH A . I 5 HOH 49 649 49 HOH HOH A . I 5 HOH 50 650 50 HOH HOH A . I 5 HOH 51 651 51 HOH HOH A . I 5 HOH 52 652 52 HOH HOH A . I 5 HOH 53 653 53 HOH HOH A . I 5 HOH 54 654 54 HOH HOH A . I 5 HOH 55 655 55 HOH HOH A . I 5 HOH 56 656 56 HOH HOH A . I 5 HOH 57 657 57 HOH HOH A . I 5 HOH 58 658 58 HOH HOH A . I 5 HOH 59 659 59 HOH HOH A . I 5 HOH 60 660 60 HOH HOH A . I 5 HOH 61 661 61 HOH HOH A . I 5 HOH 62 662 62 HOH HOH A . I 5 HOH 63 663 63 HOH HOH A . I 5 HOH 64 664 64 HOH HOH A . I 5 HOH 65 665 65 HOH HOH A . I 5 HOH 66 666 66 HOH HOH A . I 5 HOH 67 667 67 HOH HOH A . I 5 HOH 68 668 68 HOH HOH A . I 5 HOH 69 669 69 HOH HOH A . I 5 HOH 70 670 70 HOH HOH A . I 5 HOH 71 671 71 HOH HOH A . I 5 HOH 72 672 72 HOH HOH A . I 5 HOH 73 673 73 HOH HOH A . I 5 HOH 74 674 74 HOH HOH A . I 5 HOH 75 675 75 HOH HOH A . I 5 HOH 76 676 76 HOH HOH A . I 5 HOH 77 677 77 HOH HOH A . I 5 HOH 78 678 78 HOH HOH A . I 5 HOH 79 679 79 HOH HOH A . I 5 HOH 80 680 80 HOH HOH A . I 5 HOH 81 681 81 HOH HOH A . I 5 HOH 82 682 82 HOH HOH A . I 5 HOH 83 683 83 HOH HOH A . I 5 HOH 84 684 84 HOH HOH A . I 5 HOH 85 685 85 HOH HOH A . I 5 HOH 86 686 86 HOH HOH A . I 5 HOH 87 687 87 HOH HOH A . I 5 HOH 88 688 88 HOH HOH A . I 5 HOH 89 689 89 HOH HOH A . I 5 HOH 90 690 90 HOH HOH A . I 5 HOH 91 691 91 HOH HOH A . I 5 HOH 92 692 92 HOH HOH A . I 5 HOH 93 693 93 HOH HOH A . I 5 HOH 94 694 94 HOH HOH A . I 5 HOH 95 695 95 HOH HOH A . I 5 HOH 96 696 96 HOH HOH A . I 5 HOH 97 697 97 HOH HOH A . I 5 HOH 98 698 98 HOH HOH A . I 5 HOH 99 699 99 HOH HOH A . I 5 HOH 100 700 100 HOH HOH A . I 5 HOH 101 701 101 HOH HOH A . I 5 HOH 102 702 102 HOH HOH A . I 5 HOH 103 703 103 HOH HOH A . I 5 HOH 104 704 104 HOH HOH A . I 5 HOH 105 705 105 HOH HOH A . I 5 HOH 106 706 106 HOH HOH A . I 5 HOH 107 707 107 HOH HOH A . I 5 HOH 108 708 108 HOH HOH A . I 5 HOH 109 709 109 HOH HOH A . I 5 HOH 110 710 110 HOH HOH A . I 5 HOH 111 711 111 HOH HOH A . I 5 HOH 112 712 112 HOH HOH A . I 5 HOH 113 713 113 HOH HOH A . I 5 HOH 114 714 114 HOH HOH A . I 5 HOH 115 715 115 HOH HOH A . I 5 HOH 116 716 116 HOH HOH A . I 5 HOH 117 717 117 HOH HOH A . I 5 HOH 118 718 118 HOH HOH A . I 5 HOH 119 719 119 HOH HOH A . I 5 HOH 120 720 120 HOH HOH A . I 5 HOH 121 721 121 HOH HOH A . I 5 HOH 122 722 122 HOH HOH A . I 5 HOH 123 723 123 HOH HOH A . I 5 HOH 124 724 124 HOH HOH A . I 5 HOH 125 725 125 HOH HOH A . I 5 HOH 126 726 126 HOH HOH A . I 5 HOH 127 727 127 HOH HOH A . I 5 HOH 128 728 128 HOH HOH A . I 5 HOH 129 729 129 HOH HOH A . I 5 HOH 130 730 130 HOH HOH A . I 5 HOH 131 731 131 HOH HOH A . I 5 HOH 132 732 132 HOH HOH A . I 5 HOH 133 733 133 HOH HOH A . I 5 HOH 134 734 134 HOH HOH A . I 5 HOH 135 735 135 HOH HOH A . I 5 HOH 136 736 136 HOH HOH A . I 5 HOH 137 737 137 HOH HOH A . I 5 HOH 138 738 138 HOH HOH A . I 5 HOH 139 739 139 HOH HOH A . I 5 HOH 140 740 140 HOH HOH A . I 5 HOH 141 741 141 HOH HOH A . I 5 HOH 142 742 142 HOH HOH A . I 5 HOH 143 743 143 HOH HOH A . I 5 HOH 144 744 144 HOH HOH A . I 5 HOH 145 745 145 HOH HOH A . I 5 HOH 146 746 146 HOH HOH A . I 5 HOH 147 747 147 HOH HOH A . I 5 HOH 148 748 148 HOH HOH A . I 5 HOH 149 749 149 HOH HOH A . I 5 HOH 150 750 150 HOH HOH A . I 5 HOH 151 751 151 HOH HOH A . I 5 HOH 152 752 152 HOH HOH A . I 5 HOH 153 753 153 HOH HOH A . I 5 HOH 154 754 154 HOH HOH A . I 5 HOH 155 755 155 HOH HOH A . I 5 HOH 156 756 156 HOH HOH A . I 5 HOH 157 757 157 HOH HOH A . I 5 HOH 158 758 158 HOH HOH A . I 5 HOH 159 759 159 HOH HOH A . I 5 HOH 160 760 160 HOH HOH A . I 5 HOH 161 761 161 HOH HOH A . I 5 HOH 162 762 162 HOH HOH A . I 5 HOH 163 763 163 HOH HOH A . I 5 HOH 164 764 164 HOH HOH A . I 5 HOH 165 765 165 HOH HOH A . I 5 HOH 166 766 166 HOH HOH A . I 5 HOH 167 767 167 HOH HOH A . I 5 HOH 168 768 168 HOH HOH A . I 5 HOH 169 769 169 HOH HOH A . I 5 HOH 170 770 170 HOH HOH A . I 5 HOH 171 771 171 HOH HOH A . I 5 HOH 172 772 172 HOH HOH A . I 5 HOH 173 773 173 HOH HOH A . I 5 HOH 174 774 174 HOH HOH A . I 5 HOH 175 775 175 HOH HOH A . I 5 HOH 176 776 176 HOH HOH A . I 5 HOH 177 777 177 HOH HOH A . I 5 HOH 178 778 178 HOH HOH A . I 5 HOH 179 779 179 HOH HOH A . I 5 HOH 180 780 180 HOH HOH A . I 5 HOH 181 781 181 HOH HOH A . I 5 HOH 182 782 182 HOH HOH A . I 5 HOH 183 783 183 HOH HOH A . I 5 HOH 184 784 184 HOH HOH A . I 5 HOH 185 785 185 HOH HOH A . I 5 HOH 186 786 186 HOH HOH A . I 5 HOH 187 787 187 HOH HOH A . I 5 HOH 188 788 188 HOH HOH A . I 5 HOH 189 789 189 HOH HOH A . I 5 HOH 190 790 190 HOH HOH A . I 5 HOH 191 791 191 HOH HOH A . I 5 HOH 192 792 192 HOH HOH A . I 5 HOH 193 793 193 HOH HOH A . I 5 HOH 194 794 194 HOH HOH A . I 5 HOH 195 795 195 HOH HOH A . I 5 HOH 196 796 196 HOH HOH A . I 5 HOH 197 797 197 HOH HOH A . I 5 HOH 198 798 198 HOH HOH A . I 5 HOH 199 799 199 HOH HOH A . I 5 HOH 200 800 200 HOH HOH A . I 5 HOH 201 801 201 HOH HOH A . I 5 HOH 202 802 202 HOH HOH A . I 5 HOH 203 803 203 HOH HOH A . I 5 HOH 204 804 204 HOH HOH A . I 5 HOH 205 805 205 HOH HOH A . I 5 HOH 206 806 206 HOH HOH A . I 5 HOH 207 807 207 HOH HOH A . I 5 HOH 208 808 208 HOH HOH A . I 5 HOH 209 809 209 HOH HOH A . I 5 HOH 210 810 210 HOH HOH A . I 5 HOH 211 811 211 HOH HOH A . I 5 HOH 212 812 212 HOH HOH A . I 5 HOH 213 813 213 HOH HOH A . I 5 HOH 214 814 214 HOH HOH A . I 5 HOH 215 815 215 HOH HOH A . I 5 HOH 216 816 216 HOH HOH A . I 5 HOH 217 817 217 HOH HOH A . I 5 HOH 218 818 218 HOH HOH A . I 5 HOH 219 819 219 HOH HOH A . I 5 HOH 220 820 220 HOH HOH A . I 5 HOH 221 821 221 HOH HOH A . I 5 HOH 222 822 222 HOH HOH A . I 5 HOH 223 823 223 HOH HOH A . I 5 HOH 224 824 224 HOH HOH A . I 5 HOH 225 825 225 HOH HOH A . I 5 HOH 226 826 226 HOH HOH A . I 5 HOH 227 827 227 HOH HOH A . I 5 HOH 228 828 228 HOH HOH A . I 5 HOH 229 829 229 HOH HOH A . I 5 HOH 230 830 230 HOH HOH A . I 5 HOH 231 831 231 HOH HOH A . I 5 HOH 232 832 232 HOH HOH A . I 5 HOH 233 833 233 HOH HOH A . I 5 HOH 234 834 234 HOH HOH A . I 5 HOH 235 835 235 HOH HOH A . I 5 HOH 236 836 236 HOH HOH A . I 5 HOH 237 837 237 HOH HOH A . I 5 HOH 238 838 238 HOH HOH A . I 5 HOH 239 839 239 HOH HOH A . I 5 HOH 240 840 240 HOH HOH A . I 5 HOH 241 841 241 HOH HOH A . I 5 HOH 242 842 242 HOH HOH A . I 5 HOH 243 843 243 HOH HOH A . I 5 HOH 244 844 244 HOH HOH A . I 5 HOH 245 845 245 HOH HOH A . I 5 HOH 246 846 246 HOH HOH A . I 5 HOH 247 847 247 HOH HOH A . I 5 HOH 248 848 248 HOH HOH A . I 5 HOH 249 849 249 HOH HOH A . I 5 HOH 250 850 250 HOH HOH A . I 5 HOH 251 851 251 HOH HOH A . I 5 HOH 252 852 252 HOH HOH A . I 5 HOH 253 853 253 HOH HOH A . I 5 HOH 254 854 254 HOH HOH A . I 5 HOH 255 855 255 HOH HOH A . I 5 HOH 256 856 256 HOH HOH A . I 5 HOH 257 857 257 HOH HOH A . I 5 HOH 258 858 258 HOH HOH A . I 5 HOH 259 859 259 HOH HOH A . I 5 HOH 260 860 260 HOH HOH A . I 5 HOH 261 861 261 HOH HOH A . I 5 HOH 262 862 262 HOH HOH A . I 5 HOH 263 863 263 HOH HOH A . I 5 HOH 264 864 264 HOH HOH A . I 5 HOH 265 865 265 HOH HOH A . I 5 HOH 266 866 266 HOH HOH A . I 5 HOH 267 867 267 HOH HOH A . I 5 HOH 268 868 268 HOH HOH A . I 5 HOH 269 869 269 HOH HOH A . I 5 HOH 270 870 270 HOH HOH A . I 5 HOH 271 871 271 HOH HOH A . I 5 HOH 272 872 272 HOH HOH A . I 5 HOH 273 873 273 HOH HOH A . I 5 HOH 274 874 274 HOH HOH A . I 5 HOH 275 875 275 HOH HOH A . I 5 HOH 276 876 276 HOH HOH A . I 5 HOH 277 877 277 HOH HOH A . I 5 HOH 278 878 278 HOH HOH A . I 5 HOH 279 879 279 HOH HOH A . I 5 HOH 280 880 280 HOH HOH A . I 5 HOH 281 881 281 HOH HOH A . I 5 HOH 282 882 282 HOH HOH A . I 5 HOH 283 883 283 HOH HOH A . I 5 HOH 284 884 284 HOH HOH A . I 5 HOH 285 885 285 HOH HOH A . I 5 HOH 286 886 286 HOH HOH A . I 5 HOH 287 887 287 HOH HOH A . I 5 HOH 288 888 288 HOH HOH A . I 5 HOH 289 889 289 HOH HOH A . I 5 HOH 290 890 290 HOH HOH A . I 5 HOH 291 891 291 HOH HOH A . I 5 HOH 292 892 292 HOH HOH A . I 5 HOH 293 893 