data_15518 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13CO, 13Calpha and 13Cbeta Chemical Shift Assignments of Human Peroxisome Proliferator-Activated Receptor Gamma Ligand-Binding Domain Bound to GW1929 ; _BMRB_accession_number 15518 _BMRB_flat_file_name bmr15518.str _Entry_type original _Submission_date 2007-10-11 _Accession_date 2007-10-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jianyun . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 244 "13C chemical shifts" 772 "15N chemical shifts" 244 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-01-11 original author . stop_ _Original_release_date 2008-01-11 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Effect of Heterodimer Partner RXRalpha on PPARgamma Activation Function-2 Helix in Solution' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17980149 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jianyun . . 2 Chen Minghe . . 3 Stanley Susan E. . 4 Li Ellen . . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume 365 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 42 _Page_last 46 _Year 2008 _Details . loop_ _Keyword 'Allosteric communication' Heterodimerization NMR PPARgamma RXRalpha stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'GW1929-PPARgamma Ligand-Binding Domain Complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PPARgamma LBD' $Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain GW1929 $GW1929 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_Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 279 _Mol_residue_sequence ; GSHMQLNPESADLRALAKHL YDSYIKSFPLTKAKARAILT GKTTDKSPFVIYDMNSLMMG EDKIKFKHITPLQEQSKEVA IRIFQGCQFRSVEAVQEITE YAKSIPGFVNLDLNDQVTLL KYGVHEIIYTMLASLMNKDG VLISEGQGFMTREFLKSLRK PFGDFMEPKFEFAVKFNALE LDDSDLAIFIAVIILSGDRP GLLNVKPIEDIQDNLLQALE LQLKLNHPESSQLFAKLLQK MTDLRQIVTEHVQLLQVIKK TETDMSLHPLLQEIYKDLY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 200 GLY 2 201 SER 3 202 HIS 4 203 MET 5 204 GLN 6 205 LEU 7 206 ASN 8 207 PRO 9 208 GLU 10 209 SER 11 210 ALA 12 211 ASP 13 212 LEU 14 213 ARG 15 214 ALA 16 215 LEU 17 216 ALA 18 217 LYS 19 218 HIS 20 219 LEU 21 220 TYR 22 221 ASP 23 222 SER 24 223 TYR 25 224 ILE 26 225 LYS 27 226 SER 28 227 PHE 29 228 PRO 30 229 LEU 31 230 THR 32 231 LYS 33 232 ALA 34 233 LYS 35 234 ALA 36 235 ARG 37 236 ALA 38 237 ILE 39 238 LEU 40 239 THR 41 240 GLY 42 241 LYS 43 242 THR 44 243 THR 45 244 ASP 46 245 LYS 47 246 SER 48 247 PRO 49 248 PHE 50 249 VAL 51 250 ILE 52 251 TYR 53 252 ASP 54 253 MET 55 254 ASN 56 255 SER 57 256 LEU 58 257 MET 59 258 MET 60 259 GLY 61 260 GLU 62 261 ASP 63 262 LYS 64 263 ILE 65 264 LYS 66 265 PHE 67 266 LYS 68 267 HIS 69 268 ILE 70 269 THR 71 270 PRO 72 271 LEU 73 272 GLN 74 273 GLU 75 274 GLN 76 275 SER 77 276 LYS 78 277 GLU 79 278 VAL 80 279 ALA 81 280 ILE 82 281 ARG 83 282 ILE 84 283 PHE 85 284 GLN 86 285 GLY 87 286 CYS 88 287 GLN 89 288 PHE 90 289 ARG 91 290 SER 92 291 VAL 93 292 GLU 94 293 ALA 95 294 VAL 96 295 GLN 97 296 GLU 98 297 ILE 99 298 THR 100 299 GLU 101 300 TYR 102 301 ALA 103 302 LYS 104 303 SER 105 304 ILE 106 305 PRO 107 306 GLY 108 307 PHE 109 308 VAL 110 309 ASN 111 310 LEU 112 311 ASP 113 312 LEU 114 313 ASN 115 314 ASP 116 315 GLN 117 316 VAL 118 317 THR 119 318 LEU 120 319 LEU 121 320 LYS 122 321 TYR 123 322 GLY 124 323 VAL 125 324 HIS 126 325 GLU 127 326 ILE 128 327 ILE 129 328 TYR 130 329 THR 131 330 MET 132 331 LEU 133 332 ALA 134 333 SER 135 334 LEU 136 335 MET 137 336 ASN 138 337 LYS 139 338 ASP 140 339 GLY 141 340 VAL 142 341 LEU 143 342 ILE 144 343 SER 145 344 GLU 146 345 GLY 147 346 GLN 148 347 GLY 149 348 PHE 150 349 MET 151 350 THR 152 351 ARG 153 352 GLU 154 353 PHE 155 354 LEU 156 355 LYS 157 356 SER 158 357 LEU 159 358 ARG 160 359 LYS 161 360 PRO 162 361 PHE 163 362 GLY 164 363 ASP 165 364 PHE 166 365 MET 167 366 GLU 168 367 PRO 169 368 LYS 170 369 PHE 171 370 GLU 172 371 PHE 173 372 ALA 174 373 VAL 175 374 LYS 176 375 PHE 177 376 ASN 178 377 ALA 179 378 LEU 180 379 GLU 181 380 LEU 182 381 ASP 183 382 ASP 184 383 SER 185 384 ASP 186 385 LEU 187 386 ALA 188 387 ILE 189 388 PHE 190 389 ILE 191 390 ALA 192 391 VAL 193 392 ILE 194 393 ILE 195 394 LEU 196 395 SER 197 396 GLY 198 397 ASP 199 398 ARG 200 399 PRO 201 400 GLY 202 401 LEU 203 402 LEU 204 403 ASN 205 404 VAL 206 405 LYS 207 406 PRO 208 407 ILE 209 408 GLU 210 409 ASP 211 410 ILE 212 411 GLN 213 412 ASP 214 413 ASN 215 414 LEU 216 415 LEU 217 416 GLN 218 417 ALA 219 418 LEU 220 419 GLU 221 420 LEU 222 421 GLN 223 422 LEU 224 423 LYS 225 424 LEU 226 425 ASN 227 426 HIS 228 427 PRO 229 428 GLU 230 429 SER 231 430 SER 232 431 GLN 233 432 LEU 234 433 PHE 235 434 ALA 236 435 LYS 237 436 LEU 238 437 LEU 239 438 GLN 240 439 LYS 241 440 MET 242 441 THR 243 442 ASP 244 443 LEU 245 444 ARG 246 445 GLN 247 446 ILE 248 447 VAL 249 448 THR 250 449 GLU 251 450 HIS 252 451 VAL 253 452 GLN 254 453 LEU 255 454 LEU 256 455 GLN 257 456 VAL 258 457 ILE 259 458 LYS 260 459 LYS 261 460 THR 262 461 GLU 263 462 THR 264 463 ASP 265 464 MET 266 465 SER 267 466 LEU 268 467 HIS 269 468 PRO 270 469 LEU 271 470 LEU 272 471 GLN 273 472 GLU 274 473 ILE 275 474 TYR 276 475 LYS 277 476 ASP 278 477 LEU 279 478 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 17975 PPARgamma_LBD 98.57 276 100.00 100.00 0.00e+00 BMRB 17976 PPARgamma_LBD 98.57 276 100.00 100.00 0.00e+00 BMRB 17977 PPARgamma_LBD 98.57 276 100.00 100.00 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" 97.49 272 100.00 100.00 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" 97.49 272 100.00 100.00 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" 99.28 283 98.56 98.56 0.00e+00 PDB 1KNU "Ligand Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma In Complex With A Synthetic Agonist" 98.21 274 100.00 100.00 0.00e+00 PDB 1NYX "Ligand Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma In Complex With An Agonist" 98.57 276 100.00 100.00 0.00e+00 PDB 1PRG "Ligand Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma" 96.77 270 100.00 100.00 0.00e+00 PDB 1RDT "Crystal Structure Of A New Rexinoid Bound To The Rxralpha Ligand Binding Doamin In The RxralphaPPARGAMMA HETERODIMER" 99.28 284 98.19 98.19 0.00e+00 PDB 1WM0 "Ppargamma In Complex With A 2-Baba Compound" 98.57 292 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" 98.57 277 100.00 100.00 0.00e+00 PDB 1ZGY "Structural And Biochemical Basis For Selective Repression Of The Orphan Nuclear Receptor Lrh-1 By Shp" 97.49 272 100.00 100.00 0.00e+00 PDB 2ATH "Crystal Structure Of The Ligand Binding Domain Of Human Ppar-Gamma Im Complex With An Agonist" 97.13 271 100.00 100.00 0.00e+00 PDB 2F4B "Crystal Structure Of The Ligand Binding Domain Of Human Ppar-Gamma In Complex With An Agonist" 97.13 271 100.00 100.00 0.00e+00 PDB 2FVJ "A Novel Anti-adipogenic Partial Agonist Of Peroxisome Proliferator- Activated Receptor-gamma (pparg) Recruits Pparg-coactivator" 97.13 271 100.00 100.00 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" 97.13 271 100.00 100.00 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" 97.13 271 100.00 100.00 0.00e+00 PDB 2GTK "Structure-Based Design Of Indole Propionic Acids As Novel Pparag Co-Agonists" 97.13 271 100.00 100.00 0.00e+00 PDB 2HFP "Crystal Structure Of Ppar Gamma With N-Sulfonyl-2-Indole Carboxamide Ligands" 99.28 282 98.56 98.92 0.00e+00 PDB 2HWQ "Structural Basis For The Structure-Activity Relationships Of Peroxisome Proliferator-Activated Receptor Agonists" 97.13 271 100.00 100.00 0.00e+00 PDB 2HWR "Structural Basis For The Structure-Activity Relationships Of Peroxisome Proliferator-Activated Receptor Agonists" 97.13 271 100.00 100.00 0.00e+00 PDB 2I4J "Crystal Structure Of The Complex Between Ppargamma And The Agonist Lt160 (Ureidofibrate Derivative)" 102.51 286 97.20 97.20 0.00e+00 PDB 2I4P "Crystal Structure Of The Complex Between Ppargamma And The Partial Agonist Lt127 (Ureidofibrate Derivative). Structure Obtained" 102.51 286 97.20 97.20 0.00e+00 PDB 2I4Z "Crystal Structure Of The Complex Between Ppargamma And The Partial Agonist Lt127 (Ureidofibrate Derivative). This Structure Has" 102.51 286 97.20 97.20 0.00e+00 PDB 2OM9 "Ajulemic Acid, A Synthetic Cannabinoid Bound To Ppar Gamma" 100.00 278 99.64 99.64 0.00e+00 PDB 2P4Y "Crystal Structure Of Human Ppar-Gamma-Ligand Binding Domain Complexed With An Indole-Based Modulator" 98.57 277 100.00 100.00 0.00e+00 PDB 2POB "Ppargamma Ligand Binding Domain Complexed With A Farglitazar Analogue Gw4709" 97.49 272 100.00 100.00 0.00e+00 PDB 2PRG "Ligand-Binding Domain Of The Human Peroxisome Proliferator Activated Receptor Gamma" 97.13 271 100.00 100.00 0.00e+00 PDB 2Q59 "Crystal Structure Of Ppargamma Lbd Bound To Full Agonist Mrl20" 97.85 274 100.00 100.00 0.00e+00 PDB 2Q5P "Crystal Structure Of Ppargamma Bound To Partial Agonist Mrl24" 97.85 274 100.00 100.00 0.00e+00 PDB 2Q5S "Crystal Structure Of Ppargamma Bound To Partial Agonist Ntzdpa" 97.85 274 100.00 100.00 0.00e+00 PDB 2Q61 "Crystal Structure Of Ppargamma Ligand Binding Domain Bound To Partial Agonist Sr145" 97.85 274 100.00 100.00 0.00e+00 PDB 2Q6R "Crystal Structure Of Ppar Gamma Complexed With Partial Agonist Sf147" 97.85 274 100.00 100.00 0.00e+00 PDB 2Q6S "2.4 Angstrom Crystal Structure Of Ppar Gamma Complexed To Bvt.13 Without Co-Activator Peptides" 97.85 274 100.00 100.00 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" 97.13 271 100.00 100.00 0.00e+00 PDB 2QMV "High Resolution Structure Of Peroxisone Proliferation-Activated Receptor Gamma And Characterisation Of Its Interaction With The" 96.77 270 100.00 100.00 0.00e+00 PDB 2VSR "Hppargamma Ligand Binding Domain In Complex With 9-(S)-Hode" 98.21 276 100.00 100.00 0.00e+00 PDB 2VST "Hppargamma Ligand Binding Domain In Complex With 13-(S)- Hode" 98.21 276 100.00 100.00 0.00e+00 PDB 2VV0 "Hppargamma Ligand Binding Domain In Complex With Dha" 98.21 276 100.00 100.00 0.00e+00 PDB 2VV1 "Hppargamma Ligand Binding Domain In Complex With 4-Hdha" 98.21 276 100.00 100.00 0.00e+00 PDB 2VV2 "Hppargamma Ligand Binding Domain In Complex With 5-Hepa" 98.21 276 100.00 100.00 0.00e+00 PDB 2VV3 "Hppargamma Ligand Binding Domain In Complex With 4-Oxodha" 98.21 276 100.00 100.00 0.00e+00 PDB 2VV4 "Hppargamma Ligand Binding Domain In Complex With 6-Oxoote" 98.21 276 100.00 100.00 0.00e+00 PDB 2XKW "Ligand Binding Domain Of Human Ppar-Gamma In Complex With The Agonist Pioglitazone" 98.21 274 100.00 100.00 0.00e+00 PDB 2YFE "Ligand Binding Domain Of Human Ppar Gamma In Complex With Amorfrutin 1" 102.87 287 97.21 97.21 0.00e+00 PDB 2ZK0 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain" 102.51 286 97.20 97.20 0.00e+00 PDB 2ZK1 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With 15-Deoxy-Delta12,14- Prostaglandin " 102.51 286 97.20 97.20 0.00e+00 PDB 2ZK2 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With Glutathion Conjugated 15-Deoxy-Delt" 102.51 286 97.20 97.20 0.00e+00 PDB 2ZK3 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With 8-Oxo- Eicosatetraenoic Acid" 102.51 286 97.20 97.20 0.00e+00 PDB 2ZK4 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With 15-Oxo- Eicosatetraenoic Acid" 102.51 286 97.20 97.20 0.00e+00 PDB 2ZK5 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With Nitro-233" 102.51 286 97.20 97.20 0.00e+00 PDB 2ZK6 "Human Peroxisome Proliferator-Activated Receptor Gamma Ligand Binding Domain Complexed With C8-Bodipy" 102.51 286 97.20 97.20 0.00e+00 PDB 2ZNO "Human Pprr Gamma Ligand Binding Domain In Complex With A Synthetic Agonist Tipp703" 102.51 286 97.20 97.20 0.00e+00 PDB 3ADS "Human Ppargamma Ligand-Binding Domain In Complex With Indomethacin" 102.87 287 97.21 97.21 0.00e+00 PDB 3ADT "Human Ppargamma Ligand-Binding Domain In Complex With 5-Hydroxy-Indole Acetate" 102.87 287 97.21 97.21 0.00e+00 PDB 3ADU "Human Ppargamma Ligand-Binding Domain In Complex With 5-Methoxy-Indole Acetate" 102.87 287 97.21 97.21 0.00e+00 PDB 3ADV "Human Ppargamma Ligand-Binding Domain In Complex With Serotonin" 102.87 287 97.21 97.21 0.00e+00 PDB 3ADW "Human Ppargamma Ligand-Binding Domain In Complex With 5-Methoxy-Indole Acetate And 15-Oxo-Eicosatetraenoic Acid" 102.87 287 97.21 97.21 0.00e+00 PDB 3ADX "Human Ppargamma Ligand-Binding Domain In Complex With Indomethacin And Nitro-233" 102.87 287 97.21 97.21 0.00e+00 PDB 3AN3 "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mo3s" 102.51 286 97.20 97.20 0.00e+00 PDB 3AN4 "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mo4r" 102.51 286 97.20 97.20 0.00e+00 PDB 3B0Q "Human Ppar Gamma Ligand Binding Domain In Complex With Mcc555" 98.21 274 100.00 100.00 0.00e+00 PDB 3B0R "Human Ppar Gamma Ligand Binding Dmain Complexed With Gw9662 In A Covalent Bonded Form" 98.21 274 100.00 100.00 0.00e+00 PDB 3B1M "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator Cerco-A" 99.28 283 98.56 98.56 0.00e+00 PDB 3B3K "Crystal Structure Of The Complex Between Ppargamma And The Full Agonist Lt175" 102.51 286 97.20 97.20 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" 100.00 296 100.00 100.00 0.00e+00 PDB 3CDP "Crystal Structure Of Ppar-gamma Lbd Complexed With A Partial Agonist, Analogue Of Clofibric Acid" 102.51 286 97.20 97.20 0.00e+00 PDB 3CDS "Crystal Structure Of The Complex Between Ppar-Gamma And The Agonist Lt248 (Clofibric Acid Analogue)" 102.51 286 97.20 97.20 0.00e+00 PDB 3CS8 "Structural And Biochemical Basis For The Binding Selectivity Of Pparg To Pgc-1a" 97.49 275 99.63 100.00 0.00e+00 PDB 3CWD "Molecular Recognition Of Nitro-Fatty Acids By Ppar Gamma" 96.77 270 100.00 100.00 0.00e+00 PDB 3D6D "Crystal Structure Of The Complex Between Ppargamma Lbd And The Lt175(R-Enantiomer)" 102.51 286 97.20 97.20 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" 98.57 419 100.00 100.00 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" 98.57 419 100.00 100.00 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" 98.57 419 100.00 100.00 0.00e+00 PDB 3ET0 "Structure Of Ppargamma With 3-(5-Methoxy-1h-Indol-3-Yl)- Propionic Acid" 100.00 292 98.21 98.21 0.00e+00 PDB 3ET3 "Structure Of Ppargamma With 3-[5-Methoxy-1-(4-Methoxy- Benzenesulfonyl)-1h-Indol-3-Yl]-Propionic Acid" 100.00 292 98.57 98.57 0.00e+00 PDB 3FEJ "Design And Biological Evaluation Of Novel, Balanced Dual PparaG AGONISTS" 97.13 271 100.00 100.00 0.00e+00 PDB 3FUR "Crystal Structure Of Pparg In Complex With Int131" 97.49 272 100.00 100.00 0.00e+00 PDB 3G9E "Aleglitaar. A New. Potent, And Balanced Dual PparaG AGONIST For The Treatment Of Type Ii Diabetes" 97.13 271 100.00 100.00 0.00e+00 PDB 3GBK "Crystal Structure Of Human Ppar-Gamma Ligand Binding Domain Complexed With A Potent And Selective Agonist" 97.13 271 100.00 100.00 0.00e+00 PDB 3H0A "Crystal Structure Of Peroxisome Proliferator-activated Receptor Gamma (pparg) And Retinoic Acid Receptor Alpha (rxra) In Comple" 97.49 272 100.00 100.00 0.00e+00 PDB 3HO0 "Crystal Structure Of The Ppargamma-Lbd Complexed With A New Aryloxy-3phenylpropanoic Acid" 102.51 286 97.20 97.20 0.00e+00 PDB 3HOD "Crystal Structure Of The Ppargamma-Lbd Complexed With A New Aryloxy-3phenylpropanoic Acid" 102.51 286 97.20 97.20 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" 97.13 271 100.00 100.00 0.00e+00 PDB 3K8S "Crystal Structure Of Pparg In Complex With T2384" 97.49 272 100.00 100.00 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" 97.49 272 100.00 100.00 0.00e+00 PDB 3LMP "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 99.28 283 98.56 98.56 0.00e+00 PDB 3NOA "Crystal Structure Of Human Ppar-Gamma Ligand Binding Domain Complex With A Potency Improved Agonist" 97.13 271 100.00 100.00 0.00e+00 PDB 3OSI "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tetrachloro-bisphenol A (tcbpa)" 102.15 285 97.54 97.54 0.00e+00 PDB 3OSW "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tetrabromo-bisphenol A (tbbpa)" 102.15 285 97.54 97.54 0.00e+00 PDB 3PBA "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Monosulfate Tetrabromo-Bisphenol A (Monotbbpa)" 102.51 286 97.55 97.55 0.00e+00 PDB 3PO9 "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tripropyltin" 102.51 286 97.55 97.55 0.00e+00 PDB 3PRG "Ligand Binding Domain Of Human Peroxisome Proliferator Activated Receptor" 98.21 278 100.00 100.00 0.00e+00 PDB 3QT0 "Revealing A Steroid Receptor Ligand As A Unique Ppargamma Agonist" 97.13 271 100.00 100.00 0.00e+00 PDB 3R5N "Crystal Structure Of Ppargammalbd Complexed With The Agonist Magnolol" 98.21 274 100.00 100.00 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" 100.00 282 97.85 98.21 0.00e+00 PDB 3R8I "Crystal Structure Of Ppargamma With An Achiral Ureidofibrate Derivative (Rt86)" 102.87 287 97.21 97.21 0.00e+00 PDB 3S9S "Ligand Binding Domain Of Ppargamma Complexed With A Benzimidazole Partial Agonist" 99.28 284 98.56 98.56 0.00e+00 PDB 3SZ1 "Human Ppar Gamma Ligand Binding Domain In Complex With Luteolin And Myristic Acid" 100.00 278 99.64 99.64 0.00e+00 PDB 3T03 "Crystal Structure Of Ppar Gamma Ligand Binding Domain In Complex With A Novel Partial Agonist Gq-16" 99.28 284 98.56 98.56 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" 98.57 277 100.00 100.00 0.00e+00 PDB 3U9Q "Ligand Binding Domain Of Ppargamma Complexed With Decanoic Acid And Pgc-1a Peptide" 96.42 269 100.00 100.00 0.00e+00 PDB 3V9T "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 99.28 283 98.56 98.56 0.00e+00 PDB 3V9V "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 99.28 283 98.56 98.56 0.00e+00 PDB 3V9Y "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 99.28 283 98.56 98.56 0.00e+00 PDB 3VJH "Human Ppar Gamma Ligand Binding Domain In Complex With Jkpl35" 102.51 286 97.20 97.20 0.00e+00 PDB 3VJI "Human Ppar Gamma Ligand Binding Domain In Complex With Jkpl53" 102.51 286 97.20 97.20 0.00e+00 PDB 3VN2 "Crystal Structure Of Ppargamma Complexed With Telmisartan" 102.15 285 97.89 97.89 0.00e+00 PDB 3VSO "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mekt21" 102.51 286 97.20 97.20 0.00e+00 PDB 3VSP "Human Ppar Gamma Ligand Binding Domain In Complex With A Gamma Selective Agonist Mekt28" 102.51 286 97.20 97.20 0.00e+00 PDB 3WJ4 "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Tributyltin" 98.21 276 99.27 99.27 0.00e+00 PDB 3WJ5 "Crystal Structure Of Ppargamma Ligand Binding Domain In Complex With Triphenyltin" 98.21 276 99.27 99.27 0.00e+00 PDB 3WMH "Human Pprr Gamma Ligand Binding Domain In Complex With A Gammma Selective Synthetic Partial Agonist Mekt75" 102.51 286 97.20 97.20 0.00e+00 PDB 3X1H "Hppargamma Ligand Binding Domain In Complex With 5-oxo- Tricosahexaenoic Acid" 98.21 276 100.00 100.00 0.00e+00 PDB 3X1I "Hppargamma Ligand Binding Domain In Complex With 6-oxo- Tetracosahexaenoic Acid" 98.21 276 100.00 100.00 0.00e+00 PDB 4A4V "Ligand Binding Domain Of Human Ppar Gamma In Complex With Amorfrutin 2" 102.87 287 97.21 97.21 0.00e+00 PDB 4A4W "Ligand Binding Domain Of Human Ppar Gamma In Complex With Amorfrutin 2" 102.87 287 97.21 97.21 0.00e+00 PDB 4CI5 "Structural Basis For Gl479 A Dual Peroxisome Proliferator- Activated Receptor Gamma Agonist" 97.49 272 100.00 100.00 0.00e+00 PDB 4E4K "Crystal Structure Of Ppargamma With The Ligand Jo21" 102.87 287 97.21 97.21 0.00e+00 PDB 4E4Q "Crystal Structure Of Ppargamma With The Ligand Fs214" 102.87 287 97.21 97.21 0.00e+00 PDB 4EM9 "Human Ppar Gamma In Complex With Nonanoic Acids" 100.00 275 98.57 98.57 0.00e+00 PDB 4EMA "Human Peroxisome Proliferator-activated Receptor Gamma In Complex With Rosiglitazone" 100.00 275 98.57 98.57 0.00e+00 PDB 4F9M "Crystal Structure Of The Ppargamma-Lbd Complexed With A Cercosporamide Derivative Modulator" 99.28 283 98.56 98.56 0.00e+00 PDB 4FGY "Identification Of A Unique Ppar Ligand With An Unexpected Binding Mode And Antibetic Activity" 96.77 270 100.00 100.00 0.00e+00 PDB 4HEE "Crystal Structure Of Ppargamma In Complex With Compound 13" 100.00 282 97.85 98.21 0.00e+00 PDB 4JAZ "Crystal Structure Of The Complex Between Ppargamma Lbd And Trans- Resveratrol" 102.87 287 97.21 97.21 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" 102.87 287 97.21 97.21 0.00e+00 PDB 4L96 "Structure Of The Complex Between The F360l Ppargamma Mutant And The Ligand Lt175 (space Group I222)" 100.00 275 98.21 98.21 0.00e+00 PDB 4L98 "Crystal Structure Of The Complex Of F360l Ppargamma Mutant With The Ligand Lt175" 100.00 275 98.21 98.21 0.00e+00 PDB 4OJ4 "Crystal Structure Of V290m Ppargamma Mutant In Complex With Diclofenac" 100.00 278 99.28 99.64 0.00e+00 PDB 4PRG "0072 Partial Agonist Ppar Gamma Cocrystal" 96.77 270 100.00 100.00 0.00e+00 PDB 4PVU "Crystal Structure Of The Complex Between Ppargamma-lbd And The R Enantiomer Of Mbx-102 (metaglidasen)" 102.87 287 97.21 97.21 0.00e+00 PDB 4PWL "Crystal Structure Of The Complex Between Ppargamma-lbd And The S Enantiomer Of Mbx-102 (metaglidasen)" 102.87 287 97.21 97.21 0.00e+00 PDB 4R2U "Crystal Structure Of Ppargamma In Complex With Sr1664" 98.57 275 100.00 100.00 0.00e+00 PDB 4R6S "Crystal Structure Of Ppargammma In Complex With Sr1663" 98.57 275 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" 100.00 296 100.00 100.00 0.00e+00 PDB 4XTA "Mechanisms Of Ppargamma Activation By Non-steroidal Anti-inflammatory Drugs" 100.00 278 99.64 99.64 0.00e+00 PDB 4XUM "Ppargamma Ligand Binding Domain In Complex With Indomethacin" 100.00 278 99.64 99.64 0.00e+00 PDB 4Y29 "Identification Of A Novel Pparg Ligand That Regulates Metabolism" 96.42 269 100.00 100.00 0.00e+00 DBJ BAA18949 "PPAR gamma2 [Homo sapiens]" 98.92 506 99.64 99.64 0.00e+00 DBJ BAA23354 "peroxisome proliferator activated-receptor gamma [Homo sapiens]" 98.57 474 98.91 98.91 0.00e+00 DBJ BAA32540 "PPAR-gamma protein [Rattus norvegicus]" 98.57 475 98.55 99.64 0.00e+00 DBJ BAA36485 "PPAR gamma2 [Rattus norvegicus]" 98.57 505 98.55 99.64 0.00e+00 DBJ BAD20642 "peroxisome proliferator-activated receptor gamma 1a [Sus scrofa]" 98.57 475 99.64 100.00 0.00e+00 EMBL CAA07224 "peroxisome proliferator-cctivated receptor gamma 1 [Sus scrofa]" 98.57 475 98.91 99.64 0.00e+00 EMBL CAA07225 "peroxisome proliferator-activated receptor-gamma 2 [Sus scrofa]" 98.57 504 98.91 99.64 0.00e+00 EMBL CAA62152 "peroxisome proliferator activated receptor gamma [Homo sapiens]" 98.57 477 100.00 100.00 0.00e+00 EMBL CAA62153 "peroxisome proliferator activated receptor gamma [Homo sapiens]" 98.57 475 100.00 100.00 0.00e+00 EMBL CAA73032 "peroxisome proliferator activated receptor gamma 1 [Bos taurus]" 98.57 475 98.91 99.64 0.00e+00 GB AAA19971 "peroxisome proliferator-activated receptor gamma [Mus musculus]" 98.57 475 98.55 99.64 0.00e+00 GB AAA62110 "PPAR gamma [Mus musculus]" 98.57 475 97.45 98.91 0.00e+00 GB AAA62277 "peroxisome proliferator activated protein-gamma-2 [Mus musculus]" 98.57 505 98.18 99.64 0.00e+00 GB AAA80314 "peroxisome proliferator activated receptor gamma [Homo sapiens]" 98.57 477 100.00 100.00 0.00e+00 GB AAB04028 "peroxisome proliferator activated receptor gamma 2 [Homo sapiens]" 98.57 505 100.00 100.00 0.00e+00 PIR JE0279 "peroxisome proliferator-activated receptor gamma 1 - pig" 98.57 475 98.91 99.64 0.00e+00 REF NP_001019803 "peroxisome proliferator-activated receptor gamma [Canis lupus familiaris]" 98.57 505 100.00 100.00 0.00e+00 REF NP_001028032 "peroxisome proliferator-activated receptor gamma [Macaca mulatta]" 98.57 505 100.00 100.00 0.00e+00 REF NP_001075617 "peroxisome proliferator-activated receptor gamma [Oryctolagus cuniculus]" 98.57 475 98.91 100.00 0.00e+00 REF NP_001094391 "peroxisome proliferator-activated receptor gamma [Ovis aries]" 98.57 475 98.91 99.64 0.00e+00 REF NP_001106647 "peroxisome proliferator-activated receptor gamma [Felis catus]" 