data_17975 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PPARgamma LBD complexed with rosiglitazone ; _BMRB_accession_number 17975 _BMRB_flat_file_name bmr17975.str _Entry_type original _Submission_date 2011-10-05 _Accession_date 2011-10-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Ligand binding domain of PPARgamma complexed to rosiglitazone' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kojetin Douglas . . 2 Johnson Bruce . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 245 "13C chemical shifts" 750 "15N chemical shifts" 245 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-01-18 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17976 'PPARgamma LBD + MRL24' 17977 'PPARgamma LBD + MRL20' stop_ _Original_release_date 2012-01-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Ligand and Receptor Dynamics Contribute to the Mechanism of Graded PPAR Agonism.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22244763 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hughes Travis S. . 2 Chalmers Michael J. . 3 Novick Scott . . 4 Kuruvilla Dana S. . 5 Chang 'Mi Ra' . . 6 Kamenecka Theodore M. . 7 Rance Mark . . 8 Johnson Bruce A. . 9 Burris Thomas P. . 10 Griffin Patrick R. . 11 Kojetin Douglas J. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 20 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 139 _Page_last 150 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PPARgamma LBD + rosigliazone' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PPARgamma_LBD $PPARgamma_LBD rosiglitazone $240 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PPARgamma_LBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PPARgamma_LBD _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 276 _Mol_residue_sequence ; GQLNPESADLRALAKHLYDS YIKSFPLTKAKARAILTGKT TDKSPFVIYDMNSLMMGEDK IKFKHITPLQEQSKEVAIRI FQGCQFRSVEAVQEITEYAK SIPGFVNLDLNDQVTLLKYG VHEIIYTMLASLMNKDGVLI SEGQGFMTREFLKSLRKPFG DFMEPKFEFAVKFNALELDD SDLAIFIAVIILSGDRPGLL NVKPIEDIQDNLLQALELQL KLNHPESSQLFAKLLQKMTD LRQIVTEHVQLLQVIKKTET DMSLHPLLQEIYKDLY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 202 GLY 2 203 GLN 3 204 LEU 4 205 ASN 5 206 PRO 6 207 GLU 7 208 SER 8 209 ALA 9 210 ASP 10 211 LEU 11 212 ARG 12 213 ALA 13 214 LEU 14 215 ALA 15 216 LYS 16 217 HIS 17 218 LEU 18 219 TYR 19 220 ASP 20 221 SER 21 222 TYR 22 223 ILE 23 224 LYS 24 225 SER 25 226 PHE 26 227 PRO 27 228 LEU 28 229 THR 29 230 LYS 30 231 ALA 31 232 LYS 32 233 ALA 33 234 ARG 34 235 ALA 35 236 ILE 36 237 LEU 37 238 THR 38 239 GLY 39 240 LYS 40 241 THR 41 242 THR 42 243 ASP 43 244 LYS 44 245 SER 45 246 PRO 46 247 PHE 47 248 VAL 48 249 ILE 49 250 TYR 50 251 ASP 51 252 MET 52 253 ASN 53 254 SER 54 255 LEU 55 256 MET 56 257 MET 57 258 GLY 58 259 GLU 59 260 ASP 60 261 LYS 61 262 ILE 62 263 LYS 63 264 PHE 64 265 LYS 65 266 HIS 66 267 ILE 67 268 THR 68 269 PRO 69 270 LEU 70 271 GLN 71 272 GLU 72 273 GLN 73 274 SER 74 275 LYS 75 276 GLU 76 277 VAL 77 278 ALA 78 279 ILE 79 280 ARG 80 281 ILE 81 282 PHE 82 283 GLN 83 284 GLY 84 285 CYS 85 286 GLN 86 287 PHE 87 288 ARG 88 289 SER 89 290 VAL 90 291 GLU 91 292 ALA 92 293 VAL 93 294 GLN 94 295 GLU 95 296 ILE 96 297 THR 97 298 GLU 98 299 TYR 99 300 ALA 100 301 LYS 101 302 SER 102 303 ILE 103 304 PRO 104 305 GLY 105 306 PHE 106 307 VAL 107 308 ASN 108 309 LEU 109 310 ASP 110 311 LEU 111 312 ASN 112 313 ASP 113 314 GLN 114 315 VAL 115 316 THR 116 317 LEU 117 318 LEU 118 319 LYS 119 320 TYR 120 321 GLY 121 322 VAL 122 323 HIS 123 324 GLU 124 325 ILE 125 326 ILE 126 327 TYR 127 328 THR 128 329 MET 129 330 LEU 130 331 ALA 131 332 SER 132 333 LEU 133 334 MET 134 335 ASN 135 336 LYS 136 337 ASP 137 338 GLY 138 339 VAL 139 340 LEU 140 341 ILE 141 342 SER 142 343 GLU 143 344 GLY 144 345 GLN 145 346 GLY 146 347 PHE 147 348 MET 148 349 THR 149 350 ARG 150 351 GLU 151 352 PHE 152 353 LEU 153 354 LYS 154 355 SER 155 356 LEU 156 357 ARG 157 358 LYS 158 359 PRO 159 360 PHE 160 361 GLY 161 362 ASP 162 363 PHE 163 364 MET 164 365 GLU 165 366 PRO 166 367 LYS 167 368 PHE 168 369 GLU 169 370 PHE 170 371 ALA 171 372 VAL 172 373 LYS 173 374 PHE 174 375 ASN 175 376 ALA 176 377 LEU 177 378 GLU 178 379 LEU 179 380 ASP 180 381 ASP 181 382 SER 182 383 ASP 183 384 LEU 184 385 ALA 185 386 ILE 186 387 PHE 187 388 ILE 188 389 ALA 189 390 VAL 190 391 ILE 191 392 ILE 192 393 LEU 193 394 SER 194 395 GLY 195 396 ASP 196 397 ARG 197 398 PRO 198 399 GLY 199 400 LEU 200 401 LEU 201 402 ASN 202 403 VAL 203 404 LYS 204 405 PRO 205 406 ILE 206 407 GLU 207 408 ASP 208 409 ILE 209 410 GLN 210 411 ASP 211 412 ASN 212 413 LEU 213 414 LEU 214 415 GLN 215 416 ALA 216 417 LEU 217 418 GLU 218 419 LEU 219 420 GLN 220 421 LEU 221 422 LYS 222 423 LEU 223 424 ASN 224 425 HIS 225 426 PRO 226 427 GLU 227 428 SER 228 429 SER 229 430 GLN 230 431 LEU 231 432 PHE 232 433 ALA 233 434 LYS 234 435 LEU 235 436 LEU 236 437 GLN 237 438 LYS 238 439 MET 239 440 THR 240 441 ASP 241 442 LEU 242 443 ARG 243 444 GLN 244 445 ILE 245 446 VAL 246 447 THR 247 448 GLU 248 449 HIS 249 450 VAL 250 451 GLN 251 452 LEU 252 453 LEU 253 454 GLN 254 455 VAL 255 456 ILE 256 457 LYS 257 458 LYS 258 459 THR 259 460 GLU 260 461 THR 261 462 ASP 262 463 MET 263 464 SER 264 465 LEU 265 466 HIS 266 467 PRO 267 468 LEU 268 469 LEU 269 470 GLN 270 471 GLU 271 472 ILE 272 473 TYR 273 474 LYS 274 475 ASP 275 476 LEU 276 477 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 15518 Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain 99.64 279 100.00 100.00 0.00e+00 BMRB 17976 PPARgamma_LBD 100.00 276 100.00 100.00 0.00e+00 BMRB 17977 PPARgamma_LBD 100.00 276 100.00 100.00 0.00e+00 PDB 1FM6 "The 2.1 Angstrom Resolution Crystal Structure Of The Heterodimer Of The Human Rxralpha And Ppargamma Ligand Binding Domains Res" 98.55 272 100.00 100.00 0.00e+00 PDB 1FM9 "The 2.1 Angstrom Resolution Crystal Structure Of The Heterodimer Of The Human Rxralpha And Ppargamma Ligand Binding Domains Res" 98.55 272 100.00 100.00 0.00e+00 PDB 1I7I "Crystal Structure Of The Ligand Binding Domain Of Human Ppar-Gamma In Complex With The Agonist Az 242" 99.64 292 100.00 100.00 0.00e+00 PDB 1K74 "The 2.3 Angstrom Resolution Crystal Structure Of The Heterodimer Of The Human Ppargamma And Rxralpha Ligand Binding Domains Res" 98.91 283 99.63 99.63 0.00e+00 PDB 1KNU "Ligand Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma In Complex With A Synthetic Agonist" 99.28 274 100.00 100.00 0.00e+00 PDB 1NYX "Ligand Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma In Complex With An Agonist" 99.64 276 100.00 100.00 0.00e+00 PDB 1PRG "Ligand Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma" 97.83 270 100.00 100.00 0.00e+00 PDB 1RDT "Crystal Structure Of A New Rexinoid Bound To The Rxralpha Ligand Binding Doamin In The RxralphaPPARGAMMA HETERODIMER" 98.19 284 100.00 100.00 0.00e+00 PDB 1WM0 "Ppargamma In Complex With A 2-Baba Compound" 100.00 292 99.64 100.00 0.00e+00 PDB 1ZEO "Crystal Structure Of Human Ppar-Gamma Ligand Binding Domain Complexed With An Alpha-Aryloxyphenylacetic Acid Agonist" 100.00 277 99.64 99.64 0.00e+00 PDB 1ZGY "Structural And Biochemical Basis For Selective Repression Of The Orphan Nuclear Receptor Lrh-1 By Shp" 98.55 272 100.00 100.00 0.00e+00 PDB 2ATH "Crystal Structure Of The Ligand Binding Domain Of Human Ppar-Gamma Im Complex With An Agonist" 98.19 271 100.00 100.00 0.00e+00 PDB 2F4B "Crystal Structure Of The Ligand Binding Domain Of Human Ppar-Gamma In Complex With An Agonist" 98.19 271 100.00 100.00 0.00e+00 PDB 2FVJ "A Novel Anti-adipogenic Partial Agonist Of Peroxisome Proliferator- Activated Receptor-gamma (pparg) Recruits Pparg-coactivator" 98.19 271 100.00 100.00 0.00e+00 PDB 2G0G "Structure-based Drug Design Of A Novel Family Of Ppar Partial Agonists: Virtual Screening, X-ray Crystallography And In Vitro/i" 98.19 271 100.00 100.00 0.00e+00 PDB 2G0H "Structure-Based Drug Design Of A Novel Family Of Ppar Partial Agonists: Virtual Screening, X-Ray Crystallography And In VitroIN" 98.19 271 100.00 100.00 0.00e+00 PDB 2GTK "Structure-Based Design Of Indole Propionic Acids As Novel Pparag Co-Agonists" 98.19 271 100.00 100.00 0.00e+00 PDB 2HFP "Crystal Structure Of Ppar Gamma With N-Sulfonyl-2-Indole Carboxamide Ligands" 98.91 282 99.63 100.00 0.00e+00 PDB 2HWQ "Structural Basis For The Structure-Activity Relationships Of Peroxisome Proliferator-Activated Receptor Agonists" 98.19 271 100.00 100.00 0.00e+00 PDB 2HWR "Structural Basis For The Structure-Activity Relationships Of Peroxisome Proliferator-Activated Receptor Agonists" 98.19 271 100.00 100.00 0.00e+00 PDB 2I4J "Crystal Structure Of The Complex Between Ppargamma And The Agonist Lt160 (Ureidofibrate Derivative)" 99.28 286 100.00 100.00 0.00e+00 PDB 2I4P "Crystal Structure Of The Complex Between Ppargamma And The Partial Agonist Lt127 (Ureidofibrate Derivative). Structure Obtained" 99.28 286 100.00 100.00 0.00e+00 PDB 2I4Z "Crystal Structure Of The Complex Between Ppargamma And The Partial Agonist Lt127 (Ureidofibrate Derivative). This Structure Has" 99.28 286 100.00 100.00 0.00e+00 PDB 2OM9 "Ajulemic Acid, A Synthetic Cannabinoid Bound To Ppar Gamma" 99.28 278 100.00 100.00 0.00e+00 PDB 2P4Y "Crystal Structure Of Human Ppar-Gamma-Ligand Binding Domain Complexed With An Indole-Based Modulator" 100.00 277 99.64 99.64 0.00e+00 PDB 2POB "Ppargamma Ligand Binding Domain Complexed With A Farglitazar Analogue Gw4709" 98.55 272 100.00 100.00 0.00e+00 PDB 2PRG "Ligand-Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma" 98.19 271 100.00 100.00 0.00e+00 PDB 2Q59 "Crystal Structure Of Ppargamma Lbd Bound To Full Agonist Mrl20" 98.91 274 100.00 