data_19937 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Dual-phosphorylated human p38 alpha ILVM methyl resonance assignments in ADP and substrate-peptide-bound state ; _BMRB_accession_number 19937 _BMRB_flat_file_name bmr19937.str _Entry_type original _Submission_date 2014-04-24 _Accession_date 2014-04-24 _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 Tokunaga Yuji . . 2 Takeuchi Koh . . 3 Takahashi Hideo . . 4 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 126 "13C chemical shifts" 126 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-09-26 update BMRB 'update entry citation' 2014-08-05 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19930 'non-phosphorylated (apo)' 19934 'Dual-phosphorylated human p38 alpha apo' 19935 'Dual-phosphorylated human p38 alpha ADP-bound' 19936 'Dual-phosphorylated human p38 alpha MK2 334/D peptide bound' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25038803 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tokunaga Yuji . . 2 Takeuchi Koh . . 3 Takahashi Hideo . . 4 Shimada Ichio . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature structural & molecular biology' _Journal_volume 21 _Journal_issue 8 _Journal_ISSN 1545-9985 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 704 _Page_last 711 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Dual-phosphorylated human p38 alpha ADP and MK2 334/D peptide bound' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dual-phosphorylated human p38 alpha (apo)' $dual-phosphorylated_human_p38_alpha_(apo) 'MK2 334/D peptide' $MK2_334-D_peptide ADP $entity_ADP 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_dual-phosphorylated_human_p38_alpha_(apo) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common dual-phosphorylated_human_p38_alpha_(apo) _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 367 _Mol_residue_sequence ; MAHHHHHHSQERPTFYRQEL NKTIWEVPERYQNLSPVGSG AYGSVCAAFDTKTGLRVAVK KLSRPFQSIIHAKRTYRELR LLKHMKHENVIGLLDVFTPA RSLEEFNDVYLVTHLMGADL NNIVKCQKLTDDHVQFLIYQ ILRGLKYIHSADIIHRDLKP SNLAVNEDCELKILDFGLAR HTDDEMXGXVATRWYRAPEI MLNWMHYNQTVDIWSVGCIM AELLTGRTLFPGTDHIDQLK LILRLVGTPGAELLKKISSE SARNYIQSLTQMPKMNFANV FIGANPLAVDLLEKMLVLDS DKRITAAQALAHAYFAQYHD PDDEPVADPYDQSFESRDLL IDEWKSLTYDEVISFVPPPL DQEEMES ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -6 MET 2 -5 ALA 3 -4 HIS 4 -3 HIS 5 -2 HIS 6 -1 HIS 7 0 HIS 8 1 HIS 9 2 SER 10 3 GLN 11 4 GLU 12 5 ARG 13 6 PRO 14 7 THR 15 8 PHE 16 9 TYR 17 10 ARG 18 11 GLN 19 12 GLU 20 13 LEU 21 14 ASN 22 15 LYS 23 16 THR 24 17 ILE 25 18 TRP 26 19 GLU 27 20 VAL 28 21 PRO 29 22 GLU 30 23 ARG 31 24 TYR 32 25 GLN 33 26 ASN 34 27 LEU 35 28 SER 36 29 PRO 37 30 VAL 38 31 GLY 39 32 SER 40 33 GLY 41 34 ALA 42 35 TYR 43 36 GLY 44 37 SER 45 38 VAL 46 39 CYS 47 40 ALA 48 41 ALA 49 42 PHE 50 43 ASP 51 44 THR 52 45 LYS 53 46 THR 54 47 GLY 55 48 LEU 56 49 ARG 57 50 VAL 58 51 ALA 59 52 VAL 60 53 LYS 61 54 LYS 62 55 LEU 63 56 SER 64 57 ARG 65 58 PRO 66 59 PHE 67 60 GLN 68 61 SER 69 62 ILE 70 63 ILE 71 64 HIS 72 65 ALA 73 66 LYS 74 67 ARG 75 68 THR 76 69 TYR 77 70 ARG 78 71 GLU 79 72 LEU 80 73 ARG 81 74 LEU 82 75 LEU 83 76 LYS 84 77 HIS 85 78 MET 86 79 LYS 87 80 HIS 88 81 GLU 89 82 ASN 90 83 VAL 91 84 ILE 92 85 GLY 93 86 LEU 94 87 LEU 95 88 ASP 96 89 VAL 97 90 PHE 98 91 THR 99 92 PRO 100 93 ALA 101 94 ARG 102 95 SER 103 96 LEU 104 97 GLU 105 98 GLU 106 99 PHE 107 100 ASN 108 101 ASP 109 102 VAL 110 103 TYR 111 104 LEU 112 105 VAL 113 106 THR 114 107 HIS 115 108 LEU 116 109 MET 117 110 GLY 118 111 ALA 119 112 ASP 120 113 LEU 121 114 ASN 122 115 ASN 123 116 ILE 124 117 VAL 125 118 LYS 126 119 CYS 127 120 GLN 128 121 LYS 129 122 LEU 130 123 THR 131 124 ASP 132 125 ASP 133 126 HIS 134 127 VAL 135 128 GLN 136 129 PHE 137 130 LEU 138 131 ILE 139 132 TYR 140 133 GLN 141 134 ILE 142 135 LEU 143 136 ARG 144 137 GLY 145 138 LEU 146 139 LYS 147 140 TYR 148 141 ILE 149 142 HIS 150 143 SER 151 144 ALA 152 145 ASP 153 146 ILE 154 147 ILE 155 148 HIS 156 149 ARG 157 150 ASP 158 151 LEU 159 152 LYS 160 153 PRO 161 154 SER 162 155 ASN 163 156 LEU 164 157 ALA 165 158 VAL 166 159 ASN 167 160 GLU 168 161 ASP 169 162 CYS 170 163 GLU 171 164 LEU 172 165 LYS 173 166 ILE 174 167 LEU 175 168 ASP 176 169 PHE 177 170 GLY 178 171 LEU 179 172 ALA 180 173 ARG 181 174 HIS 182 175 THR 183 176 ASP 184 177 ASP 185 178 GLU 186 179 MET 187 180 TPO 188 181 GLY 189 182 PTR 190 183 VAL 191 184 ALA 192 185 THR 193 186 ARG 194 187 TRP 195 188 TYR 196 189 ARG 197 190 ALA 198 191 PRO 199 192 GLU 200 193 ILE 201 194 MET 202 195 LEU 203 196 ASN 204 197 TRP 205 198 MET 206 199 HIS 207 200 TYR 208 201 ASN 209 202 GLN 210 203 THR 211 204 VAL 212 205 ASP 213 206 ILE 214 207 TRP 215 208 SER 216 209 VAL 217 210 GLY 218 211 CYS 219 212 ILE 220 213 MET 221 214 ALA 222 215 GLU 223 216 LEU 224 217 LEU 225 218 THR 226 219 GLY 227 220 ARG 228 221 THR 229 222 LEU 230 223 PHE 231 224 PRO 232 225 GLY 233 226 THR 234 227 ASP 235 228 HIS 236 229 ILE 237 230 ASP 238 231 GLN 239 232 LEU 240 233 LYS 241 234 LEU 242 235 ILE 243 236 LEU 244 237 ARG 245 238 LEU 246 239 VAL 247 240 GLY 248 241 THR 249 242 PRO 250 243 GLY 251 244 ALA 252 245 GLU 253 246 LEU 254 247 LEU 255 248 LYS 256 249 LYS 257 250 ILE 258 251 SER 259 252 SER 260 253 GLU 261 254 SER 262 255 ALA 263 256 ARG 264 257 ASN 265 258 TYR 266 259 ILE 267 260 GLN 268 261 SER 269 262 LEU 270 263 THR 271 264 GLN 272 265 MET 273 266 PRO 274 267 LYS 275 268 MET 276 269 ASN 277 270 PHE 278 271 ALA 279 272 ASN 280 273 VAL 281 274 PHE 282 275 ILE 283 276 GLY 284 277 ALA 285 278 ASN 286 279 PRO 287 280 LEU 288 281 ALA 289 282 VAL 290 283 ASP 291 284 LEU 