98.57 505 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" 98.57 505 100.00 100.00 0.00e+00 SP O18971 "RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 gr" 98.57 505 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" 98.57 475 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" 98.57 504 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" 98.57 505 98.55 99.64 0.00e+00 TPG DAA16769 "TPA: peroxisome proliferator-activated receptor gamma [Bos taurus]" 98.57 505 98.91 99.64 0.00e+00 stop_ save_ ############# # Ligands # ############# save_GW1929 _Saveframe_category ligand _Mol_type non-polymer _Name_common GW1929 _Molecular_mass . _Details . _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 $Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain 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 $Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain 'recombinant technology' . Escherichia coli . pET15b 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 $Peroxisome_Proliferator-Activated_Receptor_Gamma_Ligand-Binding_Domain 1.0 mM '[U-13C; U-15N; U-2H]' 'potassium phosphate' 20 mM 'natural abundance' KCl 50 mM 'natural abundance' NaN3 0.05 % 'natural abundance' EDTA-d16 0.5 mM 'natural abundance' b-mercaptoethanol-d6 8 mM 'natural abundance' H20 95 % 'natural abundance' D2O 5 % . 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_4D_HNCOCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '4D HNCOCA' _Sample_label $sample_1 save_ save_4D_HNCOi-1CAi_6 _Saveframe_category NMR_applied_experiment _Experiment_name '4D HNCOi-1CAi' _Sample_label $sample_1 save_ save_4D_HNCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '4D HNCACO' _Sample_label $sample_1 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' 0.103 . M 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_1 $citation_1 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 HNCO' '3D HNCACB' 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 5 GLN H H 8.29 . 1 2 203 5 GLN C C 175.6 . 1 3 203 5 GLN CA C 55.3 . 1 4 203 5 GLN CB C 28.7 . 1 5 203 5 GLN N N 122.4 . 1 6 204 6 LEU H H 8.22 . 1 7 204 6 LEU C C 176.7 . 1 8 204 6 LEU CA C 54.6 . 1 9 204 6 LEU CB C 41.5 . 1 10 204 6 LEU N N 124.3 . 1 11 205 7 ASN H H 8.40 . 1 12 205 7 ASN C C 173.6 . 1 13 205 7 ASN CA C 51.1 . 1 14 205 7 ASN CB C 38.1 . 1 15 205 7 ASN N N 121.0 . 1 16 206 8 PRO C C 177.5 . 1 17 206 8 PRO CA C 63.6 . 1 18 206 8 PRO CB C 31.2 . 1 19 207 9 GLU H H 8.60 . 1 20 207 9 GLU C C 177.5 . 1 21 207 9 GLU CA C 56.7 . 1 22 207 9 GLU CB C 28.8 . 1 23 207 9 GLU N N 119.9 . 1 24 208 10 SER H H 8.15 . 1 25 208 10 SER C C 175.3 . 1 26 208 10 SER CA C 59.3 . 1 27 208 10 SER CB C 62.7 . 1 28 208 10 SER N N 116.8 . 1 29 209 11 ALA H H 8.28 . 1 30 209 11 ALA C C 179.6 . 1 31 209 11 ALA CA C 54.0 . 1 32 209 11 ALA CB C 17.9 . 1 33 209 11 ALA N N 125.3 . 1 34 210 12 ASP H H 8.07 . 1 35 210 12 ASP C C 178.7 . 1 36 210 12 ASP CA C 55.5 . 1 37 210 12 ASP CB C 39.8 . 1 38 210 12 ASP N N 119.7 . 1 39 211 13 LEU H H 8.04 . 1 40 211 13 LEU C C 181.4 . 1 41 211 13 LEU CA C 57.3 . 1 42 211 13 LEU CB C 41.6 . 1 43 211 13 LEU N N 122.8 . 1 44 212 14 ARG H H 8.25 . 1 45 212 14 ARG C C 179.2 . 1 46 212 14 ARG CA C 57.0 . 1 47 212 14 ARG CB C 26.9 . 1 48 212 14 ARG N N 121.0 . 1 49 213 15 ALA H H 8.16 . 1 50 213 15 ALA C C 180.9 . 1 51 213 15 ALA CA C 54.6 . 1 52 213 15 ALA CB C 17.1 . 1 53 213 15 ALA N N 125.3 . 1 54 214 16 LEU H H 7.95 . 1 55 214 16 LEU C C 178.0 . 1 56 214 16 LEU CA C 57.5 . 1 57 214 16 LEU CB C 40.7 . 1 58 214 16 LEU N N 121.9 . 1 59 215 17 ALA H H 7.52 . 1 60 215 17 ALA C C 179.9 . 1 61 215 17 ALA CA C 55.6 . 1 62 215 17 ALA CB C 18.3 . 1 63 215 17 ALA N N 120.5 . 1 64 216 18 LYS H H 7.92 . 1 65 216 18 LYS C C 177.6 . 1 66 216 18 LYS CA C 58.8 . 1 67 216 18 LYS CB C 31.4 . 1 68 216 18 LYS N N 120.4 . 1 69 217 19 HIS H H 8.34 . 1 70 217 19 HIS C C 179.4 . 1 71 217 19 HIS CA C 59.7 . 1 72 217 19 HIS CB C 30.4 . 1 73 217 19 HIS N N 120.5 . 1 74 218 20 LEU H H 8.42 . 1 75 218 20 LEU C C 178.6 . 1 76 218 20 LEU CA C 57.3 . 1 77 218 20 LEU CB C 38.9 . 1 78 218 20 LEU N N 119.3 . 1 79 219 21 TYR H H 8.25 . 1 80 219 21 TYR C C 176.8 . 1 81 219 21 TYR CA C 60.5 . 1 82 219 21 TYR CB C 36.9 . 1 83 219 21 TYR N N 120.9 . 1 84 220 22 ASP H H 8.76 . 1 85 220 22 ASP C C 179.8 . 1 86 220 22 ASP CA C 57.2 . 1 87 220 22 ASP CB C 39.3 . 1 88 220 22 ASP N N 120.0 . 1 89 221 23 SER H H 7.99 . 1 90 221 23 SER C C 176.5 . 1 91 221 23 SER CA C 60.9 . 1 92 221 23 SER CB C 61.9 . 1 93 221 23 SER N N 115.8 . 1 94 222 24 TYR H H 9.07 . 1 95 222 24 TYR C C 176.6 . 1 96 222 24 TYR CA C 60.7 . 1 97 222 24 TYR CB C 38.4 . 1 98 222 24 TYR N N 129.4 . 1 99 223 25 ILE H H 8.39 . 1 100 223 25 ILE C C 178.9 . 1 101 223 25 ILE CA C 61.6 . 1 102 223 25 ILE CB C 35.5 . 1 103 223 25 ILE N N 118.2 . 1 104 224 26 LYS H H 7.20 . 1 105 224 26 LYS C C 178.2 . 1 106 224 26 LYS CA C 58.1 . 1 107 224 26 LYS CB C 32.0 . 1 108 224 26 LYS N N 118.5 . 1 109 225 27 SER H H 7.48 . 1 110 225 27 SER C C 172.7 . 1 111 225 27 SER CA C 61.0 . 1 112 225 27 SER CB C 63.7 . 1 113 225 27 SER N N 114.6 . 1 114 226 28 PHE H H 7.31 . 1 115 226 28 PHE C C 173.3 . 1 116 226 28 PHE CA C 53.3 . 1 117 226 28 PHE CB C 37.5 . 1 118 226 28 PHE N N 118.7 . 1 119 227 29 PRO C C 177.6 . 1 120 227 29 PRO CA C 64.2 . 1 121 227 29 PRO CB C 31.8 . 1 122 228 30 LEU H H 7.71 . 1 123 228 30 LEU C C 174.8 . 1 124 228 30 LEU CA C 53.3 . 1 125 228 30 LEU CB C 40.2 . 1 126 228 30 LEU N N 119.4 . 1 127 229 31 THR H H 6.89 . 1 128 229 31 THR C C 173.9 . 1 129 229 31 THR CA C 59.8 . 1 130 229 31 THR CB C 69.3 . 1 131 229 31 THR N N 115.5 . 1 132 230 32 LYS H H 10.52 . 1 133 230 32 LYS C C 179.1 . 1 134 230 32 LYS CA C 60.8 . 1 135 230 32 LYS CB C 31.2 . 1 136 230 32 LYS N N 124.9 . 1 137 231 33 ALA H H 9.27 . 1 138 231 33 ALA C C 181.7 . 1 139 231 33 ALA CA C 54.9 . 1 140 231 33 ALA CB C 17.5 . 1 141 231 33 ALA N N 121.1 . 1 142 232 34 LYS H H 7.62 . 1 143 232 34 LYS C C 178.8 . 1 144 232 34 LYS CA C 58.8 . 1 145 232 34 LYS CB C 32.2 . 1 146 232 34 LYS N N 119.0 . 1 147 233 35 ALA H H 8.47 . 1 148 233 35 ALA C C 179.9 . 1 149 233 35 ALA CA C 55.1 . 1 150 233 35 ALA CB C 18.8 . 1 151 233 35 ALA N N 122.7 . 1 152 234 36 ARG H H 9.17 . 1 153 234 36 ARG C C 179.6 . 1 154 234 36 ARG CA C 57.7 . 1 155 234 36 ARG CB C 27.6 . 1 156 234 36 ARG N N 116.2 . 1 157 235 37 ALA H H 7.50 . 1 158 235 37 ALA C C 179.8 . 1 159 235 37 ALA CA C 54.9 . 1 160 235 37 ALA CB C 17.1 . 1 161 235 37 ALA N N 123.3 . 1 162 236 38 ILE H H 7.66 . 1 163 236 38 ILE C C 179.6 . 1 164 236 38 ILE CA C 64.7 . 1 165 236 38 ILE CB C 37.6 . 1 166 236 38 ILE N N 119.3 . 1 167 237 39 LEU H H 8.50 . 1 168 237 39 LEU C C 178.8 . 1 169 237 39 LEU CA C 57.1 . 1 170 237 39 LEU CB C 41.7 . 1 171 237 39 LEU N N 119.3 . 1 172 238 40 THR H H 7.79 . 1 173 238 40 THR C C 175.6 . 1 174 238 40 THR CA C 61.6 . 1 175 238 40 THR CB C 69.7 . 1 176 238 40 THR N N 108.1 . 1 177 239 41 GLY H H 7.51 . 1 178 239 41 GLY C C 174.8 . 1 179 239 41 GLY CA C 46.0 . 1 180 239 41 GLY N N 110.7 . 1 181 240 42 LYS H H 8.23 . 1 182 240 42 LYS C C 177.0 . 1 183 240 42 LYS CA C 55.5 . 1 184 240 42 LYS CB C 31.6 . 1 185 240 42 LYS N N 120.7 . 1 186 241 43 THR H H 7.81 . 1 187 241 43 THR C C 174.8 . 1 188 241 43 THR CA C 60.7 . 1 189 241 43 THR CB C 68.9 . 1 190 241 43 THR N N 113.5 . 1 191 242 44 THR C C 175.1 . 1 192 242 44 THR CA C 61.8 . 1 193 242 44 THR CB C 69.0 . 1 194 243 45 ASP H H 8.30 . 1 195 243 45 ASP C C 175.8 . 1 196 243 45 ASP CA C 54.5 . 1 197 243 45 ASP CB C 40.5 . 1 198 243 45 ASP N N 121.7 . 1 199 244 46 LYS H H 7.94 . 1 200 244 46 LYS C C 176.1 . 1 201 244 46 LYS CA C 55.2 . 1 202 244 46 LYS CB C 32.1 . 1 203 244 46 LYS N N 119.9 . 1 204 245 47 SER H H 8.09 . 1 205 245 47 SER CA C 56.7 . 1 206 245 47 SER CB C 62.3 . 1 207 245 47 SER N N 119.5 . 1 208 247 49 PHE C C 177.8 . 1 209 247 49 PHE CA C 63.0 . 