data_6429 #Corrected using PDB structure: 1MZNC # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 47 C CA 56.75 62.66 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 47 C CB 34.20 27.75 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #101 G C 181.01 173.23 #154 F C 181.31 175.15 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted #105 A H 10.91 8.44 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A 0.15 0.70 0.01 -0.47 0.03 # #bmr6429.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6429.str file): #HA CA CB CO N HN #N/A +0.42 +0.42 +0.01 -0.47 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.11 +/-0.13 +/-0.10 +/-0.29 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.966 0.994 0.750 0.820 0.641 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.758 0.849 0.667 1.872 0.323 # #*Note: CA and CB offsets differences were greater than 0.5ppm, # Please check for possible misassignment or deuterate effects ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N and 13C chemical shift assignments for human retinoid X receptor ligand-binding domain with and without 9-cis retinoic acid ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jianyun . . 2 Cistola David P. . 3 Ellen Li . . stop_ _BMRB_accession_number 6429 _BMRB_flat_file_name bmr6429.str _Entry_type new _Submission_date 2004-12-10 _Accession_date 2004-12-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 192 '15N chemical shifts' 188 '13C chemical shifts' 608 stop_ loop_ _Related_BMRB_accession_number _Relationship 6449 "complex with 9-cis retinoic acid" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation_1 _Saveframe_category entry_citation _Citation_title ; Analysis of ligand binding and protein dynamics of human retinoid x receptor alpha ligand-binding domain by nuclear magnetic resonance. ; _Citation_status published _Citation_type journal _PubMed_ID 16460010 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jianyun . . 2 Cistola David P. . 3 Li Ellen . . stop_ _Journal_abbreviation "Biochemistry" _Journal_volume 45 _Journal_issue 6 _Page_first 1629 _Page_last 1639 _Year 2006 loop_ _Keyword NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly_RXRalpha_LBD_1 _Saveframe_category molecular_system _Mol_system_name "RXRalpha ligand-binding domain dimer" _Abbreviation_common "RXRalpha ligand-binding domain dimer" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "retinoid X receptor alpha ligand-binding domain, chain 1" $RXRalpha_LBD_1 "retinoid X receptor alpha ligand-binding domain, chain 2" $RXRalpha_LBD_1 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_RXRalpha_LBD_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "RXRalpha ligand-binding domain" _Name_variant "RXRA LBD" _Abbreviation_common "RXRA LBD" _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 240 _Mol_residue_sequence ; TSSANEDMPVERILEAELAV EPKTETYVEANMGLNPSSPN DPVTNICQAADKQLFTLVEW AKRIPHFSELPLDDQVILLR AGWNELLIASFSHRSIAVKD GILLATGLHVHRNSAHSAGV GAIFDRVLTELVSKMRDMQM DKTELGCLRAIVLFNPDSKG LSNPAEVEALREKVYASLEA YCKHKYPEQPGRFAKLLLRL PALRSIGLKCLEHLFFFKLI GDTPIDTFLMEMLEAPHQMT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 223 THR 2 224 SER 3 225 SER 4 226 ALA 5 227 ASN 6 228 GLU 7 229 ASP 8 230 MET 9 231 PRO 10 232 VAL 11 233 GLU 12 234 ARG 13 235 ILE 14 236 LEU 15 237 GLU 16 238 ALA 17 239 GLU 18 240 LEU 19 241 ALA 20 242 VAL 21 243 GLU 22 244 PRO 23 245 LYS 24 246 THR 25 247 GLU 26 248 THR 27 249 TYR 28 250 VAL 29 251 GLU 30 252 ALA 31 253 ASN 32 254 MET 33 255 GLY 34 256 LEU 35 257 ASN 36 258 PRO 37 259 SER 38 260 SER 39 261 PRO 40 262 ASN 41 263 ASP 42 264 PRO 43 265 VAL 44 266 THR 45 267 ASN 46 268 ILE 47 269 CYS 48 270 GLN 49 271 ALA 50 272 ALA 51 273 ASP 52 274 LYS 53 275 GLN 54 276 LEU 55 277 PHE 56 278 THR 57 279 LEU 58 280 VAL 59 281 GLU 60 282 TRP 61 283 ALA 62 284 LYS 63 285 ARG 64 286 ILE 65 287 PRO 66 288 HIS 67 289 PHE 68 290 SER 69 291 GLU 70 292 LEU 71 293 PRO 72 294 LEU 73 295 ASP 74 296 ASP 75 297 GLN 76 298 VAL 77 299 ILE 78 300 LEU 79 301 LEU 80 302 ARG 81 303 ALA 82 304 GLY 83 305 TRP 84 306 ASN 85 307 GLU 86 308 LEU 87 309 LEU 88 310 ILE 89 311 ALA 90 312 SER 91 313 PHE 92 314 SER 93 315 HIS 94 316 ARG 95 317 SER 96 318 ILE 97 319 ALA 98 320 VAL 99 321 LYS 100 322 ASP 101 323 GLY 102 324 ILE 103 325 LEU 104 326 LEU 105 327 ALA 106 328 THR 107 329 GLY 108 330 LEU 109 331 HIS 110 332 VAL 111 333 HIS 112 334 ARG 113 335 ASN 114 336 SER 115 337 ALA 116 338 HIS 117 339 SER 118 340 ALA 119 341 GLY 120 342 VAL 121 343 GLY 122 344 ALA 123 345 ILE 124 346 PHE 125 347 ASP 126 348 ARG 127 349 VAL 128 350 LEU 129 351 THR 130 352 GLU 131 353 LEU 132 354 VAL 133 355 SER 134 356 LYS 135 357 MET 136 358 ARG 137 359 ASP 138 360 MET 139 361 GLN 140 362 MET 141 363 ASP 142 364 LYS 143 365 THR 144 366 GLU 145 367 LEU 146 368 GLY 147 369 CYS 148 370 LEU 149 371 ARG 150 372 ALA 151 373 