data_17940 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone resonance assignment of the activated p38 mitogen-activated protein kinase ; _BMRB_accession_number 17940 _BMRB_flat_file_name bmr17940.str _Entry_type original _Submission_date 2011-09-15 _Accession_date 2011-09-15 _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 Nielsen Gerd . . 2 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 188 "13C chemical shifts" 591 "15N chemical shifts" 188 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-14 update BMRB 'update entry citation' 2011-10-24 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6468 'mitogen-activated protein kinase p38 alpha' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR spectroscopic investigations of the activated p38 mitogen-activated protein kinase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22012687 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nielsen Gerd . . 2 Schwalbe Harald . . stop_ _Journal_abbreviation Chembiochem _Journal_name_full 'Chembiochem : a European journal of chemical biology' _Journal_volume 12 _Journal_issue 17 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2599 _Page_last 2607 _Year 2011 _Details . loop_ _Keyword activation assignment NMR p38 phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name p38alpha _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label p38alpha $p38alpha stop_ _System_molecular_weight 40211 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_p38alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p38alpha _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 349 _Mol_residue_sequence ; NSQERPTFYRQELNKTIWEV PERYQNLSPVGSGAYGSVCA AFDTKTGHRVAVKKLSRPFQ SIIHAKRTYRELRLLKHMKH ENVIGLLDVFTPARSLEEFN DVYLVTHLMGADLNNIVKCQ KLTDDHVQFLIYQILRGLKY IHSADIIHRDLKPSNLAVNE DCELKILDFGLARHTDDEMT GYVATRWYRAPEIMLNWMHY NQTVDIWSVGCIMAELLTGR TLFPGTDHIDQLKLILRLVG TPGAELLKKISSESARNYIQ SLAQMPKMNFANVFIGANPL AVDLLEKMLVLDSDKRITAA QALAHAYFAQYHDPDDEPVA DPYDQSFESRDLLIDEWKSL TYDEVISFV ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 SER 3 GLN 4 GLU 5 ARG 6 PRO 7 THR 8 PHE 9 TYR 10 ARG 11 GLN 12 GLU 13 LEU 14 ASN 15 LYS 16 THR 17 ILE 18 TRP 19 GLU 20 VAL 21 PRO 22 GLU 23 ARG 24 TYR 25 GLN 26 ASN 27 LEU 28 SER 29 PRO 30 VAL 31 GLY 32 SER 33 GLY 34 ALA 35 TYR 36 GLY 37 SER 38 VAL 39 CYS 40 ALA 41 ALA 42 PHE 43 ASP 44 THR 45 LYS 46 THR 47 GLY 48 HIS 49 ARG 50 VAL 51 ALA 52 VAL 53 LYS 54 LYS 55 LEU 56 SER 57 ARG 58 PRO 59 PHE 60 GLN 61 SER 62 ILE 63 ILE 64 HIS 65 ALA 66 LYS 67 ARG 68 THR 69 TYR 70 ARG 71 GLU 72 LEU 73 ARG 74 LEU 75 LEU 76 LYS 77 HIS 78 MET 79 LYS 80 HIS 81 GLU 82 ASN 83 VAL 84 ILE 85 GLY 86 LEU 87 LEU 88 ASP 89 VAL 90 PHE 91 THR 92 PRO 93 ALA 94 ARG 95 SER 96 LEU 97 GLU 98 GLU 99 PHE 100 ASN 101 ASP 102 VAL 103 TYR 104 LEU 105 VAL 106 THR 107 HIS 108 LEU 109 MET 110 GLY 111 ALA 112 ASP 113 LEU 114 ASN 115 ASN 116 ILE 117 VAL 118 LYS 119 CYS 120 GLN 121 LYS 122 LEU 123 THR 124 ASP 125 ASP 126 HIS 127 VAL 128 GLN 129 PHE 130 LEU 131 ILE 132 TYR 133 GLN 134 ILE 135 LEU 136 ARG 137 GLY 138 LEU 139 LYS 140 TYR 141 ILE 142 HIS 143 SER 144 ALA 145 ASP 146 ILE 147 ILE 148 HIS 149 ARG 150 ASP 151 LEU 152 LYS 153 PRO 154 SER 155 ASN 156 LEU 157 ALA 158 VAL 159 ASN 160 GLU 161 ASP 162 CYS 163 GLU 164 LEU 165 LYS 166 ILE 167 LEU 168 ASP 169 PHE 170 GLY 171 LEU 172 ALA 173 ARG 174 HIS 175 THR 176 ASP 177 ASP 178 GLU 179 MET 180 THR 181 GLY 182 TYR 183 VAL 184 ALA 185 THR 186 ARG 187 TRP 188 TYR 189 ARG 190 ALA 191 PRO 192 GLU 193 ILE 194 MET 195 LEU 196 ASN 197 TRP 198 MET 199 HIS 200 TYR 201 ASN 202 GLN 203 THR 204 VAL 205 ASP 206 ILE 207 TRP 208 SER 209 VAL 210 GLY 211 CYS 212 ILE 213 MET 214 ALA 215 GLU 216 LEU 217 LEU 218 THR 219 GLY 220 ARG 221 THR 222 LEU 223 PHE 224 PRO 225 GLY 226 THR 227 ASP 228 HIS 229 ILE 230 ASP 231 GLN 232 LEU 233 LYS 234 LEU 235 ILE 236 LEU 237 ARG 238 LEU 239 VAL 240 GLY 241 THR 242 PRO 243 GLY 244 ALA 245 GLU 246 LEU 247 LEU 248 LYS 249 LYS 250 ILE 251 SER 252 SER 253 GLU 254 SER 255 ALA 256 ARG 257 ASN 258 TYR 259 ILE 260 GLN 261 SER 262 LEU 263 ALA 264 GLN 265 MET 266 PRO 267 LYS 268 MET 269 ASN 270 PHE 271 ALA 272 ASN 273 VAL 274 PHE 275 ILE 276 GLY 277 ALA 278 ASN 279 PRO 280 LEU 281 ALA 282 VAL 283 ASP 284 LEU 285 LEU 286 GLU 287 LYS 288 MET 289 LEU 290 VAL 291 LEU 292 ASP 293 SER 294 ASP 295 LYS 296 ARG 297 ILE 298 THR 299 ALA 300 ALA 301 GLN 302 ALA 303 LEU 304 ALA 305 HIS 306 ALA 307 TYR 308 PHE 309 ALA 310 GLN 311 TYR 312 HIS 313 ASP 314 PRO 315 ASP 316 ASP 317 GLU 318 PRO 319 VAL 320 ALA 321 ASP 322 PRO 323 TYR 324 ASP 325 GLN 326 SER 327 PHE 328 GLU 329 SER 330 ARG 331 ASP 332 LEU 333 LEU 334 ILE 335 ASP 336 GLU 337 TRP 338 LYS 339 SER 340 LEU 341 THR 342 TYR 343 ASP 344 GLU 345 VAL 346 ILE 347 SER 348 PHE 349 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 100.00 352 99.14 99.14 0.00e+00 BMRB 19930 Non-phosphorylated_human_p38_alpha_(apo) 100.00 367 99.14 99.43 0.00e+00 BMRB 19934 Dual-phosphorylated_human_p38_alpha_(apo) 100.00 367 98.57 98.85 0.00e+00 BMRB 19935 Dual-phosphorylated_human_p38_alpha 100.00 367 98.57 98.85 0.00e+00 BMRB 19936 dual-phosphorylated_human_p38_alpha_(apo) 100.00 367 98.57 98.85 0.00e+00 BMRB 19937 dual-phosphorylated_human_p38_alpha_(apo) 100.00 367 98.57 98.85 0.00e+00 PDB 1A9U "The Complex Structure Of The Map Kinase P38SB203580" 99.71 379 99.43 99.43 0.00e+00 PDB 1BL6 "The Complex Structure Of The Map Kinase P38SB216995" 99.71 379 99.43 99.43 0.00e+00 PDB 1BL7 "The Complex Structure Of The Map Kinase P38SB220025" 99.71 379 99.43 99.43 0.00e+00 PDB 1BMK "The Complex Structure Of The Map Kinase P38SB218655" 99.71 379 100.00 100.00 0.00e+00 PDB 1DI9 "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" 99.71 360 99.43 99.43 0.00e+00 PDB 1IAN "Human P38 Map Kinase Inhibitor Complex" 100.00 366 99.14 99.43 0.00e+00 PDB 1KV1 "P38 Map Kinase In Complex With Inhibitor 1" 99.71 360 99.43 99.43 0.00e+00 PDB 1KV2 "Human P38 Map Kinase In Complex With Birb 796" 99.71 360 99.43 99.43 0.00e+00 PDB 1LEW "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" 99.71 360 100.00 100.00 0.00e+00 PDB 1LEZ "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" 99.71 360 100.00 100.00 0.00e+00 PDB 1M7Q "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 1OUK "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 1OUY "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 1OVE "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" 99.71 366 99.14 99.14 0.00e+00 PDB 1OZ1 "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" 99.71 372 99.43 99.43 0.00e+00 PDB 1P38 "The Structure Of The Map Kinase P38 At 2.1 Angstoms Resolution" 99.71 379 100.00 100.00 0.00e+00 PDB 1R39 "The Structure Of P38alpha" 99.71 366 99.43 99.43 0.00e+00 PDB 1R3C "The Structure Of P38alpha C162s Mutant" 99.71 366 99.14 99.14 0.00e+00 PDB 1W7H "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 1W82 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 1W83 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 1W84 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 1WBN "Fragment Based P38 Inhibitors" 99.71 360 99.43 99.43 0.00e+00 PDB 1WBO "Fragment Based P38 Inhibitors" 99.71 360 99.43 99.43 0.00e+00 PDB 1WBS "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 99.71 360 99.43 99.43 0.00e+00 PDB 1WBT "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." 