100.00 0.00e+00 PDB 2Q5P "Crystal Structure Of Ppargamma Bound To Partial Agonist Mrl24" 98.91 274 100.00 100.00 0.00e+00 PDB 2Q5S "Crystal Structure Of Ppargamma Bound To Partial Agonist Ntzdpa" 98.91 274 100.00 100.00 0.00e+00 PDB 2Q61 "Crystal Structure Of Ppargamma Ligand Binding Domain Bound To Partial Agonist Sr145" 98.91 274 100.00 100.00 0.00e+00 PDB 2Q6R "Crystal Structure Of Ppar Gamma Complexed With Partial Agonist Sf147" 98.91 274 100.00 100.00 0.00e+00 PDB 2Q6S "2.4 Angstrom Crystal Structure Of Ppar Gamma Complexed To Bvt.13 Without Co-Activator Peptides" 98.91 274 100.00 100.00 0.00e+00 PDB 2Q8S "X-Ray Crystal Structure Of The Nuclear Hormone Receptor Ppar-Gamma In A Complex With A Ppar GammaALPHA DUAL AGONIST" 98.19 271 100.00 100.00 0.00e+00 PDB 2QMV "High Resolution Structure Of Peroxisone Proliferation-Activated Receptor Gamma And Characterisation Of Its Interaction With The" 97.83 270 100.00 100.00 0.00e+00 PDB 2VSR "Hppargamma Ligand Binding Domain In Complex With 9-(S)-Hode" 100.00 276 99.64 99.64 0.00e+00 PDB 2VST "Hppargamma Ligand Binding Domain In Complex With 13-(S)- Hode" 100.00 276 99.64 99.64 0.00e+00 PDB 2VV0 "Hppargamma Ligand Binding Domain In Complex With Dha" 100.00 276 99.64 99.64 0.00e+00 PDB 2VV1 "Hppargamma Ligand Binding Domain In Complex With 4-Hdha" 100.00 276 99.64 99.64 0.00e+00 PDB 2VV2 "Hppargamma Ligand Binding Domain In Complex With 5-Hepa" 100.00 276 99.64 99.64 0.00e+00 PDB 2VV3 "Hppargamma Ligand Binding Domain In Complex With 4-Oxodha" 100.00 276 99.64 99.64 0.00e+00 PDB 2VV4 "Hppargamma Ligand Binding Domain In Complex With 6-Oxoote" 100.00 276 99.64 99.64 0.00e+00 PDB 2XKW "Ligand Binding Domain Of Human Ppar-Gamma In Complex With The Agonist Pioglitazone" 99.28 274 100.00 100.00 0.00e+00 PDB 2YFE "Ligand Binding Domain Of Human Ppar Gamma In Complex With Amorfrutin 1" 99.64 287 100.00 100.00 0.00e+00 PDB 2ZK0 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZK1 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With 15-Deoxy-Delta12,14- Prostaglandin " 99.28 286 100.00 100.00 0.00e+00 PDB 2ZK2 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With Glutathion Conjugated 15-Deoxy-Delt" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZK3 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With 8-Oxo- Eicosatetraenoic Acid" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZK4 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With 15-Oxo- Eicosatetraenoic Acid" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZK5 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With Nitro-233" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZK6 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With C8-Bodipy" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZNO "Human Pprr Gamma Ligand Binding Domain In Complex With A Synthetic Agonist Tipp703" 99.28 286 100.00 100.00 0.00e+00 PDB 2ZVT "Cys285ser Mutant Ppargamma Ligand-Binding Domain Complexed With 15-Deoxy-Delta12,14-Prostaglandin J2" 99.28 286 99.64 99.64 0.00e+00 PDB 3ADS "Human Ppargamma Ligand-Binding Domain In Complex With Indomethacin" 99.64 287 100.00 100.00 0.00e+00 PDB 3ADT "Human Ppargamma Ligand-Binding Domain In Complex With 5-Hydroxy-Indole Acetate" 99.64 287 100.00 100.00 0.00e+00 PDB 3ADU "Human Ppargamma Ligand-Binding Domain In Complex With 5-Methoxy-Indole Acetate" 99.64 287 100.00 100.00 0.00e+00 PDB 3ADV "Human Ppargamma Ligand-Binding Domain In Complex With Serotonin" 99.64 287 100.00 100.00 0.00e+00 PDB 3ADW "Human Ppargamma Ligand-Binding Domain In Complex With 5-Methoxy-Indole Acetate And 15-Oxo-Eicosatetraenoic Acid" 99.64 287 100.00 100.00 0.00e+00 PDB 3ADX "Human Ppargamma Ligand-Binding Domain In Complex With Indomethacin And Nitro-233" 99.64 287 100.00 100.00 0.00e+00 PDB 3AN3 "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mo3s" 99.28 286 100.00 100.00 0.00e+00 PDB 3AN4 "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mo4r" 99.28 286 100.00 100.00 0.00e+00 PDB 3B0Q "Human Ppar Gamma Ligand Binding Domain In Complex With Mcc555" 99.28 274 100.00 100.00 0.00e+00 PDB 3B0R "Human Ppar Gamma Ligand Binding Dmain Complexed With Gw9662 In A Covalent Bonded Form" 99.28 274 100.00 100.00 0.00e+00 PDB 3B1M "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator Cerco-A" 98.91 283 99.63 99.63 0.00e+00 PDB 3B3K "Crystal Structure Of The Complex Between Ppargamma And The Full Agonist Lt175" 99.28 286 100.00 100.00 0.00e+00 PDB 3BC5 "X-Ray Crystal Structure Of Human Ppar Gamma With 2-(5-(3-(2- (5-Methyl-2-Phenyloxazol-4-Yl)ethoxy)benzyl)-2-Phenyl-2h-1, 2,3-Tr" 99.64 296 100.00 100.00 0.00e+00 PDB 3CDP "Crystal Structure Of Ppar-gamma Lbd Complexed With A Partial Agonist, Analogue Of Clofibric Acid" 99.28 286 100.00 100.00 0.00e+00 PDB 3CDS "Crystal Structure Of The Complex Between Ppar-Gamma And The Agonist Lt248 (Clofibric Acid Analogue)" 99.28 286 100.00 100.00 0.00e+00 PDB 3CS8 "Structural And Biochemical Basis For The Binding Selectivity Of Pparg To Pgc-1a" 98.55 275 99.63 100.00 0.00e+00 PDB 3CWD "Molecular Recognition Of Nitro-Fatty Acids By Ppar Gamma" 97.83 270 100.00 100.00 0.00e+00 PDB 3D6D "Crystal Structure Of The Complex Between Ppargamma Lbd And The Lt175(R-Enantiomer)" 99.28 286 100.00 100.00 0.00e+00 PDB 3DZU "Intact Ppar Gamma - Rxr Alpha Nuclear Receptor Complex On Dna Bound With Bvt.13, 9-Cis Retinoic Acid And Ncoa2 Peptide" 99.64 419 100.00 100.00 0.00e+00 PDB 3DZY "Intact Ppar Gamma - Rxr Alpha Nuclear Receptor Complex On Dna Bound With Rosiglitazone, 9-Cis Retinoic Acid And Ncoa2 Peptide" 99.64 419 100.00 100.00 0.00e+00 PDB 3E00 "Intact Ppar Gamma - Rxr Alpha Nuclear Receptor Complex On Dna Bound With Gw9662, 9-Cis Retinoic Acid And Ncoa2 Peptide" 99.64 419 100.00 100.00 0.00e+00 PDB 3ET0 "Structure Of Ppargamma With 3-(5-Methoxy-1h-Indol-3-Yl)- Propionic Acid" 98.19 292 99.63 99.63 0.00e+00 PDB 3ET3 "Structure Of Ppargamma With 3-[5-Methoxy-1-(4-Methoxy- Benzenesulfonyl)-1h-Indol-3-Yl]-Propionic Acid" 98.19 292 100.00 100.00 0.00e+00 PDB 3FEJ "Design And Biological Evaluation Of Novel, Balanced Dual PparaG AGONISTS" 98.19 271 100.00 100.00 0.00e+00 PDB 3FUR "Crystal Structure Of Pparg In Complex With Int131" 98.55 272 100.00 100.00 0.00e+00 PDB 3G9E "Aleglitaar. A New. Potent, And Balanced Dual PparaG AGONIST For The Treatment Of Type Ii Diabetes" 98.19 271 100.00 100.00 0.00e+00 PDB 3GBK "Crystal Structure Of Human Ppar-Gamma Ligand Binding Domain Complexed With A Potent And Selective Agonist" 98.19 271 100.00 100.00 0.00e+00 PDB 3H0A "Crystal Structure Of Peroxisome Proliferator-activated Receptor Gamma (pparg) And Retinoic Acid Receptor Alpha (rxra) In Comple" 98.55 272 100.00 100.00 0.00e+00 PDB 3HO0 "Crystal Structure Of The Ppargamma-Lbd Complexed With A New Aryloxy-3phenylpropanoic Acid" 99.28 286 100.00 100.00 0.00e+00 PDB 3HOD "Crystal Structure Of The Ppargamma-Lbd Complexed With A New Aryloxy-3phenylpropanoic Acid" 99.28 286 100.00 100.00 0.00e+00 PDB 3IA6 "X-Ray Crystal Structure Of The Nuclear Hormone Receptor Ppar-Gamma In A Complex With A Ppar GammaALPHA DUAL Agonist" 98.19 271 100.00 100.00 0.00e+00 PDB 3K8S "Crystal Structure Of Pparg In Complex With T2384" 98.55 272 100.00 100.00 0.00e+00 PDB 3KMG "The X-Ray Crystal Structure Of Ppar-Gamma In Complex With An Indole Derivative Modulator, Gsk538, And An Src-1 Peptide" 98.55 272 100.00 100.00 0.00e+00 PDB 3LMP "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 98.91 283 99.63 99.63 0.00e+00 PDB 3NOA "Crystal Structure Of Human Ppar-Gamma Ligand Binding Domain Complex With A Potency Improved Agonist" 98.19 271 100.00 100.00 0.00e+00 PDB 3OSI "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tetrachloro-bisphenol A (tcbpa)" 99.28 285 100.00 100.00 0.00e+00 PDB 3OSW "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tetrabromo-bisphenol A (tbbpa)" 99.28 285 100.00 100.00 0.00e+00 PDB 3PBA "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Monosulfate Tetrabromo-Bisphenol A (Monotbbpa)" 99.64 286 100.00 100.00 0.00e+00 PDB 3PO9 "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tripropyltin" 99.64 286 100.00 100.00 0.00e+00 PDB 3PRG "Ligand Binding Domain Of Human Peroxisome Proliferator Activated Receptor" 99.28 278 100.00 100.00 0.00e+00 PDB 3QT0 "Revealing A Steroid Receptor Ligand As A Unique Ppargamma Agonist" 98.19 271 100.00 100.00 0.00e+00 PDB 3R5N "Crystal Structure Of Ppargammalbd Complexed With The Agonist Magnolol" 99.28 274 100.00 100.00 0.00e+00 PDB 3R8A "X-Ray Crystal Structure Of The Nuclear Hormone Receptor Ppar-Gamma In A Complex With A Compound With Dual Ppar Gamma Agonism An" 98.19 282 100.00 100.00 0.00e+00 PDB 3R8I "Crystal Structure Of Ppargamma With An Achiral Ureidofibrate Derivative (Rt86)" 99.64 287 100.00 100.00 0.00e+00 PDB 3S9S "Ligand Binding Domain Of Ppargamma Complexed With A Benzimidazole Partial Agonist" 98.55 284 100.00 100.00 0.00e+00 PDB 3SZ1 "Human Ppar Gamma Ligand Binding Domain In Complex With Luteolin And Myristic Acid" 99.28 278 100.00 100.00 0.00e+00 PDB 3T03 "Crystal Structure Of Ppar Gamma Ligand Binding Domain In Complex With A Novel Partial Agonist Gq-16" 98.91 284 99.63 99.63 0.00e+00 PDB 3TY0 "Structure Of Ppargamma Ligand Binding Domain In Complex With (r)-5-(3- ((3-(6-methoxybenzo[d]isoxazol-3-yl)-2-oxo-2,3-dihydro-1" 100.00 277 99.64 99.64 0.00e+00 PDB 3U9Q "Ligand Binding Domain Of Ppargamma Complexed With Decanoic Acid And Pgc-1a Peptide" 97.46 269 100.00 100.00 0.00e+00 PDB 3V9T "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 98.91 283 99.63 99.63 0.00e+00 PDB 3V9V "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 