ILE 152 374 VAL 153 375 LEU 154 376 PHE 155 377 ASN 156 378 PRO 157 379 ASP 158 380 SER 159 381 LYS 160 382 GLY 161 383 LEU 162 384 SER 163 385 ASN 164 386 PRO 165 387 ALA 166 388 GLU 167 389 VAL 168 390 GLU 169 391 ALA 170 392 LEU 171 393 ARG 172 394 GLU 173 395 LYS 174 396 VAL 175 397 TYR 176 398 ALA 177 399 SER 178 400 LEU 179 401 GLU 180 402 ALA 181 403 TYR 182 404 CYS 183 405 LYS 184 406 HIS 185 407 LYS 186 408 TYR 187 409 PRO 188 410 GLU 189 411 GLN 190 412 PRO 191 413 GLY 192 414 ARG 193 415 PHE 194 416 ALA 195 417 LYS 196 418 LEU 197 419 LEU 198 420 LEU 199 421 ARG 200 422 LEU 201 423 PRO 202 424 ALA 203 425 LEU 204 426 ARG 205 427 SER 206 428 ILE 207 429 GLY 208 430 LEU 209 431 LYS 210 432 CYS 211 433 LEU 212 434 GLU 213 435 HIS 214 436 LEU 215 437 PHE 216 438 PHE 217 439 PHE 218 440 LYS 219 441 LEU 220 442 ILE 221 443 GLY 222 444 ASP 223 445 THR 224 446 PRO 225 447 ILE 226 448 ASP 227 449 THR 228 450 PHE 229 451 LEU 230 452 MET 231 453 GLU 232 454 MET 233 455 LEU 234 456 GLU 235 457 ALA 236 458 PRO 237 459 HIS 238 460 GLN 239 461 MET 240 462 THR stop_ _Sequence_homology_query_date 2006-06-22 _Sequence_homology_query_revised_last_date 2006-05-11 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 6449 "RXRalpha ligand-binding domain" 100.00 240 100 100 10e-135 PDB 1XLS "A Chain A, Crystal Structure Of The MouseCarRXR LBD HETERODIMER Bound To Tcpobop And 9cra And ATif2 Peptide Containg The Third Lxxll Motifs" 103.45 232 100 100 1e-129 PDB 1DKF "A Chain A, Crystal Structure Of A HeterodimericComplex Of Rar And Rxr Ligand-Binding Domains" 103.00 233 99 100 10e-129 PDB 1XV9 "A Chain A, Crystal Structure Of CarRXRHETERODIMER BOUND WITH SRC1 Peptide, Fatty Acid, And5b-Pregnane-3,20-Dione" 101.69 236 100 100 1e-132 PDB 1XVP "A Chain A, Crystal Structure Of CarRXRHETERODIMER BOUND WITH SRC1 Peptide, Fatty Acid AndCitco" 101.69 236 100 100 1e-132 PDB 1FM6 "A Chain A, The 2.1 Angstrom Resolution CrystalStructure Of The Heterodimer Of The Human Rxralpha AndPpargamma Ligand Binding Domains Respectively Bound With9-Cis Retinoic Acid And Rosiglitazone And Co-ActivatorPeptides" 100.84 238 100 100 1e-133 PDB 1FM9 "A Chain A, The 2.1 Angstrom Resolution CrystalStructure Of The Heterodimer Of The Human Rxralpha AndPpargamma Ligand Binding Domains Respectively Bound With9-Cis Retinoic Acid And Gi262570 And Co-ActivatorPeptides." 100.84 238 100 100 1e-133 PDB 1G1U "A Chain A, The 2.5 Angstrom Resolution CrystalStructure Of The Rxralpha Ligand Binding Domain InTetramer In The Absence Of Ligand" 100.84 238 100 100 1e-133 PDB 1G5Y "A Chain A, The 2.0 Angstrom Resolution CrystalStructure Of The Rxralpha Ligand Binding Domain TetramerIn The Presence Of A Non-Activating Retinoic AcidIsomer." 100.84 238 100 100 1e-133 PDB 1K74 "A Chain A, The 2.3 Angstrom Resolution CrystalStructure Of The Heterodimer Of The Human Ppargamma AndRxralpha Ligand Binding Domains Respectively Bound WithGw409544 And 9-Cis Retinoic Acid And Co-ActivatorPeptides." 100.84 238 100 100 1e-133 PDB 2ACL "A Chain A, Liver X-Receptor Alpha LigandBinding Domain With Sb313987" 100.84 238 100 100 1e-133 PDB 1XDK "A Chain A, Crystal Structure Of TheRarbetaRXRALPHA LIGAND BINDING Domain Heterodimer InComplex With 9-Cis Retinoic Acid And A Fragment Of TheTrap220 Coactivator" 100.84 238 99 100 1e-132 PDB 1FBY "A Chain A, Crystal Structure Of The Human RxrAlpha Ligand Binding Domain Bound To 9-Cis Retinoic Acid" 100.42 239 100 100 1e-133 PDB 1MV9 "A Chain A, Crystal Structure Of The Human RxrAlpha Ligand Binding Domain Bound To The Eicosanoid Dha(Docosa Hexaenoic Acid) And A Coactivator Peptide" 100.00 240 100 100 10e-135 PDB 1MVC "A Chain A, Crystal Structure Of The Human RxrAlpha Ligand Binding Domain Bound To The SyntheticAgonist Compound Bms 649 And A Coactivator Peptide" 100.00 240 100 100 10e-135 PDB 1MZN "A Chain A, Crystal Structure At 1.9 AngstroemsResolution Of The Homodimer Of Human Rxr Alpha LigandBinding Domain Bound To The Synthetic Agonist CompoundBms 649 And A Coactivator Peptide" 100.00 240 100 100 10e-135 PDB 1RDT "A Chain A, Crystal Structure Of A New RexinoidBound To The Rxralpha Ligand Binding Doamin In TheRxralphaPPARGAMMA HETERODIMER" 99.17 242 100 100 1e-133 PDB 1LBD "Ligand-Binding Domain Of The Human NuclearReceptor Rxr-Alpha" 85.11 282 100 100 10e-135 DBJ BAE73032.1 "hypothetical protein [Macacafascicularis]" 51.95 462 99 99 1e-132 DBJ BAE26004.1 "unnamed protein product [Mus musculus]" 51.39 467 99 100 1e-133 EMBL CAA36982.1 "unnamed protein product [Homo sapiens]" 51.95 462 100 100 10e-135 EMBL CAH70571.1 "retinoid X receptor, alpha [Homosapiens]" 51.95 462 100 100 10e-135 EMBL CAA46962.1 "retinoid X receptor-alpha [Mus musculus]" 51.39 467 99 100 1e-133 GenBank AAH96246.1 "Retinoid X receptor, alpha [Homosapiens]" 51.95 462 100 100 10e-135 GenBank AAH96247.1 "Retinoid X receptor, alpha [Homosapiens]" 51.95 462 100 100 10e-135 GenBank AAH96248.1 "Retinoid X receptor, alpha [Homosapiens]" 51.95 462 100 100 10e-135 GenBank AAI10999.1 "Retinoid X receptor, alpha [Homosapiens]" 51.95 462 100 100 10e-135 GenBank AAH63827.1 "RXRA protein [Homo sapiens]" 46.51 516 100 100 10e-135 PRF 1609194A "retinoic acid receptor RXRalpha" 51.95 462 100 100 10e-135 REF XP_981799.1 "PREDICTED: similar to Retinoic acidreceptor RXR-alpha (Retinoid X receptor alpha) [Musmusculus]" 54.67 439 99 100 1e-133 REF NP_002948.1 "retinoid X receptor, alpha [Homosapiens]" 51.95 462 100 100 10e-135 REF NP_035435.1 "retinoid X receptor alpha [Musmusculus]" 51.39 467 99 100 1e-133 REF NP_036937.1 "retinoid X receptor alpha [Rattusnorvegicus]" 51.39 467 99 100 1e-133 REF XP_995211.1 "PREDICTED: similar to Retinoic acidreceptor RXR-alpha (Retinoid X receptor alpha) [Musmusculus]" 51.17 469 99 100 1e-133 SWISS-PROT P19793 "RXRA_HUMAN Retinoic acid receptor RXR-alpha(Retinoid X receptor alpha)" 51.95 462 100 100 10e-135 SWISS-PROT P28700 "RXRA_MOUSE Retinoic acid receptor RXR-alpha(Retinoid X receptor alpha)" 51.39 467 99 100 1e-133 SWISS-PROT Q05343 "RXRA_RAT Retinoic acid receptor RXR-alpha(Retinoid X receptor alpha)" 51.39 467 99 100 1e-133 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RXRalpha_LBD_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $RXRalpha_LBD_1 "recombinant technology" . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RXRalpha_LBD_1 1.0 mM "[U-2H; U-13C; U-15N]" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 700 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 4D TROSY-HNCOCA 4D TROSY-HNCOi-1CAi 4D TROSY-HNCACO 4D 15N,15N-NOESY 3D TROSY-HNCO 3D TROSY-HN(CA)CO 3D TROSY-HNCACB 3D TROSY HN(CO)CACB ; save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis DSS H 1 "methyl protons" ppm 0.0 direct external . . 1.0 DSS C 13 "methyl carbon" ppm 0.0 indirect external . . 1.0 DSS N 15 nitrogen ppm 0.0 indirect external . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. Tyr HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons or Trp HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_apo_chem_shift_list _Saveframe_category assigned_chemical_shifts _Details ; 9-cis retinoic acid-free RXRalpha ligand-binding domain. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "retinoid X receptor alpha ligand-binding domain, chain 1" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 SER CA C 58.72 0.2 1 2 3 SER CB C 63.42 0.2 1 3 3 SER C C 175.01 0.1 1 4 4 ALA H H 8.31 0.01 1 5 4 ALA N N 125.63 0.1 1 6 4 ALA CA C 53.82 0.2 1 7 4 ALA CB C 18.42 0.2 1 8 4 ALA C C 178.71 0.1 1 9 5 ASN H H 8.29 0.01 1 10 5 ASN N N 116.53 0.1 1 11 5 ASN CA C 54.62 0.2 1 12 5 ASN CB C 39.12 0.2 1 13 5 ASN C C 176.21 0.1 1 14 6 GLU H H 7.89 0.01 1 15 6 GLU N N 118.03 0.1 1 16 6 GLU CA C 57.72 0.2 1 17 6 GLU CB C 29.52 0.2 1 19 7 ASP H H 7.87 0.01 1 21 7 ASP CA C 55.22 0.2 1 22 7 ASP CB C 41.42 0.2 1 23 7 ASP C C 176.01 0.1 1 24 8 MET H H 7.91 0.01 1 25 8 MET N N 118.03 0.1 1 26 8 MET CA C 51.82 0.2 1 27 8 MET CB C 30.72 0.2 1 28 9 PRO CA C 62.52 0.2 1 29 9 PRO CB C 31.82 0.2 1 30 9 PRO C C 180.51 0.1 1 31 10 VAL H H 9.19 0.01 1 32 10 VAL N N 122.43 0.1 1 33 10 VAL CA C 65.12 0.2 1 34 10 VAL CB C 30.32 0.2 1 35 10 VAL C C 178.31 0.1 1 36 11 GLU H H 9.79 0.01 1 37 11 GLU N N 121.03 0.1 1 38 11 GLU CA C 60.22 0.2 1 39 11 GLU CB C 32.92 0.2 1 40 11 GLU C C 180.21 0.1 1 41 12 ARG H H 7.14 0.01 1 42 12 ARG N N 116.43 0.1 1 43 12 ARG CA C 57.52 0.2 1 44 12 ARG CB C 30.12 0.2 1 45 12 ARG C C 179.11 0.1 1 46 13 ILE H H 7.10 0.01 1 47 13 ILE N N 122.43 0.1 1 48 13 ILE CA C 65.62 0.2 1 49 13 ILE CB C 37.02 0.2 1 50 13 ILE C C 177.51 0.1 1 51 14 LEU H H 8.33 0.01 1 52 14 LEU N N 120.63 0.1 1 53 14 LEU CA C 58.22 0.2 1 54 14 LEU CB C 39.52 0.2 1 55 14 LEU C C 178.41 0.1 1 56 15 GLU H H 7.64 0.01 1 57 15 GLU N N 116.73 0.1 1 58 15 GLU CA C 59.72 0.2 1 59 15 GLU CB C 29.12 0.2 1 60 15 GLU C C 179.21 0.1 1 61 16 ALA H H 7.56 0.01 1 62 16 ALA N N 122.43 0.1 1 63 16 ALA CA C 56.02 0.2 1 64 16 ALA CB C 17.92 0.2 1 65 16 ALA C C 179.11 0.1 1 66 17 GLU H H 7.77 0.01 1 67 17 GLU N N 116.33 0.1 1 68 17 GLU CA C 59.12 0.2 1 69 17 GLU CB C 30.32 0.2 1 70 17 GLU C C 180.51 0.1 1 71 18 LEU H H 8.52 0.01 1 72 18 LEU N N 117.23 0.1 1 73 18 LEU CA C 57.12 0.2 1 74 18 LEU CB C 40.52 0.2 1 75 18 LEU C C 179.91 0.1 1 76 19 ALA H H 7.97 0.01 1 77 19 ALA N N 120.63 0.1 1 78 19 ALA CA C 54.52 0.2 1 79 19 ALA CB C 17.82 0.2 1 80 19 ALA C C 179.61 0.1 1 81 20 VAL H H 6.97 0.01 1 83 20 VAL CA C 60.52 0.2 1 84 20 VAL CB C 31.52 0.2 1 85 20 VAL C C 176.01 0.1 1 86 21 GLU H H 7.09 0.01 1 87 21 GLU N N 125.73 0.1 1 88 21 GLU CA C 54.72 0.2 1 89 21 GLU CB C 29.62 0.2 1 90 21 GLU C C 174.71 0.1 1 91 22 PRO CA C 62.92 0.2 1 92 22 PRO CB C 31.82 0.2 1 93 22 PRO C C 176.81 0.1 1 94 23 LYS H H 8.51 0.01 1 95 23 LYS N N 122.63 