99.71 360 99.43 99.43 0.00e+00 PDB 1WBV "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 99.71 360 99.43 99.43 0.00e+00 PDB 1WBW "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 99.71 360 99.43 99.43 0.00e+00 PDB 1WFC "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" 99.71 366 99.43 99.43 0.00e+00 PDB 1YQJ "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 1YW2 "Mutated Mus Musculus P38 Kinase (Mp38)" 99.71 360 99.43 99.71 0.00e+00 PDB 1YWR "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" 99.71 360 99.14 99.43 0.00e+00 PDB 1ZYJ "Human P38 Map Kinase In Complex With Inhibitor 1a" 99.71 360 99.43 99.43 0.00e+00 PDB 1ZZ2 "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" 99.71 360 99.43 99.43 0.00e+00 PDB 1ZZL "Crystal Structure Of P38 With Triazolopyridine" 99.14 351 99.42 99.42 0.00e+00 PDB 2BAJ "P38alpha Bound To Pyrazolourea" 100.00 365 99.14 99.43 0.00e+00 PDB 2BAK "P38alpha Map Kinase Bound To Mpaq" 100.00 365 99.14 99.43 0.00e+00 PDB 2BAL "P38alpha Map Kinase Bound To Pyrazoloamine" 100.00 365 98.85 99.14 0.00e+00 PDB 2BAQ "P38alpha Bound To Ro3201195" 100.00 365 98.57 99.14 0.00e+00 PDB 2EWA "Dual Binding Mode Of Pyridinylimidazole To Map Kinase P38" 99.71 379 99.43 99.43 0.00e+00 PDB 2FSL "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" 100.00 367 98.57 98.85 0.00e+00 PDB 2FSM "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" 100.00 367 98.57 98.85 0.00e+00 PDB 2FSO "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" 100.00 367 98.85 99.14 0.00e+00 PDB 2FST "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" 100.00 367 98.57 98.85 0.00e+00 PDB 2GFS "P38 Kinase Crystal Structure In Complex With Ro3201195" 99.71 372 99.43 99.43 0.00e+00 PDB 2GHL "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" 98.85 348 99.42 99.71 0.00e+00 PDB 2GHM "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" 98.85 348 99.42 99.71 0.00e+00 PDB 2GTM "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" 98.85 348 100.00 100.00 0.00e+00 PDB 2GTN "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" 98.85 348 100.00 100.00 0.00e+00 PDB 2I0H "The Structure Of P38alpha In Complex With An Arylpyridazinone" 99.71 366 99.14 99.14 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" 99.71 359 99.43 99.43 0.00e+00 PDB 2NPQ "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" 100.00 367 99.14 99.43 0.00e+00 PDB 2OKR "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 99.71 366 99.43 99.43 0.00e+00 PDB 2ONL "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 99.71 366 99.43 99.43 0.00e+00 PDB 2OZA "Structure Of P38alpha Complex" 100.00 366 99.71 100.00 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" 98.85 348 99.42 99.42 0.00e+00 PDB 2QD9 "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" 100.00 366 99.14 99.43 0.00e+00 PDB 2RG5 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" 100.00 366 99.14 99.43 0.00e+00 PDB 2RG6 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" 100.00 366 99.14 99.43 0.00e+00 PDB 2Y8O "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" 99.71 362 99.14 99.14 0.00e+00 PDB 2YIS "Triazolopyridine Inhibitors Of P38 Kinase." 99.71 359 99.43 99.43 0.00e+00 PDB 2YIW "Triazolopyridine Inhibitors Of P38 Kinase" 99.71 359 99.43 99.43 0.00e+00 PDB 2YIX "Triazolopyridine Inhibitors Of P38" 99.14 351 99.42 99.42 0.00e+00 PDB 2ZAZ "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 2ZB0 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 2ZB1 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 3BV2 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" 100.00 366 99.14 99.43 0.00e+00 PDB 3BV3 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" 100.00 366 99.14 99.43 0.00e+00 PDB 3BX5 "P38 Alpha Map Kinase Complexed With Bms-640994" 100.00 366 99.14 99.43 0.00e+00 PDB 3C5U "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" 100.00 366 99.14 99.43 0.00e+00 PDB 3CTQ "Structure Of Map Kinase P38 In Complex With A 1-O-Tolyl-1,2, 3-Triazole-4-Carboxamide" 98.85 348 99.42 99.42 0.00e+00 PDB 3D7Z "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 99.71 360 99.14 99.14 0.00e+00 PDB 3D83 "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 99.71 360 98.85 98.85 0.00e+00 PDB 3DS6 "P38 Complex With A Phthalazine Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 3DT1 "P38 Complexed With A Quinazoline Inhibitor" 99.71 383 99.43 99.43 0.00e+00 PDB 3E92 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 99.71 371 99.14 99.14 0.00e+00 PDB 3E93 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 99.71 371 99.14 99.14 0.00e+00 PDB 3FC1 "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 3FI4 "P38 Kinase Crystal Structure In Complex With Ro4499" 99.71 372 99.14 99.43 0.00e+00 PDB 3FKL "P38 Kinase Crystal Structure In Complex With Ro9552" 99.71 372 99.43 99.43 0.00e+00 PDB 3FKN "P38 Kinase Crystal Structure In Complex With Ro7125" 99.71 372 99.43 99.43 0.00e+00 PDB 3FKO "P38 Kinase Crystal Structure In Complex With Ro3668" 99.71 372 99.14 99.43 0.00e+00 PDB 3FL4 "P38 Kinase Crystal Structure In Complex With Ro5634" 99.71 372 99.43 99.43 0.00e+00 PDB 3FLN "P38 Kinase Crystal Structure In Complex With R1487" 99.71 372 99.14 99.43 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-" 99.71 372 99.43 99.43 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-" 99.71 372 99.43 99.43 0.00e+00 PDB 3FLW "P38 Kinase Crystal Structure In Complex With Pamapimod" 99.71 372 99.43 99.43 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" 99.71 372 99.43 99.43 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" 99.71 372 99.43 99.43 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-" 99.71 372 99.43 99.43 0.00e+00 PDB 3FMJ "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" 99.71 372 99.43 99.43 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-" 99.71 372 99.43 99.43 0.00e+00 PDB 3FML "P38 Kinase Crystal Structure In Complex With Ro6224" 99.71 372 99.43 99.43 0.00e+00 PDB 3FMM "P38 Kinase Crystal Structure In Complex With Ro6226" 99.71 372 99.43 99.43 0.00e+00 PDB 3FMN "P38 Kinase Crystal Structure In Complex With Ro2530" 99.71 372 99.43 99.43 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" 99.71 372 99.43 99.43 0.00e+00 PDB 3FSK "P38 Kinase Crystal Structure In Complex With Ro6257" 99.71 372 99.43 99.43 0.00e+00 PDB 3GC7 "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" 99.71 366 99.14 99.14 0.00e+00 PDB 3GCP "Human P38 Map Kinase In Complex With Sb203580" 100.00 360 97.99 97.99 0.00e+00 PDB 3GCQ "Human P38 Map Kinase In Complex With Rl45" 100.00 360 97.99 97.99 0.00e+00 PDB 3GCS "Human P38 Map Kinase In Complex With Sorafenib" 100.00 360 97.99 97.99 0.00e+00 PDB 3GCU "Human P38 Map Kinase In Complex With Rl48" 100.00 360 99.14 99.14 0.00e+00 PDB 3GCV "Human P38 Map Kinase In Complex With Rl62" 100.00 360 97.99 97.99 0.00e+00 PDB 3GFE "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 3GI3 "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" 99.71 360 99.43 99.43 0.00e+00 PDB 3HA8 "The Complex Structure Of The Map Kinase P38COMPOUND 14B" 99.71 379 99.43 99.43 0.00e+00 PDB 3HEC "P38 In Complex With Imatinib" 98.85 348 99.42 99.42 0.00e+00 PDB 3HEG "P38 In Complex With Sorafenib" 98.85 348 99.42 99.42 0.00e+00 PDB 3HL7 "Crystal Structure Of Human P38alpha Complexed With Sd-0006" 99.71 360 99.43 99.43 0.00e+00 PDB 3HLL "Crystal Structure Of Human P38alpha Complexed With Ph-797804" 99.71 360 99.43 99.43 0.00e+00 PDB 3HP2 "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" 99.71 360 99.43 99.43 0.00e+00 PDB 3HP5 "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" 99.71 360 99.43 99.43 0.00e+00 PDB 3HRB "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 359 99.43 99.43 0.00e+00 PDB 3HUB "Human P38 Map Kinase In Complex With Scios-469" 100.00 360 97.99 97.99 0.00e+00 PDB 3HUC "Human P38 Map Kinase In Complex With Rl40" 100.00 360 99.14 99.14 0.00e+00 PDB 3HV3 "Human P38 Map Kinase In Complex With Rl49" 100.00 360 97.99 97.99 0.00e+00 PDB 3HV4 "Human P38 Map Kinase In Complex With Rl51" 100.00 360 99.14 99.14 0.00e+00 PDB 3HV5 "Human P38 Map Kinase In Complex With Rl24" 100.00 360 99.14 99.14 0.00e+00 PDB 3HV6 "Human P38 Map Kinase In Complex With Rl39" 100.00 360 99.14 99.14 0.00e+00 PDB 3HV7 "Human P38 Map Kinase In Complex With Rl38" 100.00 360 99.14 99.14 0.00e+00 PDB 3HVC "Crystal Structure Of Human P38alpha Map Kinase" 99.71 362 99.43 99.43 0.00e+00 PDB 3IPH "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" 99.71 360 98.85 98.85 0.00e+00 PDB 3ITZ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 3IW5 "Human P38 Map Kinase In Complex With An Indole Derivative" 100.00 360 97.99 97.99 0.00e+00 PDB 3IW6 "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" 100.00 360 97.99 97.99 0.00e+00 PDB 3IW7 "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" 100.00 360 97.99 97.99 0.00e+00 PDB 3IW8 "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" 100.00 360 97.99 97.99 0.00e+00 PDB 3K3I "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" 98.85 350 99.42 99.42 0.00e+00 PDB 3K3J "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" 99.71 362 99.43 99.43 0.00e+00 PDB 3KF7 "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" 99.71 360 99.43 99.43 0.00e+00 PDB 3KQ7 "Structure Of Human P38alpha With N-[4-Methyl-3-(6-{[2-(1- Methylpyrrolidin-2-Yl)ethyl]amino}pyridine-3-Amido)phenyl]- 2-(Morpho" 99.71 380 99.43 99.43 0.00e+00 PDB 3L8S "Human P38 Map Kinase In Complex With Cp-547632" 100.00 360 97.99 97.99 0.00e+00 PDB 3L8X "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" 100.00 366 99.14 99.43 0.00e+00 PDB 3LFA "Human P38 Map Kinase In Complex With Dasatinib" 100.00 360 99.14 99.14 0.00e+00 PDB 3LFB "Human P38 Map Kinase In Complex With Rl98" 100.00 360 97.99 97.99 0.00e+00 PDB 3LFC "Human P38 Map Kinase In Complex With Rl99" 100.00 360 97.99 97.99 0.00e+00 PDB 3LFD "Human P38 Map Kinase In Complex With Rl113" 100.00 360 97.99 97.99 0.00e+00 PDB 3LFE "Human P38 Map Kinase In Complex With Rl116" 100.00 360 97.99 97.99 0.00e+00 PDB 3LFF "Human P38 Map Kinase In Complex With Rl166" 100.00 360 97.99 97.99 0.00e+00 PDB 3LHJ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." 99.71 366 99.43 99.43 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 " 99.71 360 99.43 99.43 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 " 99.71 360 99.14 99.14 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" 99.71 360 99.14 99.14 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" 99.71 360 99.14 99.43 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" 99.71 360 99.14 99.14 0.00e+00 PDB 3MPA "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.14 0.00e+00 PDB 3MPT "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" 99.71 371 99.43 99.43 0.00e+00 PDB 3MVL "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" 100.00 366 99.14 99.43 0.00e+00 PDB 3MVM "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" 100.00 366 99.14 99.43 0.00e+00 PDB 3MW1 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 359 99.43 99.43 0.00e+00 PDB 3NEW "P38-Alpha Complexed With Compound 10" 99.71 366 99.14 99.14 0.00e+00 PDB 3NNU "Crystal Structure Of P38 Alpha In Complex With Dp1376" 99.71 354 99.43 99.43 0.00e+00 PDB 3NNV "Crystal Structure Of P38 Alpha In Complex With Dp437" 99.71 354 99.43 99.43 0.00e+00 PDB 3NNW "Crystal Structure Of P38 Alpha In Complex With Dp802" 99.71 354 99.43 99.43 0.00e+00 PDB 3NNX "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" 99.71 354 99.14 99.14 0.00e+00 PDB 3NWW "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" 100.00 366 99.14 99.43 0.00e+00 PDB 3O8P "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.14 0.00e+00 PDB 3O8T "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.14 0.00e+00 PDB 3O8U "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.43 0.00e+00 PDB 3OBG "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.14 0.00e+00 PDB 3OBJ "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.14 0.00e+00 PDB 3OC1 "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.71 360 99.14 99.14 0.00e+00 PDB 3OCG "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" 100.00 366 99.14 99.43 0.00e+00 PDB 3OD6 "Crystal Structure Of P38alpha Y323t Active Mutant" 99.71 360 99.14 