1 210 247 49 PHE CB C 36.0 . 1 211 248 50 VAL H H 7.69 . 1 212 248 50 VAL C C 180.3 . 1 213 248 50 VAL CA C 59.3 . 1 214 248 50 VAL CB C 29.0 . 1 215 248 50 VAL N N 120.6 . 1 216 249 51 ILE H H 7.95 . 1 217 249 51 ILE C C 176.5 . 1 218 249 51 ILE CA C 63.0 . 1 219 249 51 ILE CB C 35.0 . 1 220 249 51 ILE N N 120.4 . 1 221 250 52 TYR H H 7.95 . 1 222 250 52 TYR C C 176.2 . 1 223 250 52 TYR CA C 61.1 . 1 224 250 52 TYR CB C 39.2 . 1 225 250 52 TYR N N 122.6 . 1 226 251 53 ASP H H 8.66 . 1 227 251 53 ASP C C 179.0 . 1 228 251 53 ASP CA C 58.1 . 1 229 251 53 ASP CB C 41.2 . 1 230 251 53 ASP N N 115.8 . 1 231 252 54 MET C C 177.3 . 1 232 252 54 MET CA C 58.7 . 1 233 252 54 MET CB C 31.5 . 1 234 253 55 ASN H H 8.04 . 1 235 253 55 ASN C C 177.7 . 1 236 253 55 ASN CA C 56.4 . 1 237 253 55 ASN CB C 37.7 . 1 238 253 55 ASN N N 118.0 . 1 239 254 56 SER H H 8.84 . 1 240 254 56 SER C C 177.5 . 1 241 254 56 SER CA C 61.1 . 1 242 254 56 SER CB C 68.3 . 1 243 254 56 SER N N 116.9 . 1 244 255 57 LEU H H 7.82 . 1 245 255 57 LEU C C 178.1 . 1 246 255 57 LEU CA C 58.5 . 1 247 255 57 LEU CB C 39.5 . 1 248 255 57 LEU N N 125.4 . 1 249 256 58 MET H H 7.89 . 1 250 256 58 MET C C 179.4 . 1 251 256 58 MET CA C 57.7 . 1 252 256 58 MET CB C 31.9 . 1 253 256 58 MET N N 117.3 . 1 254 257 59 MET H H 8.14 . 1 255 257 59 MET C C 178.4 . 1 256 257 59 MET CA C 57.4 . 1 257 257 59 MET CB C 32.1 . 1 258 257 59 MET N N 119.4 . 1 259 258 60 GLY H H 8.45 . 1 260 258 60 GLY C C 174.7 . 1 261 258 60 GLY CA C 46.2 . 1 262 258 60 GLY N N 109.7 . 1 263 259 61 GLU H H 8.01 . 1 264 259 61 GLU C C 177.5 . 1 265 259 61 GLU CA C 58.6 . 1 266 259 61 GLU CB C 28.8 . 1 267 259 61 GLU N N 121.1 . 1 268 260 62 ASP C C 177.0 . 1 269 260 62 ASP CA C 55.4 . 1 270 260 62 ASP CB C 41.0 . 1 271 261 63 LYS H H 7.65 . 1 272 261 63 LYS C C 176.9 . 1 273 261 63 LYS CA C 56.6 . 1 274 261 63 LYS CB C 32.5 . 1 275 261 63 LYS N N 118.2 . 1 276 262 64 ILE H H 7.89 . 1 277 262 64 ILE C C 175.2 . 1 278 262 64 ILE CA C 60.5 . 1 279 262 64 ILE CB C 37.7 . 1 280 262 64 ILE N N 119.1 . 1 281 263 65 LYS H H 7.74 . 1 282 263 65 LYS C C 176.0 . 1 283 263 65 LYS CA C 55.7 . 1 284 263 65 LYS CB C 29.7 . 1 285 263 65 LYS N N 121.6 . 1 286 264 66 PHE H H 7.83 . 1 287 264 66 PHE C C 176.3 . 1 288 264 66 PHE CA C 56.9 . 1 289 264 66 PHE CB C 39.0 . 1 290 264 66 PHE N N 121.9 . 1 291 265 67 LYS H H 8.43 . 1 292 265 67 LYS C C 176.2 . 1 293 265 67 LYS CA C 56.9 . 1 294 265 67 LYS CB C 31.9 . 1 295 265 67 LYS N N 122.8 . 1 296 269 71 PRO C C 177.3 . 1 297 269 71 PRO CA C 63.2 . 1 298 269 71 PRO CB C 31.4 . 1 299 270 72 LEU H H 8.21 . 1 300 270 72 LEU C C 177.7 . 1 301 270 72 LEU CA C 55.6 . 1 302 270 72 LEU CB C 40.8 . 1 303 270 72 LEU N N 121.3 . 1 304 271 73 GLN H H 8.13 . 1 305 271 73 GLN C C 176.1 . 1 306 271 73 GLN CA C 55.9 . 1 307 271 73 GLN CB C 28.8 . 1 308 271 73 GLN N N 119.5 . 1 309 272 74 GLU H H 8.22 . 1 310 272 74 GLU C C 176.8 . 1 311 272 74 GLU CA C 56.4 . 1 312 272 74 GLU CB C 29.3 . 1 313 272 74 GLU N N 121.6 . 1 314 273 75 GLN H H 8.24 . 1 315 273 75 GLN C C 176.8 . 1 316 273 75 GLN CA C 56.4 . 1 317 273 75 GLN CB C 29.3 . 1 318 273 75 GLN N N 121.7 . 1 319 274 76 SER H H 8.06 . 1 320 274 76 SER C C 173.7 . 1 321 274 76 SER CA C 58.0 . 1 322 274 76 SER CB C 63.1 . 1 323 274 76 SER N N 116.6 . 1 324 276 78 GLU C C 176.4 . 1 325 276 78 GLU CA C 56.1 . 1 326 276 78 GLU CB C 29.4 . 1 327 277 79 VAL H H 8.05 . 1 328 277 79 VAL C C 175.7 . 1 329 277 79 VAL CA C 61.7 . 1 330 277 79 VAL CB C 32.0 . 1 331 277 79 VAL N N 122.0 . 1 332 278 80 ALA H H 8.24 . 1 333 278 80 ALA C C 177.4 . 1 334 278 80 ALA CA C 51.9 . 1 335 278 80 ALA CB C 18.7 . 1 336 278 80 ALA N N 128.4 . 1 337 279 81 ILE H H 8.06 . 1 338 279 81 ILE C C 175.4 . 1 339 279 81 ILE CA C 60.8 . 1 340 279 81 ILE CB C 37.8 . 1 341 279 81 ILE N N 121.7 . 1 342 280 82 ARG H H 7.83 . 1 343 280 82 ARG C C 180.8 . 1 344 280 82 ARG CA C 56.9 . 1 345 280 82 ARG CB C 30.8 . 1 346 280 82 ARG N N 130.5 . 1 347 283 85 GLN C C 179.0 . 1 348 283 85 GLN CA C 58.1 . 1 349 283 85 GLN CB C 27.6 . 1 350 284 86 GLY H H 8.01 . 1 351 284 86 GLY C C 175.6 . 1 352 284 86 GLY CA C 46.9 . 1 353 284 86 GLY N N 108.2 . 1 354 285 87 CYS H H 7.74 . 1 355 285 87 CYS C C 175.4 . 1 356 285 87 CYS CA C 62.7 . 1 357 285 87 CYS CB C 24.9 . 1 358 285 87 CYS N N 123.0 . 1 359 286 88 GLN H H 6.98 . 1 360 286 88 GLN C C 176.6 . 1 361 286 88 GLN CA C 59.0 . 1 362 286 88 GLN CB C 27.9 . 1 363 286 88 GLN N N 118.1 . 1 364 287 89 PHE H H 7.43 . 1 365 287 89 PHE C C 178.7 . 1 366 287 89 PHE CA C 60.9 . 1 367 287 89 PHE CB C 37.9 . 1 368 287 89 PHE N N 116.7 . 1 369 288 90 ARG H H 7.31 . 1 370 288 90 ARG C C 177.2 . 1 371 288 90 ARG CA C 56.8 . 1 372 288 90 ARG CB C 27.6 . 1 373 288 90 ARG N N 119.2 . 1 374 289 91 SER H H 8.39 . 1 375 289 91 SER C C 176.5 . 1 376 289 91 SER CA C 61.4 . 1 377 289 91 SER CB C 63.0 . 1 378 289 91 SER N N 116.3 . 1 379 290 92 VAL H H 7.66 . 1 380 290 92 VAL C C 178.6 . 1 381 290 92 VAL CA C 66.6 . 1 382 290 92 VAL CB C 30.6 . 1 383 290 92 VAL N N 115.7 . 1 384 291 93 GLU H H 7.23 . 1 385 291 93 GLU C C 179.0 . 1 386 291 93 GLU CA C 58.9 . 1 387 291 93 GLU CB C 30.3 . 1 388 291 93 GLU N N 120.2 . 1 389 292 94 ALA H H 8.98 . 1 390 292 94 ALA C C 180.8 . 1 391 292 94 ALA CA C 54.4 . 1 392 292 94 ALA CB C 16.5 . 1 393 292 94 ALA N N 124.4 . 1 394 293 95 VAL H H 8.85 . 1 395 293 95 VAL C C 179.5 . 1 396 293 95 VAL CA C 66.6 . 1 397 293 95 VAL CB C 30.6 . 1 398 293 95 VAL N N 119.2 . 1 399 294 96 GLN H H 7.39 . 1 400 294 96 GLN C C 178.6 . 1 401 294 96 GLN CA C 58.9 . 1 402 294 96 GLN CB C 27.1 . 1 403 294 96 GLN N N 121.5 . 1 404 295 97 GLU H H 7.77 . 1 405 295 97 GLU C C 178.7 . 1 406 295 97 GLU CA C 58.8 . 1 407 295 97 GLU CB C 28.8 . 1 408 295 97 GLU N N 121.4 . 1 409 296 98 ILE H H 8.36 . 1 410 296 98 ILE C C 177.3 . 1 411 296 98 ILE CA C 65.0 . 1 412 296 98 ILE CB C 37.6 . 1 413 296 98 ILE N N 118.3 . 1 414 297 99 THR H H 8.12 . 1 415 297 99 THR C C 175.5 . 1 416 297 99 THR CA C 67.1 . 1 417 297 99 THR CB C 68.0 . 1 418 297 99 THR N N 117.4 . 1 419 298 100 GLU H H 7.46 . 1 420 298 100 GLU C C 179.5 . 1 421 298 100 GLU CA C 58.6 . 1 422 298 100 GLU CB C 28.2 . 1 423 298 100 GLU N N 120.5 . 1 424 299 101 TYR H H 7.91 . 1 425 299 101 TYR C C 178.7 . 1 426 299 101 TYR CA C 61.0 . 1 427 299 101 TYR CB C 38.0 . 1 428 299 101 TYR N N 121.6 . 1 429 300 102 ALA H H 8.77 . 1 430 300 102 ALA C C 178.1 . 1 431 300 102 ALA CA C 54.0 . 1 432 300 102 ALA CB C 17.1 . 1 433 300 102 ALA N N 122.8 . 1 434 301 103 LYS H H 7.03 . 1 435 301 103 LYS C C 178.3 . 1 436 301 103 LYS CA C 58.3 . 1 437 301 103 LYS CB C 31.3 . 1 438 301 103 LYS N N 111.1 . 1 439 302 104 SER H H 7.84 . 1 440 302 104 SER C C 175.1 . 1 441 302 104 SER CA C 58.5 . 1 442 302 104 SER CB C 63.5 . 1 443 302 104 SER N N 116.5 . 1 444 303 105 ILE H H 7.61 . 1 445 303 105 ILE C C 175.0 . 1 446 303 105 ILE CA C 60.2 . 1 447 303 105 ILE CB C 37.4 . 1 448 303 105 ILE N N 128.0 . 1 449 304 106 PRO C C 176.2 . 1 450 304 106 PRO CA C 64.7 . 1 451 304 106 PRO CB C 30.4 . 1 452 305 107 GLY H H 8.61 . 1 453 305 107 GLY C C 176.6 . 1 454 305 107 GLY CA C 45.0 . 1 455 305 107 GLY N N 112.5 . 1 456 306 108 PHE H H 8.27 . 1 457 306 108 PHE C C 177.1 . 1 458 306 108 PHE CA C 62.6 . 1 459 306 108 PHE CB C 40.1 . 1 460 306 108 PHE N N 124.5 . 1 461 307 109 VAL H H 8.17 . 1 462 307 109 VAL C C 176.0 . 1 463 307 109 VAL CA C 62.8 . 1 464 307 109 VAL CB C 30.2 . 1 465 307 109 VAL N N 107.4 . 1 466 308 110 ASN H H 7.07 . 1 467 308 110 ASN C C 175.9 . 1 468 308 110 ASN CA C 52.5 . 1 469 308 110 ASN CB C 38.7 . 1 470 308 110 ASN N N 116.9 . 1 471 309 111 LEU H H 7.14 . 1 472 309 111 LEU C C 177.6 . 1 473 309 111 LEU CA C 53.8 . 1 474 309 111 LEU CB C 41.2 . 1 475 309 111 LEU N N 121.1 . 1 476 310 112 ASP H H 9.08 . 1 477 310 112 ASP C C 177.6 . 1 478 310 112 ASP CA C 55.2 . 1 479 310 112 ASP CB C 42.6 . 