0.1 1 96 23 LYS CA C 55.62 0.2 1 97 23 LYS CB C 31.82 0.2 1 98 23 LYS C C 177.01 0.1 1 99 24 THR H H 8.05 0.01 1 100 24 THR N N 116.83 0.1 1 101 24 THR CA C 62.32 0.2 1 102 24 THR CB C 69.62 0.2 1 103 24 THR C C 174.81 0.1 1 104 25 GLU H H 8.63 0.01 1 105 25 GLU N N 123.73 0.1 1 106 25 GLU CA C 57.12 0.2 1 107 25 GLU CB C 29.82 0.2 1 108 25 GLU C C 176.61 0.1 1 109 26 THR H H 7.91 0.01 1 110 26 THR N N 114.53 0.1 1 111 26 THR CA C 62.12 0.2 1 112 26 THR CB C 69.72 0.2 1 113 26 THR C C 174.11 0.1 1 114 27 TYR H H 8.11 0.01 1 115 27 TYR N N 123.43 0.1 1 116 27 TYR CA C 57.92 0.2 1 117 27 TYR CB C 38.52 0.2 1 118 27 TYR C C 175.81 0.1 1 119 28 VAL H H 7.91 0.01 1 120 28 VAL N N 122.03 0.1 1 121 28 VAL CA C 62.02 0.2 1 122 28 VAL CB C 32.82 0.2 1 123 28 VAL C C 176.01 0.1 1 124 29 GLU H H 8.32 0.01 1 125 29 GLU N N 124.13 0.1 1 126 29 GLU CA C 57.02 0.2 1 127 29 GLU CB C 29.82 0.2 1 128 29 GLU C C 176.91 0.1 1 129 30 ALA H H 8.24 0.01 1 130 30 ALA N N 124.43 0.1 1 131 30 ALA CA C 53.22 0.2 1 132 30 ALA CB C 18.82 0.2 1 133 30 ALA C C 177.81 0.1 1 134 31 ASN H H 8.27 0.01 1 135 31 ASN N N 116.93 0.1 1 136 31 ASN CA C 53.32 0.2 1 138 31 ASN C C 175.51 0.1 1 139 32 MET H H 8.16 0.01 1 140 32 MET N N 120.23 0.1 1 141 32 MET CA C 56.12 0.2 1 142 32 MET CB C 31.92 0.2 1 143 32 MET C C 176.91 0.1 1 144 33 GLY H H 8.25 0.01 1 145 33 GLY N N 109.03 0.1 1 146 33 GLY CA C 45.42 0.2 1 147 33 GLY C C 174.11 0.1 1 148 34 LEU H H 7.88 0.01 1 150 34 LEU CA C 55.22 0.2 1 151 34 LEU CB C 41.82 0.2 1 152 34 LEU C C 177.01 0.1 1 153 35 ASN H H 8.37 0.01 1 154 35 ASN N N 119.83 0.1 1 155 35 ASN CA C 51.42 0.2 1 156 35 ASN CB C 38.82 0.2 1 157 35 ASN C C 173.51 0.1 1 158 36 PRO CA C 63.62 0.2 1 159 36 PRO CB C 31.82 0.2 1 160 36 PRO C C 177.31 0.1 1 161 37 SER H H 8.23 0.01 1 166 38 SER H H 8.00 0.01 1 168 38 SER CA C 56.22 0.2 1 169 38 SER CB C 63.42 0.2 1 170 38 SER C C 172.91 0.1 1 171 40 ASN CA C 52.92 0.2 1 172 40 ASN CB C 39.02 0.2 1 173 40 ASN C C 174.41 0.1 1 174 41 ASP H H 8.00 0.01 1 175 41 ASP N N 120.83 0.1 1 176 41 ASP CA C 52.32 0.2 1 178 41 ASP C C 173.71 0.1 1 179 42 PRO CA C 65.52 0.2 1 180 42 PRO CB C 31.82 0.2 1 181 42 PRO C C 178.41 0.1 1 182 43 VAL H H 8.09 0.01 1 183 43 VAL N N 117.93 0.1 1 184 43 VAL CA C 67.82 0.2 1 185 43 VAL C C 177.41 0.1 1 186 44 THR H H 7.53 0.01 1 187 44 THR N N 117.43 0.1 1 188 44 THR CA C 66.72 0.2 1 189 44 THR CB C 67.62 0.2 1 190 44 THR C C 177.21 0.1 1 191 45 ASN H H 7.70 0.01 1 192 45 ASN N N 118.53 0.1 1 193 45 ASN CA C 56.62 0.2 1 194 45 ASN CB C 37.62 0.2 1 195 45 ASN C C 178.51 0.1 1 196 46 ILE H H 8.61 0.01 1 197 46 ILE N N 123.53 0.1 1 198 46 ILE CA C 66.32 0.2 1 199 46 ILE CB C 37.42 0.2 1 200 46 ILE C C 177.21 0.1 1 201 47 CYS H H 8.58 0.01 1 202 47 CYS N N 117.83 0.1 1 203 47 CYS CA C 57.02 0.2 1 204 47 CYS CB C 33.92 0.2 1 205 47 CYS C C 176.91 0.1 1 206 48 GLN H H 8.24 0.01 1 207 48 GLN N N 120.43 0.1 1 208 48 GLN CA C 59.12 0.2 1 209 48 GLN CB C 27.92 0.2 1 210 48 GLN C C 179.41 0.1 1 211 49 ALA H H 7.48 0.01 1 212 49 ALA N N 123.43 0.1 1 213 49 ALA CA C 55.22 0.2 1 214 49 ALA CB C 18.92 0.2 1 215 49 ALA C C 178.31 0.1 1 216 50 ALA H H 8.42 0.01 1 217 50 ALA N N 121.23 0.1 1 218 50 ALA CA C 55.82 0.2 1 219 50 ALA CB C 19.02 0.2 1 220 50 ALA C C 179.21 0.1 1 221 51 ASP H H 8.17 0.01 1 222 51 ASP N N 116.73 0.1 1 223 51 ASP CA C 57.62 0.2 1 224 51 ASP CB C 40.52 0.2 1 225 51 ASP C C 178.81 0.1 1 226 52 LYS H H 7.33 0.01 1 227 52 LYS N N 118.93 0.1 1 228 52 LYS CA C 59.42 0.2 1 229 52 LYS CB C 32.12 0.2 1 230 52 LYS C C 179.41 0.1 1 231 53 GLN H H 7.98 0.01 1 232 53 GLN N N 115.93 0.1 1 233 53 GLN CA C 56.32 0.2 1 234 53 GLN CB C 30.62 0.2 1 235 53 GLN C C 179.71 0.1 1 236 54 LEU H H 8.94 0.01 1 237 54 LEU N N 125.43 0.1 1 241 55 PHE H H 7.42 0.01 1 243 55 PHE CA C 61.32 0.2 1 244 55 PHE CB C 38.92 0.2 1 245 55 PHE C C 177.91 0.1 1 246 56 THR H H 7.33 0.01 1 247 56 THR N N 107.53 0.1 1 248 57 LEU CA C 58.22 0.2 1 249 57 LEU CB C 41.82 0.2 1 250 57 LEU C C 178.61 0.1 1 251 58 VAL H H 7.96 0.01 1 252 58 VAL N N 117.03 0.1 1 253 58 VAL CA C 66.72 0.2 1 254 58 VAL CB C 30.82 0.2 1 255 58 VAL C C 176.81 0.1 1 256 59 GLU H H 7.32 0.01 1 257 59 GLU N N 118.43 0.1 1 258 59 GLU CA C 58.72 0.2 1 259 59 GLU CB C 28.72 0.2 1 260 59 GLU C C 178.71 0.1 1 261 60 TRP H H 8.01 0.01 1 262 60 TRP N N 119.03 0.1 1 263 60 TRP CA C 62.12 0.2 1 264 60 TRP CB C 27.92 0.2 1 265 60 TRP C C 176.61 0.1 1 266 61 ALA H H 8.12 0.01 1 267 61 ALA N N 120.23 0.1 1 268 61 ALA CA C 54.72 0.2 1 269 61 ALA CB C 17.42 0.2 1 270 61 ALA C C 179.21 0.1 1 271 62 LYS H H 7.79 0.01 1 272 62 LYS N N 111.33 0.1 1 273 62 LYS CA C 59.12 0.2 1 274 62 LYS CB C 32.02 0.2 1 275 62 LYS C C 178.81 0.1 1 276 63 ARG H H 7.28 0.01 1 278 63 ARG CA C 56.22 0.2 1 279 63 ARG CB C 30.32 0.2 1 280 63 ARG C C 176.51 0.1 1 281 64 ILE H H 7.38 0.01 1 282 64 ILE N N 125.93 0.1 1 283 64 ILE CA C 55.62 