99.14 0.00e+00 PDB 3ODY "Crystal Structure Of P38alpha Y323q Active Mutant" 99.71 360 99.14 99.14 0.00e+00 PDB 3ODZ "Crystal Structure Of P38alpha Y323r Active Mutant" 99.71 360 99.14 99.14 0.00e+00 PDB 3OEF "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" 99.71 360 99.14 99.43 0.00e+00 PDB 3P4K "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" 99.71 370 99.71 100.00 0.00e+00 PDB 3P5K "P38 Inhibitor-Bound" 100.00 366 99.71 100.00 0.00e+00 PDB 3P78 "P38 Inhibitor-Bound" 100.00 366 99.71 100.00 0.00e+00 PDB 3P79 "P38 Inhibitor-Bound" 100.00 366 99.71 100.00 0.00e+00 PDB 3P7A "P38 Inhibitor-Bound" 100.00 366 99.71 100.00 0.00e+00 PDB 3P7B "P38 Inhibitor-Bound" 100.00 366 99.71 100.00 0.00e+00 PDB 3P7C "P38 Inhibitor-Bound" 100.00 366 99.71 100.00 0.00e+00 PDB 3PG3 "Human P38 Map Kinase In Complex With Rl182" 100.00 360 97.99 97.99 0.00e+00 PDB 3PY3 "Crystal Structure Of Phosphorylated P38alpha Map Kinase" 99.71 380 99.43 99.43 0.00e+00 PDB 3QUD "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" 100.00 360 99.14 99.14 0.00e+00 PDB 3QUE "Human P38 Map Kinase In Complex With Skepinone-l" 100.00 360 99.14 99.14 0.00e+00 PDB 3RIN "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.71 360 99.43 99.43 0.00e+00 PDB 3ROC "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" 99.71 360 99.43 99.43 0.00e+00 PDB 3S3I "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.14 349 99.42 99.42 0.00e+00 PDB 3S4Q "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" 100.00 366 99.14 99.43 0.00e+00 PDB 3TG1 "Crystal Structure Of P38alpha In Complex With A Mapk Docking Partner" 99.71 380 100.00 100.00 0.00e+00 PDB 3U8W "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" 99.71 366 99.43 99.43 0.00e+00 PDB 3UVP "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" 100.00 360 99.14 99.14 0.00e+00 PDB 3UVQ "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" 100.00 360 99.14 99.14 0.00e+00 PDB 3UVR "Human P38 Map Kinase In Complex With Km064" 100.00 360 99.14 99.14 0.00e+00 PDB 3ZS5 "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" 100.00 362 99.14 99.43 0.00e+00 PDB 3ZSG "X-Ray Structure Of P38alpha Bound To Tak-715" 100.00 362 99.14 99.43 0.00e+00 PDB 3ZSH "X-Ray Structure Of P38alpha Bound To Scio-469" 100.00 362 99.14 99.43 0.00e+00 PDB 3ZSI "X-Ray Structure Of P38alpha Bound To Vx-745" 100.00 362 99.14 99.43 0.00e+00 PDB 3ZYA "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" 99.71 366 99.43 99.43 0.00e+00 PDB 4A9Y "P38alpha Map Kinase Bound To Cmpd 8" 100.00 365 99.14 99.43 0.00e+00 PDB 4AA0 "P38alpha Map Kinase Bound To Cmpd 2" 100.00 365 99.14 99.43 0.00e+00 PDB 4AA4 "P38alpha Map Kinase Bound To Cmpd 22" 100.00 365 99.14 99.43 0.00e+00 PDB 4AA5 "P38alpha Map Kinase Bound To Cmpd 33" 100.00 365 98.85 99.14 0.00e+00 PDB 4AAC "P38alpha Map Kinase Bound To Cmpd 29" 100.00 365 99.14 99.43 0.00e+00 PDB 4DLI "Human P38 Map Kinase In Complex With Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4DLJ "Human P38 Map Kinase In Complex With Rl163" 100.00 360 99.14 99.14 0.00e+00 PDB 4E5A "The W197a Mutant Of P38a Map Kinase" 99.71 360 99.14 99.14 0.00e+00 PDB 4E5B "Structure Of P38a Map Kinase Without Bog" 99.71 360 99.43 99.43 0.00e+00 PDB 4E6A "P38a-pia23 Complex" 99.71 360 99.43 99.43 0.00e+00 PDB 4E6C "P38a-perifosine Complex" 99.71 360 99.43 99.43 0.00e+00 PDB 4E8A "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" 99.71 360 99.43 99.43 0.00e+00 PDB 4EH2 "Human P38 Map Kinase In Complex With Np-F1 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH3 "Human P38 Map Kinase In Complex With Np-F2 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH4 "Human P38 Map Kinase In Complex With Np-F3 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH5 "Human P38 Map Kinase In Complex With Np-F4 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH6 "Human P38 Map Kinase In Complex With Np-F5 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH7 "Human P38 Map Kinase In Complex With Np-F6 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH8 "Human P38 Map Kinase In Complex With Np-F7 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EH9 "Human P38 Map Kinase In Complex With Np-F11 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EHV "Human P38 Map Kinase In Complex With Np-F10 And Rl87" 100.00 360 99.14 99.14 0.00e+00 PDB 4EWQ "Human P38 Alpha Mapk In Complex With A Pyridazine Based Inhibitor" 99.71 383 99.14 99.14 0.00e+00 PDB 4F9W "Human P38alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" 99.71 383 99.43 99.43 0.00e+00 PDB 4F9Y "Human P38 Alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" 99.71 383 99.43 99.43 0.00e+00 PDB 4FA2 "Human P38 Alpha Mitogen-activated Kinase In Complex With Sb239063" 99.71 383 99.43 99.43 0.00e+00 PDB 4GEO "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" 99.71 367 97.99 97.99 0.00e+00 PDB 4KA3 "Structure Of Map Kinase In Complex With A Docking Peptide" 99.71 360 100.00 100.00 0.00e+00 PDB 4KIN "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 100.00 366 99.14 99.43 0.00e+00 PDB 4KIP "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 2-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 100.00 366 99.14 99.43 0.00e+00 PDB 4KIQ "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With Ethyl 6-((5-(cyclopropylcarbamoyl)-2-methylpheny" 100.00 366 99.14 99.43 0.00e+00 PDB 4L8M "Human P38 Map Kinase In Complex With A Dibenzoxepinone" 100.00 360 99.14 99.14 0.00e+00 PDB 4LOO "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" 99.71 361 100.00 100.00 0.00e+00 PDB 4LOP "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" 99.71 361 100.00 100.00 0.00e+00 PDB 4LOQ "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" 99.71 361 100.00 100.00 0.00e+00 PDB 4R3C "Crystal Structure Of P38 Alpha Map Kinase In Complex With A Novel Isoform Selective Drug Candidate" 99.71 383 99.14 99.14 0.00e+00 PDB 4TYH "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" 98.57 348 100.00 100.00 0.00e+00 DBJ BAB85654 "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" 72.49 307 99.60 99.60 0.00e+00 DBJ BAE21782 "unnamed protein product [Mus musculus]" 99.71 360 100.00 100.00 0.00e+00 DBJ BAE30324 "unnamed protein product [Mus musculus]" 77.94 283 100.00 100.00 0.00e+00 DBJ BAE31659 "unnamed protein product [Mus musculus]" 77.94 283 100.00 100.00 0.00e+00 DBJ BAF84398 "unnamed protein product [Homo sapiens]" 99.71 360 99.14 99.14 0.00e+00 EMBL CAG38743 "MAPK14 [Homo sapiens]" 99.71 360 99.43 99.43 0.00e+00 GB AAA20888 "MAP kinase [Mus musculus]" 