292 285 LEU 293 286 GLU 294 287 LYS 295 288 MET 296 289 LEU 297 290 VAL 298 291 LEU 299 292 ASP 300 293 SER 301 294 ASP 302 295 LYS 303 296 ARG 304 297 ILE 305 298 THR 306 299 ALA 307 300 ALA 308 301 GLN 309 302 ALA 310 303 LEU 311 304 ALA 312 305 HIS 313 306 ALA 314 307 TYR 315 308 PHE 316 309 ALA 317 310 GLN 318 311 TYR 319 312 HIS 320 313 ASP 321 314 PRO 322 315 ASP 323 316 ASP 324 317 GLU 325 318 PRO 326 319 VAL 327 320 ALA 328 321 ASP 329 322 PRO 330 323 TYR 331 324 ASP 332 325 GLN 333 326 SER 334 327 PHE 335 328 GLU 336 329 SER 337 330 ARG 338 331 ASP 339 332 LEU 340 333 LEU 341 334 ILE 342 335 ASP 343 336 GLU 344 337 TRP 345 338 LYS 346 339 SER 347 340 LEU 348 341 THR 349 342 TYR 350 343 ASP 351 344 GLU 352 345 VAL 353 346 ILE 354 347 SER 355 348 PHE 356 349 VAL 357 350 PRO 358 351 PRO 359 352 PRO 360 353 LEU 361 354 ASP 362 355 GLN 363 356 GLU 364 357 GLU 365 358 MET 366 359 GLU 367 360 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 17471 p38_alpha 95.64 352 98.86 98.86 0.00e+00 BMRB 17940 p38alpha 95.10 349 98.57 98.85 0.00e+00 BMRB 19930 Non-phosphorylated_human_p38_alpha_(apo) 100.00 367 99.46 99.46 0.00e+00 BMRB 19934 Dual-phosphorylated_human_p38_alpha_(apo) 100.00 367 100.00 100.00 0.00e+00 BMRB 19935 Dual-phosphorylated_human_p38_alpha 100.00 367 100.00 100.00 0.00e+00 BMRB 19936 dual-phosphorylated_human_p38_alpha_(apo) 100.00 367 100.00 100.00 0.00e+00 PDB 1DI9 "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" 97.82 360 99.44 99.44 0.00e+00 PDB 1IAN "Human P38 Map Kinase Inhibitor Complex" 99.18 366 99.45 99.45 0.00e+00 PDB 1KV1 "P38 Map Kinase In Complex With Inhibitor 1" 97.82 360 99.44 99.44 0.00e+00 PDB 1KV2 "Human P38 Map Kinase In Complex With Birb 796" 97.82 360 99.44 99.44 0.00e+00 PDB 1LEW "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" 97.82 360 98.89 98.89 0.00e+00 PDB 1LEZ "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" 97.82 360 98.89 98.89 0.00e+00 PDB 1M7Q "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 1OUK "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 1OUY "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 1OVE "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" 99.18 366 98.08 98.08 0.00e+00 PDB 1OZ1 "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" 100.54 372 98.37 98.64 0.00e+00 PDB 1R39 "The Structure Of P38alpha" 99.18 366 98.35 98.35 0.00e+00 PDB 1R3C "The Structure Of P38alpha C162s Mutant" 99.18 366 98.08 98.08 0.00e+00 PDB 1W7H "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 1W82 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 1W83 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 1W84 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 1WBN "Fragment Based P38 Inhibitors" 97.82 360 99.44 99.44 0.00e+00 PDB 1WBO "Fragment Based P38 Inhibitors" 97.82 360 99.44 99.44 0.00e+00 PDB 1WBS "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 97.82 360 99.44 99.44 0.00e+00 PDB 1WBT "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." 97.82 360 99.44 99.44 0.00e+00 PDB 1WBV "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 97.82 360 99.44 99.44 0.00e+00 PDB 1WBW "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 97.82 360 99.44 99.44 0.00e+00 PDB 1WFC "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" 99.18 366 98.35 98.35 0.00e+00 PDB 1YQJ "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 1YW2 "Mutated Mus Musculus P38 Kinase (Mp38)" 97.82 360 98.89 98.89 0.00e+00 PDB 1YWR "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" 97.82 360 99.16 99.16 0.00e+00 PDB 1ZYJ "Human P38 Map Kinase In Complex With Inhibitor 1a" 97.82 360 99.44 99.44 0.00e+00 PDB 1ZZ2 "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" 97.82 360 99.44 99.44 0.00e+00 PDB 1ZZL "Crystal Structure Of P38 With Triazolopyridine" 95.64 351 99.43 99.43 0.00e+00 PDB 2BAJ "P38alpha Bound To Pyrazolourea" 99.46 365 99.45 99.45 0.00e+00 PDB 2BAK "P38alpha Map Kinase Bound To Mpaq" 99.46 365 99.45 99.45 0.00e+00 PDB 2BAL "P38alpha Map Kinase Bound To Pyrazoloamine" 99.46 365 99.18 99.18 0.00e+00 PDB 2BAQ "P38alpha Bound To Ro3201195" 99.46 365 98.90 99.18 0.00e+00 PDB 2FSL "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" 100.00 367 98.91 98.91 0.00e+00 PDB 2FSM "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" 100.00 367 98.91 98.91 0.00e+00 PDB 2FSO "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" 100.00 367 99.18 99.18 0.00e+00 PDB 2FST "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" 100.00 367 98.91 98.91 0.00e+00 PDB 2GFS "P38 Kinase Crystal Structure In Complex With Ro3201195" 100.54 372 98.37 98.64 0.00e+00 PDB 2GHL "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" 94.82 348 98.85 98.85 0.00e+00 PDB 2GHM "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" 94.82 348 98.85 98.85 0.00e+00 PDB 2GTM "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" 94.82 348 98.85 98.85 0.00e+00 PDB 2GTN "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" 94.82 348 98.85 98.85 0.00e+00 PDB 2I0H "The Structure Of P38alpha In Complex With An Arylpyridazinone" 99.18 366 98.08 98.08 0.00e+00 PDB 2LGC "Joint Nmr And X-Ray Refinement Reveals The Structure Of A Novel Dibenzo[a,D]cycloheptenone InhibitorP38 MAP KINASE COMPLEX IN S" 97.55 359 98.32 98.32 0.00e+00 PDB 2NPQ "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" 100.00 367 99.46 99.46 0.00e+00 PDB 2OKR "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 99.18 366 98.35 98.35 0.00e+00 PDB 2ONL "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 99.18 366 98.35 98.35 0.00e+00 PDB 2OZA "Structure Of P38alpha Complex" 99.18 366 98.90 98.90 0.00e+00 PDB 2PUU "Crystal Structure Of P38 Complex With 1-(5-Tert-Butyl-2-P- Tolyl-2h-Pyrazol-3-Yl)-3-[4-(6-Morpholin-4-Ylmethyl- Pyridin-3-Yl)na" 94.82 348 98.28 98.28 0.00e+00 PDB 2QD9 "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" 99.18 366 99.45 99.45 0.00e+00 PDB 2RG5 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" 99.18 366 99.45 99.45 0.00e+00 PDB 2RG6 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" 99.18 366 99.45 99.45 0.00e+00 PDB 2Y8O "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" 97.82 362 99.16 99.16 0.00e+00 PDB 2YIS "Triazolopyridine Inhibitors Of P38 Kinase." 