0.2 1 284 64 ILE CB C 33.82 0.2 1 285 64 ILE C C 174.91 0.1 1 286 65 PRO CA C 64.72 0.2 1 287 65 PRO CB C 31.22 0.2 1 288 65 PRO C C 174.71 0.1 1 289 66 HIS H H 7.95 0.01 1 290 66 HIS N N 110.63 0.1 1 291 66 HIS CA C 58.82 0.2 1 292 66 HIS CB C 27.82 0.2 1 293 66 HIS C C 176.21 0.1 1 294 67 PHE H H 8.03 0.01 1 295 67 PHE N N 124.63 0.1 1 296 67 PHE CA C 63.42 0.2 1 297 67 PHE CB C 39.12 0.2 1 298 67 PHE C C 177.11 0.1 1 299 68 SER H H 9.05 0.01 1 300 68 SER N N 109.93 0.1 1 301 68 SER CA C 60.52 0.2 1 302 68 SER CB C 62.92 0.2 1 303 68 SER C C 174.31 0.1 1 304 69 GLU H H 7.18 0.01 1 306 69 GLU CA C 56.42 0.2 1 307 69 GLU CB C 29.52 0.2 1 308 69 GLU C C 178.11 0.1 1 309 70 LEU H H 7.22 0.01 1 310 70 LEU N N 121.53 0.1 1 311 70 LEU CA C 53.62 0.2 1 312 70 LEU CB C 40.22 0.2 1 313 70 LEU C C 174.91 0.1 1 314 71 PRO CA C 63.32 0.2 1 315 71 PRO CB C 31.62 0.2 1 316 71 PRO C C 178.11 0.1 1 317 72 LEU H H 8.70 0.01 1 318 72 LEU N N 128.13 0.1 1 319 72 LEU CA C 58.82 0.2 1 320 72 LEU CB C 41.22 0.2 1 321 72 LEU C C 178.51 0.1 1 322 73 ASP H H 8.59 0.01 1 323 73 ASP N N 113.93 0.1 1 324 73 ASP CA C 57.32 0.2 1 325 73 ASP CB C 40.32 0.2 1 326 73 ASP C C 179.11 0.1 1 327 74 ASP H H 7.01 0.01 1 328 74 ASP N N 118.03 0.1 1 329 74 ASP CA C 57.02 0.2 1 330 74 ASP CB C 40.22 0.2 1 331 74 ASP C C 177.51 0.1 1 332 75 GLN H H 7.76 0.01 1 333 75 GLN N N 120.23 0.1 1 334 75 GLN CA C 59.92 0.2 1 335 75 GLN CB C 29.12 0.2 1 336 75 GLN C C 178.71 0.1 1 337 76 VAL H H 7.68 0.01 1 338 76 VAL N N 115.93 0.1 1 339 76 VAL CA C 66.92 0.2 1 340 76 VAL CB C 31.32 0.2 1 341 76 VAL C C 178.01 0.1 1 342 77 ILE H H 7.52 0.01 1 343 77 ILE N N 120.23 0.1 1 344 77 ILE CA C 65.72 0.2 1 345 77 ILE CB C 38.02 0.2 1 346 77 ILE C C 179.11 0.1 1 347 78 LEU H H 8.49 0.01 1 348 78 LEU N N 118.43 0.1 1 349 78 LEU CA C 58.02 0.2 1 350 78 LEU CB C 39.72 0.2 1 351 78 LEU C C 181.61 0.1 1 352 79 LEU H H 7.99 0.01 1 353 79 LEU N N 120.03 0.1 1 354 79 LEU CA C 58.32 0.2 1 355 79 LEU CB C 41.42 0.2 1 356 79 LEU C C 178.81 0.1 1 357 80 ARG H H 8.94 0.01 1 358 80 ARG N N 119.83 0.1 1 359 80 ARG CA C 60.12 0.2 1 361 80 ARG C C 178.51 0.1 1 362 81 ALA H H 8.46 0.01 1 364 81 ALA CA C 54.12 0.2 1 365 81 ALA CB C 18.32 0.2 1 366 81 ALA C C 180.31 0.1 1 367 82 GLY H H 7.71 0.01 1 368 82 GLY N N 102.83 0.1 1 369 82 GLY CA C 46.12 0.2 1 370 82 GLY C C 176.01 0.1 1 371 83 TRP H H 8.06 0.01 1 372 83 TRP CA C 61.32 0.2 1 373 83 TRP CB C 27.12 0.2 1 374 83 TRP C C 175.11 0.1 1 375 84 ASN H H 7.15 0.01 1 376 84 ASN N N 116.93 0.1 1 377 84 ASN CA C 57.32 0.2 1 378 84 ASN CB C 34.82 0.2 1 379 84 ASN C C 176.11 0.1 1 380 85 GLU H H 6.93 0.01 1 381 85 GLU N N 120.63 0.1 1 382 85 GLU CA C 60.52 0.2 1 383 85 GLU CB C 30.62 0.2 1 384 85 GLU C C 178.51 0.1 1 385 86 LEU H H 8.32 0.01 1 386 86 LEU N N 117.43 0.1 1 387 86 LEU CA C 58.02 0.2 1 388 86 LEU CB C 40.52 0.2 1 389 86 LEU C C 180.71 0.1 1 390 87 LEU H H 8.14 0.01 1 391 87 LEU N N 118.63 0.1 1 392 87 LEU CA C 57.72 0.2 1 393 87 LEU CB C 41.22 0.2 1 394 87 LEU C C 180.21 0.1 1 395 88 ILE H H 7.92 0.01 1 396 88 ILE N N 120.03 0.1 1 397 88 ILE CA C 63.12 0.2 1 398 88 ILE CB C 37.62 0.2 1 399 88 ILE C C 179.01 0.1 1 400 89 ALA H H 8.13 0.01 1 401 89 ALA N N 122.63 0.1 1 402 89 ALA CA C 55.62 0.2 1 403 89 ALA CB C 16.12 0.2 1 404 89 ALA C C 177.91 0.1 1 405 90 SER H H 6.64 0.01 1 406 90 SER N N 108.83 0.1 1 407 90 SER CA C 62.82 0.2 1 408 90 SER CB C 63.42 0.2 1 409 90 SER C C 178.21 0.1 1 410 91 PHE H H 8.01 0.01 1 411 91 PHE N N 118.93 0.1 1 412 91 PHE CA C 59.92 0.2 1 413 91 PHE CB C 36.02 0.2 1 414 91 PHE C C 179.11 0.1 1 415 92 SER H H 7.58 0.01 1 416 92 SER N N 125.03 0.1 1 417 92 SER CA C 63.72 0.2 1 418 92 SER CB C 62.22 0.2 1 419 92 SER C C 174.31 0.1 1 420 93 HIS H H 7.34 0.01 1 421 93 HIS N N 121.33 0.1 1 422 93 HIS CA C 62.02 0.2 1 423 93 HIS CB C 32.52 0.2 1 424 93 HIS C C 178.71 0.1 1 425 94 ARG H H 7.63 0.01 1 426 94 ARG N N 118.93 0.1 1 427 94 ARG CA C 58.12 0.2 1 428 94 ARG CB C 30.92 0.2 1 429 94 ARG C C 178.11 0.1 1 430 95 SER H H 7.34 0.01 1 431 95 SER N N 110.53 0.1 1 432 95 SER CA C 60.22 0.2 1 433 95 SER CB C 63.02 0.2 1 434 95 SER C C 173.51 0.1 1 435 96 ILE H H 7.17 0.01 1 436 96 ILE N N 117.53 0.1 1 437 96 ILE CA C 65.22 0.2 1 438 96 ILE CB C 38.02 0.2 1 439 96 ILE C C 176.81 0.1 1 440 97 ALA H H 7.46 0.01 1 441 97 ALA N N 119.83 0.1 1 442 97 ALA CA C 52.72 0.2 1 443 97 ALA CB C 19.42 0.2 1 444 97 ALA C C 177.21 0.1 1 445 98 VAL H H 7.60 0.01 1 446 98 VAL N N 115.83 0.1 1 447 98 VAL CA C 60.22 0.2 1 448 98 VAL CB C 33.02 0.2 1 449 98 VAL C C 175.21 0.1 1 450 99 LYS H H 8.54 0.01 1 451 99 LYS N N 124.23 0.1 1 452 99 LYS CA C 55.82 0.2 1 454 99 LYS C C 176.71 0.1 1 455 100 ASP H H 8.86 0.01 1 456 100 ASP N N 121.93 0.1 1 457 100 ASP CA C 55.32 0.2 1 458 100 ASP CB C 40.02 0.2 1 459 100 ASP C C 174.21 0.1 1 460 101 GLY H H 7.50 0.01 1 461 101 GLY N N 102.73 0.1 1 462 101 