293 HOH HOH A . I 5 HOH 294 894 294 HOH HOH A . I 5 HOH 295 895 295 HOH HOH A . I 5 HOH 296 896 296 HOH HOH A . I 5 HOH 297 897 297 HOH HOH A . I 5 HOH 298 898 298 HOH HOH A . I 5 HOH 299 899 299 HOH HOH A . I 5 HOH 300 900 300 HOH HOH A . I 5 HOH 301 901 301 HOH HOH A . I 5 HOH 302 902 302 HOH HOH A . I 5 HOH 303 903 303 HOH HOH A . I 5 HOH 304 904 304 HOH HOH A . I 5 HOH 305 905 305 HOH HOH A . I 5 HOH 306 906 306 HOH HOH A . I 5 HOH 307 907 307 HOH HOH A . I 5 HOH 308 908 308 HOH HOH A . I 5 HOH 309 909 309 HOH HOH A . I 5 HOH 310 910 310 HOH HOH A . I 5 HOH 311 911 311 HOH HOH A . I 5 HOH 312 912 312 HOH HOH A . I 5 HOH 313 913 313 HOH HOH A . I 5 HOH 314 914 314 HOH HOH A . I 5 HOH 315 915 315 HOH HOH A . I 5 HOH 316 916 316 HOH HOH A . I 5 HOH 317 917 317 HOH HOH A . I 5 HOH 318 918 318 HOH HOH A . I 5 HOH 319 919 319 HOH HOH A . I 5 HOH 320 920 320 HOH HOH A . I 5 HOH 321 921 321 HOH HOH A . I 5 HOH 322 922 322 HOH HOH A . I 5 HOH 323 923 323 HOH HOH A . I 5 HOH 324 924 324 HOH HOH A . I 5 HOH 325 925 325 HOH HOH A . I 5 HOH 326 926 326 HOH HOH A . I 5 HOH 327 927 327 HOH HOH A . I 5 HOH 328 928 328 HOH HOH A . I 5 HOH 329 929 329 HOH HOH A . I 5 HOH 330 930 330 HOH HOH A . I 5 HOH 331 931 331 HOH HOH A . I 5 HOH 332 932 332 HOH HOH A . I 5 HOH 333 933 333 HOH HOH A . I 5 HOH 334 934 334 HOH HOH A . I 5 HOH 335 935 335 HOH HOH A . I 5 HOH 336 936 336 HOH HOH A . I 5 HOH 337 937 337 HOH HOH A . I 5 HOH 338 938 338 HOH HOH A . I 5 HOH 339 939 339 HOH HOH A . I 5 HOH 340 940 340 HOH HOH A . I 5 HOH 341 941 341 HOH HOH A . I 5 HOH 342 942 342 HOH HOH A . I 5 HOH 343 943 343 HOH HOH A . I 5 HOH 344 944 344 HOH HOH A . I 5 HOH 345 945 345 HOH HOH A . I 5 HOH 346 946 346 HOH HOH A . I 5 HOH 347 947 347 HOH HOH A . I 5 HOH 348 948 348 HOH HOH A . I 5 HOH 349 949 349 HOH HOH A . I 5 HOH 350 950 350 HOH HOH A . I 5 HOH 351 951 351 HOH HOH A . I 5 HOH 352 952 352 HOH HOH A . I 5 HOH 353 953 353 HOH HOH A . I 5 HOH 354 954 354 HOH HOH A . I 5 HOH 355 955 355 HOH HOH A . I 5 HOH 356 956 356 HOH HOH A . I 5 HOH 357 957 357 HOH HOH A . I 5 HOH 358 958 358 HOH HOH A . I 5 HOH 359 959 359 HOH HOH A . I 5 HOH 360 960 360 HOH HOH A . I 5 HOH 361 961 361 HOH HOH A . I 5 HOH 362 962 362 HOH HOH A . I 5 HOH 363 963 363 HOH HOH A . I 5 HOH 364 964 364 HOH HOH A . I 5 HOH 365 965 365 HOH HOH A . I 5 HOH 366 966 366 HOH HOH A . I 5 HOH 367 967 367 HOH HOH A . I 5 HOH 368 968 368 HOH HOH A . I 5 HOH 369 969 369 HOH HOH A . I 5 HOH 370 970 370 HOH HOH A . I 5 HOH 371 971 371 HOH HOH A . I 5 HOH 372 972 372 HOH HOH A . I 5 HOH 373 973 373 HOH HOH A . I 5 HOH 374 974 374 HOH HOH A . I 5 HOH 375 975 375 HOH HOH A . I 5 HOH 376 976 376 HOH HOH A . I 5 HOH 377 977 377 HOH HOH A . I 5 HOH 378 978 378 HOH HOH A . I 5 HOH 379 979 379 HOH HOH A . I 5 HOH 380 980 380 HOH HOH A . I 5 HOH 381 981 381 HOH HOH A . I 5 HOH 382 982 382 HOH HOH A . I 5 HOH 383 983 383 HOH HOH A . I 5 HOH 384 984 384 HOH HOH A . I 5 HOH 385 985 385 HOH HOH A . I 5 HOH 386 986 386 HOH HOH A . I 5 HOH 387 987 387 HOH HOH A . I 5 HOH 388 988 388 HOH HOH A . I 5 HOH 389 989 389 HOH HOH A . I 5 HOH 390 990 390 HOH HOH A . I 5 HOH 391 991 391 HOH HOH A . I 5 HOH 392 992 392 HOH HOH A . I 5 HOH 393 993 393 HOH HOH A . I 5 HOH 394 994 394 HOH HOH A . I 5 HOH 395 995 395 HOH HOH A . I 5 HOH 396 996 396 HOH HOH A . I 5 HOH 397 997 397 HOH HOH A . I 5 HOH 398 998 398 HOH HOH A . I 5 HOH 399 999 399 HOH HOH A . I 5 HOH 400 1000 400 HOH HOH A . I 5 HOH 401 1001 401 HOH HOH A . I 5 HOH 402 1002 402 HOH HOH A . I 5 HOH 403 1003 403 HOH HOH A . I 5 HOH 404 1004 404 HOH HOH A . I 5 HOH 405 1005 405 HOH HOH A . I 5 HOH 406 1006 406 HOH HOH A . I 5 HOH 407 1007 407 HOH HOH A . I 5 HOH 408 1008 408 HOH HOH A . I 5 HOH 409 1009 409 HOH HOH A . I 5 HOH 410 1010 410 HOH HOH A . I 5 HOH 411 1011 411 HOH HOH A . I 5 HOH 412 1012 412 HOH HOH A . I 5 HOH 413 1013 413 HOH HOH A . I 5 HOH 414 1014 414 HOH HOH A . I 5 HOH 415 1015 415 HOH HOH A . I 5 HOH 416 1016 416 HOH HOH A . I 5 HOH 417 1017 417 HOH HOH A . I 5 HOH 418 1018 418 HOH HOH A . I 5 HOH 419 1019 419 HOH HOH A . I 5 HOH 420 1020 420 HOH HOH A . I 5 HOH 421 1021 421 HOH HOH A . I 5 HOH 422 1022 422 HOH HOH A . I 5 HOH 423 1023 423 HOH HOH A . I 5 HOH 424 1024 424 HOH HOH A . I 5 HOH 425 1025 425 HOH HOH A . I 5 HOH 426 1026 426 HOH HOH A . I 5 HOH 427 1027 427 HOH HOH A . I 5 HOH 428 1028 428 HOH HOH A . I 5 HOH 429 1029 429 HOH HOH A . I 5 HOH 430 1030 430 HOH HOH A . I 5 HOH 431 1031 431 HOH HOH A . I 5 HOH 432 1032 432 HOH HOH A . I 5 HOH 433 1033 433 HOH HOH A . I 5 HOH 434 1034 434 HOH HOH A . I 5 HOH 435 1035 435 HOH HOH A . I 5 HOH 436 1036 436 HOH HOH A . I 5 HOH 437 1037 437 HOH HOH A . I 5 HOH 438 1038 438 HOH HOH A . I 5 HOH 439 1039 439 HOH HOH A . I 5 HOH 440 1040 440 HOH HOH A . I 5 HOH 441 1041 441 HOH HOH A . I 5 HOH 442 1042 442 HOH HOH A . I 5 HOH 443 1043 443 HOH HOH A . I 5 HOH 444 1044 444 HOH HOH A . I 5 HOH 445 1045 445 HOH HOH A . I 5 HOH 446 1046 446 HOH HOH A . I 5 HOH 447 1047 447 HOH HOH A . I 5 HOH 448 1048 448 HOH HOH A . I 5 HOH 449 1049 449 HOH HOH A . I 5 HOH 450 1050 450 HOH HOH A . I 5 HOH 451 1051 451 HOH HOH A . I 5 HOH 452 1052 452 HOH