1 480 310 112 ASP N N 124.3 . 1 481 311 113 LEU H H 8.58 . 1 482 311 113 LEU C C 179.1 . 1 483 311 113 LEU CA C 58.4 . 1 484 311 113 LEU CB C 41.2 . 1 485 311 113 LEU N N 128.5 . 1 486 312 114 ASN H H 8.66 . 1 487 312 114 ASN C C 178.1 . 1 488 312 114 ASN CA C 56.2 . 1 489 312 114 ASN CB C 37.7 . 1 490 312 114 ASN N N 115.7 . 1 491 313 115 ASP H H 7.55 . 1 492 313 115 ASP C C 177.9 . 1 493 313 115 ASP CA C 57.0 . 1 494 313 115 ASP CB C 39.0 . 1 495 313 115 ASP N N 121.0 . 1 496 314 116 GLN H H 8.01 . 1 497 314 116 GLN C C 178.3 . 1 498 314 116 GLN CA C 59.9 . 1 499 314 116 GLN CB C 28.5 . 1 500 314 116 GLN N N 119.9 . 1 501 315 117 VAL H H 7.46 . 1 502 315 117 VAL C C 179.3 . 1 503 315 117 VAL CA C 66.3 . 1 504 315 117 VAL CB C 30.8 . 1 505 315 117 VAL N N 117.3 . 1 506 316 118 THR H H 8.34 . 1 507 316 118 THR C C 176.1 . 1 508 316 118 THR CA C 66.6 . 1 509 316 118 THR CB C 67.9 . 1 510 316 118 THR N N 120.9 . 1 511 317 119 LEU H H 8.90 . 1 512 317 119 LEU C C 182.3 . 1 513 317 119 LEU CA C 57.6 . 1 514 317 119 LEU CB C 39.5 . 1 515 317 119 LEU N N 120.5 . 1 516 318 120 LEU H H 8.06 . 1 517 318 120 LEU C C 177.5 . 1 518 318 120 LEU CA C 57.7 . 1 519 318 120 LEU CB C 40.7 . 1 520 318 120 LEU N N 120.8 . 1 521 319 121 LYS H H 8.64 . 1 522 319 121 LYS C C 176.5 . 1 523 319 121 LYS CA C 59.8 . 1 524 319 121 LYS CB C 32.6 . 1 525 319 121 LYS N N 122.3 . 1 526 320 122 TYR H H 7.44 . 1 527 320 122 TYR C C 176.8 . 1 528 320 122 TYR CA C 59.6 . 1 529 320 122 TYR CB C 39.0 . 1 530 320 122 TYR N N 109.4 . 1 531 321 123 GLY H H 7.96 . 1 532 321 123 GLY C C 175.7 . 1 533 321 123 GLY CA C 46.0 . 1 534 321 123 GLY N N 106.2 . 1 535 322 124 VAL H H 8.12 . 1 536 322 124 VAL C C 177.2 . 1 537 322 124 VAL CA C 67.0 . 1 538 322 124 VAL CB C 30.5 . 1 539 322 124 VAL N N 116.1 . 1 540 323 125 HIS H H 8.77 . 1 541 323 125 HIS C C 176.4 . 1 542 323 125 HIS CA C 63.9 . 1 543 323 125 HIS CB C 29.3 . 1 544 323 125 HIS N N 119.0 . 1 545 324 126 GLU H H 7.01 . 1 546 324 126 GLU C C 179.7 . 1 547 324 126 GLU CA C 59.4 . 1 548 324 126 GLU CB C 28.9 . 1 549 324 126 GLU N N 118.1 . 1 550 325 127 ILE H H 7.59 . 1 551 325 127 ILE C C 177.4 . 1 552 325 127 ILE CA C 64.4 . 1 553 325 127 ILE CB C 35.6 . 1 554 325 127 ILE N N 119.6 . 1 555 326 128 ILE H H 8.62 . 1 556 326 128 ILE C C 179.5 . 1 557 326 128 ILE CA C 66.0 . 1 558 326 128 ILE CB C 36.0 . 1 559 326 128 ILE N N 124.0 . 1 560 327 129 TYR H H 7.63 . 1 561 327 129 TYR C C 177.8 . 1 562 327 129 TYR CA C 59.6 . 1 563 327 129 TYR CB C 35.1 . 1 564 327 129 TYR N N 117.6 . 1 565 328 130 THR H H 7.34 . 1 566 328 130 THR C C 176.2 . 1 567 328 130 THR CA C 68.2 . 1 568 328 130 THR CB C 67.5 . 1 569 328 130 THR N N 118.5 . 1 570 329 131 MET H H 8.45 . 1 571 329 131 MET C C 179.2 . 1 572 329 131 MET CA C 58.2 . 1 573 329 131 MET CB C 31.5 . 1 574 329 131 MET N N 119.2 . 1 575 330 132 LEU H H 8.57 . 1 576 330 132 LEU C C 179.3 . 1 577 330 132 LEU CA C 56.8 . 1 578 330 132 LEU CB C 41.5 . 1 579 330 132 LEU N N 123.4 . 1 580 331 133 ALA H H 7.10 . 1 581 331 133 ALA C C 179.5 . 1 582 331 133 ALA CA C 55.3 . 1 583 331 133 ALA CB C 16.1 . 1 584 331 133 ALA N N 118.4 . 1 585 332 134 SER H H 7.28 . 1 586 332 134 SER C C 173.6 . 1 587 332 134 SER CA C 60.7 . 1 588 332 134 SER CB C 62.7 . 1 589 332 134 SER N N 112.6 . 1 590 333 135 LEU H H 7.59 . 1 591 333 135 LEU C C 175.0 . 1 592 333 135 LEU CA C 53.9 . 1 593 333 135 LEU CB C 41.2 . 1 594 333 135 LEU N N 118.6 . 1 595 334 136 MET H H 7.43 . 1 596 334 136 MET C C 177.0 . 1 597 334 136 MET CA C 55.0 . 1 598 334 136 MET CB C 36.6 . 1 599 334 136 MET N N 117.4 . 1 600 335 137 ASN H H 8.76 . 1 601 335 137 ASN C C 175.6 . 1 602 335 137 ASN CA C 51.3 . 1 603 335 137 ASN CB C 39.7 . 1 604 335 137 ASN N N 118.8 . 1 605 336 138 LYS H H 8.33 . 1 606 336 138 LYS C C 175.9 . 1 607 336 138 LYS CA C 58.3 . 1 608 336 138 LYS CB C 31.1 . 1 609 336 138 LYS N N 113.5 . 1 610 337 139 ASP H H 8.30 . 1 611 337 139 ASP C C 178.0 . 1 612 337 139 ASP CA C 54.6 . 1 613 337 139 ASP CB C 42.9 . 1 614 337 139 ASP N N 116.0 . 1 615 338 140 GLY H H 8.16 . 1 616 338 140 GLY C C 169.0 . 1 617 338 140 GLY CA C 48.0 . 1 618 338 140 GLY N N 111.7 . 1 619 339 141 VAL H H 8.13 . 1 620 339 141 VAL C C 172.6 . 1 621 339 141 VAL CA C 56.9 . 1 622 339 141 VAL CB C 36.1 . 1 623 339 141 VAL N N 116.6 . 1 624 340 142 LEU H H 8.63 . 1 625 340 142 LEU C C 176.1 . 1 626 340 142 LEU CA C 54.8 . 1 627 340 142 LEU CB C 43.3 . 1 628 340 142 LEU N N 127.9 . 1 629 341 143 ILE H H 8.33 . 1 630 341 143 ILE C C 176.8 . 1 631 341 143 ILE CA C 58.4 . 1 632 341 143 ILE CB C 41.3 . 1 633 341 143 ILE N N 113.6 . 1 634 342 144 SER H H 8.64 . 1 635 342 144 SER C C 176.0 . 1 636 342 144 SER CA C 58.0 . 1 637 342 144 SER CB C 61.3 . 1 638 342 144 SER N N 117.3 . 1 639 343 145 GLU H H 9.04 . 1 640 343 145 GLU C C 176.0 . 1 641 343 145 GLU CA C 57.3 . 1 642 343 145 GLU CB C 26.8 . 1 643 343 145 GLU N N 116.9 . 1 644 344 146 GLY H H 7.80 . 1 645 344 146 GLY C C 173.3 . 1 646 344 146 GLY CA C 44.9 . 1 647 344 146 GLY N N 104.7 . 1 648 345 147 GLN H H 7.86 . 1 649 345 147 GLN C C 176.8 . 1 650 345 147 GLN CA C 56.9 . 1 651 345 147 GLN CB C 30.5 . 1 652 345 147 GLN N N 116.8 . 1 653 346 148 GLY H H 7.94 . 1 654 346 148 GLY C C 171.2 . 1 655 346 148 GLY CA C 43.2 . 1 656 346 148 GLY N N 104.2 . 1 657 347 149 PHE H H 8.93 . 1 658 347 149 PHE C C 173.1 . 1 659 347 149 PHE CA C 56.2 . 1 660 347 149 PHE CB C 41.5 . 1 661 347 149 PHE N N 123.8 . 1 662 348 150 MET H H 8.91 . 1 663 348 150 MET C C 175.8 . 1 664 348 150 MET CA C 53.6 . 1 665 348 150 MET CB C 35.1 . 1 666 348 150 MET N N 128.5 . 1 667 349 151 THR H H 8.48 . 1 668 349 151 THR C C 174.5 . 1 669 349 151 THR CA C 61.6 . 1 670 349 151 THR CB C 69.2 . 1 671 349 151 THR N N 115.9 . 1 672 350 152 ARG H H 8.60 . 1 673 350 152 ARG C C 179.3 . 1 674 350 152 ARG CA C 58.5 . 1 675 350 152 ARG CB C 30.2 . 1 676 350 152 ARG N N 126.4 . 1 677 351 153 GLU H H 8.64 . 1 678 351 153 GLU C C 178.7 . 1 679 351 153 GLU CA C 58.8 . 1 680 351 153 GLU CB C 28.6 . 1 681 351 153 GLU N N 119.0 . 1 682 352 154 PHE H H 7.86 . 1 683 352 154 PHE C C 179.1 . 1 684 352 154 PHE CA C 59.4 . 1 685 352 154 PHE CB C 38.1 . 1 686 352 154 PHE N N 121.9 . 1 687 353 155 LEU H H 7.68 . 1 688 353 155 LEU C C 177.4 . 1 689 353 155 LEU CA C 57.8 . 1 690 353 155 LEU CB C 41.0 . 1 691 353 155 LEU N N 120.2 . 1 692 354 156 LYS H H 7.69 . 1 693 354 156 LYS C C 177.2 . 1 694 354 156 LYS CA C 57.0 . 1 695 354 156 LYS CB C 32.0 . 1 696 354 156 LYS N N 117.0 . 1 697 355 157 SER H H 7.59 . 1 698 355 157 SER C C 174.3 . 1 699 355 157 SER CA C 58.9 . 1 700 355 157 SER CB C 63.5 . 1 701 355 157 SER N N 114.6 . 1 702 356 158 LEU H H 6.64 . 1 703 356 158 LEU C C 176.5 . 1 704 356 158 LEU CA C 54.0 . 1 705 356 158 LEU CB C 41.8 . 1 706 356 158 LEU N N 121.1 . 1 707 357 159 ARG H H 8.67 . 1 708 357 159 ARG C C 176.3 . 1 709 357 159 ARG CA C 55.2 . 1 710 357 159 ARG CB C 29.1 . 1 711 357 159 ARG N N 120.8 . 1 712 358 160 LYS H H 8.70 . 1 713 358 160 LYS C C 176.2 . 1 714 358 160 LYS CA C 55.2 . 1 715 358 160 LYS CB C 30.9 . 1 716 358 160 LYS N N 124.3 . 1 717 359 161 PRO C C 176.3 . 1 718 359 161 PRO CA C 63.6 . 1 719 359 161 PRO CB C 32.7 . 1 720 360 162 PHE H H 8.78 . 1 721 360 162 PHE C C 177.7 . 1 722 360 162 PHE CA C 61.4 . 1 723 360 162 PHE CB C 38.2 . 1 724 360 162 PHE N N 124.6 . 1 725 361 163 GLY H H 7.41 . 1 726 361 163 GLY C C 174.5 . 1 727 361 163 GLY CA C 46.2 . 1 728 361 163 GLY N N 105.4 . 1 729 362 164 ASP H H 7.75 . 1 730 362 164 ASP C C 177.2 . 1 731 362 164 ASP CA C 54.3 . 1 732 362 164 ASP CB C 40.9 . 1 733 362 164 ASP N N 120.1 . 1 734 363 165 PHE H H 7.13 . 1 735 363 165 PHE C C 177.9 . 1 736 363 165 PHE CA C 62.0 . 1 737 363 165 PHE CB C 39.0 . 1 738 363 165 PHE N N 117.5 . 1 739 364 166 MET H H 8.48 . 1 740 364 166 MET C C 179.4 . 1 741 364 166 MET CA C 54.4 . 1 742 364 166 MET CB C 29.0 . 