GLY CA C 46.82 0.2 1 463 101 GLY C C 181.01 0.1 1 464 102 ILE H H 8.42 0.01 1 465 102 ILE N N 110.43 0.1 1 466 102 ILE CA C 58.32 0.2 1 467 102 ILE CB C 41.42 0.2 1 468 102 ILE C C 173.31 0.1 1 469 103 LEU H H 8.26 0.01 1 470 103 LEU N N 124.13 0.1 1 471 103 LEU CA C 53.22 0.2 1 472 103 LEU CB C 42.62 0.2 1 473 103 LEU C C 175.31 0.1 1 474 104 LEU H H 8.61 0.01 1 475 104 LEU N N 122.43 0.1 1 476 104 LEU CA C 53.62 0.2 1 477 104 LEU CB C 42.72 0.2 1 478 104 LEU C C 180.91 0.1 1 479 105 ALA H H 10.88 0.01 1 480 105 ALA N N 126.33 0.1 1 481 105 ALA CA C 54.42 0.2 1 483 105 ALA C C 177.41 0.1 1 484 106 THR H H 6.97 0.01 1 485 106 THR N N 101.63 0.1 1 486 106 THR CA C 60.62 0.2 1 487 106 THR CB C 69.02 0.2 1 488 106 THR C C 175.61 0.1 1 489 107 GLY H H 8.06 0.01 1 490 107 GLY N N 109.13 0.1 1 491 107 GLY CA C 45.12 0.2 1 492 107 GLY C C 172.91 0.1 1 493 108 LEU H H 6.32 0.01 1 494 108 LEU N N 119.13 0.1 1 495 108 LEU CA C 54.32 0.2 1 496 108 LEU CB C 43.42 0.2 1 497 108 LEU C C 175.01 0.1 1 498 109 HIS H H 8.42 0.01 1 499 109 HIS N N 121.33 0.1 1 500 109 HIS CA C 54.72 0.2 1 501 109 HIS CB C 32.22 0.2 1 502 109 HIS C C 175.71 0.1 1 503 110 VAL H H 8.56 0.01 1 504 110 VAL N N 124.13 0.1 1 505 110 VAL CA C 61.32 0.2 1 506 110 VAL CB C 33.02 0.2 1 507 110 VAL C C 174.41 0.1 1 508 111 HIS H H 8.81 0.01 1 513 112 ARG H H 8.50 0.01 1 515 112 ARG CA C 60.22 0.2 1 516 112 ARG CB C 30.32 0.2 1 517 112 ARG C C 177.91 0.1 1 518 114 SER CA C 60.52 0.2 1 519 114 SER CB C 62.02 0.2 1 520 114 SER C C 176.61 0.1 1 521 115 ALA H H 7.21 0.01 1 522 115 ALA N N 123.23 0.1 1 523 115 ALA CA C 55.02 0.2 1 524 115 ALA CB C 16.72 0.2 1 525 115 ALA C C 179.21 0.1 1 526 116 HIS H H 8.22 0.01 1 527 116 HIS N N 116.53 0.1 1 528 116 HIS CA C 60.62 0.2 1 529 116 HIS CB C 30.72 0.2 1 530 116 HIS C C 180.21 0.1 1 531 117 SER H H 8.05 0.01 1 532 117 SER N N 117.13 0.1 1 533 117 SER CA C 61.52 0.2 1 535 117 SER C C 174.71 0.1 1 536 118 ALA H H 7.33 0.01 1 537 118 ALA N N 120.83 0.1 1 538 118 ALA CA C 52.02 0.2 1 539 118 ALA CB C 19.62 0.2 1 540 118 ALA C C 177.51 0.1 1 541 119 GLY H H 7.50 0.01 1 542 119 GLY N N 104.53 0.1 1 543 119 GLY CA C 46.42 0.2 1 544 119 GLY C C 175.71 0.1 1 545 120 VAL H H 7.45 0.01 1 550 121 GLY H H 8.47 0.01 1 554 124 PHE CA C 62.52 0.2 1 555 124 PHE CB C 40.82 0.2 1 556 124 PHE C C 177.31 0.1 1 557 125 ASP H H 8.90 0.01 1 558 125 ASP N N 117.63 0.1 1 559 125 ASP CA C 57.52 0.2 1 560 125 ASP CB C 39.52 0.2 1 561 125 ASP C C 179.91 0.1 1 562 126 ARG H H 7.59 0.01 1 563 126 ARG N N 120.43 0.1 1 564 126 ARG CA C 60.72 0.2 1 565 126 ARG CB C 29.32 0.2 1 566 126 ARG C C 178.81 0.1 1 567 127 VAL H H 7.81 0.01 1 568 127 VAL N N 119.63 0.1 1 569 127 VAL CA C 67.02 0.2 1 570 127 VAL CB C 30.02 0.2 1 571 127 VAL C C 179.11 0.1 1 572 128 LEU H H 8.00 0.01 1 573 128 LEU N N 118.13 0.1 1 574 128 LEU CA C 58.22 0.2 1 575 128 LEU CB C 40.62 0.2 1 576 128 LEU C C 179.31 0.1 1 577 129 THR H H 8.57 0.01 1 578 129 THR N N 113.83 0.1 1 579 129 THR CA C 65.52 0.2 1 580 129 THR CB C 69.72 0.2 1 581 129 THR C C 176.01 0.1 1 582 130 GLU H H 8.76 0.01 1 583 130 GLU N N 118.33 0.1 1 584 130 GLU CA C 57.62 0.2 1 585 130 GLU CB C 33.02 0.2 1 586 130 GLU C C 176.61 0.1 1 587 131 LEU H H 6.94 0.01 1 588 131 LEU N N 112.63 0.1 1 589 131 LEU CA C 55.82 0.2 1 590 131 LEU CB C 42.02 0.2 1 591 131 LEU C C 176.31 0.1 1 592 132 VAL H H 8.34 0.01 1 593 132 VAL N N 119.43 0.1 1 594 132 VAL CA C 67.72 0.2 1 596 132 VAL C C 178.91 0.1 1 597 133 SER H H 8.66 0.01 1 598 133 SER N N 111.13 0.1 1 600 133 SER CB C 62.42 0.2 1 601 133 SER C C 176.01 0.1 1 602 134 LYS H H 6.07 0.01 1 604 134 LYS CA C 57.32 0.2 1 605 134 LYS C C 179.61 0.1 1 606 135 MET H H 8.39 0.01 1 607 135 MET N N 119.33 0.1 1 608 135 MET CB C 31.52 0.2 1 609 135 MET C C 177.61 0.1 1 610 136 ARG H H 8.45 0.01 1 611 136 ARG CA C 59.32 0.2 1 612 136 ARG CB C 29.52 0.2 1 613 136 ARG C C 180.11 0.1 1 614 137 ASP H H 8.53 0.01 1 616 137 ASP CA C 57.42 0.2 1 617 137 ASP CB C 40.32 0.2 1 618 137 ASP C C 177.91 0.1 1 619 138 MET H H 7.39 0.01 1 620 138 MET N N 113.23 0.1 1 621 138 MET CA C 55.42 0.2 1 622 138 MET CB C 33.82 0.2 1 623 138 MET C C 175.11 0.1 1 624 139 GLN H H 7.87 0.01 1 625 139 GLN CA C 56.32 0.2 1 626 139 GLN CB C 25.72 0.2 1 627 139 GLN C C 176.11 0.1 1 628 140 MET H H 7.90 0.01 1 629 140 MET N N 119.33 0.1 1 630 140 MET CA C 56.92 0.2 1 631 140 MET CB C 34.42 0.2 1 632 140 MET C C 177.21 0.1 1 633 141 ASP H H 10.56 0.01 1 634 141 ASP N N 136.13 0.1 1 635 141 ASP CA C 53.02 0.2 1 636 141 ASP CB C 41.82 0.2 1 637 141 ASP C C 176.41 0.1 1 638 142 LYS H H 8.39 0.01 1 639 142 LYS N N 115.43 0.1 1 640 142 LYS CA C 59.42 0.2 1 641 142 LYS CB C 32.12 0.2 1 642 142 LYS C C 179.11 0.1 1 643 143 THR H H 8.13 0.01 1 644 143 THR N N 120.03 0.1 1 645 143 THR CA C 67.82 0.2 1 646 143 THR CB C 71.02 0.2 1 647 143 THR C C 176.51 0.1 1 648 144 GLU H H 8.80 0.01 1 