99.71 360 100.00 100.00 0.00e+00 GB AAA57456 "CSaids binding protein [Homo sapiens]" 99.71 360 99.43 99.43 0.00e+00 GB AAA74301 "MAP kinase [Homo sapiens]" 99.71 360 99.43 99.43 0.00e+00 GB AAB51285 "p38 mitogen activated protein kinase [Rattus norvegicus]" 99.71 360 98.85 99.43 0.00e+00 GB AAC36131 "p38 mitogen activated protein kinase [Canis lupus familiaris]" 99.71 360 98.85 99.43 0.00e+00 PRF 2111247A "p38 mitogen-activated protein kinase" 99.71 360 99.43 99.43 0.00e+00 PRF 2124426A "Mxi2 protein" 80.23 297 98.93 98.93 0.00e+00 REF NP_001003206 "mitogen-activated protein kinase 14 [Canis lupus familiaris]" 99.71 360 98.85 99.43 0.00e+00 REF NP_001136366 "mitogen-activated protein kinase 14 [Ovis aries]" 99.71 360 99.43 99.43 0.00e+00 REF NP_001161985 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.94 283 100.00 100.00 0.00e+00 REF NP_001161986 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.94 283 100.00 100.00 0.00e+00 REF NP_036081 "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" 99.71 360 100.00 100.00 0.00e+00 SP O02812 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " 99.71 360 98.85 99.43 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" 99.71 360 100.00 100.00 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" 99.71 360 99.14 99.71 0.00e+00 SP Q16539 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" 99.71 360 99.43 99.43 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $p38alpha Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name _Details $p38alpha 'recombinant technology' . Escherichia coli BL21(DE3) pLysS 'pET DUET' 'dual expression of p38 and MKK6 for double phosphorylation of p38' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'activated by double phosphorylation (pT180 and pY182)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p38alpha 0.5 mM '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 6.8 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name p38alpha _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 6 6 PRO C C 175.705 0.1 1 2 6 6 PRO CA C 61.801 0.1 1 3 6 6 PRO CB C 31.409 0.1 1 4 7 7 THR H H 8.491 0.02 1 5 7 7 THR C C 173.882 0.1 1 6 7 7 THR CA C 62.251 0.1 1 7 7 7 THR CB C 69.022 0.1 1 8 7 7 THR N N 117.423 0.1 1 9 8 8 PHE H H 8.788 0.02 1 10 8 8 PHE C C 175.904 0.1 1 11 8 8 PHE CA C 56.166 0.1 1 12 8 8 PHE CB C 41.157 0.1 1 13 8 8 PHE N N 127.243 0.1 1 14 9 9 TYR H H 9.147 0.02 1 15 9 9 TYR C C 172.51 0.1 1 16 9 9 TYR CA C 55.102 0.1 1 17 9 9 TYR CB C 40.07 0.1 1 18 9 9 TYR N N 120.254 0.1 1 19 10 10 ARG H H 8.442 0.02 1 20 10 10 ARG C C 176.048 0.1 1 21 10 10 ARG CA C 53.685 0.1 1 22 10 10 ARG CB C 32.739 0.1 1 23 10 10 ARG N N 120.053 0.1 1 24 11 11 GLN H H 9.056 0.02 1 25 11 11 GLN C C 173.016 0.1 1 26 11 11 GLN CA C 54.025 0.1 1 27 11 11 GLN CB C 32.251 0.1 1 28 11 11 GLN N N 122.993 0.1 1 29 12 12 GLU H H 8.866 0.02 1 30 12 12 GLU C C 175.741 0.1 1 31 12 12 GLU CA C 54.758 0.1 1 32 12 12 GLU CB C 29.815 0.1 1 33 12 12 GLU N N 125.846 0.1 1 34 13 13 LEU H H 9.021 0.02 1 35 13 13 LEU CA C 53.341 0.1 1 36 13 13 LEU CB C 43.466 0.1 1 37 13 13 LEU N N 128.688 0.1 1 38 14 14 ASN C C 175.055 0.1 1 39 14 14 ASN CA C 53.822 0.1 1 40 14 14 ASN CB C 36.627 0.1 1 41 15 15 LYS H H 8.891 0.02 1 42 15 15 LYS C C 175.489 0.1 1 43 15 15 LYS CA C 57.229 0.1 1 44 15 15 LYS CB C 28.82 0.1 1 45 15 15 LYS N N 110.119 0.1 1 46 16 16 THR H H 7.892 0.02 1 47 16 16 THR C C 172.564 0.1 1 48 16 16 THR CA C 60.61 0.1 1 49 16 16 THR CB C 70.75 0.1 1 50 16 16 THR N N 115.832 0.1 1 51 17 17 ILE H H 8.62 0.02 1 52 17 17 ILE C C 175.579 0.1 1 53 17 17 ILE CA C 59.658 0.1 1 54 17 17 ILE CB C 36.02 0.1 1 55 17 17 ILE N N 125.469 0.1 1 56 18 18 TRP H H 9.31 0.02 1 57 18 18 TRP C C 174.731 0.1 1 58 18 18 TRP CA C 56.295 0.1 1 59 18 18 TRP CB C 28.416 0.1 1 60 18 18 TRP N N 131.223 0.1 1 61 19 19 GLU H H 8.295 0.02 1 62 19 19 GLU C C 173.268 0.1 1 63 19 19 GLU CA C 54.094 0.1 1 64 19 19 GLU CB C 30.327 0.1 1 65 19 19 GLU N N 128.016 0.1 1 66 20 20 VAL H H 7.67 0.02 1 67 20 20 VAL CA C 55.337 0.1 1 68 20 20 VAL CB C 33.233 0.1 1 69 20 20 VAL N N 112.562 0.1 1 70 21 21 PRO C C 177.167 0.1 1 71 21 21 PRO CA C 60.991 0.1 1 72 21 21 PRO CB C 31.386 0.1 1 73 22 22 GLU H H 8.147 0.02 1 74 22 22 GLU C C 176.229 0.1 1 75 22 22 GLU CA C 57.657 0.1 1 76 22 22 GLU CB C 28.759 0.1 1 77 22 22 GLU N N 119.022 0.1 1 78 23 23 ARG H H 7.453 0.02 1 79 23 23 ARG C C 174.767 0.1 1 80 23 23 ARG CA C 57.139 0.1 1 81 23 23 ARG CB C 29.928 0.1 1 82 23 23 ARG N N 117.672 0.1 1 83 24 24 TYR H H 7.834 0.02 1 84 24 24 TYR C C 174.514 0.1 1 85 24 24 TYR CA C 56.159 0.1 1 86 24 24 TYR CB C 36.882 0.1 1 87 24 24 TYR N N 118.072 0.1 1 88 25 25 GLN H H 9.148 0.02 1 89 25 25 GLN C C 174.857 0.1 1 90 25 25 GLN CA C 52.76 0.1 1 91 25 25 GLN CB C 32.442 0.1 1 92 25 25 GLN N N 122.55 0.1 1 93 26 26 ASN H H 8.858 0.02 1 94 26 26 ASN C C 173.99 0.1 1 95 26 26 ASN CA C 53.186 0.1 1 96 26 26 ASN CB C 36.215 0.1 1 97 26 26 ASN N N 117.787 0.1 1 98 27 27 LEU H H 8.53 0.02 1 99 27 27 LEU C C 179.153 0.1 1 100 27 27 LEU CA C 56.135 0.1 1 101 27 27 LEU CB C 40.405 0.1 1 102 27 27 LEU N N 119.89 0.1 1 103 28 28 SER H H 8.774 0.02 1 104 28 28 SER CA C 53.84 0.1 1 105 28 28 SER CB C 64.233 0.1 1 106 28 28 SER N N 116.102 0.1 1 107 29 29 PRO C C 176.12 0.1 1 108 29 29 PRO CA C 63.773 0.1 1 109 29 29 PRO CB C 30.706 0.1 1 110 30 30 VAL H H 8.638 0.02 1 111 30 30 VAL C C 176.193 0.1 1 112 30 30 VAL CA C 61.125 0.1 1 113 30 30 VAL CB C 32.947 0.1 1 114 30 30 VAL N N 120.95 0.1 1 115 31 31 GLY H H 7.394 0.02 1 116 31 31 GLY C C 172.817 0.1 1 117 31 31 GLY CA C 44.658 0.1 1 118 31 31 GLY N N 108.423 0.1 1 119 32 32 SER H H 8.417 0.02 1 120 32 32 SER C C 173.774 0.1 1 121 32 32 SER CA C 57.253 0.1 1 122 32 32 SER CB C 64.487 0.1 1 123 32 32 SER N N 115.357 0.1 1 124 33 33 GLY H H 8.205 0.02 1 125 33 33 GLY CA C 44.117 0.1 1 126 33 33 GLY N N 110.435 0.1 1 127 38 38 VAL H H 8.474 0.02 1 128 38 38 VAL C C 176.337 0.1 1 129 38 38 VAL CA C 60.649 0.1 1 130 38 38 VAL CB C 35.17 0.1 1 131 38 38 VAL N N 122.494 0.1 1 132 39 39 CYS H H 9.342 0.02 1 133 39 39 CYS C C 173.449 0.1 1 134 39 39 CYS CA C 57.255 0.1 1 135 39 39 CYS CB C 30.418 0.1 1 136 39 39 CYS N N 125.274 0.1 1 137 40 40 ALA H H 8.817 0.02 1 138 40 40 ALA C C 176.427 0.1 1 139 40 40 ALA CA C 49.911 0.1 1 140 40 40 ALA CB C 19.625 0.1 1 141 40 40 ALA N N 125.343 0.1 1 142 41 41 ALA H H 9.01 0.02 1 143 41 41 ALA C C 175.218 0.1 1 144 41 41 ALA CA C 49.725 0.1 1 145 41 41 ALA CB C 22.198 0.1 1 146 41 41 ALA N N 120.793 0.1 1 147 42 42 PHE H H 9.351 0.02 1 