1 743 364 166 MET N N 115.6 . 1 744 365 167 GLU H H 8.47 . 1 745 365 167 GLU C C 174.7 . 1 746 365 167 GLU CA C 60.3 . 1 747 365 167 GLU CB C 27.0 . 1 748 365 167 GLU N N 124.9 . 1 749 366 168 PRO C C 180.1 . 1 750 366 168 PRO CA C 64.9 . 1 751 366 168 PRO CB C 30.9 . 1 752 367 169 LYS H H 7.35 . 1 753 367 169 LYS C C 178.5 . 1 754 367 169 LYS CA C 60.1 . 1 755 367 169 LYS CB C 30.9 . 1 756 367 169 LYS N N 118.4 . 1 757 368 170 PHE H H 8.05 . 1 758 368 170 PHE C C 178.8 . 1 759 368 170 PHE CA C 62.4 . 1 760 368 170 PHE CB C 38.5 . 1 761 368 170 PHE N N 119.7 . 1 762 369 171 GLU H H 8.35 . 1 763 369 171 GLU C C 179.9 . 1 764 369 171 GLU CA C 58.9 . 1 765 369 171 GLU CB C 28.8 . 1 766 369 171 GLU N N 118.0 . 1 767 370 172 PHE H H 7.66 . 1 768 370 172 PHE C C 177.0 . 1 769 370 172 PHE CA C 60.6 . 1 770 370 172 PHE CB C 38.5 . 1 771 370 172 PHE N N 119.6 . 1 772 371 173 ALA H H 8.62 . 1 773 371 173 ALA C C 179.1 . 1 774 371 173 ALA CA C 55.6 . 1 775 371 173 ALA CB C 20.0 . 1 776 371 173 ALA N N 123.2 . 1 777 372 174 VAL H H 8.23 . 1 778 372 174 VAL C C 179.6 . 1 779 372 174 VAL CA C 66.1 . 1 780 372 174 VAL CB C 31.0 . 1 781 372 174 VAL N N 116.8 . 1 782 373 175 LYS H H 6.79 . 1 783 373 175 LYS C C 178.8 . 1 784 373 175 LYS CA C 58.3 . 1 785 373 175 LYS CB C 31.8 . 1 786 373 175 LYS N N 119.0 . 1 787 374 176 PHE H H 8.91 . 1 788 374 176 PHE C C 179.5 . 1 789 374 176 PHE CA C 61.6 . 1 790 374 176 PHE CB C 39.8 . 1 791 374 176 PHE N N 123.5 . 1 792 375 177 ASN H H 9.52 . 1 793 375 177 ASN C C 179.1 . 1 794 375 177 ASN CA C 54.3 . 1 795 375 177 ASN CB C 36.5 . 1 796 375 177 ASN N N 119.9 . 1 797 376 178 ALA H H 7.05 . 1 798 376 178 ALA C C 178.2 . 1 799 376 178 ALA CA C 53.3 . 1 800 376 178 ALA CB C 16.9 . 1 801 376 178 ALA N N 123.7 . 1 802 377 179 LEU H H 7.22 . 1 803 377 179 LEU C C 176.1 . 1 804 377 179 LEU CA C 55.5 . 1 805 377 179 LEU CB C 39.5 . 1 806 377 179 LEU N N 116.3 . 1 807 378 180 GLU H H 7.32 . 1 808 378 180 GLU C C 175.6 . 1 809 378 180 GLU CA C 56.1 . 1 810 378 180 GLU CB C 25.8 . 1 811 378 180 GLU N N 110.2 . 1 812 379 181 LEU H H 8.03 . 1 813 379 181 LEU C C 178.5 . 1 814 379 181 LEU CA C 54.6 . 1 815 379 181 LEU CB C 40.6 . 1 816 379 181 LEU N N 116.7 . 1 817 380 182 ASP H H 9.63 . 1 818 380 182 ASP C C 176.9 . 1 819 380 182 ASP CA C 51.2 . 1 820 380 182 ASP CB C 42.4 . 1 821 380 182 ASP N N 123.1 . 1 822 381 183 ASP H H 8.78 . 1 823 381 183 ASP C C 176.3 . 1 824 381 183 ASP CA C 58.7 . 1 825 381 183 ASP CB C 43.5 . 1 826 381 183 ASP N N 117.0 . 1 827 382 184 SER H H 8.14 . 1 828 382 184 SER C C 176.6 . 1 829 382 184 SER CA C 61.2 . 1 830 382 184 SER N N 116.1 . 1 831 383 185 ASP H H 7.58 . 1 832 383 185 ASP C C 179.2 . 1 833 383 185 ASP CA C 56.8 . 1 834 383 185 ASP CB C 42.4 . 1 835 383 185 ASP N N 123.3 . 1 836 384 186 LEU H H 8.52 . 1 837 384 186 LEU C C 178.4 . 1 838 384 186 LEU CA C 57.6 . 1 839 384 186 LEU CB C 41.7 . 1 840 384 186 LEU N N 120.6 . 1 841 385 187 ALA H H 8.11 . 1 842 385 187 ALA C C 179.8 . 1 843 385 187 ALA CA C 55.1 . 1 844 385 187 ALA CB C 17.9 . 1 845 385 187 ALA N N 119.0 . 1 846 386 188 ILE H H 6.99 . 1 847 386 188 ILE CA C 63.4 . 1 848 386 188 ILE CB C 37.8 . 1 849 386 188 ILE N N 114.2 . 1 850 392 194 ILE C C 177.7 . 1 851 392 194 ILE CA C 64.5 . 1 852 392 194 ILE CB C 35.8 . 1 853 393 195 LEU H H 7.48 . 1 854 393 195 LEU C C 173.4 . 1 855 393 195 LEU CA C 51.3 . 1 856 393 195 LEU CB C 35.0 . 1 857 393 195 LEU N N 126.2 . 1 858 394 196 SER H H 6.82 . 1 859 394 196 SER C C 174.4 . 1 860 394 196 SER CA C 58.1 . 1 861 394 196 SER CB C 63.8 . 1 862 394 196 SER N N 113.8 . 1 863 395 197 GLY H H 8.56 . 1 864 395 197 GLY C C 173.1 . 1 865 395 197 GLY CA C 45.5 . 1 866 395 197 GLY N N 111.8 . 1 867 396 198 ASP H H 8.10 . 1 868 396 198 ASP C C 176.8 . 1 869 396 198 ASP CA C 52.1 . 1 870 396 198 ASP CB C 39.2 . 1 871 396 198 ASP N N 117.1 . 1 872 397 199 ARG H H 6.62 . 1 873 397 199 ARG C C 173.3 . 1 874 397 199 ARG CA C 52.1 . 1 875 397 199 ARG CB C 26.6 . 1 876 397 199 ARG N N 116.5 . 1 877 398 200 PRO C C 177.4 . 1 878 398 200 PRO CA C 62.7 . 1 879 398 200 PRO CB C 31.0 . 1 880 399 201 GLY H H 8.39 . 1 881 399 201 GLY C C 176.2 . 1 882 399 201 GLY CA C 45.1 . 1 883 399 201 GLY N N 107.7 . 1 884 400 202 LEU H H 6.78 . 1 885 400 202 LEU C C 177.3 . 1 886 400 202 LEU CA C 54.4 . 1 887 400 202 LEU CB C 42.2 . 1 888 400 202 LEU N N 120.2 . 1 889 401 203 LEU H H 11.53 . 1 890 401 203 LEU C C 178.9 . 1 891 401 203 LEU CA C 56.4 . 1 892 401 203 LEU CB C 41.4 . 1 893 401 203 LEU N N 128.2 . 1 894 402 204 ASN H H 8.98 . 1 895 402 204 ASN C C 174.7 . 1 896 402 204 ASN CA C 50.8 . 1 897 402 204 ASN CB C 37.8 . 1 898 402 204 ASN N N 120.3 . 1 899 403 205 VAL H H 8.34 . 1 900 403 205 VAL C C 177.6 . 1 901 403 205 VAL CA C 65.8 . 1 902 403 205 VAL CB C 31.8 . 1 903 403 205 VAL N N 122.6 . 1 904 404 206 LYS H H 8.26 . 1 905 404 206 LYS C C 175.0 . 1 906 404 206 LYS CA C 60.3 . 1 907 404 206 LYS CB C 28.5 . 1 908 404 206 LYS N N 121.6 . 1 909 405 207 PRO C C 179.5 . 1 910 405 207 PRO CA C 65.1 . 1 911 405 207 PRO CB C 30.2 . 1 912 406 208 ILE H H 6.73 . 1 913 406 208 ILE C C 177.2 . 1 914 406 208 ILE CA C 64.9 . 1 915 406 208 ILE CB C 37.9 . 1 916 406 208 ILE N N 118.6 . 1 917 407 209 GLU H H 8.13 . 1 918 407 209 GLU C C 179.5 . 1 919 407 209 GLU CA C 59.0 . 1 920 407 209 GLU CB C 28.7 . 1 921 407 209 GLU N N 120.5 . 1 922 408 210 ASP H H 8.47 . 1 923 408 210 ASP C C 179.6 . 1 924 408 210 ASP CA C 57.2 . 1 925 408 210 ASP CB C 39.6 . 1 926 408 210 ASP N N 119.4 . 1 927 409 211 ILE H H 7.44 . 1 928 409 211 ILE C C 179.1 . 1 929 409 211 ILE CA C 65.0 . 1 930 409 211 ILE CB C 37.7 . 1 931 409 211 ILE N N 121.1 . 1 932 410 212 GLN H H 9.08 . 1 933 410 212 GLN C C 178.4 . 1 934 410 212 GLN CA C 59.6 . 1 935 410 212 GLN CB C 27.5 . 1 936 410 212 GLN N N 121.9 . 1 937 411 213 ASP H H 8.87 . 1 938 411 213 ASP C C 178.9 . 1 939 411 213 ASP CA C 57.6 . 1 940 411 213 ASP CB C 40.7 . 1 941 411 213 ASP N N 118.4 . 1 942 412 214 ASN H H 7.18 . 1 943 412 214 ASN C C 177.7 . 1 944 412 214 ASN CA C 56.2 . 1 945 412 214 ASN CB C 38.6 . 1 946 412 214 ASN N N 118.5 . 1 947 413 215 LEU H H 8.30 . 1 948 413 215 LEU C C 179.1 . 1 949 413 215 LEU CA C 57.5 . 1 950 413 215 LEU CB C 42.1 . 1 951 413 215 LEU N N 119.9 . 1 952 414 216 LEU H H 9.33 . 1 953 414 216 LEU C C 180.1 . 1 954 414 216 LEU CA C 58.1 . 1 955 414 216 LEU CB C 41.1 . 1 956 414 216 LEU N N 121.8 . 1 957 415 217 GLN H H 7.99 . 1 958 415 217 GLN C C 180.0 . 1 959 415 217 GLN CA C 58.9 . 1 960 415 217 GLN CB C 28.4 . 1 961 415 217 GLN N N 119.6 . 1 962 416 218 ALA H H 8.43 . 1 963 416 218 ALA C C 180.1 . 1 964 416 218 ALA CA C 54.5 . 1 965 416 218 ALA CB C 16.5 . 1 966 416 218 ALA N N 122.9 . 1 967 417 219 LEU H H 9.11 . 1 968 417 219 LEU C C 176.7 . 1 969 417 219 LEU CA C 57.4 . 1 970 417 219 LEU CB C 40.8 . 1 971 417 219 LEU N N 122.7 . 1 972 418 220 GLU H H 8.50 . 1 973 418 220 GLU C C 178.7 . 1 974 418 220 GLU CA C 60.0 . 1 975 418 220 GLU CB C 28.1 . 1 976 418 220 GLU N N 121.3 . 1 977 419 221 LEU H H 7.43 . 1 978 419 221 LEU C C 177.6 . 1 979 419 221 LEU CA C 57.4 . 1 980 419 221 LEU CB C 40.6 . 1 981 419 221 LEU N N 118.8 . 1 982 420 222 GLN H H 7.95 . 1 983 420 222 GLN C C 178.1 . 1 984 420 222 GLN CA C 57.8 . 1 985 420 222 GLN CB C 26.8 . 1 986 420 222 GLN N N 118.7 . 1 987 421 223 LEU H H 8.52 . 1 988 421 223 LEU C C 179.6 . 1 989 421 223 LEU CA C 57.8 . 1 990 421 223 LEU CB C 40.1 . 1 991 421 223 LEU N N 117.3 . 1 992 422 224 LYS H H 7.79 . 1 993 422 224 LYS C C 178.6 . 1 994 422 224 LYS CA C 58.8 . 1 995 422 224 LYS CB C 31.5 . 1 996 422 224 LYS N N 121.1 . 1 997 423 225 LEU H H 7.93 . 1 998 423 225 LEU C C 179.3 . 1 999 423 225 LEU CA C 56.1 . 1 1000 423 225 LEU CB C 41.3 . 1 1001 423 225 LEU N N 117.1 . 1 1002 424 226 ASN H H 8.40 . 1 1003 424 226 ASN C C 175.2 . 1 1004 424 226 ASN CA C 52.8 . 1 1005 424 226 ASN CB C 40.1 . 1 1006 424 226 ASN N N 116.0 . 