649 144 GLU N N 124.43 0.1 1 650 144 GLU CA C 60.12 0.2 1 652 144 GLU C C 178.71 0.1 1 653 145 LEU H H 8.05 0.01 1 654 145 LEU N N 118.13 0.1 1 655 145 LEU CA C 57.42 0.2 1 656 145 LEU CB C 39.72 0.2 1 657 145 LEU C C 178.91 0.1 1 658 146 GLY H H 8.09 0.01 1 659 146 GLY N N 106.43 0.1 1 660 146 GLY CA C 47.62 0.2 1 661 146 GLY C C 176.21 0.1 1 662 147 CYS H H 8.36 0.01 1 663 147 CYS N N 118.33 0.1 1 664 147 CYS CA C 64.32 0.2 1 665 147 CYS CB C 29.32 0.2 1 666 147 CYS C C 177.01 0.1 1 667 148 LEU H H 8.46 0.01 1 668 148 LEU N N 120.63 0.1 1 669 148 LEU CA C 58.62 0.2 1 670 148 LEU CB C 40.92 0.2 1 671 148 LEU C C 179.21 0.1 1 672 149 ARG H H 8.56 0.01 1 673 149 ARG N N 116.73 0.1 1 674 149 ARG CA C 61.52 0.2 1 675 149 ARG CB C 29.32 0.2 1 676 149 ARG C C 177.61 0.1 1 677 150 ALA H H 8.62 0.01 1 678 150 ALA N N 122.23 0.1 1 679 150 ALA CA C 55.32 0.2 1 681 150 ALA C C 178.41 0.1 1 682 151 ILE H H 8.27 0.01 1 683 151 ILE N N 119.63 0.1 1 684 151 ILE CA C 67.02 0.2 1 685 151 ILE CB C 37.72 0.2 1 686 151 ILE C C 178.51 0.1 1 687 152 VAL H H 8.72 0.01 1 688 152 VAL N N 109.13 0.1 1 689 152 VAL CA C 66.02 0.2 1 690 152 VAL C C 176.31 0.1 1 691 153 LEU H H 7.93 0.01 1 692 153 LEU N N 122.63 0.1 1 693 153 LEU CA C 58.12 0.2 1 694 153 LEU CB C 41.42 0.2 1 695 153 LEU C C 178.61 0.1 1 696 154 PHE H H 7.19 0.01 1 698 154 PHE CA C 57.32 0.2 1 699 154 PHE CB C 40.22 0.2 1 700 154 PHE C C 181.31 0.1 1 701 155 ASN H H 8.19 0.01 1 702 155 ASN N N 118.53 0.1 1 703 155 ASN CA C 56.12 0.2 1 704 155 ASN CB C 39.72 0.2 1 705 155 ASN C C 177.41 0.1 1 706 156 PRO CA C 63.42 0.2 1 707 156 PRO CB C 32.12 0.2 1 708 156 PRO C C 175.71 0.1 1 709 157 ASP H H 7.79 0.01 1 710 157 ASP N N 118.93 0.1 1 711 157 ASP CA C 54.72 0.2 1 712 157 ASP CB C 40.92 0.2 1 713 157 ASP C C 176.61 0.1 1 714 158 SER H H 6.96 0.01 1 715 158 SER N N 117.13 0.1 1 716 158 SER CA C 60.02 0.2 1 718 158 SER C C 174.01 0.1 1 719 159 LYS H H 8.62 0.01 1 720 159 LYS N N 127.93 0.1 1 721 159 LYS CA C 57.42 0.2 1 722 159 LYS CB C 31.62 0.2 1 723 159 LYS C C 177.71 0.1 1 724 160 GLY H H 8.78 0.01 1 725 160 GLY N N 110.83 0.1 1 726 160 GLY CA C 44.62 0.2 1 727 160 GLY C C 174.81 0.1 1 728 161 LEU H H 6.73 0.01 1 729 161 LEU N N 119.13 0.1 1 730 161 LEU CA C 55.02 0.2 1 731 161 LEU CB C 42.32 0.2 1 732 161 LEU C C 178.31 0.1 1 733 162 SER H H 10.89 0.01 1 735 162 SER CA C 61.12 0.2 1 736 162 SER CB C 62.62 0.2 1 737 162 SER C C 176.51 0.1 1 738 163 ASN H H 8.36 0.01 1 739 163 ASN N N 118.33 0.1 1 740 163 ASN CA C 51.12 0.2 1 741 163 ASN CB C 37.62 0.2 1 742 163 ASN C C 173.31 0.1 1 743 164 PRO CA C 65.62 0.2 1 744 164 PRO CB C 31.22 0.2 1 745 164 PRO C C 177.81 0.1 1 746 165 ALA H H 7.99 0.01 1 747 165 ALA N N 119.63 0.1 1 748 165 ALA CA C 55.22 0.2 1 749 165 ALA CB C 17.62 0.2 1 750 165 ALA C C 181.21 0.1 1 751 166 GLU H H 7.49 0.01 1 752 166 GLU N N 119.93 0.1 1 753 166 GLU CA C 58.52 0.2 1 754 166 GLU CB C 29.12 0.2 1 755 166 GLU C C 178.81 0.1 1 756 167 VAL H H 6.96 0.01 1 757 167 VAL N N 119.23 0.1 1 758 167 VAL CA C 67.02 0.2 1 759 167 VAL CB C 31.02 0.2 1 760 167 VAL C C 177.41 0.1 1 761 168 GLU H H 8.47 0.01 1 762 168 GLU N N 121.13 0.1 1 763 168 GLU CA C 59.72 0.2 1 764 168 GLU CB C 29.02 0.2 1 765 168 GLU C C 178.01 0.1 1 766 169 ALA H H 7.72 0.01 1 767 169 ALA N N 120.83 0.1 1 768 169 ALA CA C 55.02 0.2 1 769 169 ALA CB C 17.52 0.2 1 770 169 ALA C C 180.81 0.1 1 771 170 LEU H H 7.39 0.01 1 772 170 LEU N N 119.73 0.1 1 773 170 LEU CA C 57.92 0.2 1 774 170 LEU CB C 38.92 0.2 1 775 170 LEU C C 178.41 0.1 1 776 171 ARG H H 8.07 0.01 1 777 171 ARG N N 120.23 0.1 1 778 171 ARG CA C 60.62 0.2 1 779 171 ARG CB C 29.82 0.2 1 780 171 ARG C C 177.11 0.1 1 781 172 GLU H H 7.95 0.01 1 782 172 GLU N N 117.63 0.1 1 783 172 GLU CA C 57.72 0.2 1 784 172 GLU CB C 30.32 0.2 1 785 172 GLU C C 178.31 0.1 1 786 173 LYS H H 7.48 0.01 1 787 173 LYS N N 118.53 0.1 1 788 173 LYS CA C 59.42 0.2 1 789 173 LYS CB C 32.22 0.2 1 790 173 LYS C C 180.21 0.1 1 791 174 VAL H H 7.88 0.01 1 792 174 VAL N N 117.73 0.1 1 793 174 VAL CA C 67.12 0.2 1 794 174 VAL CB C 31.22 0.2 1 795 174 VAL C C 178.61 0.1 1 796 175 TYR H H 8.78 0.01 1 797 175 TYR N N 117.13 0.1 1 798 175 TYR CA C 60.82 0.2 1 799 175 TYR CB C 36.32 0.2 1 800 175 TYR C C 178.01 0.1 1 801 176 ALA H H 8.56 0.01 1 802 176 ALA N N 126.83 0.1 1 803 176 ALA CA C 55.42 0.2 1 804 176 ALA CB C 17.62 0.2 1 805 176 ALA C C 181.51 0.1 1 806 177 SER H H 7.80 0.01 1 807 177 SER N N 117.43 0.1 1 808 177 SER CA C 61.72 0.2 1 809 177 SER CB C 62.82 0.2 1 810 177 SER C C 177.61 0.1 1 811 178 LEU H H 9.08 0.01 1 812 178 LEU N N 124.23 0.1 1 813 178 LEU CA C 58.12 0.2 1 814 178 LEU CB C 41.12 0.2 1 815 178 LEU C C 177.01 0.1 1 816 179 GLU H H 8.46 0.01 1 817 179 GLU N N 120.63 0.1 1 818 179 GLU CA C 60.92 0.2 1 819 179 GLU CB C 27.92 0.2 1 820 179 GLU C C 178.21 0.1 1 821 180 ALA H H 7.43 0.01 1 822 180 ALA N N 