148 42 42 PHE C C 174.045 0.1 1 149 42 42 PHE CA C 56.97 0.1 1 150 42 42 PHE CB C 39.929 0.1 1 151 42 42 PHE N N 122.124 0.1 1 152 43 43 ASP H H 8.126 0.02 1 153 43 43 ASP C C 176.481 0.1 1 154 43 43 ASP CA C 51.306 0.1 1 155 43 43 ASP CB C 41.04 0.1 1 156 43 43 ASP N N 126.137 0.1 1 157 44 44 THR H H 8.898 0.02 1 158 44 44 THR C C 176.463 0.1 1 159 44 44 THR CA C 63.02 0.1 1 160 44 44 THR CB C 68.711 0.1 1 161 44 44 THR N N 117.658 0.1 1 162 45 45 LYS H H 7.997 0.02 1 163 45 45 LYS C C 177.799 0.1 1 164 45 45 LYS CA C 57.875 0.1 1 165 45 45 LYS CB C 31.536 0.1 1 166 45 45 LYS N N 121.957 0.1 1 167 46 46 THR H H 6.638 0.02 1 168 46 46 THR C C 176.066 0.1 1 169 46 46 THR CA C 60.827 0.1 1 170 46 46 THR CB C 70.253 0.1 1 171 46 46 THR N N 105.024 0.1 1 172 47 47 GLY H H 8.333 0.02 1 173 47 47 GLY C C 173.633 0.1 1 174 47 47 GLY CA C 45.206 0.1 1 175 47 47 GLY N N 111.313 0.1 1 176 48 48 HIS H H 7.137 0.02 1 177 48 48 HIS C C 174.063 0.1 1 178 48 48 HIS CA C 53.073 0.1 1 179 48 48 HIS CB C 31.281 0.1 1 180 48 48 HIS N N 116.761 0.1 1 181 49 49 ARG H H 8.703 0.02 1 182 49 49 ARG CA C 55.442 0.1 1 183 49 49 ARG CB C 30.056 0.1 1 184 49 49 ARG N N 121.012 0.1 1 185 50 50 VAL H H 8.974 0.02 1 186 50 50 VAL C C 172.907 0.1 1 187 50 50 VAL N N 116.464 0.1 1 188 51 51 ALA H H 8.75 0.02 1 189 51 51 ALA C C 175.814 0.1 1 190 51 51 ALA N N 122.476 0.1 1 191 52 52 VAL H H 9.256 0.02 1 192 52 52 VAL C C 171.879 0.1 1 193 52 52 VAL N N 122.187 0.1 1 194 53 53 LYS C C 174.37 0.1 1 195 53 53 LYS CA C 53.342 0.1 1 196 53 53 LYS CB C 34.275 0.1 1 197 54 54 LYS H H 8.587 0.02 1 198 54 54 LYS C C 176.283 0.1 1 199 54 54 LYS CA C 53.798 0.1 1 200 54 54 LYS CB C 32.781 0.1 1 201 54 54 LYS N N 128.383 0.1 1 202 55 55 LEU C C 176.481 0.1 1 203 55 55 LEU CA C 54.546 0.1 1 204 55 55 LEU CB C 39.12 0.1 1 205 56 56 SER H H 8.1 0.02 1 206 56 56 SER C C 173.81 0.1 1 207 56 56 SER CA C 56.678 0.1 1 208 56 56 SER CB C 62.736 0.1 1 209 56 56 SER N N 117.895 0.1 1 210 57 57 ARG H H 8.749 0.02 1 211 57 57 ARG CA C 55.294 0.1 1 212 57 57 ARG CB C 28.417 0.1 1 213 57 57 ARG N N 122.957 0.1 1 214 58 58 PRO C C 175.38 0.1 1 215 58 58 PRO CA C 59.387 0.1 1 216 58 58 PRO CB C 30.458 0.1 1 217 59 59 PHE H H 7.931 0.02 1 218 59 59 PHE C C 176.583 0.1 1 219 59 59 PHE CA C 53.775 0.1 1 220 59 59 PHE CB C 37.137 0.1 1 221 59 59 PHE N N 112.261 0.1 1 222 60 60 GLN H H 7.026 0.02 1 223 60 60 GLN C C 174.46 0.1 1 224 60 60 GLN CA C 56.774 0.1 1 225 60 60 GLN CB C 28.772 0.1 1 226 60 60 GLN N N 115.971 0.1 1 227 61 61 SER H H 7.453 0.02 1 228 61 61 SER CA C 55.81 0.1 1 229 61 61 SER CB C 66.412 0.1 1 230 61 61 SER N N 110.103 0.1 1 231 63 63 ILE C C 179.047 0.1 1 232 63 63 ILE CA C 62.992 0.1 1 233 64 64 HIS H H 7.703 0.02 1 234 64 64 HIS C C 177.113 0.1 1 235 64 64 HIS CA C 60.869 0.1 1 236 64 64 HIS CB C 34.705 0.1 1 237 64 64 HIS N N 119.633 0.1 1 238 65 65 ALA H H 8.635 0.02 1 239 65 65 ALA CA C 54.405 0.1 1 240 65 65 ALA CB C 18.524 0.1 1 241 65 65 ALA N N 123.619 0.1 1 242 78 78 MET C C 176.301 0.1 1 243 79 79 LYS H H 8.489 0.02 1 244 79 79 LYS C C 173.196 0.1 1 245 79 79 LYS CA C 53.92 0.1 1 246 79 79 LYS CB C 31.822 0.1 1 247 79 79 LYS N N 128.524 0.1 1 248 80 80 HIS H H 8.707 0.02 1 249 80 80 HIS C C 175.344 0.1 1 250 80 80 HIS CA C 56.716 0.1 1 251 80 80 HIS CB C 32.667 0.1 1 252 80 80 HIS N N 124.068 0.1 1 253 81 81 GLU H H 8.075 0.02 1 254 81 81 GLU C C 177.889 0.1 1 255 81 81 GLU CA C 58.493 0.1 1 256 81 81 GLU CB C 29.082 0.1 1 257 81 81 GLU N N 125.671 0.1 1 258 82 82 ASN H H 11.396 0.02 1 259 82 82 ASN C C 174.171 0.1 1 260 82 82 ASN CA C 53.006 0.1 1 261 82 82 ASN CB C 40.327 0.1 1 262 82 82 ASN N N 118.341 0.1 1 263 83 83 VAL H H 7.696 0.02 1 264 83 83 VAL CA C 60.809 0.1 1 265 83 83 VAL CB C 34.793 0.1 1 266 83 83 VAL N N 119.773 0.1 1 267 84 84 ILE C C 171.588 0.1 1 268 84 84 ILE CA C 59.507 0.1 1 269 85 85 GLY H H 7.629 0.02 1 270 85 85 GLY CA C 43.105 0.1 1 271 85 85 GLY N N 109.601 0.1 1 272 86 86 LEU C C 176.445 0.1 1 273 86 86 LEU CA C 53.154 0.1 1 274 86 86 LEU CB C 42.722 0.1 1 275 87 87 LEU H H 9.09 0.02 1 276 87 87 LEU CA C 54.766 0.1 1 277 87 87 LEU CB C 40.029 0.1 1 278 87 87 LEU N N 126.437 0.1 1 279 88 88 ASP C C 172.607 0.1 1 280 88 88 ASP CA C 51.912 0.1 1 281 88 88 ASP CB C 41.833 0.1 1 282 89 89 VAL H H 7.914 0.02 1 283 89 89 VAL CA C 58.759 0.1 1 284 89 89 VAL CB C 32.742 0.1 1 285 89 89 VAL N N 120.34 0.1 1 286 90 90 PHE H H 8.285 0.02 1 287 90 90 PHE C C 172.799 0.1 1 288 90 90 PHE CA C 54.74 0.1 1 289 90 90 PHE CB C 41.013 0.1 1 290 90 90 PHE N N 119.08 0.1 1 291 91 91 THR H H 8.971 0.02 1 292 91 91 THR CA C 56.791 0.1 1 293 91 91 THR CB C 71.767 0.1 1 294 91 91 THR N N 113.621 0.1 1 295 92 92 PRO C C 176.572 0.1 1 296 92 92 PRO CA C 61.92 0.1 1 297 92 92 PRO CB C 30.446 0.1 1 298 93 93 ALA H H 7.733 0.02 1 299 93 93 ALA C C 178.503 0.1 1 300 93 93 ALA CA C 52.177 0.1 1 301 93 93 ALA CB C 19.62 0.1 1 302 93 93 ALA N N 122.401 0.1 1 303 94 94 ARG H H 9.291 0.02 1 304 94 94 ARG C C 175.073 0.1 1 305 94 94 ARG CA C 55.314 0.1 1 306 94 94 ARG CB C 29.799 0.1 1 307 94 94 ARG N N 121.34 0.1 1 308 95 95 SER H H 7.406 0.02 1 309 95 95 SER C C 173.659 0.1 1 310 95 95 SER CA C 55.81 0.1 1 311 95 95 SER CB C 65.428 0.1 1 312 95 95 SER N N 111.322 0.1 1 313 96 96 LEU H H 8.484 0.02 1 314 96 96 LEU C C 178.864 0.1 1 315 96 96 LEU CA C 56.212 0.1 1 316 96 96 LEU CB C 40.165 0.1 1 317 96 96 LEU N N 122.532 0.1 1 318 97 97 GLU H H 8.333 0.02 1 319 97 97 GLU C C 177.51 0.1 1 320 97 97 GLU CA C 58.598 0.1 1 321 97 97 GLU CB C 27.819 0.1 1 322 97 97 GLU N N 117.359 0.1 1 323 98 98 GLU H H 7.052 0.02 1 324 98 98 GLU C C 175.398 0.1 1 325 98 98 GLU CA C 54.067 0.1 1 326 98 98 GLU CB C 30.301 0.1 1 327 98 98 GLU N N 115.472 0.1 1 328 99 99 PHE H H 7.322 0.02 1 329 99 99 PHE C C 173.142 0.1 1 330 99 99 PHE CA C 56.315 0.1 1 331 99 99 PHE CB C 37.987 0.1 1 332 99 99 PHE N N 122.242 0.1 1 333 100 100 ASN H H 8.571 0.02 1 334 100 100 ASN C C 172.456 0.1 1 335 100 100 ASN CA C 53.415 0.1 1 336 100 100 ASN CB C 41.836 0.1 1 337 100 100 ASN N N 125.659 0.1 1 338 101 101 ASP H H 7.626 0.02 1 339 101 101 ASP C C 174.406 0.1 1 340 101 101 ASP CA C 52.501 0.1 1 341 101 101 ASP CB C 43.824 0.1 1 342 101 101 ASP N N 115.842 0.1 1 343 102 102 VAL H H 8.468 0.02 1 344 102 102 VAL CA C 60.908 0.1 1 345 102 102 VAL CB C 34.523 0.1 1 346 102 102 VAL N N 121.302 0.1 1 347 103 103 TYR CA C 54.796 0.1 1 348 104 104 LEU H H 8.862 0.02 1 349 104 104 LEU C C 174.586 0.1 1 350 104 104 LEU CA C 56.316 0.1 1 351 104 104 LEU N N 119.46 0.1 1 352 105 105 VAL H H 8.349 0.02 1 353 