97.82 359 99.44 99.44 0.00e+00 PDB 2YIW "Triazolopyridine Inhibitors Of P38 Kinase" 97.82 359 99.44 99.44 0.00e+00 PDB 2YIX "Triazolopyridine Inhibitors Of P38" 95.64 351 99.43 99.43 0.00e+00 PDB 2ZAZ "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 2ZB0 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 2ZB1 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 3BV2 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" 99.18 366 99.45 99.45 0.00e+00 PDB 3BV3 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" 99.18 366 99.45 99.45 0.00e+00 PDB 3BX5 "P38 Alpha Map Kinase Complexed With Bms-640994" 99.18 366 99.45 99.45 0.00e+00 PDB 3C5U "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" 99.18 366 99.45 99.45 0.00e+00 PDB 3CTQ "Structure Of Map Kinase P38 In Complex With A 1-O-Tolyl-1,2, 3-Triazole-4-Carboxamide" 94.82 348 98.28 98.28 0.00e+00 PDB 3D7Z "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 97.82 360 99.16 99.16 0.00e+00 PDB 3D83 "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 97.82 360 98.89 98.89 0.00e+00 PDB 3DS6 "P38 Complex With A Phthalazine Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 3E92 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 100.27 371 98.10 98.10 0.00e+00 PDB 3E93 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 100.27 371 98.10 98.10 0.00e+00 PDB 3FC1 "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 3FI4 "P38 Kinase Crystal Structure In Complex With Ro4499" 100.54 372 98.10 98.64 0.00e+00 PDB 3FKL "P38 Kinase Crystal Structure In Complex With Ro9552" 100.54 372 98.37 98.64 0.00e+00 PDB 3FKN "P38 Kinase Crystal Structure In Complex With Ro7125" 100.54 372 98.37 98.64 0.00e+00 PDB 3FKO "P38 Kinase Crystal Structure In Complex With Ro3668" 100.54 372 98.10 98.64 0.00e+00 PDB 3FL4 "P38 Kinase Crystal Structure In Complex With Ro5634" 100.54 372 98.37 98.64 0.00e+00 PDB 3FLN "P38 Kinase Crystal Structure In Complex With R1487" 100.54 372 98.10 98.64 0.00e+00 PDB 3FLQ "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((S)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" 100.54 372 98.37 98.64 0.00e+00 PDB 3FLS "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((R)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" 100.54 372 98.37 98.64 0.00e+00 PDB 3FLW "P38 Kinase Crystal Structure In Complex With Pamapimod" 100.54 372 98.37 98.64 0.00e+00 PDB 3FLY "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-Isopropylamino-8-Methyl-8h-Pyrido[2,3- D]pyrimidin-7-O" 100.54 372 98.37 98.64 0.00e+00 PDB 3FLZ "P38 Kinase Crystal Structure In Complex With 8-Methyl-6-Phenoxy-2- (Tetrahydro-Pyran-4-Ylamino)-8h-Pyrido[2,3-D]pyrimidin-7-One" 100.54 372 98.37 98.64 0.00e+00 PDB 3FMH "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((R)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" 100.54 372 98.37 98.64 0.00e+00 PDB 3FMJ "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" 100.54 372 98.37 98.64 0.00e+00 PDB 3FMK "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((S)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" 100.54 372 98.37 98.64 0.00e+00 PDB 3FML "P38 Kinase Crystal Structure In Complex With Ro6224" 100.54 372 98.37 98.64 0.00e+00 PDB 3FMM "P38 Kinase Crystal Structure In Complex With Ro6226" 100.54 372 98.37 98.64 0.00e+00 PDB 3FMN "P38 Kinase Crystal Structure In Complex With Ro2530" 100.54 372 98.37 98.64 0.00e+00 PDB 3FSF "P38 Kinase Crystal Structure In Complex With 3-(2,6- Dichloro-Phenyl)-7-[4-(2-Diethylamino-Ethoxy)-Phenylamino]- 1-Methyl-3,4-D" 100.54 372 98.37 98.64 0.00e+00 PDB 3FSK "P38 Kinase Crystal Structure In Complex With Ro6257" 100.54 372 98.37 98.64 0.00e+00 PDB 3GC7 "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" 99.18 366 98.08 98.08 0.00e+00 PDB 3GCP "Human P38 Map Kinase In Complex With Sb203580" 97.82 360 98.33 98.33 0.00e+00 PDB 3GCQ "Human P38 Map Kinase In Complex With Rl45" 97.82 360 98.33 98.33 0.00e+00 PDB 3GCS "Human P38 Map Kinase In Complex With Sorafenib" 97.82 360 98.33 98.33 0.00e+00 PDB 3GCU "Human P38 Map Kinase In Complex With Rl48" 97.82 360 99.44 99.44 0.00e+00 PDB 3GCV "Human P38 Map Kinase In Complex With Rl62" 97.82 360 98.33 98.33 0.00e+00 PDB 3GFE "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 3GI3 "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" 97.82 360 98.89 98.89 0.00e+00 PDB 3HEC "P38 In Complex With Imatinib" 94.82 348 99.43 99.43 0.00e+00 PDB 3HEG "P38 In Complex With Sorafenib" 94.82 348 99.43 99.43 0.00e+00 PDB 3HL7 "Crystal Structure Of Human P38alpha Complexed With Sd-0006" 97.82 360 99.44 99.44 0.00e+00 PDB 3HLL "Crystal Structure Of Human P38alpha Complexed With Ph-797804" 97.82 360 99.44 99.44 0.00e+00 PDB 3HP2 "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" 97.82 360 99.44 99.44 0.00e+00 PDB 3HP5 "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" 97.82 360 99.44 99.44 0.00e+00 PDB 3HRB "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 