98.91 283 99.63 99.63 0.00e+00 PDB 3V9Y "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 98.91 283 99.63 99.63 0.00e+00 PDB 3VJH "Human Ppar Gamma Ligand Binding Domain In Complex With Jkpl35" 99.28 286 100.00 100.00 0.00e+00 PDB 3VJI "Human Ppar Gamma Ligand Binding Domain In Complex With Jkpl53" 99.28 286 100.00 100.00 0.00e+00 PDB 3VN2 "Crystal Structure Of Ppargamma Complexed With Telmisartan" 99.64 285 100.00 100.00 0.00e+00 PDB 3VSO "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mekt21" 99.28 286 100.00 100.00 0.00e+00 PDB 3VSP "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mekt28" 99.28 286 100.00 100.00 0.00e+00 PDB 3WJ4 "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tributyltin" 100.00 276 98.91 98.91 0.00e+00 PDB 3WJ5 "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Triphenyltin" 100.00 276 98.91 98.91 0.00e+00 PDB 3WMH "Human Pprr Gamma Ligand Binding Domain In Complex With A Gammma Selective Synthetic Partial Agonist Mekt75" 99.28 286 100.00 100.00 0.00e+00 PDB 3X1H "Hppargamma Ligand Binding Domain In Complex With 5-oxo- Tricosahexaenoic Acid" 100.00 276 99.64 99.64 0.00e+00 PDB 3X1I "Hppargamma Ligand Binding Domain In Complex With 6-oxo- Tetracosahexaenoic Acid" 100.00 276 99.64 99.64 0.00e+00 PDB 4A4V "Ligand Binding Domain Of Human Ppar Gamma In Complex With Amorfrutin 2" 99.64 287 100.00 100.00 0.00e+00 PDB 4A4W "Ligand Binding Domain Of Human Ppar Gamma In Complex With Amorfrutin 2" 99.64 287 100.00 100.00 0.00e+00 PDB 4CI5 "Structural Basis For Gl479 A Dual Peroxisome Proliferator- Activated Receptor Gamma Agonist" 98.55 272 100.00 100.00 0.00e+00 PDB 4E4K "Crystal Structure Of Ppargamma With The Ligand Jo21" 99.64 287 100.00 100.00 0.00e+00 PDB 4E4Q "Crystal Structure Of Ppargamma With The Ligand Fs214" 99.64 287 100.00 100.00 0.00e+00 PDB 4EM9 "Human Ppar Gamma In Complex With Nonanoic Acids" 98.19 275 100.00 100.00 0.00e+00 PDB 4EMA "Human Peroxisome Proliferator-activated Receptor Gamma In Complex With Rosiglitazone" 98.19 275 100.00 100.00 0.00e+00 PDB 4F9M "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 98.91 283 99.63 99.63 0.00e+00 PDB 4FGY "Identification Of A Unique Ppar Ligand With An Unexpected Binding Mode And Antibetic Activity" 97.83 270 100.00 100.00 0.00e+00 PDB 4HEE "Crystal Structure Of Ppargamma In Complex With Compound 13" 98.19 282 100.00 100.00 0.00e+00 PDB 4JAZ "Crystal Structure Of The Complex Between Ppargamma Lbd And Trans- Resveratrol" 99.64 287 100.00 100.00 0.00e+00 PDB 4JL4 "Crystal Structure Of The Complex Between Ppargamma Lbd And The Ligand Lj570 [(2s)-3-(biphenyl-4-yl)-2-(biphenyl-4-yloxy)propano" 99.64 287 100.00 100.00 0.00e+00 PDB 4L96 "Structure Of The Complex Between The F360l Ppargamma Mutant And The Ligand Lt175 (space Group I222)" 98.19 275 99.63 99.63 0.00e+00 PDB 4L98 "Crystal Structure Of The Complex Of F360l Ppargamma Mutant With The Ligand Lt175" 98.19 275 99.63 99.63 0.00e+00 PDB 4O8F "Crystal Structure Of The Complex Between Ppargamma Mutant R357a And Rosiglitazone" 99.64 287 99.64 99.64 0.00e+00 PDB 4OJ4 "Crystal Structure Of V290m Ppargamma Mutant In Complex With Diclofenac" 99.28 278 99.64 100.00 0.00e+00 PDB 4PRG "0072 Partial Agonist Ppar Gamma Cocrystal" 97.83 270 100.00 100.00 0.00e+00 PDB 4PVU "Crystal Structure Of The Complex Between Ppargamma-lbd And The R Enantiomer Of Mbx-102 (metaglidasen)" 99.64 287 100.00 100.00 0.00e+00 PDB 4PWL "Crystal Structure Of The Complex Between Ppargamma-lbd And The S Enantiomer Of Mbx-102 (metaglidasen)" 99.64 287 100.00 100.00 0.00e+00 PDB 4R2U "Crystal Structure Of Ppargamma In Complex With Sr1664" 99.64 275 100.00 100.00 0.00e+00 PDB 4R6S "Crystal Structure Of Ppargammma In Complex With Sr1663" 99.64 275 99.64 99.64 0.00e+00 PDB 4XLD "Crystal Structure Of The Human Pparg-lbd/rosiglitazone Complex Obtained By Dry Co-crystallization And In Situ Diffraction" 99.64 296 100.00 100.00 0.00e+00 PDB 4XTA "Mechanisms Of Ppargamma Activation By Non-steroidal Anti-inflammatory Drugs" 99.28 278 100.00 100.00 0.00e+00 PDB 4XUM "Ppargamma Ligand Binding Domain In Complex With Indomethacin" 99.28 278 100.00 100.00 0.00e+00 PDB 4Y29 "Identification Of A Novel Pparg Ligand That Regulates Metabolism" 97.46 269 100.00 100.00 0.00e+00 DBJ BAA18949 "PPAR gamma2 [Homo sapiens]" 100.00 506 99.64 99.64 0.00e+00 DBJ BAA23354 "peroxisome proliferator activated-receptor gamma [Homo sapiens]" 99.64 474 98.91 98.91 0.00e+00 DBJ BAA32540 "PPAR-gamma protein [Rattus norvegicus]" 99.64 475 98.55 99.64 0.00e+00 DBJ BAA36485 "PPAR gamma2 [Rattus norvegicus]" 99.64 505 98.55 99.64 0.00e+00 DBJ BAD20642 "peroxisome proliferator-activated receptor gamma 1a [Sus scrofa]" 99.64 475 99.64 100.00 0.00e+00 EMBL CAA07224 "peroxisome proliferator-cctivated receptor gamma 1 [Sus scrofa]" 99.64 475 98.91 99.64 0.00e+00 EMBL CAA07225 "peroxisome proliferator-activated receptor-gamma 2 [Sus scrofa]" 99.64 504 98.91 99.64 0.00e+00 EMBL CAA62152 "peroxisome proliferator activated receptor gamma [Homo sapiens]" 99.64 477 100.00 100.00 0.00e+00 EMBL CAA62153 "peroxisome proliferator activated receptor gamma [Homo sapiens]" 99.64 475 100.00 100.00 0.00e+00 EMBL CAA73032 "peroxisome proliferator activated receptor gamma 1 [Bos taurus]" 99.64 475 98.91 99.64 0.00e+00 GB AAA19971 "peroxisome proliferator-activated receptor gamma [Mus musculus]" 99.64 475 98.55 99.64 0.00e+00 GB AAA62110 "PPAR gamma [Mus musculus]" 99.64 475 97.45 98.91 0.00e+00 GB AAA62277 "peroxisome proliferator activated protein-gamma-2 [Mus musculus]" 99.64 505 98.18 99.64 0.00e+00 GB AAA80314 "peroxisome proliferator activated receptor gamma [Homo sapiens]" 99.64 477 100.00 100.00 0.00e+00 GB AAB04028 "peroxisome proliferator activated receptor gamma 2 [Homo sapiens]" 99.64 505 100.00 100.00 0.00e+00 PIR JE0279 "peroxisome proliferator-activated receptor gamma 1 - pig" 99.64 475 98.91 99.64 0.00e+00 REF NP_001019803 "peroxisome proliferator-activated receptor gamma [Canis lupus familiaris]" 99.64 505 100.00 100.00 0.00e+00 REF NP_001028032 "peroxisome proliferator-activated receptor gamma [Macaca mulatta]" 99.64 505 100.00 100.00 0.00e+00 REF NP_001075617 "peroxisome proliferator-activated receptor gamma [Oryctolagus cuniculus]" 99.64 475 98.91 100.00 0.00e+00 REF NP_001094391 "peroxisome proliferator-activated receptor gamma [Ovis aries]" 99.64 475 98.91 99.64 0.00e+00 REF NP_001106647 "peroxisome proliferator-activated receptor gamma [Felis catus]" 99.64 505 99.27 99.64 0.00e+00 SP O18924 "RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 gr" 99.64 505 100.00 100.00 0.00e+00 SP O18971 "RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 gr" 99.64 505 98.91 99.64 0.00e+00 SP O19052 "RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 gr" 99.64 475 98.91 100.00 0.00e+00 SP O62807 "RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 gr" 99.64 504 99.64 100.00 0.00e+00 SP O88275 "RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 gr" 99.64 505 98.55 99.64 0.00e+00 TPG DAA16769 "TPA: peroxisome proliferator-activated receptor gamma [Bos taurus]" 99.64 505 98.91 99.64 0.00e+00 stop_ save_ ############# # Ligands # ############# save_240 _Saveframe_category ligand _Mol_type non-polymer _Name_common "240 ((2S)-2-(2-{[1-(4-METHOXYBENZOYL)-2-METHYL-5-(TRIFLUOROMETHOXY)-1H-INDOL-3-YL]METHYL}PHENOXY)PROPANOIC ACID)" _BMRB_code . _PDB_code 240 _Molecular_mass 527.488 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Oct 19 10:54:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons OAD OAD O . 0 . ? CAY CAY C . 0 . ? OAF OAF O . 0 . ? CBJ CBJ C . 0 . ? CAC CAC C . 0 . ? OAW OAW O . 0 . ? CBF CBF C . 0 . ? CAO CAO C . 0 . ? CAK CAK C . 0 . ? CAJ CAJ C . 0 . ? CAN CAN C . 0 . ? CBE CBE C . 0 . ? CAU CAU C . 0 . ? CBG CBG C . 0 . ? CBA CBA C . 0 . ? CAB CAB C . 0 . ? CBH CBH C . 0 . ? CAT CAT C . 0 . ? CBC CBC C . 0 . ? OAX OAX O . 0 . ? CBL CBL C . 0 . ? FAG FAG F . 0 . ? FAI FAI F . 0 . ? FAH FAH F . 0 . ? CAR CAR C . 0 . ? CAS CAS C . 0 . ? CBI CBI C . 0 . ? NBK NBK N . 0 . ? CAZ CAZ C . 0 . ? OAE OAE O . 0 . ? CBD CBD C . 0 . ? CAQ CAQ C . 0 . ? CAM CAM C . 0 . ? CAP CAP C . 0 . ? CAL CAL C . 0 . ? CBB CBB C . 0 . ? OAV OAV O . 0 . ? CAA CAA C . 0 . ? HOAD HOAD H . 0 . ? HBJ HBJ H . 0 . ? HAC1 HAC1 H . 0 . ? HAC2 HAC2 H . 0 . ? HAC3 HAC3 H . 0 . ? HAO HAO H . 0 . ? HAK HAK H . 0 . ? HAJ HAJ H . 0 . ? HAN HAN H . 0 . ? HAU1 HAU1 H . 0 . ? HAU2 HAU2 H . 0 . ? HAB1 HAB1 H . 0 . ? HAB2 HAB2 H . 0 . ? HAB3 HAB3 H . 0 . ? HAT HAT H . 0 . ? HAR HAR H . 0 . ? HAS HAS H . 0 . ? HAQ HAQ H . 0 . ? HAM HAM H . 0 . ? HAP HAP H . 