HOH A . I 5 HOH 453 1053 453 HOH HOH A . I 5 HOH 454 1054 454 HOH HOH A . I 5 HOH 455 1055 455 HOH HOH A . I 5 HOH 456 1056 456 HOH HOH A . I 5 HOH 457 1057 457 HOH HOH A . I 5 HOH 458 1058 458 HOH HOH A . I 5 HOH 459 1059 459 HOH HOH A . I 5 HOH 460 1060 460 HOH HOH A . I 5 HOH 461 1061 461 HOH HOH A . I 5 HOH 462 1062 462 HOH HOH A . I 5 HOH 463 1063 463 HOH HOH A . I 5 HOH 464 1064 464 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 371 A ASN 386 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 151 A ASN 166 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 140 A ASN 155 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_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 873 ? I HOH . 2 1 A HOH 981 ? I 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 NE2 ? A HIS 223 ? A HIS 238 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD2 ? A ASP 222 ? A ASP 237 ? 1_555 96.4 ? 2 NE2 ? A HIS 223 ? A HIS 238 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD1 ? A ASP 19 ? A ASP 34 ? 1_555 106.8 ? 3 OD2 ? A ASP 222 ? A ASP 237 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD1 ? A ASP 19 ? A ASP 34 ? 1_555 114.4 ? 4 NE2 ? A HIS 223 ? A HIS 238 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OG1 ? A THR 55 ? A THR 70 ? 1_555 106.3 ? 5 OD2 ? A ASP 222 ? A ASP 237 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OG1 ? A THR 55 ? A THR 70 ? 1_555 106.5 ? 6 OD1 ? A ASP 19 ? A ASP 34 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OG1 ? A THR 55 ? A THR 70 ? 1_555 122.9 ? 7 NE2 ? A HIS 223 ? A HIS 238 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD2 ? A ASP 19 ? A ASP 34 ? 1_555 160.0 ? 8 OD2 ? A ASP 222 ? A ASP 237 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD2 ? A ASP 19 ? A ASP 34 ? 1_555 87.5 ? 9 OD1 ? A ASP 19 ? A ASP 34 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD2 ? A ASP 19 ? A ASP 34 ? 1_555 54.3 ? 10 OG1 ? A THR 55 ? A THR 70 ? 1_555 ZN ? G ZN . ? A ZN 506 ? 1_555 OD2 ? A ASP 19 ? A ASP 34 ? 1_555 91.3 ? 11 O2P ? F AMP . ? A AMP 505 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 NE2 ? A HIS 178 ? A HIS 193 ? 1_555 137.2 ? 12 O2P ? F AMP . ? A AMP 505 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 NE2 ? A HIS 321 ? A HIS 336 ? 1_555 104.9 ? 13 NE2 ? A HIS 178 ? A HIS 193 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 NE2 ? A HIS 321 ? A HIS 336 ? 1_555 100.6 ? 14 O2P ? F AMP . ? A AMP 505 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD1 ? A ASP 174 ? A ASP 189 ? 1_555 107.6 ? 15 NE2 ? A HIS 178 ? A HIS 193 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD1 ? A ASP 174 ? A ASP 189 ? 