105 105 VAL C C 175.561 0.1 1 354 105 105 VAL CA C 60.206 0.1 1 355 105 105 VAL CB C 31.199 0.1 1 356 105 105 VAL N N 123.588 0.1 1 357 106 106 THR H H 9.144 0.02 1 358 106 106 THR CA C 58.705 0.1 1 359 106 106 THR CB C 73.265 0.1 1 360 106 106 THR N N 118.256 0.1 1 361 110 110 GLY C C 172.962 0.1 1 362 110 110 GLY CA C 45.076 0.1 1 363 111 111 ALA H H 7.915 0.02 1 364 111 111 ALA CA C 50.914 0.1 1 365 111 111 ALA CB C 20.171 0.1 1 366 111 111 ALA N N 123.725 0.1 1 367 114 114 ASN C C 175.718 0.1 1 368 115 115 ASN H H 7.887 0.02 1 369 115 115 ASN C C 176.856 0.1 1 370 115 115 ASN CA C 58.362 0.1 1 371 115 115 ASN CB C 39.622 0.1 1 372 115 115 ASN N N 122.109 0.1 1 373 116 116 ILE H H 7.526 0.02 1 374 116 116 ILE C C 177.456 0.1 1 375 116 116 ILE CA C 62.678 0.1 1 376 116 116 ILE CB C 40.585 0.1 1 377 116 116 ILE N N 118.713 0.1 1 378 117 117 VAL H H 7.593 0.02 1 379 117 117 VAL C C 177.42 0.1 1 380 117 117 VAL CA C 64.038 0.1 1 381 117 117 VAL CB C 30.607 0.1 1 382 117 117 VAL N N 116.648 0.1 1 383 118 118 LYS H H 7.381 0.02 1 384 118 118 LYS C C 178.16 0.1 1 385 118 118 LYS CA C 57.312 0.1 1 386 118 118 LYS CB C 31.557 0.1 1 387 118 118 LYS N N 117.325 0.1 1 388 119 119 CYS H H 7.622 0.02 1 389 119 119 CYS C C 174.192 0.1 1 390 119 119 CYS CA C 59.035 0.1 1 391 119 119 CYS CB C 28.549 0.1 1 392 119 119 CYS N N 114.389 0.1 1 393 120 120 GLN H H 8.042 0.02 1 394 120 120 GLN C C 173.81 0.1 1 395 120 120 GLN CA C 54.396 0.1 1 396 120 120 GLN CB C 29.995 0.1 1 397 120 120 GLN N N 119.596 0.1 1 398 121 121 LYS H H 8.23 0.02 1 399 121 121 LYS C C 176.283 0.1 1 400 121 121 LYS CA C 54.815 0.1 1 401 121 121 LYS CB C 31.263 0.1 1 402 121 121 LYS N N 121.946 0.1 1 403 122 122 LEU H H 8.567 0.02 1 404 122 122 LEU C C 173.954 0.1 1 405 122 122 LEU CA C 53.836 0.1 1 406 122 122 LEU CB C 41.602 0.1 1 407 122 122 LEU N N 126.678 0.1 1 408 123 123 THR H H 8.984 0.02 1 409 123 123 THR C C 175.814 0.1 1 410 123 123 THR CA C 59.784 0.1 1 411 123 123 THR CB C 72.263 0.1 1 412 123 123 THR N N 121.526 0.1 1 413 124 124 ASP H H 8.993 0.02 1 414 124 124 ASP C C 177.637 0.1 1 415 124 124 ASP CA C 57.626 0.1 1 416 124 124 ASP CB C 42.075 0.1 1 417 124 124 ASP N N 120.993 0.1 1 418 125 125 ASP H H 8.014 0.02 1 419 125 125 ASP C C 177.406 0.1 1 420 125 125 ASP CA C 56.436 0.1 1 421 125 125 ASP CB C 39.895 0.1 1 422 125 125 ASP N N 115.472 0.1 1 423 126 126 HIS H H 7.576 0.02 1 424 126 126 HIS C C 177.998 0.1 1 425 126 126 HIS CA C 59.477 0.1 1 426 126 126 HIS N N 118.366 0.1 1 427 127 127 VAL H H 8.162 0.02 1 428 127 127 VAL C C 177.601 0.1 1 429 127 127 VAL CA C 67.987 0.1 1 430 127 127 VAL CB C 29.96 0.1 1 431 127 127 VAL N N 120.118 0.1 1 432 128 128 GLN H H 8.437 0.02 1 433 128 128 GLN C C 177.889 0.1 1 434 128 128 GLN CA C 58.598 0.1 1 435 128 128 GLN CB C 29.346 0.1 1 436 128 128 GLN N N 118.324 0.1 1 437 129 129 PHE H H 7.464 0.02 1 438 129 129 PHE C C 179.532 0.1 1 439 129 129 PHE CA C 57.633 0.1 1 440 129 129 PHE CB C 38.784 0.1 1 441 129 129 PHE N N 116.242 0.1 1 442 130 130 LEU H H 8.805 0.02 1 443 130 130 LEU CA C 57.711 0.1 1 444 130 130 LEU CB C 41.429 0.1 1 445 130 130 LEU N N 120.687 0.1 1 446 136 136 ARG C C 179.785 0.1 1 447 136 136 ARG CA C 59.697 0.1 1 448 136 136 ARG CB C 28.881 0.1 1 449 137 137 GLY H H 8.152 0.02 1 450 137 137 GLY C C 174.911 0.1 1 451 137 137 GLY CA C 46.153 0.1 1 452 137 137 GLY N N 107.288 0.1 1 453 138 138 LEU H H 8.687 0.02 1 454 138 138 LEU C C 177.366 0.1 1 455 138 138 LEU CA C 56.271 0.1 1 456 138 138 LEU CB C 40.345 0.1 1 457 138 138 LEU N N 121.615 0.1 1 458 139 139 LYS C C 179.406 0.1 1 459 139 139 LYS CA C 59.165 0.1 1 460 139 139 LYS CB C 31.112 0.1 1 461 140 140 TYR H H 6.853 0.02 1 462 140 140 TYR CA C 60.819 0.1 1 463 140 140 TYR CB C 37.124 0.1 1 464 140 140 TYR N N 118.302 0.1 1 465 141 141 ILE C C 177.194 0.1 1 466 141 141 ILE CA C 65.583 0.1 1 467 142 142 HIS H H 9.521 0.02 1 468 142 142 HIS CA C 56.442 0.1 1 469 142 142 HIS CB C 30.116 0.1 1 470 142 142 HIS N N 119.549 0.1 1 471 143 143 SER C C 174.568 0.1 1 472 143 143 SER CA C 60.533 0.1 1 473 143 143 SER CB C 62.095 0.1 1 474 144 144 ALA H H 7.441 0.02 1 475 144 144 ALA CA C 50.473 0.1 1 476 144 144 ALA CB C 17.18 0.1 1 477 144 144 ALA N N 126.251 0.1 1 478 145 145 ASP H H 8.19 0.02 1 479 145 145 ASP CA C 54.721 0.1 1 480 145 145 ASP CB C 38.33 0.1 1 481 145 145 ASP N N 115.105 0.1 1 482 156 156 LEU H H 7.07 0.02 1 483 156 156 LEU C C 175.471 0.1 1 484 156 156 LEU CA C 51.423 0.1 1 485 156 156 LEU N N 119.414 0.1 1 486 157 157 ALA H H 8.537 0.02 1 487 157 157 ALA CA C 49.577 0.1 1 488 157 157 ALA CB C 20.749 0.1 1 489 157 157 ALA N N 125.164 0.1 1 490 158 158 VAL CA C 67.496 0.1 1 491 175 175 THR C C 176.915 0.1 1 492 175 175 THR CA C 62.246 0.1 1 493 175 175 THR CB C 63.104 0.1 1 494 176 176 ASP H H 8.352 0.02 1 495 176 176 ASP C C 175.896 0.1 1 496 176 176 ASP CA C 55.377 0.1 1 497 176 176 ASP CB C 29.5 0.1 1 498 176 176 ASP N N 122.004 0.1 1 499 177 177 ASP H H 8.359 0.02 1 500 177 177 ASP C C 176.509 0.1 1 501 177 177 ASP CA C 52.898 0.1 1 502 177 177 ASP CB C 27.912 0.1 1 503 177 177 ASP N N 122.642 0.1 1 504 178 178 GLU H H 8.83 0.02 1 505 178 178 GLU C C 174.23 0.1 1 506 178 178 GLU CA C 52.928 0.1 1 507 178 178 GLU CB C 32.541 0.1 1 508 178 178 GLU N N 117.549 0.1 1 509 179 179 MET H H 8.571 0.02 1 510 179 179 MET C C 174.731 0.1 1 511 179 179 MET CA C 52.92 0.1 1 512 179 179 MET CB C 32.463 0.1 1 513 179 179 MET N N 120.449 0.1 1 514 180 180 THR H H 8.833 0.02 1 515 180 180 THR C C 177.059 0.1 1 516 180 180 THR CA C 63.12 0.1 1 517 180 180 THR CB C 68.853 0.1 1 518 180 180 THR N N 117.374 0.1 1 519 181 181 GLY H H 8.259 0.02 1 520 181 181 GLY C C 174.168 0.1 1 521 181 181 GLY CA C 45.06 0.1 1 522 181 181 GLY N N 108.384 0.1 1 523 182 182 TYR H H 7.716 0.02 1 524 182 182 TYR C C 176.14 0.1 1 525 182 182 TYR CA C 53.439 0.1 1 526 182 182 TYR CB C 42.512 0.1 1 527 182 182 TYR N N 121.649 0.1 1 528 183 183 VAL H H 8.118 0.02 1 529 183 183 VAL CA C 61.339 0.1 1 530 183 183 VAL CB C 31.815 0.1 1 531 183 183 VAL N N 125.111 0.1 1 532 206 206 ILE C C 177.975 0.1 1 533 207 207 TRP H H 7.529 0.02 1 534 207 207 TRP N N 121.064 0.1 1 535 208 208 SER C C 176.48 0.1 1 536 208 208 SER CA C 61.708 0.1 1 537 209 209 VAL H H 8.019 0.02 1 538 209 209 VAL C C 177.085 0.1 1 539 209 209 VAL CA C 67.061 0.1 1 540 209 209 VAL CB C 29.336 0.1 1 541 209 209 VAL N N 119.904 0.1 1 542 210 210 GLY H H 8.541 0.02 1 543 210 210 GLY C C 174.586 0.1 1 544 210 210 GLY CA C 47.393 0.1 1 545 210 210 GLY N N 110.328 0.1 1 546 211 211 CYS H H 7.938 0.02 1 547 211 