0 . ? HAL HAL H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HAA3 HAA3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING OAD CAY ? ? SING OAD HOAD ? ? DOUB CAY OAF ? ? SING CAY CBJ ? ? SING CBJ CAC ? ? SING CBJ OAW ? ? SING CBJ HBJ ? ? SING CAC HAC1 ? ? SING CAC HAC2 ? ? SING CAC HAC3 ? ? SING OAW CBF ? ? SING CBF CAO ? ? DOUB CBF CBE ? ? DOUB CAO CAK ? ? SING CAO HAO ? ? SING CAK CAJ ? ? SING CAK HAK ? ? DOUB CAJ CAN ? ? SING CAJ HAJ ? ? SING CAN CBE ? ? SING CAN HAN ? ? SING CBE CAU ? ? SING CAU CBG ? ? SING CAU HAU1 ? ? SING CAU HAU2 ? ? DOUB CBG CBA ? ? SING CBG CBH ? ? SING CBA CAB ? ? SING CBA NBK ? ? SING CAB HAB1 ? ? SING CAB HAB2 ? ? SING CAB HAB3 ? ? DOUB CBH CBI ? ? SING CBH CAT ? ? DOUB CAT CBC ? ? SING CAT HAT ? ? SING CBC CAR ? ? SING CBC OAX ? ? SING OAX CBL ? ? SING CBL FAH ? ? SING CBL FAI ? ? SING CBL FAG ? ? DOUB CAR CAS ? ? SING CAR HAR ? ? SING CAS CBI ? ? SING CAS HAS ? ? SING CBI NBK ? ? SING NBK CAZ ? ? SING CAZ CBD ? ? DOUB CAZ OAE ? ? DOUB CBD CAP ? ? SING CBD CAQ ? ? DOUB CAQ CAM ? ? SING CAQ HAQ ? ? SING CAM CBB ? ? SING CAM HAM ? ? SING CAP CAL ? ? SING CAP HAP ? ? DOUB CAL CBB ? ? SING CAL HAL ? ? SING CBB OAV ? ? SING OAV CAA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CAA HAA3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PPARgamma_LBD 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 $PPARgamma_LBD 'recombinant technology' . Escherichia coli . pET-46 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PPARgamma_LBD 1 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' $240 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_TROSY-HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $sample_1 save_ save_3D_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CA' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CA)CB' _Sample_label $sample_1 save_ save_3D_TROSY-HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY-HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY-HSQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7.4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 _Indirect_shift_ratio water C 13 protons ppm 4.7 na indirect . . . 0.251449530 water H 1 protons ppm 4.7 internal direct . . . 1 water N 15 protons ppm 4.7 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 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) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D TROSY-HNCO' '3D TROSY-HNCA' '3D TROSY-HN(CO)CA' '3D TROSY-HN(CA)CB' '3D TROSY-HN(COCA)CB' '3D 1H-15N NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PPARgamma_LBD _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 203 2 GLN C C 175.8236 0.0000 1 2 203 2 GLN CA C 55.3285 0.0000 1 3 203 2 GLN CB C 29.0897 0.0000 1 4 204 3 LEU H H 8.3790 0.0000 1 5 204 3 LEU C C 176.6334 0.0000 1 6 204 3 LEU CA C 54.5386 0.0000 1 7 204 3 LEU CB C 41.4190 0.0000 1 8 204 3 LEU N N 124.0369 0.0000 1 9 205 4 ASN H H 8.4588 0.0000 1 10 205 4 ASN CA C 50.9055 0.0000 1 11 205 4 ASN CB C 38.1294 0.0000 1 12 205 4 ASN N N 121.2531 0.0000 1 13 206 5 PRO C C 177.2527 0.0000 1 14 206 5 PRO CA C 63.2624 0.0000 1 15 206 5 PRO CB C 31.2474 0.0000 1 16 207 6 GLU H H 8.5933 0.0000 1 17 207 6 GLU C C 177.3758 0.0000 1 18 207 6 GLU CA C 56.2379 0.0000 1 19 207 6 GLU CB C 28.8681 0.0000 1 20 207 6 GLU N N 120.1802 0.0000 1 21 208 7 SER H H 8.2169 0.0000 1 22 208 7 SER C C 175.2928 0.0000 1 23 208 7 SER CA C 59.3104 0.0000 1 24 208 7 SER CB C 62.6585 0.0000 1 25 208 7 SER N N 117.1885 0.0000 1 26 209 8 ALA H H 8.3532 0.0000 1 27 209 8 ALA C C 179.4702 0.0000 1 28 209 8 ALA CA C 53.8111 0.0000 1 29 209 8 ALA CB C 17.7087 0.0000 1 30 209 8 ALA N N 125.0833 0.0000 1 31 210 9 ASP H H 7.9886 0.0000 1 32 210 9 ASP C C 178.6031 0.0000 1 33 210 9 ASP CA C 55.2457 0.0000 1 34 210 9 ASP CB C 39.8150 0.0000 1 35 210 9 ASP N N 119.4008 0.0000 1 36 211 10 LEU H H 8.0644 0.0000 1 37 211 10 LEU C C 181.2963 0.0000 1 38 211 10 LEU CA C 57.0919 0.0000 1 39 211 10 LEU CB C 41.5154 0.0000 1 40 211 10 LEU N N 122.7601 0.0000 1 41 212 11 ARG H H 8.2850 0.0000 1 42 212 11 ARG C C 179.1148 0.0000 1 43 212 11 ARG CA C 56.8359 0.0000 1 44 212 11 ARG CB C 26.8489 0.0000 1 45 212 11 ARG N N 120.9006 0.0000 1 46 213 12 ALA H H 8.1468 0.0000 1 47 213 12 ALA C C 180.8538 0.0000 1 48 213 12 ALA CA C 54.4683 0.0000 1 49 213 12 ALA CB C 16.9799 0.0000 1 50 213 12 ALA N N 125.1405 0.0000 1 51 214 13 LEU H H 7.9410 0.0000 1 52 214 13 LEU C C 177.9318 0.0000 1 53 214 13 LEU CA C 57.2862 0.0000 1 54 214 13 LEU CB C 40.6310 0.0000 1 55 214 13 LEU N N 121.6573 0.0000 1 56 215 14 ALA H H 7.5372 0.0000 1 57 215 14 ALA C C 179.7900 0.0000 1 58 215 14 ALA CA C 55.4400 0.0000 1 59 215 14 ALA CB C 18.2230 0.0000 1 60 215 14 ALA N N 120.4704 0.0000 1 61 216 15 LYS H H 7.9180 0.0000 1 62 216 15 LYS C C 177.5656 0.0000 1 63 216 15 LYS CA C 58.6466 0.0000 1 64 216 15 LYS CB C 31.3126 0.0000 1 65 216 15 LYS N N 120.2939 0.0000 1 66 217 16 HIS H H 8.3478 0.0000 1 67 217 16 HIS C C 179.3144 0.0000 1 68 217 16 HIS CA C 59.5431 0.0000 1 69 217 16 HIS CB C 30.5838 0.0000 1 70 217 16 HIS N N 120.3505 0.0000 1 71 218 17 LEU H H 8.4485 0.0000 1 72 218 17 LEU C C 178.5475 0.0000 1 73 218 17 LEU CA C 57.1224 0.0000 1 74 218 17 LEU CB C 38.8433 0.0000 1 75 218 17 LEU N N 119.2312 0.0000 1 76 219 18 TYR H H 8.2624 0.0000 1 77 219 18 TYR C C 176.7090 0.0000 1 78 219 18 TYR CA C 60.2303 0.0000 1 79 219 18 TYR CB C 36.7894 0.0000 1 80 219 18 TYR N N 120.8228 0.0000 1 81 220 19 ASP H H 8.7564 0.0000 1 82 220 19 ASP C C 179.6981 0.0000 1 83 220 19 ASP CA C 56.9943 0.0000 1 84 220 19 ASP CB C 39.3291 0.0000 1 85 220 19 ASP N N 119.9086 0.0000 1 86 221 20 SER H H 8.0084 0.0000 1 87 221 20 SER C C 176.4214 0.0000 1 88 221 20 SER CA C 60.7581 0.0000 1 89 221 20 SER CB C 61.8733 0.0000 1 90 221 20 SER N N 115.7027 0.0000 1 91 222 21 TYR H H 9.0967 0.0000 1 92 222 21 TYR C C 176.4701 0.0000 1 93 222 21 TYR CA C 60.5772 0.0000 1 94 222 21 TYR CB C 38.2123 0.0000 1 95 222 21 TYR N N 129.2664 0.0000 1 96 223 22 ILE H H 8.3859 0.0000 1 97 223 22 ILE C C 178.9435 0.0000 1 98 223 22 ILE CA C 61.3550 0.0000 1 99 223 22 ILE CB C 35.4423 0.0000 1 100 223 22 ILE N N 118.2591 0.0000 1 101 224 23 LYS H H 7.2404 0.0000 1 102 224 23 LYS C C 178.0742 0.0000 1 103 224 23 LYS CA C 57.9888 0.0000 1 104 224 23 LYS CB C 32.0413 0.0000 1 105 224 23 LYS N N 118.6249 0.0000 1 106 225 24 SER H H 7.5130 0.0000 1 107 225 24 SER C C 172.6691 0.0000 1 108 225 24 SER CA C 60.9850 0.0000 1 109 225 24 SER CB C 63.6311 0.0000 1 110 225 24 SER N N 114.6025 0.0000 1 111 226 25 PHE H H 7.3908 0.0000 1 112 226 25 PHE CA C 53.1723 0.0000 1 113 226 25 PHE CB C 37.3857 0.0000 1 114 226 25 PHE N N 118.4992 0.0000 1 115 227 26 PRO C C 177.6238 0.0000 1 116 227 26 PRO CA C 63.9986 0.0000 1 117 227 26 PRO CB C 31.7656 0.0000 1 118 228 27 LEU H H 7.7720 0.0000 1 119 228 27 LEU C C 174.8490 0.0000 1 120 228 27 LEU CA C 53.1676 0.0000 1 121 228 27 LEU CB C 39.8207 0.0000 1 122 228 27 LEU N N 119.6067 0.0000 1 123 229 28 THR H H 6.8794 0.0000 1 124 229 28 THR C C 173.8656 0.0000 1 125 229 28 THR CA C 59.6690 0.0000 1 126 229 28 THR CB C 69.2758 0.0000 1 127 229 28 THR N N 115.3492 0.0000 1 128 230 29 LYS H H 10.5531 0.0000 1 129 230 29 LYS C C 179.0464 0.0000 1 130 230 29 LYS CA C 60.5900 0.0000 1 131 230 29 LYS CB C 31.1742 0.0000 1 132 230 29 LYS N N 124.9321 0.0000 1 133 231 30 ALA H H 9.2912 0.0000 1 134 231 30 ALA C C 181.6342 0.0000 1 135 231 30 ALA CA C 54.7157 0.0000 1 136 231 30 ALA CB C 17.4449 0.0000 1 137 231 30 ALA N N 121.0778 0.0000 1 138 232 31 LYS H H 7.6334 0.0000 1 139 232 31 LYS C C 178.7784 0.0000 1 140 232 31 LYS CA C 58.6766 0.0000 1 141 232 31 LYS CB C 32.0561 0.0000 1 142 232 31 LYS N N 118.8857 0.0000 1 143 233 32 ALA H H 8.4219 0.0000 1 144 233 32 ALA C C 179.7939 0.0000 1 145 233 32 ALA CA C 54.9221 0.0000 1 146 233 32 ALA CB C 18.6804 0.0000 1 147 233 32 ALA N N 122.5660 0.0000 1 148 234 33 ARG H H 9.1660 0.0000 1 149 234 33 ARG C C 179.5718 0.0000 1 150 234 33 ARG CA C 57.5777 0.0000 1 151 234 33 ARG CB C 27.5685 0.0000 1 152 234 33 ARG N N 116.1888 0.0000 1 153 235 34 ALA H H 7.5275 0.0000 1 154 235 34 ALA C C 179.6916 0.0000 1 155 235 34 ALA CA C 54.7242 0.0000 1 156 235 34 ALA CB C 16.9799 0.0000 1 157 235 34 ALA N N 123.2397 0.0000 1 158 236 35 ILE H H 7.6421 0.0000 1 159 236 35 ILE C C 179.4197 0.0000 1 160 236 35 ILE CA C 64.5129 0.0000 1 161 236 35 ILE CB C 37.6834 0.0000 1 162 236 35 ILE N N 118.9518 0.0000 1 163 237 36 LEU H H 8.4688 0.0000 1 164 237 36 LEU C C 178.6940 0.0000 1 165 237 36 LEU CA C 56.8975 0.0000 1 166 237 36 LEU CB C 41.7584 0.0000 1 167 237 36 LEU N N 119.4103 0.0000 1 168 238 37 THR H H 7.7999 0.0000 1 169 238 37 THR C C 175.5306 0.0000 1 170 238 37 THR CA C 61.4645 0.0000 1 171 238 37 THR CB C 69.6949 0.0000 1 172 238 37 THR N N 107.8814 0.0000 1 173 239 38 GLY H H 7.5103 0.0000 1 174 239 38 GLY C C 174.7612 0.0000 1 175 239 38 GLY CA C 45.7670 0.0000 1 176 239 38 GLY N N 110.4869 0.0000 1 177 240 39 LYS H H 8.2316 0.0000 1 178 240 39 LYS C C 176.9113 0.0000 1 179 240 39 LYS CA C 55.4400 0.0000 1 180 240 39 LYS CB C 31.5555 0.0000 1 181 240 39 LYS N N 120.5504 0.0000 1 182 241 40 THR H H 7.8122 0.0000 1 183 241 40 THR CA C 60.5010 0.0000 1 184 241 40 THR CB C 68.9661 0.0000 1 185 241 40 THR N N 113.4095 0.0000 1 186 243 42 ASP C C 175.7610 0.0000 1 187 243 42 ASP CA C 54.3535 0.0000 1 188 243 42 ASP CB C 40.3008 0.0000 1 189 244 43 LYS H H 7.9244 0.0000 1 190 244 43 LYS C C 176.0147 0.0000 1 191 244 43 LYS CA C 55.0513 0.0000 1 192 244 43 LYS CB C 32.0633 0.0000 1 193 244 43 LYS N N 119.7354 0.0000 1 194 245 44 SER H H 8.0841 0.0000 1 195 245 44 SER CA C 56.4057 0.0000 1 196 245 44 SER CB C 62.2976 0.0000 1 197 245 44 SER N N 119.4100 0.0000 1 198 246 45 PRO C C 175.8375 0.0000 1 199 246 45 PRO CA C 62.1140 0.0000 1 200 246 45 PRO CB C 30.8005 0.0000 1 201 247 46 PHE H H 8.0476 0.0000 1 202 247 46 PHE C C 175.0488 0.0000 1 203 247 46 PHE CA C 58.2525 0.0000 1 204 247 46 PHE CB C 39.3291 0.0000 1 205 247 46 PHE N N 124.4036 0.0000 1 206 248 47 VAL H H 7.9953 0.0000 1 207 248 47 VAL C C 174.6154 0.0000 1 208 248 47 VAL CA C 62.5366 0.0000 1 209 248 47 VAL CB C 31.0740 0.0000 1 210 248 47 VAL N N 106.4262 0.0000 1 211 249 48 ILE H H 9.1973 0.0000 1 212 249 48 ILE C C 173.3840 0.0000 1 213 249 48 ILE CA C 60.6871 0.0000 1 214 249 48 ILE CB C 38.3574 0.0000 1 215 249 48 ILE N N 128.3176 0.0000 1 216 250 49 TYR H H 8.1340 0.0000 1 217 250 49 TYR C C 173.2892 0.0000 1 218 250 49 TYR CA C 54.3358 0.0000 1 219 250 49 TYR CB C 38.6003 0.0000 1 220 250 49 TYR N N 122.7490 0.0000 1 221 251 50 ASP H H 7.2438 0.0000 1 222 251 50 