359 99.44 99.44 0.00e+00 PDB 3HUB "Human P38 Map Kinase In Complex With Scios-469" 97.82 360 98.33 98.33 0.00e+00 PDB 3HUC "Human P38 Map Kinase In Complex With Rl40" 97.82 360 99.44 99.44 0.00e+00 PDB 3HV3 "Human P38 Map Kinase In Complex With Rl49" 97.82 360 98.33 98.33 0.00e+00 PDB 3HV4 "Human P38 Map Kinase In Complex With Rl51" 97.82 360 99.44 99.44 0.00e+00 PDB 3HV5 "Human P38 Map Kinase In Complex With Rl24" 97.82 360 99.44 99.44 0.00e+00 PDB 3HV6 "Human P38 Map Kinase In Complex With Rl39" 97.82 360 99.44 99.44 0.00e+00 PDB 3HV7 "Human P38 Map Kinase In Complex With Rl38" 97.82 360 99.44 99.44 0.00e+00 PDB 3HVC "Crystal Structure Of Human P38alpha Map Kinase" 97.82 362 99.44 99.44 0.00e+00 PDB 3IPH "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" 97.82 360 98.89 98.89 0.00e+00 PDB 3ITZ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 3IW5 "Human P38 Map Kinase In Complex With An Indole Derivative" 97.82 360 98.33 98.33 0.00e+00 PDB 3IW6 "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" 97.82 360 98.33 98.33 0.00e+00 PDB 3IW7 "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" 97.82 360 98.33 98.33 0.00e+00 PDB 3IW8 "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" 97.82 360 98.33 98.33 0.00e+00 PDB 3K3I "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" 94.82 350 99.43 99.43 0.00e+00 PDB 3K3J "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" 97.82 362 99.44 99.44 0.00e+00 PDB 3KF7 "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" 97.82 360 99.44 99.44 0.00e+00 PDB 3L8S "Human P38 Map Kinase In Complex With Cp-547632" 97.82 360 98.33 98.33 0.00e+00 PDB 3L8X "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" 99.18 366 99.45 99.45 0.00e+00 PDB 3LFA "Human P38 Map Kinase In Complex With Dasatinib" 97.82 360 99.44 99.44 0.00e+00 PDB 3LFB "Human P38 Map Kinase In Complex With Rl98" 97.82 360 98.33 98.33 0.00e+00 PDB 3LFC "Human P38 Map Kinase In Complex With Rl99" 97.82 360 98.33 98.33 0.00e+00 PDB 3LFD "Human P38 Map Kinase In Complex With Rl113" 97.82 360 98.33 98.33 0.00e+00 PDB 3LFE "Human P38 Map Kinase In Complex With Rl116" 97.82 360 98.33 98.33 0.00e+00 PDB 3LFF "Human P38 Map Kinase In Complex With Rl166" 97.82 360 98.33 98.33 0.00e+00 PDB 3LHJ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." 99.18 366 98.35 98.35 0.00e+00 PDB 3MGY "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " 97.82 360 99.44 99.44 0.00e+00 PDB 3MH0 "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " 97.82 360 99.16 99.16 0.00e+00 PDB 3MH1 "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" 97.82 360 99.16 99.16 0.00e+00 PDB 3MH2 "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" 97.82 360 99.16 99.44 0.00e+00 PDB 3MH3 "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" 97.82 360 99.16 99.16 0.00e+00 PDB 3MPA "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.16 0.00e+00 PDB 3MPT "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" 100.27 371 98.37 98.37 0.00e+00 PDB 3MVL "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" 99.18 366 99.45 99.45 0.00e+00 PDB 3MVM "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" 99.18 366 99.45 99.45 0.00e+00 PDB 3MW1 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 359 99.44 99.44 0.00e+00 PDB 3NEW "P38-Alpha Complexed With Compound 10" 99.18 366 98.08 98.08 0.00e+00 PDB 3NNU "Crystal Structure Of P38 Alpha In Complex With Dp1376" 96.19 354 99.43 99.43 0.00e+00 PDB 3NNV "Crystal Structure Of P38 Alpha In Complex With Dp437" 96.19 354 99.43 99.43 0.00e+00 PDB 3NNW "Crystal Structure Of P38 Alpha In Complex With Dp802" 96.19 354 99.43 99.43 0.00e+00 PDB 3NNX "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" 96.19 354 99.72 99.72 0.00e+00 PDB 3NWW "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" 99.18 366 99.45 99.45 0.00e+00 PDB 3O8P "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.16 0.00e+00 PDB 3O8T "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.16 0.00e+00 PDB 3O8U "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.44 0.00e+00 PDB 3OBG "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.16 0.00e+00 PDB 3OBJ "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.16 0.00e+00 PDB 3OC1 "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 97.82 360 99.16 99.16 0.00e+00 PDB 3OCG "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" 99.18 366 99.45 99.45 0.00e+00 PDB 3OD6 "Crystal Structure Of P38alpha Y323t Active Mutant" 97.82 360 99.16 99.16 0.00e+00 PDB 3ODY "Crystal Structure Of P38alpha Y323q Active Mutant" 97.82 360 99.16 99.16 0.00e+00 PDB 3ODZ "Crystal Structure Of P38alpha Y323r Active Mutant" 97.82 360 99.16 99.16 0.00e+00 PDB 3OEF "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" 97.82 360 99.16 99.44 0.00e+00 PDB 3P4K "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" 100.82 370 97.84 98.11 0.00e+00 PDB 3P5K "P38 Inhibitor-Bound" 99.18 366 98.90 98.90 0.00e+00 PDB 3P78 "P38 Inhibitor-Bound" 99.18 366 98.90 98.90 0.00e+00 PDB 3P79 "P38 Inhibitor-Bound" 99.18 366 98.90 98.90 0.00e+00 PDB 3P7A "P38 Inhibitor-Bound" 99.18 366 98.90 98.90 0.00e+00 PDB 3P7B "P38 Inhibitor-Bound" 99.18 366 98.90 98.90 0.00e+00 PDB 3P7C "P38 Inhibitor-Bound" 99.18 366 98.90 98.90 0.00e+00 PDB 3PG3 "Human P38 Map Kinase In Complex With Rl182" 97.82 360 98.33 98.33 0.00e+00 PDB 3QUD "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" 97.82 360 99.44 99.44 0.00e+00 PDB 3QUE "Human P38 Map Kinase In Complex With Skepinone-l" 97.82 360 99.44 99.44 0.00e+00 PDB 3RIN "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 97.82 360 99.44 99.44 