1_555 104.0 ? 16 NE2 ? A HIS 321 ? A HIS 336 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD1 ? A ASP 174 ? A ASP 189 ? 1_555 94.4 ? 17 O2P ? F AMP . ? A AMP 505 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 O ? I HOH . ? A HOH 874 ? 1_555 53.2 ? 18 NE2 ? A HIS 178 ? A HIS 193 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 O ? I HOH . ? A HOH 874 ? 1_555 89.1 ? 19 NE2 ? A HIS 321 ? A HIS 336 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 O ? I HOH . ? A HOH 874 ? 1_555 150.3 ? 20 OD1 ? A ASP 174 ? A ASP 189 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 O ? I HOH . ? A HOH 874 ? 1_555 110.6 ? 21 O2P ? F AMP . ? A AMP 505 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD2 ? A ASP 174 ? A ASP 189 ? 1_555 82.6 ? 22 NE2 ? A HIS 178 ? A HIS 193 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD2 ? A ASP 174 ? A ASP 189 ? 1_555 93.6 ? 23 NE2 ? A HIS 321 ? A HIS 336 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD2 ? A ASP 174 ? A ASP 189 ? 1_555 147.8 ? 24 OD1 ? A ASP 174 ? A ASP 189 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD2 ? A ASP 174 ? A ASP 189 ? 1_555 54.0 ? 25 O ? I HOH . ? A HOH 874 ? 1_555 ZN ? H ZN . ? A ZN 507 ? 1_555 OD2 ? A ASP 174 ? A ASP 189 ? 1_555 57.4 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-12-18 2 'Structure model' 1 1 2014-02-26 3 'Structure model' 1 2 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' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 3 'Structure model' '_software.classification' 2 3 'Structure model' '_software.contact_author' 3 3 'Structure model' '_software.contact_author_email' 4 3 'Structure model' '_software.date' 5 3 'Structure model' '_software.language' 6 3 'Structure model' '_software.location' 7 3 'Structure model' '_software.name' 8 3 'Structure model' '_software.type' 9 3 'Structure model' '_software.version' # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 DENZO . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data reduction' http://www.hkl-xray.com/ ? ? 2 SCALEPACK . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 3 PHENIX 1.8.2_1309 ? package 'Paul D. Adams' PDAdams@lbl.gov refinement http://www.phenix-online.org/ C++ ? 4 PDB_EXTRACT 3.11 'April 22, 2011' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 1027 ? ? O A HOH 1057 ? ? 1.87 2 1 O A HOH 946 ? ? O A HOH 948 ? ? 1.88 3 1 O A HOH 1044 ? ? O A HOH 1060 ? ? 1.89 4 1 O A HOH 974 ? ? O A HOH 1008 ? ? 1.91 5 1 O A HOH 916 ? ? O A HOH 1045 ? ? 1.93 6 1 OD2 A ASP 104 ? ? O A HOH 809 ? ? 