ASP C C 173.9100 0.0000 1 223 251 50 ASP CA C 52.3380 0.0000 1 224 251 50 ASP CB C 39.3835 0.0000 1 225 251 50 ASP N N 120.6722 0.0000 1 226 252 51 MET H H 8.4565 0.0000 1 227 252 51 MET C C 177.9824 0.0000 1 228 252 51 MET CA C 57.5811 0.0000 1 229 252 51 MET CB C 30.5568 0.0000 1 230 252 51 MET N N 117.3299 0.0000 1 231 253 52 ASN H H 8.0429 0.0000 1 232 253 52 ASN C C 177.6116 0.0000 1 233 253 52 ASN CA C 56.3162 0.0000 1 234 253 52 ASN CB C 37.6585 0.0000 1 235 253 52 ASN N N 118.6009 0.0000 1 236 254 53 SER H H 8.9136 0.0000 1 237 254 53 SER C C 177.8075 0.0000 1 238 254 53 SER CA C 61.2657 0.0000 1 239 254 53 SER CB C 62.1000 0.0000 1 240 254 53 SER N N 117.0190 0.0000 1 241 255 54 LEU H H 7.8302 0.0000 1 242 255 54 LEU C C 177.9148 0.0000 1 243 255 54 LEU CA C 58.4377 0.0000 1 244 255 54 LEU CB C 39.0895 0.0000 1 245 255 54 LEU N N 125.2881 0.0000 1 246 256 55 MET H H 7.8108 0.0000 1 247 256 55 MET C C 179.6405 0.0000 1 248 256 55 MET CA C 57.9594 0.0000 1 249 256 55 MET N N 117.4982 0.0000 1 250 257 56 MET H H 8.1422 0.0000 1 251 257 56 MET C C 178.4692 0.0000 1 252 257 56 MET CA C 57.4602 0.0000 1 253 257 56 MET CB C 32.0413 0.0000 1 254 257 56 MET N N 118.8925 0.0000 1 255 258 57 GLY H H 8.5256 0.0000 1 256 258 57 GLY C C 174.8504 0.0000 1 257 258 57 GLY CA C 46.0698 0.0000 1 258 258 57 GLY N N 109.5852 0.0000 1 259 259 58 GLU H H 8.1962 0.0000 1 260 259 58 GLU C C 177.7003 0.0000 1 261 259 58 GLU CA C 59.0564 0.0000 1 262 259 58 GLU N N 121.2538 0.0000 1 263 260 59 ASP H H 7.5792 0.0000 1 264 260 59 ASP CA C 59.0570 0.0000 1 265 260 59 ASP N N 117.0055 0.0000 1 266 261 60 LYS C C 179.1409 0.0000 1 267 262 61 ILE H H 8.3137 0.0000 1 268 262 61 ILE C C 178.7197 0.0000 1 269 262 61 ILE CA C 56.8004 0.0000 1 270 262 61 ILE CB C 41.5953 0.0000 1 271 262 61 ILE N N 118.6466 0.0000 1 272 263 62 LYS H H 7.8255 0.0000 1 273 263 62 LYS C C 176.2223 0.0000 1 274 263 62 LYS CA C 61.9997 0.0000 1 275 263 62 LYS N N 109.4700 0.0000 1 276 264 63 PHE H H 8.5024 0.0000 1 277 264 63 PHE C C 177.6992 0.0000 1 278 264 63 PHE CA C 55.4870 0.0000 1 279 264 63 PHE N N 124.2385 0.0000 1 280 265 64 LYS H H 8.1327 0.0000 1 281 265 64 LYS C C 176.5210 0.0000 1 282 265 64 LYS CA C 55.8475 0.0000 1 283 265 64 LYS CB C 28.4873 0.0000 1 284 265 64 LYS N N 118.8026 0.0000 1 285 266 65 HIS H H 7.6102 0.0000 1 286 266 65 HIS C C 176.6795 0.0000 1 287 266 65 HIS CA C 56.3228 0.0000 1 288 266 65 HIS CB C 29.1951 0.0000 1 289 266 65 HIS N N 117.1849 0.0000 1 290 267 66 ILE H H 8.0950 0.0000 1 291 267 66 ILE CA C 55.4551 0.0000 1 292 267 66 ILE CB C 40.5437 0.0000 1 293 267 66 ILE N N 120.5170 0.0000 1 294 274 73 SER C C 174.9993 0.0000 1 295 274 73 SER CA C 58.1764 0.0000 1 296 274 73 SER CB C 62.6313 0.0000 1 297 275 74 LYS H H 8.1257 0.0000 1 298 275 74 LYS C C 176.2281 0.0000 1 299 275 74 LYS CA C 55.3229 0.0000 1 300 275 74 LYS CB C 32.7701 0.0000 1 301 275 74 LYS N N 123.9788 0.0000 1 302 276 75 GLU H H 8.3733 0.0000 1 303 276 75 GLU C C 177.1246 0.0000 1 304 276 75 GLU CA C 55.5484 0.0000 1 305 276 75 GLU CB C 29.3691 0.0000 1 306 276 75 GLU N N 121.5441 0.0000 1 307 277 76 VAL H H 8.5527 0.0000 1 308 277 76 VAL C C 176.6071 0.0000 1 309 277 76 VAL CA C 66.4201 0.0000 1 310 277 76 VAL CB C 31.1652 0.0000 1 311 277 76 VAL N N 125.7041 0.0000 1 312 278 77 ALA H H 8.7303 0.0000 1 313 278 77 ALA C C 178.2592 0.0000 1 314 278 77 ALA CA C 55.2327 0.0000 1 315 278 77 ALA CB C 18.0439 0.0000 1 316 278 77 ALA N N 120.3239 0.0000 1 317 279 78 ILE H H 6.5114 0.0000 1 318 279 78 ILE C C 177.6982 0.0000 1 319 279 78 ILE CA C 62.3842 0.0000 1 320 279 78 ILE CB C 35.7349 0.0000 1 321 279 78 ILE N N 114.0596 0.0000 1 322 280 79 ARG H H 7.9021 0.0000 1 323 280 79 ARG C C 180.4155 0.0000 1 324 280 79 ARG CA C 59.6381 0.0000 1 325 280 79 ARG CB C 29.3176 0.0000 1 326 280 79 ARG N N 120.6445 0.0000 1 327 281 80 ILE H H 8.2971 0.0000 1 328 281 80 ILE C C 177.1310 0.0000 1 329 281 80 ILE CA C 63.8937 0.0000 1 330 281 80 ILE CB C 35.9867 0.0000 1 331 281 80 ILE N N 120.0750 0.0000 1 332 282 81 PHE H H 7.9361 0.0000 1 333 282 81 PHE C C 178.0703 0.0000 1 334 282 81 PHE CA C 60.6324 0.0000 1 335 282 81 PHE CB C 38.8433 0.0000 1 336 282 81 PHE N N 122.1806 0.0000 1 337 283 82 GLN H H 8.9267 0.0000 1 338 283 82 GLN C C 178.0010 0.0000 1 339 283 82 GLN CA C 58.7743 0.0000 1 340 283 82 GLN CB C 27.4257 0.0000 1 341 283 82 GLN N N 117.7525 0.0000 1 342 284 83 GLY H H 7.9224 0.0000 1 343 284 83 GLY C C 175.8017 0.0000 1 344 284 83 GLY CA C 47.0363 0.0000 1 345 284 83 GLY N N 109.0183 0.0000 1 346 285 84 CYS H H 7.4060 0.0000 1 347 285 84 CYS C C 176.2203 0.0000 1 348 285 84 CYS CA C 63.2483 0.0000 1 349 285 84 CYS CB C 24.7900 0.0000 1 350 285 84 CYS N N 121.2002 0.0000 1 351 286 85 GLN H H 7.2808 0.0000 1 352 286 85 GLN C C 177.7034 0.0000 1 353 286 85 GLN CA C 59.3576 0.0000 1 354 286 85 GLN CB C 28.2297 0.0000 1 355 286 85 GLN N N 118.4501 0.0000 1 356 287 86 PHE H H 8.0754 0.0000 1 357 287 86 PHE C C 178.7470 0.0000 1 358 287 86 PHE CA C 60.3782 0.0000 1 359 287 86 PHE CB C 37.0082 0.0000 1 360 287 86 PHE N N 117.7374 0.0000 1 361 288 87 ARG H H 7.7701 0.0000 1 362 288 87 ARG C C 178.1953 0.0000 1 363 288 87 ARG CA C 57.2797 0.0000 1 364 288 87 ARG CB C 27.9712 0.0000 1 365 288 87 ARG N N 121.0654 0.0000 1 366 289 88 SER H H 8.2469 0.0000 1 367 289 88 SER C C 175.5816 0.0000 1 368 289 88 SER CA C 61.6379 0.0000 1 369 289 88 SER CB C 62.8929 0.0000 1 370 289 88 SER N N 117.6847 0.0000 1 371 290 89 VAL H H 7.8255 0.0000 1 372 290 89 VAL C C 178.4390 0.0000 1 373 290 89 VAL CA C 66.6843 0.0000 1 374 290 89 VAL CB C 30.2983 0.0000 1 375 290 89 VAL N N 120.1247 0.0000 1 376 291 90 GLU H H 7.3196 0.0000 1 377 291 90 GLU C C 179.1946 0.0000 1 378 291 90 GLU CA C 58.6717 0.0000 1 379 291 90 GLU CB C 30.0397 0.0000 1 380 291 90 GLU N N 120.1641 0.0000 1 381 292 91 ALA H H 8.7543 0.0000 1 382 292 91 ALA C C 180.1186 0.0000 1 383 292 91 ALA CA C 54.0797 0.0000 1 384 292 91 ALA CB C 16.8111 0.0000 1 385 292 91 ALA N N 123.8590 0.0000 1 386 293 92 VAL H H 8.9022 0.0000 1 387 293 92 VAL C C 179.2750 0.0000 1 388 293 92 VAL CA C 66.7767 0.0000 1 389 293 92 VAL CB C 30.5657 0.0000 1 390 293 92 VAL N N 118.8623 0.0000 1 391 294 93 GLN H H 7.2483 0.0000 1 392 294 93 GLN C C 178.3336 0.0000 1 393 294 93 GLN CA C 58.5215 0.0000 1 394 294 93 GLN CB C 27.0983 0.0000 1 395 294 93 GLN N N 121.2671 0.0000 1 396 295 94 GLU H H 7.4131 0.0000 1 397 295 94 GLU C C 178.3044 0.0000 1 398 295 94 GLU CA C 58.6466 0.0000 1 399 295 94 GLU CB C 28.6404 0.0000 1 400 295 94 GLU N N 121.0876 0.0000 1 401 296 95 ILE H H 8.8429 0.0000 1 402 296 95 ILE C C 177.2933 0.0000 1 403 296 95 ILE CA C 64.7464 0.0000 1 404 296 95 ILE CB C 37.8716 0.0000 1 405 296 95 ILE N N 118.0720 0.0000 1 406 297 96 THR H H 8.1479 0.0000 1 407 297 96 THR C C 175.4519 0.0000 1 408 297 96 THR CA C 67.1545 0.0000 1 409 297 96 THR CB C 68.2998 0.0000 1 410 297 96 THR N N 117.3897 0.0000 1 411 298 97 GLU H H 7.4388 0.0000 1 412 298 97 GLU C C 179.3539 0.0000 1 413 298 97 GLU CA C 58.5428 0.0000 1 414 298 97 GLU CB C 28.1545 0.0000 1 415 298 97 GLU N N 120.5291 0.0000 1 416 299 98 TYR H H 7.9808 0.0000 1 417 299 98 TYR C C 178.7465 0.0000 1 418 299 98 TYR CA C 60.9001 0.0000 1 419 299 98 TYR CB C 38.1145 0.0000 1 420 299 98 TYR N N 121.4640 0.0000 1 421 300 99 ALA H H 8.9199 0.0000 1 422 300 99 ALA C C 178.2232 0.0000 1 423 300 99 ALA CA C 53.8853 0.0000 1 424 300 99 ALA CB C 16.8529 0.0000 1 425 300 99 ALA N N 123.1571 0.0000 1 426 301 100 LYS H H 7.1357 0.0000 1 427 301 100 LYS C C 178.1807 0.0000 1 428 301 100 LYS CA C 58.2502 0.0000 1 429 301 100 LYS CB C 31.3326 0.0000 1 430 301 100 LYS N N 111.2895 0.0000 1 431 302 101 SER H H 7.8230 0.0000 1 432 302 101 SER C C 175.0537 0.0000 1 433 302 101 SER CA C 58.4550 0.0000 1 434 302 101 SER CB C 63.3788 0.0000 1 435 302 101 SER N N 116.4463 0.0000 1 436 303 102 ILE H H 7.6956 0.0000 1 437 303 102 ILE CA C 60.0039 0.0000 1 438 303 102 ILE CB C 37.3857 0.0000 1 439 303 102 ILE N N 128.3087 0.0000 1 440 304 103 PRO C C 176.2166 0.0000 1 441 304 103 PRO CA C 64.5244 0.0000 1 442 304 103 PRO CB C 30.2983 0.0000 1 443 305 104 GLY H H 8.6195 0.0000 1 444 305 104 GLY C C 176.5857 0.0000 1 445 305 104 GLY CA C 44.7744 0.0000 1 446 305 104 GLY N N 112.4378 0.0000 1 447 306 105 PHE H H 8.2598 0.0000 1 448 306 105 PHE C C 176.9889 0.0000 1 449 306 105 PHE CA C 62.4362 0.0000 1 450 306 105 PHE CB C 40.0579 0.0000 1 451 306 105 PHE N N 124.4453 0.0000 1 452 307 106 VAL H H 8.2081 0.0000 1 453 307 106 VAL C C 175.9487 0.0000 1 454 307 106 VAL CA C 62.7208 0.0000 1 455 307 106 VAL CB C 30.3291 0.0000 1 456 307 106 VAL N N 107.3212 0.0000 1 457 308 107 ASN H H 7.0676 0.0000 1 458 308 107 ASN C C 175.8832 0.0000 1 459 308 107 ASN CA C 52.4278 0.0000 1 460 308 107 ASN CB C 38.6003 0.0000 1 461 308 107 ASN N N 116.7419 0.0000 1 462 309 108 LEU H H 7.1517 0.0000 1 463 309 108 LEU C C 177.5437 0.0000 1 464 309 108 LEU CA C 53.6910 0.0000 1 465 309 108 LEU CB C 41.2937 0.0000 1 466 309 108 LEU N N 121.0182 0.0000 1 467 310 109 ASP H H 9.0761 0.0000 1 468 310 109 ASP C C 177.5790 0.0000 1 469 310 109 ASP CA C 55.0261 0.0000 1 470 310 109 ASP CB C 42.4951 0.0000 1 471 310 109 ASP N N 124.1712 0.0000 1 472 311 110 LEU H H 8.5820 0.0000 1 473 311 110 LEU C C 179.0621 0.0000 1 474 311 110 LEU CA C 58.2523 0.0000 1 475 311 110 LEU CB C 41.2725 0.0000 1 476 311 110 LEU N N 128.3283 0.0000 1 477 312 111 ASN H H 8.6748 0.0000 1 478 312 111 ASN C C 178.0522 0.0000 1 479 312 111 ASN CA C 56.0667 0.0000 1 480 312 111 ASN CB C 37.6286 0.0000 1 481 312 111 ASN N N 115.6673 0.0000 1 482 313 112 ASP H H 7.5533 