0.00e+00 PDB 3ROC "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" 97.82 360 99.44 99.44 0.00e+00 PDB 3S3I "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 95.10 349 99.43 99.43 0.00e+00 PDB 3S4Q "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" 99.18 366 99.45 99.45 0.00e+00 PDB 3U8W "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" 99.18 366 98.35 98.35 0.00e+00 PDB 3UVP "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" 97.82 360 99.44 99.44 0.00e+00 PDB 3UVQ "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" 97.82 360 99.44 99.44 0.00e+00 PDB 3UVR "Human P38 Map Kinase In Complex With Km064" 97.82 360 99.44 99.44 0.00e+00 PDB 3ZS5 "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" 98.09 362 99.44 99.44 0.00e+00 PDB 3ZSG "X-Ray Structure Of P38alpha Bound To Tak-715" 98.09 362 99.44 99.44 0.00e+00 PDB 3ZSH "X-Ray Structure Of P38alpha Bound To Scio-469" 98.09 362 99.44 99.44 0.00e+00 PDB 3ZSI "X-Ray Structure Of P38alpha Bound To Vx-745" 98.09 362 99.44 99.44 0.00e+00 PDB 3ZYA "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" 99.18 366 98.35 98.35 0.00e+00 PDB 4A9Y "P38alpha Map Kinase Bound To Cmpd 8" 99.46 365 99.45 99.45 0.00e+00 PDB 4AA0 "P38alpha Map Kinase Bound To Cmpd 2" 99.46 365 99.45 99.45 0.00e+00 PDB 4AA4 "P38alpha Map Kinase Bound To Cmpd 22" 99.46 365 99.45 99.45 0.00e+00 PDB 4AA5 "P38alpha Map Kinase Bound To Cmpd 33" 99.46 365 99.18 99.18 0.00e+00 PDB 4AAC "P38alpha Map Kinase Bound To Cmpd 29" 99.46 365 99.45 99.45 0.00e+00 PDB 4DLI "Human P38 Map Kinase In Complex With Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4DLJ "Human P38 Map Kinase In Complex With Rl163" 97.82 360 99.44 99.44 0.00e+00 PDB 4E5A "The W197a Mutant Of P38a Map Kinase" 97.82 360 99.16 99.16 0.00e+00 PDB 4E5B "Structure Of P38a Map Kinase Without Bog" 97.82 360 99.44 99.44 0.00e+00 PDB 4E6A "P38a-pia23 Complex" 97.82 360 99.44 99.44 0.00e+00 PDB 4E6C "P38a-perifosine Complex" 97.82 360 99.44 99.44 0.00e+00 PDB 4E8A "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH2 "Human P38 Map Kinase In Complex With Np-F1 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH3 "Human P38 Map Kinase In Complex With Np-F2 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH4 "Human P38 Map Kinase In Complex With Np-F3 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH5 "Human P38 Map Kinase In Complex With Np-F4 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH6 "Human P38 Map Kinase In Complex With Np-F5 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH7 "Human P38 Map Kinase In Complex With Np-F6 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH8 "Human P38 Map Kinase In Complex With Np-F7 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EH9 "Human P38 Map Kinase In Complex With Np-F11 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4EHV "Human P38 Map Kinase In Complex With Np-F10 And Rl87" 97.82 360 99.44 99.44 0.00e+00 PDB 4GEO "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" 100.00 367 97.55 97.55 0.00e+00 PDB 4KA3 "Structure Of Map Kinase In Complex With A Docking Peptide" 97.82 360 98.89 98.89 0.00e+00 PDB 4KIN "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 99.18 366 99.45 99.45 0.00e+00 PDB 4KIP "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 2-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 99.18 366 99.45 99.45 0.00e+00 PDB 4KIQ "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With Ethyl 6-((5-(cyclopropylcarbamoyl)-2-methylpheny" 99.18 366 99.45 99.45 0.00e+00 PDB 4L8M "Human P38 Map Kinase In Complex With A Dibenzoxepinone" 97.82 360 99.44 99.44 0.00e+00 PDB 4LOO "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" 97.82 361 98.89 98.89 0.00e+00 PDB 4LOP "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" 97.82 361 98.89 98.89 0.00e+00 PDB 4LOQ "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" 97.82 361 98.89 98.89 0.00e+00 PDB 4TYH "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" 94.82 348 98.85 98.85 0.00e+00 DBJ BAB85654 "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" 68.94 307 99.21 99.21 0.00e+00 DBJ BAE21782 "unnamed protein product [Mus musculus]" 97.82 360 98.89 98.89 0.00e+00 DBJ BAE30324 "unnamed protein product [Mus musculus]" 77.11 283 98.94 98.94 0.00e+00 DBJ BAE31659 "unnamed protein product [Mus musculus]" 77.11 283 98.94 98.94 0.00e+00 DBJ BAF84398 "unnamed protein product [Homo sapiens]" 97.82 360 99.16 99.16 0.00e+00 EMBL CAG38743 "MAPK14 [Homo sapiens]" 97.82 360 99.44 99.44 0.00e+00 GB AAA20888 "MAP kinase [Mus musculus]" 97.82 360 98.89 98.89 0.00e+00 GB AAA57456 "CSaids binding protein [Homo sapiens]" 97.82 360 99.44 99.44 0.00e+00 GB AAA74301 "MAP kinase [Homo sapiens]" 97.82 360 99.44 99.44 0.00e+00 GB AAB51285 "p38 mitogen activated protein kinase [Rattus norvegicus]" 97.82 360 97.49 98.33 0.00e+00 GB AAC36131 "p38 mitogen activated protein kinase [Canis lupus familiaris]" 97.82 360 98.89 99.44 0.00e+00 PRF 2111247A "p38 mitogen-activated protein kinase" 97.82 360 99.44 99.44 0.00e+00 PRF 2124426A "Mxi2 protein" 76.29 297 98.93 98.93 0.00e+00 REF NP_001003206 "mitogen-activated protein kinase 14 [Canis lupus familiaris]" 97.82 360 98.89 99.44 0.00e+00 REF NP_001136366 "mitogen-activated protein kinase 14 [Ovis aries]" 97.82 360 99.44 99.44 0.00e+00 REF NP_001161985 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.11 283 98.94 98.94 0.00e+00 REF NP_001161986 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.11 283 98.94 98.94 0.00e+00 REF NP_036081 "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" 97.82 360 98.89 