1.94 7 1 O A HOH 941 ? ? O A HOH 998 ? ? 1.94 8 1 O A HOH 958 ? ? O A HOH 975 ? ? 1.95 9 1 O A HOH 937 ? ? O A HOH 1034 ? ? 1.96 10 1 O2P A AMP 505 ? ? O A HOH 874 ? ? 1.96 11 1 O A HOH 915 ? ? O A HOH 953 ? ? 1.98 12 1 O A HOH 985 ? ? O A HOH 986 ? ? 2.00 13 1 O A HOH 677 ? ? O A HOH 1032 ? ? 2.00 14 1 OE2 A GLU 328 ? ? O A HOH 859 ? ? 2.00 15 1 O A HOH 822 ? ? O A HOH 875 ? ? 2.02 16 1 O A HOH 963 ? ? O A HOH 967 ? ? 2.05 17 1 O A HOH 850 ? ? O A HOH 1020 ? ? 2.07 18 1 O A HOH 979 ? ? O A HOH 1003 ? ? 2.08 19 1 O A HOH 1059 ? ? O A HOH 1064 ? ? 2.09 20 1 O A HOH 922 ? ? O A HOH 1044 ? ? 2.09 21 1 O A HOH 882 ? ? O A HOH 1050 ? ? 2.09 22 1 OD1 A ASP 145 ? ? O A HOH 933 ? ? 2.10 23 1 OD2 A ASP 104 ? ? O A HOH 1042 ? ? 2.10 24 1 O A HOH 693 ? ? O A HOH 969 ? ? 2.13 25 1 O A HOH 835 ? ? O A HOH 1051 ? ? 2.13 26 1 O A HOH 720 ? ? O A HOH 989 ? ? 2.15 27 1 NZ A LYS 274 ? ? O A HOH 959 ? ? 2.15 28 1 O A HOH 917 ? ? O A HOH 1017 ? ? 2.16 29 1 "O2'" A AMP 505 ? ? O A HOH 983 ? ? 2.17 30 1 O A HOH 888 ? ? O A HOH 939 ? ? 2.17 31 1 O A HOH 945 ? ? O A HOH 946 ? ? 2.18 32 1 O A HOH 950 ? ? O A HOH 956 ? ? 2.19 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 930 ? ? 1_555 O A HOH 932 ? ? 4_445 1.73 2 1 O A HOH 919 ? ? 1_555 O A HOH 920 ? ? 2_556 1.93 # 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 MET A 135 ? ? 87.78 5.41 2 1 ASN A 173 ? ? -93.45 -133.32 3 1 SER A 174 ? ? 68.17 127.81 4 1 LEU A 265 ? ? -102.68 -67.88 5 1 ILE A 275 ? ? -124.10 -169.58 6 1 ASN A 276 ? ? -39.42 117.24 7 1 TYR A 305 ? ? -143.24 52.83 8 1 GLN A 306 ? ? -133.00 -43.91 9 1 ASP A 339 ? ? -29.29 121.91 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LEU 24 ? CG ? A LEU 9 CG 2 1 Y 1 A LEU 24 ? CD1 ? A LEU 9 CD1 3 1 Y 1 A LEU 24 ? CD2 ? A LEU 9 CD2 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A PHE 16 ? A PHE 1 2 1 Y 1 A ARG 17 ? A ARG 2 3 1 Y 1 A SER 18 ? A SER 3 4 1 Y 1 A ASP 19 ? A ASP 4 5 1 Y 1 A SER 20 ? A SER 5 6 1 Y 1 A SER 21 ? A SER 6 7 1 Y 1 A SER 22 ? A SER 7 8 1 Y 1 A SER 23 ? A SER 8 9 1 Y 1 A ASN 403 ? A ASN 388 10 1 Y 1 A LEU 404 ? A LEU 389 11 1 Y 1 A PRO 405 ? A PRO 390 12 1 Y 1 A GLU 406 ? A GLU 391 13 1 Y 1 A ALA 407 ? A ALA 392 14 1 Y 1 A LEU 408 ? A LEU 393 15 1 Y 1 A ILE 409 ? A ILE 394 16 1 Y 1 A ASN 410 ? A ASN 395 17 1 Y 1 A GLU 411 ? A GLU 396 18 1 Y 1 A ASN 412 ? A ASN 397 19 1 Y 1 A LEU 413 ? A LEU 398 20 1 Y 1 A TYR 414 ? A TYR 399 21 1 Y 1 A PHE 415 ? A PHE 400 22 1 Y 1 A GLN 416 ? A GLN 401 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'ADENOSINE MONOPHOSPHATE' AMP 4 'ZINC ION' ZN 5 water HOH #