0.0000 1 483 313 112 ASP C C 177.9253 0.0000 1 484 313 112 ASP CA C 56.8360 0.0000 1 485 313 112 ASP CB C 38.9289 0.0000 1 486 313 112 ASP N N 120.8985 0.0000 1 487 314 113 GLN H H 8.0221 0.0000 1 488 314 113 GLN C C 178.2590 0.0000 1 489 314 113 GLN CA C 59.8487 0.0000 1 490 314 113 GLN CB C 28.2799 0.0000 1 491 314 113 GLN N N 119.8936 0.0000 1 492 315 114 VAL H H 7.4745 0.0000 1 493 315 114 VAL C C 179.4703 0.0000 1 494 315 114 VAL CA C 66.1015 0.0000 1 495 315 114 VAL CB C 30.9910 0.0000 1 496 315 114 VAL N N 117.1853 0.0000 1 497 316 115 THR H H 8.3423 0.0000 1 498 316 115 THR C C 176.0344 0.0000 1 499 316 115 THR CA C 66.5045 0.0000 1 500 316 115 THR CB C 67.8056 0.0000 1 501 316 115 THR N N 121.2013 0.0000 1 502 317 116 LEU H H 8.9305 0.0000 1 503 317 116 LEU C C 182.359 0.0000 1 504 317 116 LEU CA C 57.4892 0.0000 1 505 317 116 LEU CB C 39.5544 0.0000 1 506 317 116 LEU N N 120.4660 0.0000 1 507 318 117 LEU H H 8.0885 0.0000 1 508 318 117 LEU C C 177.3748 0.0000 1 509 318 117 LEU CA C 57.6549 0.0000 1 510 318 117 LEU CB C 40.3008 0.0000 1 511 318 117 LEU N N 120.5237 0.0000 1 512 319 118 LYS H H 8.5798 0.0000 1 513 319 118 LYS C C 176.2511 0.0000 1 514 319 118 LYS CA C 59.6475 0.0000 1 515 319 118 LYS CB C 32.5727 0.0000 1 516 319 118 LYS N N 122.6725 0.0000 1 517 320 119 TYR H H 7.4393 0.0000 1 518 320 119 TYR C C 176.9122 0.0000 1 519 320 119 TYR CA C 59.6512 0.0000 1 520 320 119 TYR CB C 39.0862 0.0000 1 521 320 119 TYR N N 109.3539 0.0000 1 522 321 120 GLY H H 8.0329 0.0000 1 523 321 120 GLY C C 176.0552 0.0000 1 524 321 120 GLY CA C 45.7647 0.0000 1 525 321 120 GLY N N 106.2208 0.0000 1 526 322 121 VAL H H 8.1368 0.0000 1 527 322 121 VAL C C 177.4277 0.0000 1 528 322 121 VAL CA C 67.0638 0.0000 1 529 322 121 VAL CB C 30.6202 0.0000 1 530 322 121 VAL N N 114.9511 0.0000 1 531 323 122 HIS H H 8.9739 0.0000 1 532 323 122 HIS C C 176.6022 0.0000 1 533 323 122 HIS CA C 63.9466 0.0000 1 534 323 122 HIS CB C 29.5477 0.0000 1 535 323 122 HIS N N 118.0481 0.0000 1 536 324 123 GLU H H 6.9784 0.0000 1 537 324 123 GLU C C 179.5058 0.0000 1 538 324 123 GLU CA C 59.2025 0.0000 1 539 324 123 GLU CB C 28.7469 0.0000 1 540 324 123 GLU N N 118.2398 0.0000 1 541 325 124 ILE H H 7.8086 0.0000 1 542 325 124 ILE C C 177.4019 0.0000 1 543 325 124 ILE CA C 64.2824 0.0000 1 544 325 124 ILE CB C 36.2562 0.0000 1 545 325 124 ILE N N 119.9713 0.0000 1 546 326 125 ILE H H 8.8563 0.0000 1 547 326 125 ILE C C 179.3559 0.0000 1 548 326 125 ILE CA C 65.5402 0.0000 1 549 326 125 ILE CB C 36.5038 0.0000 1 550 326 125 ILE N N 123.7121 0.0000 1 551 327 126 TYR H H 7.8301 0.0000 1 552 327 126 TYR C C 177.8367 0.0000 1 553 327 126 TYR CA C 59.8282 0.0000 1 554 327 126 TYR CB C 35.4696 0.0000 1 555 327 126 TYR N N 117.3051 0.0000 1 556 328 127 THR H H 7.4193 0.0000 1 557 328 127 THR C C 176.4091 0.0000 1 558 328 127 THR CA C 68.1970 0.0000 1 559 328 127 THR CB C 67.5592 0.0000 1 560 328 127 THR N N 118.9907 0.0000 1 561 329 128 MET H H 8.5629 0.0000 1 562 329 128 MET C C 179.2904 0.0000 1 563 329 128 MET CA C 58.2094 0.0000 1 564 329 128 MET CB C 31.5911 0.0000 1 565 329 128 MET N N 119.4462 0.0000 1 566 330 129 LEU H H 8.4986 0.0000 1 567 330 129 LEU C C 179.1840 0.0000 1 568 330 129 LEU CA C 56.6088 0.0000 1 569 330 129 LEU CB C 41.5532 0.0000 1 570 330 129 LEU N N 123.0655 0.0000 1 571 331 130 ALA H H 7.1681 0.0000 1 572 331 130 ALA C C 179.6154 0.0000 1 573 331 130 ALA CA C 55.1484 0.0000 1 574 331 130 ALA CB C 16.0351 0.0000 1 575 331 130 ALA N N 118.7970 0.0000 1 576 332 131 SER H H 7.2403 0.0000 1 577 332 131 SER C C 173.4624 0.0000 1 578 332 131 SER CA C 60.6597 0.0000 1 579 332 131 SER CB C 62.6743 0.0000 1 580 332 131 SER N N 112.4825 0.0000 1 581 333 132 LEU H H 7.6309 0.0000 1 582 333 132 LEU C C 174.9080 0.0000 1 583 333 132 LEU CA C 53.9801 0.0000 1 584 333 132 LEU CB C 41.0623 0.0000 1 585 333 132 LEU N N 119.1079 0.0000 1 586 334 133 MET H H 7.4703 0.0000 1 587 334 133 MET C C 176.8037 0.0000 1 588 334 133 MET CA C 54.7598 0.0000 1 589 334 133 MET CB C 36.6478 0.0000 1 590 334 133 MET N N 117.5213 0.0000 1 591 335 134 ASN H H 8.8054 0.0000 1 592 335 134 ASN C C 175.4538 0.0000 1 593 335 134 ASN CA C 51.2067 0.0000 1 594 335 134 ASN CB C 39.6099 0.0000 1 595 335 134 ASN N N 118.2599 0.0000 1 596 336 135 LYS H H 8.3546 0.0000 1 597 336 135 LYS C C 175.8770 0.0000 1 598 336 135 LYS CA C 58.1607 0.0000 1 599 336 135 LYS CB C 31.0702 0.0000 1 600 336 135 LYS N N 113.4210 0.0000 1 601 337 136 ASP H H 8.3292 0.0000 1 602 337 136 ASP C C 178.0392 0.0000 1 603 337 136 ASP CA C 54.4007 0.0000 1 604 337 136 ASP CB C 42.7382 0.0000 1 605 337 136 ASP N N 115.7596 0.0000 1 606 338 137 GLY H H 8.1619 0.0000 1 607 338 137 GLY C C 168.8457 0.0000 1 608 338 137 GLY CA C 47.7412 0.0000 1 609 338 137 GLY N N 111.5718 0.0000 1 610 339 138 VAL H H 8.0928 0.0000 1 611 339 138 VAL C C 172.4796 0.0000 1 612 339 138 VAL CA C 56.7603 0.0000 1 613 339 138 VAL CB C 35.9880 0.0000 1 614 339 138 VAL N N 116.6047 0.0000 1 615 340 139 LEU H H 8.6068 0.0000 1 616 340 139 LEU C C 176.0468 0.0000 1 617 340 139 LEU CA C 54.7430 0.0000 1 618 340 139 LEU CB C 43.2159 0.0000 1 619 340 139 LEU N N 127.6841 0.0000 1 620 341 140 ILE H H 8.3355 0.0000 1 621 341 140 ILE C C 176.5915 0.0000 1 622 341 140 ILE CA C 58.0560 0.0000 1 623 341 140 ILE CB C 41.1517 0.0000 1 624 341 140 ILE N N 113.4256 0.0000 1 625 342 141 SER H H 8.7240 0.0000 1 626 342 141 SER C C 179.2508 0.0000 1 627 342 141 SER CA C 57.9556 0.0000 1 628 342 141 SER CB C 61.4055 0.0000 1 629 342 141 SER N N 117.8753 0.0000 1 630 343 142 GLU H H 8.1869 0.0000 1 631 343 142 GLU C C 175.9740 0.0000 1 632 343 142 GLU CA C 56.9428 0.0000 1 633 343 142 GLU N N 119.3823 0.0000 1 634 344 143 GLY H H 7.8086 0.0000 1 635 344 143 GLY CA C 44.6982 0.0000 1 636 344 143 GLY N N 104.591 0.0000 1 637 345 144 GLN C C 176.9366 0.0000 1 638 345 144 GLN CA C 56.8221 0.0000 1 639 345 144 GLN CB C 30.0979 0.0000 1 640 346 145 GLY H H 7.9074 0.0000 1 641 346 145 GLY C C 171.1267 0.0000 1 642 346 145 GLY CA C 43.2353 0.0000 1 643 346 145 GLY N N 103.919 0.0000 1 644 347 146 PHE H H 8.9459 0.0000 1 645 347 146 PHE C C 172.8941 0.0000 1 646 347 146 PHE CA C 56.1202 0.0000 1 647 347 146 PHE CB C 41.5805 0.0000 1 648 347 146 PHE N N 123.6272 0.0000 1 649 348 147 MET H H 8.9239 0.0000 1 650 348 147 MET C C 175.4915 0.0000 1 651 348 147 MET CA C 53.4353 0.0000 1 652 348 147 MET CB C 35.2012 0.0000 1 653 348 147 MET N N 128.6424 0.0000 1 654 349 148 THR H H 8.5260 0.0000 1 655 349 148 THR C C 174.4056 0.0000 1 656 349 148 THR CA C 61.3667 0.0000 1 657 349 148 THR CB C 69.1975 0.0000 1 658 349 148 THR N N 116.2563 0.0000 1 659 350 149 ARG H H 8.6226 0.0000 1 660 350 149 ARG C C 178.9792 0.0000 1 661 350 149 ARG CA C 58.3361 0.0000 1 662 350 149 ARG CB C 30.3602 0.0000 1 663 350 149 ARG N N 126.2838 0.0000 1 664 351 150 GLU H H 8.5310 0.0000 1 665 351 150 GLU C C 178.5423 0.0000 1 666 351 150 GLU CA C 58.6183 0.0000 1 667 351 150 GLU CB C 28.5679 0.0000 1 668 351 150 GLU N N 118.2849 0.0000 1 669 352 151 PHE H H 7.9799 0.0000 1 670 352 151 PHE C C 179.1477 0.0000 1 671 352 151 PHE CA C 59.8748 0.0000 1 672 352 151 PHE CB C 37.8716 0.0000 1 673 352 151 PHE N N 121.9359 0.0000 1 674 353 152 LEU H H 7.6040 0.0000 1 675 353 152 LEU C C 177.5463 0.0000 1 676 353 152 LEU CA C 57.9581 0.0000 1 677 353 152 LEU CB C 40.7867 0.0000 1 678 353 152 LEU N N 121.2137 0.0000 1 679 354 153 LYS H H 7.7327 0.0000 1 680 354 153 LYS C C 177.2070 0.0000 1 681 354 153 LYS CA C 56.9535 0.0000 1 682 354 153 LYS CB C 32.0413 0.0000 1 683 354 153 LYS N N 116.7673 0.0000 1 684 355 154 SER H H 7.5290 0.0000 1 685 355 154 SER C C 174.3590 0.0000 1 686 355 154 SER CA C 58.6253 0.0000 1 687 355 154 SER CB C 63.3788 0.0000 1 688 355 154 SER N N 114.2228 0.0000 1 689 356 155 LEU H H 6.7968 0.0000 1 690 356 155 LEU C C 176.4062 0.0000 1 691 356 155 LEU CA C 53.9825 0.0000 1 692 356 155 LEU CB C 41.2725 0.0000 1 693 356 155 LEU N N 122.4855 0.0000 1 694 357 156 ARG H H 8.5459 0.0000 1 695 357 156 ARG C C 176.5200 0.0000 1 696 357 156 ARG CA C 54.9498 0.0000 1 697 357 156 ARG CB C 28.8833 0.0000 1 698 357 156 ARG N N 119.5486 0.0000 1 699 358 157 LYS H H 8.5945 0.0000 1 700 358 157 LYS CA C 54.9543 0.0000 1 701 358 157 LYS CB C 30.5838 0.0000 1 702 358 157 LYS N N 123.6600 0.0000 1 703 359 158 PRO C C 175.6241 0.0000 1 704 359 158 PRO CA C 63.3283 0.0000 1 705 359 158 PRO CB C 32.2843 0.0000 1 706 360 159 PHE H H 8.5536 0.0000 1 707 360 159 PHE C C 176.8037 0.0000 1 708 360 159 PHE CA C 61.0264 0.0000 1 709 360 159 PHE CB C 38.4705 0.0000 1 710 360 159 PHE N N 123.7984 0.0000 1 711 361 160 GLY H H 7.3229 0.0000 1 712 361 160 GLY C C 174.7427 0.0000 1 713 361 160 GLY CA C 46.5635 0.0000 1 714 361 160 GLY N N 106.9514 0.0000 1 715 362 161 ASP H H 7.5270 0.0000 1 716 362 161 ASP C C 178.4198 0.0000 1 717 362 161 ASP CA C 53.9865 0.0000 1 718 362 161 ASP CB C 41.1580 0.0000 1 719 362 161 ASP N N 117.8206 0.0000 1 720 363 162 PHE H H 7.7371 0.0000 1 721 363 162 PHE C C 176.2283 0.0000 1 722 363 162 PHE CA C 59.9533 0.0000 1 723 363 162 PHE CB C 38.9604 0.0000 1 724 363 162 PHE N N 119.7103 0.0000 1 725 364 163 MET H H 8.7231 0.0000 1 726 364 163 MET C C 179.1485 0.0000 1 727 364 163 MET CA C 53.4286 0.0000 1 728 364 163 MET CB C 30.2983 0.0000 1 729 364 163 MET N N 117.5704 0.0000 1 730 365 164 GLU H H 8.0354 0.0000 1 731 365 164 GLU CA C 60.3127 0.0000 1 732 365 164 GLU CB C 27.1828 0.0000 1 733 365 164 GLU N N 124.9497 0.0000 1 734 366 165 PRO C C 179.7149 0.0000 1 735 366 165 PRO CA C 64.7854 0.0000 1 736 366 165 PRO CB C 30.5838 0.0000 1 737 367 166 LYS H H 7.1668 