1 1007 425 227 HIS H H 7.71 . 1 1008 425 227 HIS C C 173.2 . 1 1009 425 227 HIS CA C 51.7 . 1 1010 425 227 HIS CB C 28.1 . 1 1011 425 227 HIS N N 115.1 . 1 1012 426 228 PRO C C 178.1 . 1 1013 426 228 PRO CA C 64.5 . 1 1014 426 228 PRO CB C 31.1 . 1 1015 427 229 GLU H H 8.93 . 1 1016 427 229 GLU C C 176.6 . 1 1017 427 229 GLU CA C 56.1 . 1 1018 427 229 GLU CB C 27.9 . 1 1019 427 229 GLU N N 117.6 . 1 1020 428 230 SER H H 7.57 . 1 1021 428 230 SER C C 175.1 . 1 1022 428 230 SER CA C 56.3 . 1 1023 428 230 SER CB C 62.4 . 1 1024 428 230 SER N N 117.1 . 1 1025 430 232 GLN C C 175.5 . 1 1026 430 232 GLN CA C 55.7 . 1 1027 430 232 GLN CB C 27.0 . 1 1028 431 233 LEU H H 7.18 . 1 1029 431 233 LEU C C 177.3 . 1 1030 431 233 LEU CA C 58.0 . 1 1031 431 233 LEU CB C 40.6 . 1 1032 431 233 LEU N N 121.3 . 1 1033 432 234 PHE H H 8.57 . 1 1034 432 234 PHE C C 175.9 . 1 1035 432 234 PHE CA C 60.9 . 1 1036 432 234 PHE CB C 37.9 . 1 1037 432 234 PHE N N 118.6 . 1 1038 433 235 ALA H H 7.91 . 1 1039 433 235 ALA C C 181.4 . 1 1040 433 235 ALA CA C 54.7 . 1 1041 433 235 ALA CB C 17.6 . 1 1042 433 235 ALA N N 120.1 . 1 1043 434 236 LYS H H 8.08 . 1 1044 434 236 LYS C C 179.7 . 1 1045 434 236 LYS CA C 58.8 . 1 1046 434 236 LYS CB C 31.9 . 1 1047 434 236 LYS N N 118.1 . 1 1048 435 237 LEU H H 8.62 . 1 1049 435 237 LEU C C 178.8 . 1 1050 435 237 LEU CA C 57.2 . 1 1051 435 237 LEU CB C 40.4 . 1 1052 435 237 LEU N N 122.3 . 1 1053 436 238 LEU H H 7.96 . 1 1054 436 238 LEU C C 181.7 . 1 1055 436 238 LEU CA C 57.7 . 1 1056 436 238 LEU CB C 39.3 . 1 1057 436 238 LEU N N 118.5 . 1 1058 437 239 GLN H H 7.52 . 1 1059 437 239 GLN C C 178.5 . 1 1060 437 239 GLN CA C 58.0 . 1 1061 437 239 GLN CB C 27.6 . 1 1062 437 239 GLN N N 118.6 . 1 1063 438 240 LYS H H 7.85 . 1 1064 438 240 LYS C C 178.6 . 1 1065 438 240 LYS CA C 56.0 . 1 1066 438 240 LYS CB C 30.2 . 1 1067 438 240 LYS N N 116.6 . 1 1068 439 241 MET H H 7.87 . 1 1069 439 241 MET C C 178.8 . 1 1070 439 241 MET CA C 59.8 . 1 1071 439 241 MET CB C 31.9 . 1 1072 439 241 MET N N 117.2 . 1 1073 440 242 THR H H 7.53 . 1 1074 440 242 THR C C 177.0 . 1 1075 440 242 THR CA C 65.7 . 1 1076 440 242 THR CB C 67.9 . 1 1077 440 242 THR N N 115.5 . 1 1078 441 243 ASP H H 7.55 . 1 1079 441 243 ASP C C 179.1 . 1 1080 441 243 ASP CA C 57.2 . 1 1081 441 243 ASP CB C 39.8 . 1 1082 441 243 ASP N N 123.9 . 1 1083 442 244 LEU H H 8.03 . 1 1084 442 244 LEU C C 178.2 . 1 1085 442 244 LEU CA C 57.6 . 1 1086 442 244 LEU CB C 42.5 . 1 1087 442 244 LEU N N 120.1 . 1 1088 443 245 ARG H H 7.34 . 1 1089 443 245 ARG C C 179.2 . 1 1090 443 245 ARG CA C 59.4 . 1 1091 443 245 ARG CB C 28.3 . 1 1092 443 245 ARG N N 117.2 . 1 1093 444 246 GLN H H 7.40 . 1 1094 444 246 GLN C C 178.2 . 1 1095 444 246 GLN CA C 58.1 . 1 1096 444 246 GLN CB C 27.1 . 1 1097 444 246 GLN N N 119.3 . 1 1098 445 247 ILE H H 7.66 . 1 1099 445 247 ILE C C 179.7 . 1 1100 445 247 ILE CA C 63.9 . 1 1101 445 247 ILE CB C 36.2 . 1 1102 445 247 ILE N N 120.2 . 1 1103 446 248 VAL H H 7.84 . 1 1104 446 248 VAL C C 177.9 . 1 1105 446 248 VAL CA C 66.8 . 1 1106 446 248 VAL CB C 31.1 . 1 1107 446 248 VAL N N 121.5 . 1 1108 447 249 THR H H 8.01 . 1 1109 447 249 THR C C 177.4 . 1 1110 447 249 THR CA C 66.3 . 1 1111 447 249 THR CB C 68.1 . 1 1112 447 249 THR N N 114.7 . 1 1113 448 250 GLU H H 8.05 . 1 1114 448 250 GLU C C 178.3 . 1 1115 448 250 GLU CA C 58.7 . 1 1116 448 250 GLU CB C 29.4 . 1 1117 448 250 GLU N N 122.4 . 1 1118 449 251 HIS H H 8.04 . 1 1119 449 251 HIS C C 177.3 . 1 1120 449 251 HIS CA C 60.1 . 1 1121 449 251 HIS CB C 31.3 . 1 1122 449 251 HIS N N 123.0 . 1 1123 450 252 VAL H H 8.36 . 1 1124 450 252 VAL C C 178.5 . 1 1125 450 252 VAL CA C 66.3 . 1 1126 450 252 VAL CB C 31.1 . 1 1127 450 252 VAL N N 118.2 . 1 1128 451 253 GLN H H 7.34 . 1 1129 451 253 GLN C C 179.2 . 1 1130 451 253 GLN CA C 58.4 . 1 1131 451 253 GLN CB C 27.0 . 1 1132 451 253 GLN N N 118.2 . 1 1133 452 254 LEU H H 7.53 . 1 1134 452 254 LEU C C 179.8 . 1 1135 452 254 LEU CA C 57.3 . 1 1136 452 254 LEU CB C 40.5 . 1 1137 452 254 LEU N N 122.3 . 1 1138 453 255 LEU H H 8.18 . 1 1139 453 255 LEU C C 180.3 . 1 1140 453 255 LEU CA C 57.6 . 1 1141 453 255 LEU CB C 40.3 . 1 1142 453 255 LEU N N 120.4 . 1 1143 454 256 GLN H H 7.90 . 1 1144 454 256 GLN C C 178.7 . 1 1145 454 256 GLN CA C 58.2 . 1 1146 454 256 GLN CB C 27.2 . 1 1147 454 256 GLN N N 119.2 . 1 1148 455 257 VAL H H 7.54 . 1 1149 455 257 VAL C C 180.0 . 1 1150 455 257 VAL CA C 66.0 . 1 1151 455 257 VAL CB C 30.5 . 1 1152 455 257 VAL N N 121.2 . 1 1153 456 258 ILE H H 7.58 . 1 1154 456 258 ILE C C 177.2 . 1 1155 456 258 ILE CA C 64.0 . 1 1156 456 258 ILE CB C 35.8 . 1 1157 456 258 ILE N N 121.4 . 1 1158 457 259 LYS H H 7.74 . 1 1159 457 259 LYS C C 177.9 . 1 1160 457 259 LYS CA C 58.1 . 1 1161 457 259 LYS CB C 31.4 . 1 1162 457 259 LYS N N 120.0 . 1 1163 458 260 LYS H H 7.50 . 1 1164 458 260 LYS C C 178.1 . 1 1165 458 260 LYS CA C 57.5 . 1 1166 458 260 LYS CB C 32.6 . 1 1167 458 260 LYS N N 115.5 . 1 1168 459 261 THR H H 7.64 . 1 1169 459 261 THR C C 174.9 . 1 1170 459 261 THR CA C 62.6 . 1 1171 459 261 THR CB C 70.4 . 1 1172 459 261 THR N N 108.4 . 1 1173 460 262 GLU H H 8.19 . 1 1174 460 262 GLU C C 176.7 . 1 1175 460 262 GLU CA C 54.1 . 1 1176 460 262 GLU CB C 28.3 . 1 1177 460 262 GLU N N 123.9 . 1 1178 461 263 THR H H 8.07 . 1 1179 461 263 THR C C 175.0 . 1 1180 461 263 THR CA C 63.2 . 1 1181 461 263 THR CB C 68.8 . 1 1182 461 263 THR N N 114.8 . 1 1183 462 264 ASP H H 8.57 . 1 1184 462 264 ASP C C 175.6 . 1 1185 462 264 ASP CA C 54.4 . 1 1186 462 264 ASP CB C 39.8 . 1 1187 462 264 ASP N N 120.6 . 1 1188 463 265 MET H H 7.68 . 1 1189 463 265 MET C C 175.1 . 1 1190 463 265 MET CA C 54.4 . 1 1191 463 265 MET CB C 32.1 . 1 1192 463 265 MET N N 120.0 . 1 1193 464 266 SER H H 8.12 . 1 1194 464 266 SER C C 173.9 . 1 1195 464 266 SER CA C 57.2 . 1 1196 464 266 SER CB C 64.1 . 1 1197 464 266 SER N N 117.6 . 1 1198 465 267 LEU H H 8.50 . 1 1199 465 267 LEU C C 177.3 . 1 1200 465 267 LEU CA C 53.5 . 1 1201 465 267 LEU CB C 43.0 . 1 1202 465 267 LEU N N 124.3 . 1 1203 466 268 HIS H H 8.70 . 1 1204 466 268 HIS C C 175.1 . 1 1205 466 268 HIS CA C 55.7 . 1 1206 466 268 HIS CB C 31.5 . 1 1207 466 268 HIS N N 125.8 . 1 1208 467 269 PRO C C 179.1 . 1 1209 467 269 PRO CA C 65.6 . 1 1210 467 269 PRO CB C 31.5 . 1 1211 468 270 LEU H H 11.27 . 1 1212 468 270 LEU C C 180.1 . 1 1213 468 270 LEU CA C 58.2 . 1 1214 468 270 LEU CB C 41.3 . 1 1215 468 270 LEU N N 124.7 . 1 1216 469 271 LEU H H 7.13 . 1 1217 469 271 LEU C C 179.1 . 1 1218 469 271 LEU CA C 56.4 . 1 1219 469 271 LEU CB C 40.5 . 1 1220 469 271 LEU N N 116.1 . 1 1221 470 272 GLN H H 8.51 . 1 1222 470 272 GLN C C 178.6 . 1 1223 470 272 GLN CA C 59.3 . 1 1224 470 272 GLN CB C 27.8 . 1 1225 470 272 GLN N N 118.6 . 1 1226 471 273 GLU H H 7.59 . 1 1227 471 273 GLU C C 178.6 . 1 1228 471 273 GLU CA C 58.5 . 1 1229 471 273 GLU CB C 28.6 . 1 1230 471 273 GLU N N 118.0 . 1 1231 472 274 ILE H H 7.49 . 1 1232 472 274 ILE C C 177.9 . 1 1233 472 274 ILE CA C 65.3 . 1 1234 472 274 ILE CB C 37.8 . 1 1235 472 274 ILE N N 120.6 . 1 1236 473 275 TYR H H 8.13 . 1 1237 473 275 TYR C C 177.0 . 1 1238 473 275 TYR CA C 59.7 . 1 1239 473 275 TYR CB C 37.1 . 1 1240 473 275 TYR N N 114.7 . 1 1241 474 276 LYS H H 7.43 . 1 1242 474 276 LYS C C 176.8 . 1 1243 474 276 LYS CA C 58.1 . 1 1244 474 276 LYS CB C 30.8 . 1 1245 474 276 LYS N N 123.3 . 1 1246 475 277 ASP H H 8.76 . 1 1247 475 277 ASP C C 175.1 . 1 1248 475 277 ASP CA C 55.6 . 1 1249 475 277 ASP CB C 39.4 . 1 1250 475 277 ASP N N 122.5 . 1 1251 476 278 LEU H H 7.58 . 1 1252 476 278 LEU C C 176.1 . 1 1253 476 278 LEU CA C 56.1 . 1 1254 476 278 LEU CB C 41.9 . 1 1255 476 278 LEU N N 121.6 . 1 1256 477 279 TYR H H 7.65 . 1 1257 477 279 TYR C C 180.1 . 1 1258 477 279 TYR CA C 59.6 . 1 1259 477 279 TYR CB C 39.5 . 1 1260 477 279 TYR N N 123.2 . 1 stop_ save_