98.89 0.00e+00 SP O02812 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " 97.82 360 98.89 99.44 0.00e+00 SP P47811 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" 97.82 360 98.89 98.89 0.00e+00 SP P70618 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" 97.82 360 98.05 98.61 0.00e+00 SP Q16539 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" 97.82 360 99.44 99.44 0.00e+00 stop_ save_ save_MK2_334-D_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MK2_334/D_peptide _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 86 _Mol_residue_sequence ; GPMQSTKVPQTPLHTSRVLK EDKERWEDVKEEMTSALATM RVDYEQIKIKKIEDASNPLL LKRRKKARALEAAALAHWLE HHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 326 GLY 2 327 PRO 3 328 MET 4 329 GLN 5 330 SER 6 331 THR 7 332 LYS 8 333 VAL 9 334 PRO 10 335 GLN 11 336 THR 12 337 PRO 13 338 LEU 14 339 HIS 15 340 THR 16 341 SER 17 342 ARG 18 343 VAL 19 344 LEU 20 345 LYS 21 346 GLU 22 347 ASP 23 348 LYS 24 349 GLU 25 350 ARG 26 351 TRP 27 352 GLU 28 353 ASP 29 354 VAL 30 355 LYS 31 356 GLU 32 357 GLU 33 358 MET 34 359 THR 35 360 SER 36 361 ALA 37 362 LEU 38 363 ALA 39 364 THR 40 365 MET 41 366 ARG 42 367 VAL 43 368 ASP 44 369 TYR 45 370 GLU 46 371 GLN 47 372 ILE 48 373 LYS 49 374 ILE 50 375 LYS 51 376 LYS 52 377 ILE 53 378 GLU 54 379 ASP 55 380 ALA 56 381 SER 57 382 ASN 58 383 PRO 59 384 LEU 60 385 LEU 61 386 LEU 62 387 LYS 63 388 ARG 64 389 ARG 65 390 LYS 66 391 LYS 67 392 ALA 68 393 ARG 69 394 ALA 70 395 LEU 71 396 GLU 72 397 ALA 73 398 ALA 74 399 ALA 75 400 LEU 76 401 ALA 77 402 HIS 78 403 TRP 79 404 LEU 80 405 GLU 81 406 HIS 82 407 HIS 83 408 HIS 84 409 HIS 85 410 HIS 86 411 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 19936 MK2_334/D_peptide 100.00 86 100.00 100.00 9.89e-54 PDB 1KWP "Crystal Structure Of Mapkap2" 87.21 400 100.00 100.00 3.28e-41 PDB 1NXK "Crystal Structure Of Staurosporine Bound To Map Kap Kinase 2" 86.05 400 98.65 98.65 2.78e-39 PDB 1NY3 "Crystal Structure Of Adp Bound To Map Kap Kinase 2" 87.21 400 100.00 100.00 3.28e-41 PDB 2ONL "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 87.21 406 100.00 100.00 4.00e-41 PDB 2OZA "Structure Of P38alpha Complex" 87.21 356 100.00 100.00 2.00e-41 PDB 2P3G "Crystal Structure Of A Pyrrolopyridine Inhibitor Bound To Mapkap Kinase-2" 53.49 327 100.00 100.00 9.62e-22 PDB 3FYJ "Crystal Structure Of An Optimzied Benzothiophene Inhibitor Bound To Mapkap Kinase-2 (Mk-2)" 53.49 327 100.00 100.00 9.62e-22 PDB 3FYK "Crystal Structure Of A Benzthiophene Lead Bound To Mapkap Kinase-2 (Mk-2)" 53.49 327 100.00 100.00 9.62e-22 DBJ BAE33092 "unnamed protein product [Mus musculus]" 87.21 386 97.33 98.67 8.98e-40 DBJ BAJ20782 "mitogen-activated protein kinase-activated protein kinase 2 [synthetic construct]" 87.21 400 100.00 100.00 3.28e-41 EMBL CAA53094 "MAP kinase activated protein kinase-2 [Homo sapiens]" 87.21 396 100.00 100.00 2.52e-41 EMBL CAA54183 "MAP kinase-activated protein kinase 2 [Mus musculus]" 87.21 385 97.33 98.67 7.10e-40 EMBL CAA57700 "MapKap kinase 2 [Cricetulus longicaudatus]" 87.21 329 98.67 100.00 5.05e-41 GB AAH24559 "Mapkapk2 protein, partial [Mus musculus]" 87.21 181 97.33 98.67 1.86e-41 GB AAH36060 "Mitogen-activated protein kinase-activated protein kinase 2 [Homo sapiens]" 87.21 400 100.00 100.00 3.28e-41 GB AAH52584 "Mitogen-activated protein kinase-activated protein kinase 2 [Homo sapiens]" 87.21 400 100.00 100.00 3.28e-41 GB AAH63064 "MAP kinase-activated protein kinase 2 [Mus musculus]" 87.21 386 97.33 98.67 8.98e-40 GB AIC55551 "MAPKAPK2, partial [synthetic construct]" 87.21 400 100.00 100.00 3.28e-41 REF NP_032577 "MAP kinase-activated protein kinase 2 [Mus musculus]" 87.21 386 97.33 98.67 8.98e-40 REF NP_116584 "MAP kinase-activated protein kinase 2 isoform 2 [Homo sapiens]" 87.21 400 100.00 100.00 3.28e-41 REF XP_001085549 "PREDICTED: MAP kinase-activated protein kinase 2 isoform 2 [Macaca mulatta]" 87.21 402 100.00 100.00 3.72e-41 REF XP_001164988 "PREDICTED: MAP kinase-activated protein kinase 2 [Pan troglodytes]" 87.21 400 100.00 100.00 3.60e-41 REF XP_001255255 "PREDICTED: MAP kinase-activated protein kinase 2 isoform X1 [Bos taurus]" 87.21 533 100.00 100.00 1.06e-40 SP P49136 "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" 87.21 329 98.67 100.00 5.05e-41 SP P49137 "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" 87.21 400 100.00 100.00 3.28e-41 SP P49138 "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" 87.21 386 97.33 98.67 8.98e-40 SP P49139 "RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP" 87.21 366 100.00 100.00 2.94e-41 TPG DAA21536 "TPA: MAP kinase-activated protein kinase 2-like [Bos taurus]" 87.21 509 100.00 100.00 1.46e-40 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_TPO _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOTHREONINE _BMRB_code TPO _PDB_code TPO _Standard_residue_derivative . _Molecular_mass 199.099 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG2 CG2 C . 0 . ? OG1 OG1 O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB HB H . 0 . ? HG21 HG21 H . 0 . ? HG22 HG22 H . 0 . ? HG23 HG23 H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? HXT HXT 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 N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG2 ? ? SING CB OG1 ? ? SING CB HB ? ? SING CG2 HG21 ? ? SING CG2 HG22 ? ? SING CG2 HG23 ? ? SING OG1 P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common O-PHOSPHOTYROSINE _BMRB_code PTR _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P 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 N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ save_ ############# # Ligands # ############# save_ADP _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common ADENOSINE-5'-DIPHOSPHATE _BMRB_code ADP _PDB_code ADP _Molecular_mass 427.201 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O3B O3B O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOB2 HOB2 H . 