0.0000 1 738 367 166 LYS C C 178.3583 0.0000 1 739 367 166 LYS CA C 60.2910 0.0000 1 740 367 166 LYS CB C 30.5738 0.0000 1 741 367 166 LYS N N 117.8715 0.0000 1 742 368 167 PHE H H 8.0201 0.0000 1 743 368 167 PHE C C 178.5972 0.0000 1 744 368 167 PHE CA C 62.2271 0.0000 1 745 368 167 PHE CB C 38.6075 0.0000 1 746 368 167 PHE N N 119.3650 0.0000 1 747 369 168 GLU H H 8.3116 0.0000 1 748 369 168 GLU C C 179.7618 0.0000 1 749 369 168 GLU CA C 58.7282 0.0000 1 750 369 168 GLU CB C 28.7469 0.0000 1 751 369 168 GLU N N 117.7472 0.0000 1 752 370 169 PHE H H 7.6130 0.0000 1 753 370 169 PHE C C 176.8081 0.0000 1 754 370 169 PHE CA C 60.3956 0.0000 1 755 370 169 PHE CB C 38.3574 0.0000 1 756 370 169 PHE N N 119.1751 0.0000 1 757 371 170 ALA H H 8.4710 0.0000 1 758 371 170 ALA C C 179.0446 0.0000 1 759 371 170 ALA CA C 55.3489 0.0000 1 760 371 170 ALA CB C 20.0303 0.0000 1 761 371 170 ALA N N 123.1089 0.0000 1 762 372 171 VAL H H 8.2691 0.0000 1 763 372 171 VAL C C 179.5966 0.0000 1 764 372 171 VAL CA C 65.9368 0.0000 1 765 372 171 VAL CB C 31.0740 0.0000 1 766 372 171 VAL N N 116.5761 0.0000 1 767 373 172 LYS H H 6.8119 0.0000 1 768 373 172 LYS C C 178.7111 0.0000 1 769 373 172 LYS CA C 58.2003 0.0000 1 770 373 172 LYS CB C 31.9355 0.0000 1 771 373 172 LYS N N 118.9804 0.0000 1 772 374 173 PHE H H 8.8801 0.0000 1 773 374 173 PHE C C 179.4748 0.0000 1 774 374 173 PHE CA C 61.3184 0.0000 1 775 374 173 PHE CB C 39.8150 0.0000 1 776 374 173 PHE N N 123.2680 0.0000 1 777 375 174 ASN H H 9.5037 0.0000 1 778 375 174 ASN C C 179.0451 0.0000 1 779 375 174 ASN CA C 54.1066 0.0000 1 780 375 174 ASN CB C 36.5038 0.0000 1 781 375 174 ASN N N 119.9655 0.0000 1 782 376 175 ALA H H 7.0555 0.0000 1 783 376 175 ALA C C 178.1682 0.0000 1 784 376 175 ALA CA C 53.2121 0.0000 1 785 376 175 ALA CB C 16.8529 0.0000 1 786 376 175 ALA N N 123.4909 0.0000 1 787 377 176 LEU H H 7.2037 0.0000 1 788 377 176 LEU C C 175.9942 0.0000 1 789 377 176 LEU CA C 55.2711 0.0000 1 790 377 176 LEU CB C 39.6066 0.0000 1 791 377 176 LEU N N 116.2026 0.0000 1 792 378 177 GLU H H 7.3435 0.0000 1 793 378 177 GLU C C 175.5169 0.0000 1 794 378 177 GLU CA C 55.9827 0.0000 1 795 378 177 GLU CB C 25.7253 0.0000 1 796 378 177 GLU N N 110.1182 0.0000 1 797 379 178 LEU H H 7.9730 0.0000 1 798 379 178 LEU C C 178.4623 0.0000 1 799 379 178 LEU CA C 54.4683 0.0000 1 800 379 178 LEU CB C 40.5437 0.0000 1 801 379 178 LEU N N 116.4374 0.0000 1 802 380 179 ASP H H 9.6363 0.0000 1 803 380 179 ASP C C 176.8953 0.0000 1 804 380 179 ASP CA C 50.9843 0.0000 1 805 380 179 ASP CB C 42.2442 0.0000 1 806 380 179 ASP N N 123.0407 0.0000 1 807 381 180 ASP H H 8.7801 0.0000 1 808 381 180 ASP C C 176.2225 0.0000 1 809 381 180 ASP CA C 58.5447 0.0000 1 810 381 180 ASP CB C 43.4589 0.0000 1 811 381 180 ASP N N 116.9520 0.0000 1 812 382 181 SER H H 8.1523 0.0000 1 813 382 181 SER C C 176.5576 0.0000 1 814 382 181 SER CA C 61.1961 0.0000 1 815 382 181 SER CB C 62.4071 0.0000 1 816 382 181 SER N N 116.2015 0.0000 1 817 383 182 ASP H H 7.5705 0.0000 1 818 383 182 ASP C C 179.1709 0.0000 1 819 383 182 ASP CA C 56.5874 0.0000 1 820 383 182 ASP CB C 42.6140 0.0000 1 821 383 182 ASP N N 123.2773 0.0000 1 822 384 183 LEU H H 8.5492 0.0000 1 823 384 183 LEU C C 178.3990 0.0000 1 824 384 183 LEU CA C 57.3427 0.0000 1 825 384 183 LEU CB C 41.4768 0.0000 1 826 384 183 LEU N N 120.4764 0.0000 1 827 385 184 ALA H H 8.1127 0.0000 1 828 385 184 ALA C C 180.2648 0.0000 1 829 385 184 ALA CA C 54.9542 0.0000 1 830 385 184 ALA CB C 16.4684 0.0000 1 831 385 184 ALA N N 118.8658 0.0000 1 832 386 185 ILE H H 7.0144 0.0000 1 833 386 185 ILE CA C 63.4039 0.0000 1 834 386 185 ILE CB C 37.6286 0.0000 1 835 386 185 ILE N N 114.5756 0.0000 1 836 391 190 ILE C C 178.9694 0.0000 1 837 391 190 ILE CA C 64.5739 0.0000 1 838 392 191 ILE H H 7.4566 0.0000 1 839 392 191 ILE C C 177.5885 0.0000 1 840 392 191 ILE CA C 64.6889 0.0000 1 841 392 191 ILE CB C 36.2087 0.0000 1 842 392 191 ILE N N 117.5778 0.0000 1 843 393 192 LEU H H 7.4808 0.0000 1 844 393 192 LEU C C 173.3381 0.0000 1 845 393 192 LEU CA C 51.0674 0.0000 1 846 393 192 LEU CB C 34.9815 0.0000 1 847 393 192 LEU N N 125.8278 0.0000 1 848 394 193 SER H H 6.8496 0.0000 1 849 394 193 SER C C 174.2861 0.0000 1 850 394 193 SER CA C 57.9659 0.0000 1 851 394 193 SER CB C 63.8882 0.0000 1 852 394 193 SER N N 113.8627 0.0000 1 853 395 194 GLY H H 8.5678 0.0000 1 854 395 194 GLY C C 172.8902 0.0000 1 855 395 194 GLY CA C 45.2373 0.0000 1 856 395 194 GLY N N 111.7391 0.0000 1 857 396 195 ASP H H 8.1288 0.0000 1 858 396 195 ASP C C 176.7691 0.0000 1 859 396 195 ASP CA C 51.9262 0.0000 1 860 396 195 ASP CB C 39.0862 0.0000 1 861 396 195 ASP N N 116.8905 0.0000 1 862 397 196 ARG H H 6.6188 0.0000 1 863 397 196 ARG CA C 51.9336 0.0000 1 864 397 196 ARG CB C 26.6451 0.0000 1 865 397 196 ARG N N 116.4065 0.0000 1 866 398 197 PRO C C 177.4211 0.0000 1 867 398 197 PRO CA C 62.5453 0.0000 1 868 398 197 PRO CB C 31.0740 0.0000 1 869 399 198 GLY H H 8.3977 0.0000 1 870 399 198 GLY C C 176.1169 0.0000 1 871 399 198 GLY CA C 44.9786 0.0000 1 872 399 198 GLY N N 107.6208 0.0000 1 873 400 199 LEU H H 6.7787 0.0000 1 874 400 199 LEU C C 177.2437 0.0000 1 875 400 199 LEU CA C 54.2527 0.0000 1 876 400 199 LEU CB C 42.1588 0.0000 1 877 400 199 LEU N N 120.0934 0.0000 1 878 401 200 LEU H H 11.5426 0.0000 1 879 401 200 LEU C C 178.8780 0.0000 1 880 401 200 LEU CA C 56.2459 0.0000 1 881 401 200 LEU CB C 41.4166 0.0000 1 882 401 200 LEU N N 128.0888 0.0000 1 883 402 201 ASN H H 8.9941 0.0000 1 884 402 201 ASN C C 174.6736 0.0000 1 885 402 201 ASN CA C 50.6322 0.0000 1 886 402 201 ASN CB C 37.7600 0.0000 1 887 402 201 ASN N N 120.1669 0.0000 1 888 403 202 VAL H H 8.3282 0.0000 1 889 403 202 VAL C C 177.5461 0.0000 1 890 403 202 VAL CA C 65.6428 0.0000 1 891 403 202 VAL CB C 31.7984 0.0000 1 892 403 202 VAL N N 122.4561 0.0000 1 893 404 203 LYS H H 8.2640 0.0000 1 894 404 203 LYS CA C 60.1668 0.0000 1 895 404 203 LYS CB C 28.3974 0.0000 1 896 404 203 LYS N N 121.4510 0.0000 1 897 405 204 PRO C C 179.5008 0.0000 1 898 405 204 PRO CA C 64.8654 0.0000 1 899 405 204 PRO CB C 30.0979 0.0000 1 900 406 205 ILE H H 6.7527 0.0000 1 901 406 205 ILE C C 177.1305 0.0000 1 902 406 205 ILE CA C 64.7284 0.0000 1 903 406 205 ILE CB C 37.9006 0.0000 1 904 406 205 ILE N N 118.4787 0.0000 1 905 407 206 GLU H H 8.1160 0.0000 1 906 407 206 GLU C C 179.4197 0.0000 1 907 407 206 GLU CA C 58.8824 0.0000 1 908 407 206 GLU CB C 28.7327 0.0000 1 909 407 206 GLU N N 120.3550 0.0000 1 910 408 207 ASP H H 8.4593 0.0000 1 911 408 207 ASP C C 179.5868 0.0000 1 912 408 207 ASP CA C 57.0533 0.0000 1 913 408 207 ASP CB C 39.5681 0.0000 1 914 408 207 ASP N N 119.2102 0.0000 1 915 409 208 ILE H H 7.4280 0.0000 1 916 409 208 ILE C C 179.0774 0.0000 1 917 409 208 ILE CA C 64.8529 0.0000 1 918 409 208 ILE CB C 37.8322 0.0000 1 919 409 208 ILE N N 121.0057 0.0000 1 920 410 209 GLN H H 9.0722 0.0000 1 921 410 209 GLN C C 178.3044 0.0000 1 922 410 209 GLN CA C 59.4729 0.0000 1 923 410 209 GLN CB C 27.4257 0.0000 1 924 410 209 GLN N N 121.8190 0.0000 1 925 411 210 ASP H H 8.8692 0.0000 1 926 411 210 ASP C C 178.7771 0.0000 1 927 411 210 ASP CA C 57.4806 0.0000 1 928 411 210 ASP CB C 40.7067 0.0000 1 929 411 210 ASP N N 118.2613 0.0000 1 930 412 211 ASN H H 7.1667 0.0000 1 931 412 211 ASN C C 177.6388 0.0000 1 932 412 211 ASN CA C 56.0409 0.0000 1 933 412 211 ASN CB C 38.6003 0.0000 1 934 412 211 ASN N N 118.2925 0.0000 1 935 413 212 LEU H H 8.2837 0.0000 1 936 413 212 LEU C C 179.0672 0.0000 1 937 413 212 LEU CA C 57.3624 0.0000 1 938 413 212 LEU CB C 41.9965 0.0000 1 939 413 212 LEU N N 119.7723 0.0000 1 940 414 213 LEU H H 9.3297 0.0000 1 941 414 213 LEU C C 180.0100 0.0000 1 942 414 213 LEU CA C 57.9344 0.0000 1 943 414 213 LEU CB C 41.2666 0.0000 1 944 414 213 LEU N N 121.7657 0.0000 1 945 415 214 GLN H H 7.9703 0.0000 1 946 415 214 GLN C C 179.9591 0.0000 1 947 415 214 GLN CA C 58.6466 0.0000 1 948 415 214 GLN CB C 28.3279 0.0000 1 949 415 214 GLN N N 119.4240 0.0000 1 950 416 215 ALA H H 8.4093 0.0000 1 951 416 215 ALA C C 179.9811 0.0000 1 952 416 215 ALA CA C 54.3712 0.0000 1 953 416 215 ALA CB C 16.4941 0.0000 1 954 416 215 ALA N N 122.7486 0.0000 1 955 417 216 LEU H H 9.1117 0.0000 1 956 417 216 LEU C C 176.6472 0.0000 1 957 417 216 LEU CA C 57.2528 0.0000 1 958 417 216 LEU CB C 40.5624 0.0000 1 959 417 216 LEU N N 122.5602 0.0000 1 960 418 217 GLU H H 8.4775 0.0000 1 961 418 217 GLU C C 178.6324 0.0000 1 962 418 217 GLU CA C 59.8089 0.0000 1 963 418 217 GLU CB C 27.9357 0.0000 1 964 418 217 GLU N N 121.1516 0.0000 1 965 419 218 LEU H H 7.4030 0.0000 1 966 419 218 LEU C C 177.5060 0.0000 1 967 419 218 LEU CA C 57.2627 0.0000 1 968 419 218 LEU CB C 40.5437 0.0000 1 969 419 218 LEU N N 118.6725 0.0000 1 970 420 219 GLN H H 7.9596 0.0000 1 971 420 219 GLN C C 178.0548 0.0000 1 972 420 219 GLN CA C 57.6443 0.0000 1 973 420 219 GLN CB C 26.7132 0.0000 1 974 420 219 GLN N N 118.5921 0.0000 1 975 421 220 LEU H H 8.5068 0.0000 1 976 421 220 LEU C C 179.5138 0.0000 1 977 421 220 LEU CA C 57.5777 0.0000 1 978 421 220 LEU CB C 40.0579 0.0000 1 979 421 220 LEU N N 117.1872 0.0000 1 980 422 221 LYS H H 7.7897 0.0000 1 981 422 221 LYS C C 178.5606 0.0000 1 982 422 221 LYS CA C 58.6466 0.0000 1 983 422 221 LYS CB C 31.3840 0.0000 1 984 422 221 LYS N N 121.0077 0.0000 1 985 423 222 LEU H H 7.9265 0.0000 1 986 423 222 LEU C C 179.2090 0.0000 1 987 423 222 LEU CA C 56.0179 0.0000 1 988 423 222 LEU CB C 41.2725 0.0000 1 989 423 222 LEU N N 116.9378 0.0000 1 990 424 223 ASN H H 8.4296 0.0000 1 991 424 223 ASN C C 175.1535 0.0000 1 992 424 223 ASN CA C 52.6721 