118.73 0.1 1 823 180 ALA CA C 55.12 0.2 1 824 180 ALA CB C 17.62 0.2 1 825 180 ALA C C 180.41 0.1 1 826 181 TYR H H 8.17 0.01 1 827 181 TYR N N 120.73 0.1 1 828 181 TYR CA C 61.72 0.2 1 829 181 TYR CB C 37.72 0.2 1 830 181 TYR C C 177.71 0.1 1 831 182 CYS H H 9.25 0.01 1 832 182 CYS N N 119.33 0.1 1 833 182 CYS CA C 65.22 0.2 1 834 182 CYS CB C 27.22 0.2 1 835 182 CYS C C 178.51 0.1 1 836 183 LYS H H 8.31 0.01 1 837 183 LYS N N 119.23 0.1 1 838 183 LYS CA C 59.22 0.2 1 839 183 LYS CB C 31.92 0.2 1 840 183 LYS C C 177.51 0.1 1 841 184 HIS H H 7.52 0.01 1 842 184 HIS N N 116.73 0.1 1 843 184 HIS CA C 58.12 0.2 1 844 184 HIS CB C 30.72 0.2 1 845 184 HIS C C 176.91 0.1 1 846 185 LYS H H 8.31 0.01 1 848 185 LYS CA C 56.52 0.2 1 849 185 LYS CB C 31.82 0.2 1 850 185 LYS C C 176.31 0.1 1 851 186 TYR H H 7.74 0.01 1 852 186 TYR N N 115.23 0.1 1 853 186 TYR CA C 54.32 0.2 1 854 186 TYR CB C 37.92 0.2 1 855 186 TYR C C 174.61 0.1 1 856 187 PRO CA C 65.02 0.2 1 857 187 PRO CB C 31.02 0.2 1 858 187 PRO C C 178.51 0.1 1 859 188 GLU H H 9.31 0.01 1 864 189 GLN H H 7.78 0.01 1 866 189 GLN CA C 52.72 0.2 1 868 189 GLN C C 174.01 0.1 1 869 191 GLY CA C 45.82 0.2 1 870 191 GLY C C 174.51 0.1 1 871 192 ARG H H 7.68 0.01 1 873 192 ARG CA C 60.52 0.2 1 874 192 ARG CB C 31.02 0.2 1 875 192 ARG C C 176.81 0.1 1 876 193 PHE H H 8.92 0.01 1 877 193 PHE N N 118.23 0.1 1 878 193 PHE CA C 60.32 0.2 1 879 193 PHE CB C 38.92 0.2 1 880 193 PHE C C 176.31 0.1 1 881 194 ALA H H 7.98 0.01 1 882 194 ALA CA C 54.72 0.2 1 883 194 ALA CB C 17.62 0.2 1 884 194 ALA C C 178.41 0.1 1 885 195 LYS H H 7.60 0.01 1 890 196 LEU H H 7.99 0.01 1 895 201 PRO CA C 66.92 0.2 1 896 201 PRO C C 177.71 0.1 1 897 202 ALA H H 7.26 0.01 1 898 202 ALA N N 120.23 0.1 1 899 202 ALA CA C 55.32 0.2 1 900 202 ALA C C 178.91 0.1 1 901 203 LEU H H 7.72 0.01 1 902 203 LEU N N 118.03 0.1 1 903 203 LEU CA C 58.32 0.2 1 906 204 ARG H H 7.85 0.01 1 911 205 SER H H 8.17 0.01 1 914 220 ILE CA C 60.12 0.2 1 915 220 ILE C C 175.71 0.1 1 916 221 GLY H H 8.23 0.01 1 917 221 GLY N N 111.33 0.1 1 918 221 GLY CA C 45.22 0.2 1 919 221 GLY C C 173.91 0.1 1 920 222 ASP H H 8.31 0.01 1 925 223 THR H H 7.98 0.01 1 930 228 PHE CA C 59.82 0.2 1 931 228 PHE C C 177.11 0.1 1 932 229 LEU H H 7.98 0.01 1 933 229 LEU N N 118.23 0.1 1 934 229 LEU CA C 57.32 0.2 1 935 229 LEU CB C 41.42 0.2 1 936 229 LEU C C 178.41 0.1 1 937 230 MET H H 7.85 0.01 1 938 230 MET N N 117.13 0.1 1 939 230 MET CA C 58.82 0.2 1 940 230 MET CB C 31.82 0.2 1 941 230 MET C C 178.01 0.1 1 942 231 GLU H H 7.97 0.01 1 943 231 GLU N N 118.03 0.1 1 944 231 GLU CA C 58.92 0.2 1 945 231 GLU CB C 29.02 0.2 1 946 231 GLU C C 179.31 0.1 1 947 232 MET H H 7.73 0.01 1 948 232 MET N N 116.53 0.1 1 949 232 MET CA C 57.22 0.2 1 950 232 MET CB C 32.82 0.2 1 951 232 MET C C 178.11 0.1 1 952 233 LEU H H 7.90 0.01 1 953 233 LEU N N 120.03 0.1 1 954 233 LEU CA C 56.62 0.2 1 955 233 LEU CB C 41.82 0.2 1 956 233 LEU C C 177.91 0.1 1 957 234 GLU H H 7.79 0.01 1 959 234 GLU CA C 56.92 0.2 1 960 234 GLU CB C 30.12 0.2 1 961 234 GLU C C 176.01 0.1 1 962 235 ALA H H 7.68 0.01 1 963 235 ALA N N 125.03 0.1 1 964 235 ALA CA C 51.02 0.2 1 966 235 ALA C C 175.71 0.1 1 967 236 PRO CA C 63.12 0.2 1 968 236 PRO CB C 31.62 0.2 1 969 236 PRO C C 177.11 0.1 1 970 237 HIS H H 8.25 0.01 1 971 237 HIS N N 119.83 0.1 1 972 237 HIS CA C 56.12 0.2 1 973 237 HIS C C 175.31 0.1 1 974 238 GLN H H 8.29 0.01 1 975 238 GLN N N 122.03 0.1 1 976 238 GLN CA C 55.92 0.2 1 977 238 GLN CB C 29.32 0.2 1 978 238 GLN C C 175.71 0.1 1 979 239 MET H H 8.46 0.01 1 984 240 THR H H 7.72 0.01 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_Citation_2 _Saveframe_category citation _Citation_title ; Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha ; _Citation_type journal _PubMed_ID 7760929 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bourguet William . . stop_ _Journal_abbreviation Nature _Journal_volume 375 _Journal_issue 6530 _Page_first 377 _Page_last 382 _Year 1995 loop_ _Keyword "X-ray structure" stop_ save_ save_Citation_3 _Saveframe_category citation _Citation_title ; Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid ; _Citation_type journal _PubMed_ID 10835357 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Egea Pascal F . stop_ _Journal_abbreviation "EMBO J." _Journal_volume 19 _Journal_issue 11 _Page_first 2592 _Page_last 2601 _Year 2000 loop_ _Keyword "X-ray structure" stop_ save_ save_Citation_4 _Saveframe_category citation _Citation_title ; Ligand-induced Stabilization of PPARgamma Monitored by NMR Spectroscopy: Implications for Nuclear Receptor Activation ; _Citation_type journal _PubMed_ID 10764590 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johnson Bruce A . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 298 _Journal_issue 2 _Page_first 187 _Page_last 194 _Year 2000 loop_ _Keyword NMR stop_ save_