0 . ? HOB3 HOB3 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 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 DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING O3B HOB3 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dual-phosphorylated_human_p38_alpha_(apo) human 9606 Eukaryota Metazoa Homo sapiens $MK2_334-D_peptide 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 $dual-phosphorylated_human_p38_alpha_(apo) 'recombinant technology' . Escherichia coli . pET15b $MK2_334-D_peptide 'recombinant technology' . Escherichia coli . pET28b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $dual-phosphorylated_human_p38_alpha_(apo) 0.2 mM '[U-2H15N13C, ILVM-methyl-1H13C]' TRIS 25 mM '[U-100% 2H]' 'potassium chloride' 150 mM 'natural abundance' DTT 5 mM [U-2H] $MK2_334-D_peptide 0.2 mM 'natural abundance' $entity_ADP 5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller, R.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_(H)CC(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH _Sample_label $sample_4 save_ save_H(CCCO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH _Sample_label $sample_4 save_ save_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_4 save_ save_3D_1H-13C_NOESY_aliphatic_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_4 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 7.5 . pH pressure 1 . atm 'ionic strength' 150 . mM 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 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 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_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label (H)CC(CO)NH H(CCCO)NH HCCH-TOCSY '3D 1H-13C NOESY aliphatic' stop_ loop_ _Sample_label $sample_4 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'dual-phosphorylated human p38 alpha (apo)' _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 13 20 LEU HD1 H 0.31 0.014 2 2 13 20 LEU HD2 H 0.587 0.014 2 3 13 20 LEU CD1 C 25.421 0.045 1 4 13 20 LEU CD2 C 24.34 0.045 1 5 17 24 ILE HD1 H 0.739 0.014 1 6 17 24 ILE CD1 C 10.653 0.045 1 7 20 27 VAL HG1 H 0.865 0.014 2 8 20 27 VAL HG2 H 0.636 0.014 2 9 20 27 VAL CG1 C 21.572 0.045 1 10 20 27 VAL CG2 C 19.325 0.045 1 11 27 34 LEU HD1 H 0.7 0.014 2 12 27 34 LEU HD2 H 0.566 0.014 2 13 27 34 LEU CD1 C 24.654 0.045 1 14 27 34 LEU CD2 C 24.392 0.045 1 15 48 55 LEU HD1 H 0.772 0.014 2 16 48 55 LEU HD2 H 0.908 0.014 2 17 48 55 LEU CD1 C 24.826 0.045 1 18 48 55 LEU CD2 C 22.347 0.045 1 19 50 57 VAL HG1 H 0.767 0.014 2 20 50 57 VAL HG2 H 0.603 0.014 2 21 50 57 VAL CG1 C 22.138 0.045 1 22 50 57 VAL CG2 C 18.523 0.045 1 23 52 59 VAL HG1 H 1.044 0.014 2 24 52 59 VAL HG2 H 0.482 0.014 2 25 52 59 VAL CG1 C 22.267 0.045 1 26 52 59 VAL CG2 C 20.211 0.045 1 27 55 62 LEU HD1 H 0.765 0.014 2 28 55 62 LEU HD2 H 0.726 0.014 2 29 55 62 LEU CD1 C 25.449 0.045 1 30 55 62 LEU CD2 C 22.873 0.045 1 31 62 69 ILE HD1 H 0.935 0.014 1 32 62 69 ILE CD1 C 13.704 0.045 1 33 63 70 ILE HD1 H 0.849 0.014 1 34 63 70 ILE CD1 C 12.348 0.045 1 35 72 79 LEU HD1 H 0.875 0.014 2 36 72 79 LEU HD2 H 0.923 0.014 2 37 72 79 LEU CD1 C 24.764 0.045 1 38 72 79 LEU CD2 C 28.551 0.045 1 39 74 81 LEU HD1 H 0.627 0.014 2 40 74 81 LEU HD2 H 0.48 0.014 2 41 74 81 LEU CD1 C 25.306 0.045 1 42 74 81 LEU CD2 C 23.952 0.045 1 43 78 85 MET HE H 1.566 0.014 1 44 78 85 MET CE C 17.877 0.045 1 45 83 90 VAL HG1 H 1.307 0.014 2 46 83 90 VAL HG2 H 0.848 0.014 2 47 83 90 VAL CG1 C 22.584 0.045 1 48 83 90 VAL CG2 C 21.704 0.045 1 49 84 91 ILE HD1 H 1.187 0.014 1 50 84 91 ILE CD1 C 15.151 0.045 1 51 89 96 VAL HG1 H 0.716 0.014 2 52 89 96 VAL HG2 H 0.966 0.014 2 53 89 96 VAL CG1 C 20.125 0.045 1 54 89 96 VAL CG2 C 22.93 0.045 1 55 102 109 VAL HG1 H 0.795 0.014 2 56 102 109 VAL HG2 H 0.956 0.014 2 57 102 109 VAL CG1 C 21.171 0.045 1 58 102 109 VAL CG2 C 22.306 0.045 1 59 105 112 VAL HG1 H 0.871 0.014 2 60 105 112 VAL HG2 H 0.734 0.014 2 61 105 112 VAL CG1 C 20.851 0.045 1 62 105 112 VAL CG2 C 21.145 0.045 1 63 109 116 MET HE H 1.798 0.014 1 64 109 116 MET CE C 17.405 0.045 1 65 113 120 LEU HD1 H 0.771 0.014 2 66 113 120 LEU HD2 H 0.703 0.014 2 67 113 120 LEU CD1 C 24.363 0.045 1 68 113 120 LEU CD2 C 24.932 0.045 1 69 116 123 ILE HD1 H 0.617 0.014 1 70 116 123 ILE CD1 C 10.845 0.045 1 71 117 124 VAL HG1 H 1.029 0.014 2 72 117 124 VAL HG2 H 1.064 0.014 2 73 117 124 VAL CG1 C 21.298 0.045 1 74 117 124 VAL CG2 C 22.78 0.045 1 75 122 129 LEU HD1 H 0.779 0.014 2 76 122 129 LEU HD2 H 0.316 0.014 2 77 122 129 LEU CD1 C 25.77 0.045 1 78 122 129 LEU CD2 C 21.845 0.045 1 79 127 134 VAL HG1 H 1.159 0.014 2 80 127 134 VAL HG2 H 1.04 0.014 2 81 127 134 VAL CG1 C 23.134 0.045 1 82 127 134 VAL CG2 C 23.242 0.045 1 83 131 138 ILE HD1 H 0.54 0.014 1 84 131 138 ILE CD1 C 8.354 0.045 1 85 134 141 ILE HD1 H 0.607 0.014 1 86 134 141 ILE CD1 C 14.867 0.045 1 87 135 142 LEU HD1 H 0.704 0.014 2 88 135 142 LEU HD2 H 0.742 0.014 2 89 135 142 LEU CD1 C 28.299 0.045 1 90 135 142 LEU CD2 C 22.15 0.045 1 91 141 148 ILE HD1 H 0.765 0.014 1 92 141 148 ILE CD1 C 13.741 0.045 1 93 147 154 ILE HD1 H 0.483 0.014 1 94 147 154 ILE CD1 C 13.192 0.045 1 95 156 163 LEU HD1 H 0.632 0.014 2 96 156 163 LEU HD2 H 0.75 0.014 2 97 156 163 LEU CD1 C 28.249 0.045 1 98 156 163 LEU CD2 C 25.731 0.045 1 99 158 165 VAL