0.0000 1 993 424 223 ASN CB C 40.0579 0.0000 1 994 424 223 ASN N N 116.0151 0.0000 1 995 425 224 HIS H H 7.7121 0.0000 1 996 425 224 HIS CA C 51.6175 0.0000 1 997 425 224 HIS CB C 28.1545 0.0000 1 998 425 224 HIS N N 114.9231 0.0000 1 999 426 225 PRO C C 178.0703 0.0000 1 1000 426 225 PRO CA C 64.3140 0.0000 1 1001 426 225 PRO CB C 31.0276 0.0000 1 1002 427 226 GLU H H 8.9412 0.0000 1 1003 427 226 GLU C C 176.5217 0.0000 1 1004 427 226 GLU CA C 55.9255 0.0000 1 1005 427 226 GLU CB C 27.9116 0.0000 1 1006 427 226 GLU N N 117.5623 0.0000 1 1007 428 227 SER H H 7.5735 0.0000 1 1008 428 227 SER CA C 56.3541 0.0000 1 1009 428 227 SER CB C 62.3612 0.0000 1 1010 428 227 SER N N 116.9765 0.0000 1 1011 430 229 GLN C C 175.4088 0.0000 1 1012 430 229 GLN CA C 55.5296 0.0000 1 1013 430 229 GLN CB C 26.9399 0.0000 1 1014 431 230 LEU H H 7.1870 0.0000 1 1015 431 230 LEU C C 177.3614 0.0000 1 1016 431 230 LEU CA C 57.7721 0.0000 1 1017 431 230 LEU CB C 40.5437 0.0000 1 1018 431 230 LEU N N 121.1314 0.0000 1 1019 432 231 PHE H H 8.6067 0.0000 1 1020 432 231 PHE C C 175.8535 0.0000 1 1021 432 231 PHE CA C 60.7843 0.0000 1 1022 432 231 PHE CB C 37.8807 0.0000 1 1023 432 231 PHE N N 118.6093 0.0000 1 1024 433 232 ALA H H 7.9372 0.0000 1 1025 433 232 ALA C C 181.4068 0.0000 1 1026 433 232 ALA CA C 54.5693 0.0000 1 1027 433 232 ALA CB C 17.4658 0.0000 1 1028 433 232 ALA N N 120.1563 0.0000 1 1029 434 233 LYS H H 8.0872 0.0000 1 1030 434 233 LYS C C 179.7402 0.0000 1 1031 434 233 LYS CA C 58.6843 0.0000 1 1032 434 233 LYS CB C 31.8497 0.0000 1 1033 434 233 LYS N N 117.9494 0.0000 1 1034 435 234 LEU H H 8.6520 0.0000 1 1035 435 234 LEU C C 178.7906 0.0000 1 1036 435 234 LEU CA C 56.9947 0.0000 1 1037 435 234 LEU CB C 40.3008 0.0000 1 1038 435 234 LEU N N 122.3696 0.0000 1 1039 436 235 LEU H H 8.0156 0.0000 1 1040 436 235 LEU C C 181.6847 0.0000 1 1041 436 235 LEU CA C 57.5777 0.0000 1 1042 436 235 LEU CB C 39.3481 0.0000 1 1043 436 235 LEU N N 118.8501 0.0000 1 1044 437 236 GLN H H 7.5189 0.0000 1 1045 437 236 GLN C C 178.5570 0.0000 1 1046 437 236 GLN CA C 58.0274 0.0000 1 1047 437 236 GLN CB C 27.6687 0.0000 1 1048 437 236 GLN N N 118.6266 0.0000 1 1049 438 237 LYS H H 7.8795 0.0000 1 1050 438 237 LYS C C 178.6457 0.0000 1 1051 438 237 LYS CA C 55.9259 0.0000 1 1052 438 237 LYS CB C 30.0979 0.0000 1 1053 438 237 LYS N N 116.5892 0.0000 1 1054 439 238 MET H H 7.8899 0.0000 1 1055 439 238 MET C C 178.7900 0.0000 1 1056 439 238 MET CA C 59.8476 0.0000 1 1057 439 238 MET CB C 32.0821 0.0000 1 1058 439 238 MET N N 117.5121 0.0000 1 1059 440 239 THR H H 7.5062 0.0000 1 1060 440 239 THR C C 176.9316 0.0000 1 1061 440 239 THR CA C 65.6428 0.0000 1 1062 440 239 THR CB C 67.7914 0.0000 1 1063 440 239 THR N N 116.0894 0.0000 1 1064 441 240 ASP H H 7.6390 0.0000 1 1065 441 240 ASP C C 178.9401 0.0000 1 1066 441 240 ASP CA C 56.9947 0.0000 1 1067 441 240 ASP CB C 39.8652 0.0000 1 1068 441 240 ASP N N 123.8726 0.0000 1 1069 442 241 LEU H H 8.1143 0.0000 1 1070 442 241 LEU C C 178.1065 0.0000 1 1071 442 241 LEU CA C 57.3850 0.0000 1 1072 442 241 LEU CB C 42.4396 0.0000 1 1073 442 241 LEU N N 120.7035 0.0000 1 1074 443 242 ARG H H 7.2976 0.0000 1 1075 443 242 ARG C C 179.3555 0.0000 1 1076 443 242 ARG CA C 59.0039 0.0000 1 1077 443 242 ARG CB C 28.3974 0.0000 1 1078 443 242 ARG N N 117.6931 0.0000 1 1079 444 243 GLN H H 7.5226 0.0000 1 1080 444 243 GLN C C 178.0824 0.0000 1 1081 444 243 GLN CA C 57.9653 0.0000 1 1082 444 243 GLN CB C 27.0914 0.0000 1 1083 444 243 GLN N N 119.4287 0.0000 1 1084 445 244 ILE H H 7.7966 0.0000 1 1085 445 244 ILE C C 179.7937 0.0000 1 1086 445 244 ILE CA C 63.4821 0.0000 1 1087 445 244 ILE CB C 36.0449 0.0000 1 1088 445 244 ILE N N 119.4300 0.0000 1 1089 446 245 VAL H H 7.7790 0.0000 1 1090 446 245 VAL C C 177.8052 0.0000 1 1091 446 245 VAL CA C 67.1975 0.0000 1 1092 446 245 VAL CB C 30.8558 0.0000 1 1093 446 245 VAL N N 121.8322 0.0000 1 1094 447 246 THR H H 8.3325 0.0000 1 1095 447 246 THR C C 177.7067 0.0000 1 1096 447 246 THR CA C 66.5173 0.0000 1 1097 447 246 THR CB C 67.8335 0.0000 1 1098 447 246 THR N N 115.9033 0.0000 1 1099 448 247 GLU H H 8.3864 0.0000 1 1100 448 247 GLU C C 179.2374 0.0000 1 1101 448 247 GLU CA C 58.7160 0.0000 1 1102 448 247 GLU CB C 29.0054 0.0000 1 1103 448 247 GLU N N 121.6555 0.0000 1 1104 449 248 HIS H H 8.1974 0.0000 1 1105 449 248 HIS C C 177.2338 0.0000 1 1106 449 248 HIS CA C 60.0552 0.0000 1 1107 449 248 HIS N N 123.8620 0.0000 1 1108 450 249 VAL H H 8.6067 0.0000 1 1109 450 249 VAL C C 178.7117 0.0000 1 1110 450 249 VAL CA C 66.7410 0.0000 1 1111 450 249 VAL CB C 30.8154 0.0000 1 1112 450 249 VAL N N 119.4299 0.0000 1 1113 451 250 GLN H H 7.5596 0.0000 1 1114 451 250 GLN C C 179.0182 0.0000 1 1115 451 250 GLN CA C 58.3750 0.0000 1 1116 451 250 GLN CB C 26.9399 0.0000 1 1117 451 250 GLN N N 118.8054 0.0000 1 1118 452 251 LEU H H 7.7070 0.0000 1 1119 452 251 LEU C C 179.2130 0.0000 1 1120 452 251 LEU CA C 57.2155 0.0000 1 1121 452 251 LEU CB C 39.6517 0.0000 1 1122 452 251 LEU N N 123.6062 0.0000 1 1123 453 252 LEU H H 8.4039 0.0000 1 1124 453 252 LEU C C 179.2208 0.0000 1 1125 453 252 LEU CA C 57.0919 0.0000 1 1126 453 252 LEU CB C 40.5437 0.0000 1 1127 453 252 LEU N N 120.0951 0.0000 1 1128 454 253 GLN H H 7.6277 0.0000 1 1129 454 253 GLN C C 178.8565 0.0000 1 1130 454 253 GLN CA C 58.0055 0.0000 1 1131 454 253 GLN CB C 27.1266 0.0000 1 1132 454 253 GLN N N 117.7051 0.0000 1 1133 455 254 VAL H H 7.3462 0.0000 1 1134 455 254 VAL C C 179.7561 0.0000 1 1135 455 254 VAL CA C 65.7399 0.0000 1 1136 455 254 VAL CB C 30.8267 0.0000 1 1137 455 254 VAL N N 121.2170 0.0000 1 1138 456 255 ILE H H 8.2562 0.0000 1 1139 456 255 ILE C C 177.3557 0.0000 1 1140 456 255 ILE CA C 65.1724 0.0000 1 1141 456 255 ILE CB C 37.0060 0.0000 1 1142 456 255 ILE N N 122.7362 0.0000 1 1143 457 256 LYS H H 8.1459 0.0000 1 1144 457 256 LYS C C 177.8285 0.0000 1 1145 457 256 LYS CA C 58.1662 0.0000 1 1146 457 256 LYS CB C 31.5648 0.0000 1 1147 457 256 LYS N N 118.7372 0.0000 1 1148 458 257 LYS H H 7.3177 0.0000 1 1149 458 257 LYS C C 177.9318 0.0000 1 1150 458 257 LYS CA C 57.4806 0.0000 1 1151 458 257 LYS CB C 32.2263 0.0000 1 1152 458 257 LYS N N 115.9120 0.0000 1 1153 459 258 THR H H 7.5360 0.0000 1 1154 459 258 THR C C 175.0035 0.0000 1 1155 459 258 THR CA C 62.6753 0.0000 1 1156 459 258 THR CB C 69.9378 0.0000 1 1157 459 258 THR N N 108.8593 0.0000 1 1158 460 259 GLU H H 8.2091 0.0000 1 1159 460 259 GLU C C 176.6141 0.0000 1 1160 460 259 GLU CA C 53.8853 0.0000 1 1161 460 259 GLU CB C 27.6687 0.0000 1 1162 460 259 GLU N N 123.2496 0.0000 1 1163 461 260 THR H H 8.0276 0.0000 1 1164 461 260 THR C C 175.2148 0.0000 1 1165 461 260 THR CA C 63.6424 0.0000 1 1166 461 260 THR CB C 68.4802 0.0000 1 1167 461 260 THR N N 115.6525 0.0000 1 1168 462 261 ASP H H 8.5518 0.0000 1 1169 462 261 ASP C C 175.3439 0.0000 1 1170 462 261 ASP CA C 53.5938 0.0000 1 1171 462 261 ASP CB C 40.1539 0.0000 1 1172 462 261 ASP N N 120.8901 0.0000 1 1173 463 262 MET H H 7.6777 0.0000 1 1174 463 262 MET C C 175.0267 0.0000 1 1175 463 262 MET CA C 55.1485 0.0000 1 1176 463 262 MET CB C 32.2843 0.0000 1 1177 463 262 MET N N 120.6756 0.0000 1 1178 464 263 SER H H 8.3857 0.0000 1 1179 464 263 SER C C 173.5583 0.0000 1 1180 464 263 SER CA C 56.8922 0.0000 1 1181 464 263 SER CB C 64.0133 0.0000 1 1182 464 263 SER N N 120.8906 0.0000 1 1183 465 264 LEU H H 8.5167 0.0000 1 1184 465 264 LEU C C 176.5800 0.0000 1 1185 465 264 LEU CA C 53.0553 0.0000 1 1186 465 264 LEU CB C 43.2265 0.0000 1 1187 465 264 LEU N N 125.6924 0.0000 1 1188 466 265 HIS H H 8.4576 0.0000 1 1189 466 265 HIS CA C 55.8736 0.0000 1 1190 466 265 HIS CB C 31.2411 0.0000 1 1191 466 265 HIS N N 126.4339 0.0000 1 1192 467 266 PRO C C 179.3171 0.0000 1 1193 467 266 PRO CA C 65.4295 0.0000 1 1194 467 266 PRO CB C 31.5555 0.0000 1 1195 468 267 LEU H H 10.9149 0.0000 1 1196 468 267 LEU C C 180.2359 0.0000 1 1197 468 267 LEU CA C 57.7977 0.0000 1 1198 468 267 LEU CB C 41.0296 0.0000 1 1199 468 267 LEU N N 124.0221 0.0000 1 1200 469 268 LEU H H 7.1241 0.0000 1 1201 469 268 LEU C C 178.7487 0.0000 1 1202 469 268 LEU CA C 55.9827 0.0000 1 1203 469 268 LEU CB C 39.9512 0.0000 1 1204 469 268 LEU N N 116.3734 0.0000 1 1205 470 269 GLN H H 8.5307 0.0000 1 1206 470 269 GLN C C 178.3743 0.0000 1 1207 470 269 GLN CA C 59.0353 0.0000 1 1208 470 269 GLN CB C 27.6687 0.0000 1 1209 470 269 GLN N N 119.2264 0.0000 1 1210 471 270 GLU H H 7.2748 0.0000 1 1211 471 270 GLU C C 178.1883 0.0000 1 1212 471 270 GLU CA C 58.2579 0.0000 1 1213 471 270 GLU CB C 28.6404 0.0000 1 1214 471 270 GLU N N 117.3139 0.0000 1 1215 472 271 ILE H H 7.4171 0.0000 1 1216 472 271 ILE C C 177.8009 0.0000 1 1217 472 271 ILE CA C 65.0597 0.0000 1 1218 472 271 ILE CB C 37.8148 0.0000 1 1219 472 271 ILE N N 120.1762 0.0000 1 1220 473 272 TYR H H 8.3850 0.0000 1 1221 473 272 TYR C C 177.2564 0.0000 1 1222 473 272 TYR CA C 60.1041 0.0000 1 1223 473 272 TYR CB C 37.3207 0.0000 1 1224 473 272 TYR N N 113.9564 0.0000 1 1225 474 273 LYS H H 7.3832 0.0000 1 1226 474 273 LYS CA C 57.9021 0.0000 1 1227 474 273 LYS CB C 30.5838 0.0000 1 1228 474 273 LYS N N 122.7335 0.0000 1 1229 475 274 ASP C C 174.9703 0.0000 1 1230 475 274 ASP CA C 55.4384 0.0000 1 1231 475 274 ASP CB C 39.2611 0.0000 1 1232 476 275 LEU H H 7.5413 0.0000 1 1233 476 275 LEU C C 176.0638 0.0000 1 1234 476 275 LEU CA C 56.2098 0.0000 1 1235 476 275 LEU CB C 42.0013 0.0000 1 1236 476 275 LEU N N 121.6581 0.0000 1 1237 477 276 TYR H H 7.4806 0.0000 1 1238 477 276 TYR CA C 59.3434 0.0000 1 1239 477 276 TYR CB C 40.3008 0.0000 1 1240 477 276 TYR N N 121.5469 0.0000 1 stop_ save_