HG1 H 0.847 0.014 2 100 158 165 VAL HG2 H 0.666 0.014 2 101 158 165 VAL CG1 C 21.902 0.045 1 102 158 165 VAL CG2 C 20.723 0.045 1 103 164 171 LEU HD1 H 0.68 0.014 2 104 164 171 LEU HD2 H -0.041 0.014 2 105 164 171 LEU CD1 C 27.175 0.045 1 106 164 171 LEU CD2 C 22.104 0.045 1 107 166 173 ILE HD1 H 0.945 0.014 1 108 166 173 ILE CD1 C 14.98 0.045 1 109 167 174 LEU HD1 H 0.208 0.014 2 110 167 174 LEU HD2 H -0.013 0.014 2 111 167 174 LEU CD1 C 21.391 0.045 1 112 167 174 LEU CD2 C 23.673 0.045 1 113 171 178 LEU HD1 H 0.153 0.014 2 114 171 178 LEU HD2 H 0.684 0.014 2 115 171 178 LEU CD1 C 23.374 0.045 1 116 171 178 LEU CD2 C 26.765 0.045 1 117 179 186 MET HE H 1.616 0.014 1 118 179 186 MET CE C 18.377 0.045 1 119 193 200 ILE HD1 H 0.814 0.014 1 120 193 200 ILE CD1 C 14.666 0.045 1 121 194 201 MET HE H 1.853 0.014 1 122 194 201 MET CE C 17.313 0.045 1 123 198 205 MET HE H 2.008 0.014 1 124 198 205 MET CE C 17.095 0.045 1 125 204 211 VAL HG1 H 1.347 0.014 2 126 204 211 VAL HG2 H 1.107 0.014 2 127 204 211 VAL CG1 C 22.382 0.045 1 128 204 211 VAL CG2 C 18.322 0.045 1 129 206 213 ILE HD1 H 0.656 0.014 1 130 206 213 ILE CD1 C 8.095 0.045 1 131 209 216 VAL HG1 H 0.819 0.014 2 132 209 216 VAL HG2 H 0.982 0.014 2 133 209 216 VAL CG1 C 22.484 0.045 1 134 209 216 VAL CG2 C 24.639 0.045 1 135 212 219 ILE HD1 H 0.355 0.014 1 136 212 219 ILE CD1 C 13.621 0.045 1 137 213 220 MET HE H 1.744 0.014 1 138 213 220 MET CE C 20.165 0.045 1 139 216 223 LEU HD1 H 0.792 0.014 2 140 216 223 LEU HD2 H 0.674 0.014 2 141 216 223 LEU CD1 C 26.123 0.045 1 142 216 223 LEU CD2 C 21.521 0.045 1 143 217 224 LEU HD1 H 0.528 0.014 2 144 217 224 LEU HD2 H 0.967 0.014 2 145 217 224 LEU CD1 C 26.274 0.045 1 146 217 224 LEU CD2 C 24.232 0.045 1 147 222 229 LEU HD1 H 0.436 0.014 2 148 222 229 LEU HD2 H 0.245 0.014 2 149 222 229 LEU CD1 C 21.496 0.045 1 150 222 229 LEU CD2 C 28.458 0.045 1 151 229 236 ILE HD1 H 0.453 0.014 1 152 229 236 ILE CD1 C 10.403 0.045 1 153 235 242 ILE HD1 H 0.646 0.014 1 154 235 242 ILE CD1 C 14.06 0.045 1 155 236 243 LEU HD1 H 0.732 0.014 2 156 236 243 LEU HD2 H 0.823 0.014 2 157 236 243 LEU CD1 C 26.394 0.045 1 158 236 243 LEU CD2 C 22.849 0.045 1 159 238 245 LEU HD1 H 0.633 0.014 2 160 238 245 LEU HD2 H 0.72 0.014 2 161 238 245 LEU CD1 C 23.948 0.045 1 162 238 245 LEU CD2 C 26.404 0.045 1 163 239 246 VAL HG1 H 1.446 0.014 2 164 239 246 VAL HG2 H 1.279 0.014 2 165 239 246 VAL CG1 C 22.209 0.045 1 166 239 246 VAL CG2 C 19.963 0.045 1 167 259 266 ILE HD1 H 0.81 0.014 1 168 259 266 ILE CD1 C 12.674 0.045 1 169 262 269 LEU HD1 H 0.794 0.014 2 170 262 269 LEU HD2 H 0.75 0.014 2 171 262 269 LEU CD1 C 24.935 0.045 1 172 262 269 LEU CD2 C 23.93 0.045 1 173 265 272 MET HE H 2.076 0.014 1 174 265 272 MET CE C 17.394 0.045 1 175 268 275 MET HE H 2.067 0.014 1 176 268 275 MET CE C 17.054 0.045 1 177 273 280 VAL HG1 H -0.158 0.014 2 178 273 280 VAL HG2 H 0.69 0.014 2 179 273 280 VAL CG1 C 19.466 0.045 1 180 273 280 VAL CG2 C 21.243 0.045 1 181 275 282 ILE HD1 H 0.863 0.014 1 182 275 282 ILE CD1 C 12.238 0.045 1 183 280 287 LEU HD1 H 0.954 0.014 2 184 280 287 LEU HD2 H 0.871 0.014 2 185 280 287 LEU CD1 C 25.48 0.045 1 186 280 287 LEU CD2 C 22.621 0.045 1 187 282 289 VAL HG1 H 1.006 0.014 2 188 282 289 VAL HG2 H 0.983 0.014 2 189 282 289 VAL CG1 C 22.768 0.045 1 190 282 289 VAL CG2 C 23.63 0.045 1 191 284 291 LEU HD1 H 0.659 0.014 2 192 284 291 LEU HD2 H 0.698 0.014 2 193 284 291 LEU CD1 C 22.53 0.045 1 194 284 291 LEU CD2 C 28.344 0.045 1 195 285 292 LEU HD1 H -0.037 0.014 2 196 285 292 LEU HD2 H 0.571 0.014 2 197 285 292 LEU CD1 C 24.459 0.045 1 198 285 292 LEU CD2 C 24.828 0.045 1 199 288 295 MET HE H 1.919 0.014 1 200 288 295 MET CE C 18.665 0.045 1 201 289 296 LEU HD1 H 0.517 0.014 2 202 289 296 LEU HD2 H -0.273 0.014 2 203 289 296 LEU CD1 C 26.496 0.045 1 204 289 296 LEU CD2 C 21.624 0.045 1 205 290 297 VAL HG1 H 1.078 0.014 2 206 290 297 VAL HG2 H 0.962 0.014 2 207 290 297 VAL CG1 C 21.886 0.045 1 208 290 297 VAL CG2 C 21.369 0.045 1 209 291 298 LEU HD1 H 0.869 0.014 2 210 291 298 LEU HD2 H 0.845 0.014 2 211 291 298 LEU CD1 C 24.454 0.045 1 212 291 298 LEU CD2 C 24.003 0.045 1 213 297 304 ILE HD1 H 0.83 0.014 1 214 297 304 ILE CD1 C 13.974 0.045 1 215 303 310 LEU HD1 H 0.755 0.014 2 216 303 310 LEU HD2 H 0.424 0.014 2 217 303 310 LEU CD1 C 27.018 0.045 1 218 303 310 LEU CD2 C 25.11 0.045 1 219 319 326 VAL HG1 H 1.093 0.014 2 220 319 326 VAL HG2 H 0.945 0.014 2 221 319 326 VAL CG1 C 22.469 0.045 1 222 319 326 VAL CG2 C 17.25 0.045 1 223 332 339 LEU HD1 H -0.488 0.014 2 224 332 339 LEU HD2 H 0.281 0.014 2 225 332 339 LEU CD1 C 24.378 0.045 1 226 332 339 LEU CD2 C 22.358 0.045 1 227 333 340 LEU HD1 H 0.959 0.014 2 228 333 340 LEU HD2 H 0.959 0.014 2 229 333 340 LEU CD1 C 25.209 0.045 1 230 333 340 LEU CD2 C 22.094 0.045 1 231 334 341 ILE HD1 H 1.238 0.014 1 232 334 341 ILE CD1 C 13.439 0.045 1 233 340 347 LEU HD1 H 0.152 0.014 2 234 340 347 LEU HD2 H 0.579 0.014 2 235 340 347 LEU CD1 C 25.515 0.045 1 236 340 347 LEU CD2 C 22.748 0.045 1 237 345 352 VAL HG1 H 0.889 0.014 2 238 345 352 VAL HG2 H 1.121 0.014 2 239 345 352 VAL CG1 C 21.156 0.045 1 240 345 352 VAL CG2 C 23.141 0.045 1 241 346 353 ILE HD1 H 0.506 0.014 1 242 346 353 ILE CD1 C 11.828 0.045 1 243 349 356 VAL HG1 H 0.869 0.014 2 244 349 356 VAL HG2 H 0.829 0.014 2 245 349 356 VAL CG1 C 20.412 0.045 1 246 349 356 VAL CG2 C 20.447 0.045 1 247 353 360 LEU HD1 H 0.925 0.014 2 248 353 360 LEU HD2 H 0.877 0.014 2 249 353 360 LEU CD1 C 25.049 0.045 1 250 353 360 LEU CD2 C 23.422 0.045 1 251 358 365 MET HE H 2.105 0.014 1 252 358 365 MET CE C 17.046 0.045 1 stop_ save_