211 CYS C C 179.153 0.1 1 548 211 211 CYS CA C 63.446 0.1 1 549 211 211 CYS CB C 27.462 0.1 1 550 211 211 CYS N N 119.114 0.1 1 551 212 212 ILE H H 8.449 0.02 1 552 212 212 ILE C C 176.278 0.1 1 553 212 212 ILE CA C 65.066 0.1 1 554 212 212 ILE CB C 37.52 0.1 1 555 212 212 ILE N N 124.304 0.1 1 556 213 213 MET H H 9.323 0.02 1 557 213 213 MET C C 176.969 0.1 1 558 213 213 MET CA C 59.622 0.1 1 559 213 213 MET CB C 31.041 0.1 1 560 213 213 MET N N 120.528 0.1 1 561 214 214 ALA H H 8.189 0.02 1 562 214 214 ALA C C 178.823 0.1 1 563 214 214 ALA CA C 54.805 0.1 1 564 214 214 ALA CB C 19.504 0.1 1 565 214 214 ALA N N 118.323 0.1 1 566 215 215 GLU H H 7.155 0.02 1 567 215 215 GLU CA C 57.18 0.1 1 568 215 215 GLU CB C 28.584 0.1 1 569 215 215 GLU N N 120.016 0.1 1 570 216 216 LEU C C 178.846 0.1 1 571 216 216 LEU CA C 58.004 0.1 1 572 216 216 LEU CB C 40.794 0.1 1 573 217 217 LEU H H 7.853 0.02 1 574 217 217 LEU C C 179.369 0.1 1 575 217 217 LEU CA C 56.301 0.1 1 576 217 217 LEU CB C 42.001 0.1 1 577 217 217 LEU N N 115.897 0.1 1 578 218 218 THR H H 7.962 0.02 1 579 218 218 THR C C 176.463 0.1 1 580 218 218 THR CA C 61.553 0.1 1 581 218 218 THR CB C 71.339 0.1 1 582 218 218 THR N N 106.011 0.1 1 583 219 219 GLY H H 8.454 0.02 1 584 219 219 GLY C C 173.395 0.1 1 585 219 219 GLY CA C 44.956 0.1 1 586 219 219 GLY N N 112.802 0.1 1 587 220 220 ARG H H 8.032 0.02 1 588 220 220 ARG C C 174.478 0.1 1 589 220 220 ARG CA C 53.187 0.1 1 590 220 220 ARG CB C 31.944 0.1 1 591 220 220 ARG N N 119.089 0.1 1 592 221 221 THR H H 7.948 0.02 1 593 221 221 THR C C 174.388 0.1 1 594 221 221 THR CA C 63.014 0.1 1 595 221 221 THR CB C 68.86 0.1 1 596 221 221 THR N N 119.967 0.1 1 597 222 222 LEU H H 7.856 0.02 1 598 222 222 LEU C C 177.546 0.1 1 599 222 222 LEU CA C 52.374 0.1 1 600 222 222 LEU CB C 41.007 0.1 1 601 222 222 LEU N N 117.881 0.1 1 602 223 223 PHE H H 9.448 0.02 1 603 223 223 PHE CA C 58.788 0.1 1 604 223 223 PHE CB C 36.84 0.1 1 605 223 223 PHE N N 130.026 0.1 1 606 224 224 PRO C C 178.28 0.1 1 607 224 224 PRO CA C 55.631 0.1 1 608 225 225 GLY H H 8.373 0.02 1 609 225 225 GLY C C 176.175 0.1 1 610 225 225 GLY CA C 44.439 0.1 1 611 225 225 GLY N N 113.907 0.1 1 612 226 226 THR H H 10.134 0.02 1 613 226 226 THR CA C 61.677 0.1 1 614 226 226 THR CB C 64.997 0.1 1 615 226 226 THR N N 116.918 0.1 1 616 254 254 SER C C 177.601 0.1 1 617 254 254 SER CA C 60.285 0.1 1 618 254 254 SER CB C 69.291 0.1 1 619 255 255 ALA H H 7.716 0.02 1 620 255 255 ALA CA C 53.98 0.1 1 621 255 255 ALA CB C 17.746 0.1 1 622 255 255 ALA N N 125.593 0.1 1 623 259 259 ILE C C 178.286 0.1 1 624 260 260 GLN H H 8.121 0.02 1 625 260 260 GLN C C 176.301 0.1 1 626 260 260 GLN CA C 57.699 0.1 1 627 260 260 GLN CB C 27.273 0.1 1 628 260 260 GLN N N 118.169 0.1 1 629 261 261 SER H H 7.47 0.02 1 630 261 261 SER C C 174.153 0.1 1 631 261 261 SER CA C 58.793 0.1 1 632 261 261 SER CB C 63.151 0.1 1 633 261 261 SER N N 114.073 0.1 1 634 262 262 LEU H H 6.995 0.02 1 635 262 262 LEU C C 177.221 0.1 1 636 262 262 LEU CA C 53.747 0.1 1 637 262 262 LEU CB C 41.192 0.1 1 638 262 262 LEU N N 123.13 0.1 1 639 263 263 ALA H H 8.054 0.02 1 640 263 263 ALA C C 175.434 0.1 1 641 263 263 ALA CA C 51.858 0.1 1 642 263 263 ALA CB C 17.487 0.1 1 643 263 263 ALA N N 124.239 0.1 1 644 264 264 GLN H H 8.246 0.02 1 645 264 264 GLN C C 176.213 0.1 1 646 264 264 GLN CA C 53.909 0.1 1 647 264 264 GLN CB C 28.246 0.1 1 648 264 264 GLN N N 119.579 0.1 1 649 265 265 MET H H 8.726 0.02 1 650 265 265 MET CA C 54.473 0.1 1 651 265 265 MET N N 124.682 0.1 1 652 266 266 PRO C C 175.868 0.1 1 653 266 266 PRO CA C 61.087 0.1 1 654 266 266 PRO CB C 30.967 0.1 1 655 267 267 LYS H H 8.282 0.02 1 656 267 267 LYS C C 177.691 0.1 1 657 267 267 LYS CA C 56.057 0.1 1 658 267 267 LYS CB C 32.237 0.1 1 659 267 267 LYS N N 120.658 0.1 1 660 268 268 MET H H 8.427 0.02 1 661 268 268 MET C C 174.478 0.1 1 662 268 268 MET CA C 55.243 0.1 1 663 268 268 MET CB C 32.241 0.1 1 664 268 268 MET N N 126.083 0.1 1 665 269 269 ASN H H 8.652 0.02 1 666 269 269 ASN C C 176.084 0.1 1 667 269 269 ASN CA C 50.947 0.1 1 668 269 269 ASN CB C 39.821 0.1 1 669 269 269 ASN N N 130.749 0.1 1 670 270 270 PHE H H 8.572 0.02 1 671 270 270 PHE C C 177.925 0.1 1 672 270 270 PHE CA C 59.174 0.1 1 673 270 270 PHE CB C 39.591 0.1 1 674 270 270 PHE N N 114.416 0.1 1 675 271 271 ALA H H 8.561 0.02 1 676 271 271 ALA C C 178.611 0.1 1 677 271 271 ALA CA C 53.752 0.1 1 678 271 271 ALA CB C 16.78 0.1 1 679 271 271 ALA N N 122.315 0.1 1 680 272 272 ASN H H 7.483 0.02 1 681 272 272 ASN C C 175.344 0.1 1 682 272 272 ASN CA C 52.827 0.1 1 683 272 272 ASN CB C 37.935 0.1 1 684 272 272 ASN N N 113.241 0.1 1 685 273 273 VAL H H 7.235 0.02 1 686 273 273 VAL C C 176.499 0.1 1 687 273 273 VAL CA C 63.471 0.1 1 688 273 273 VAL CB C 31.837 0.1 1 689 273 273 VAL N N 120.104 0.1 1 690 274 274 PHE H H 7.635 0.02 1 691 274 274 PHE C C 175.471 0.1 1 692 274 274 PHE CA C 55.22 0.1 1 693 274 274 PHE CB C 36.094 0.1 1 694 274 274 PHE N N 120.723 0.1 1 695 275 275 ILE H H 6.9 0.02 1 696 275 275 ILE C C 177.889 0.1 1 697 275 275 ILE CA C 61.579 0.1 1 698 275 275 ILE CB C 36.596 0.1 1 699 275 275 ILE N N 120.929 0.1 1 700 276 276 GLY H H 9.012 0.02 1 701 276 276 GLY C C 173.99 0.1 1 702 276 276 GLY CA C 44.198 0.1 1 703 276 276 GLY N N 116.306 0.1 1 704 277 277 ALA H H 7.438 0.02 1 705 277 277 ALA C C 176.915 0.1 1 706 277 277 ALA CA C 50.418 0.1 1 707 277 277 ALA CB C 18.843 0.1 1 708 277 277 ALA N N 122.042 0.1 1 709 278 278 ASN H H 9.101 0.02 1 710 278 278 ASN CA C 50.39 0.1 1 711 278 278 ASN CB C 38.628 0.1 1 712 278 278 ASN N N 122.591 0.1 1 713 279 279 PRO C C 179.893 0.1 1 714 279 279 PRO CA C 64.533 0.1 1 715 279 279 PRO CB C 31.335 0.1 1 716 280 280 LEU H H 8.462 0.02 1 717 280 280 LEU C C 178.684 0.1 1 718 280 280 LEU CA C 56.397 0.1 1 719 280 280 LEU CB C 41.704 0.1 1 720 280 280 LEU N N 117.197 0.1 1 721 281 281 ALA H H 7.133 0.02 1 722 281 281 ALA C C 178.972 0.1 1 723 281 281 ALA CA C 53.147 0.1 1 724 281 281 ALA CB C 16.767 0.1 1 725 281 281 ALA N N 121.128 0.1 1 726 282 282 VAL H H 7.114 0.02 1 727 282 282 VAL C C 176.283 0.1 1 728 282 282 VAL CA C 65.984 0.1 1 729 282 282 VAL CB C 30.298 0.1 1 730 282 282 VAL N N 116.421 0.1 1 731 290 290 VAL C C 176.77 0.1 1 732 290 290 VAL CA C 66.113 0.1 1 733 290 290 VAL CB C 30.263 0.1 1 734 291 291 LEU H H 7.512 0.02 1 735 291 291 LEU CA C 57.281 0.1 1 736 291 291 LEU CB C 42.589 0.1 1 737 291 291 LEU N N 118.023 0.1 1 738 294 294 ASP C C 177.077 0.1 1 739 294 294 ASP CA C 55.711 0.1 1 740 295 295 LYS H H 7.651 0.02 1 741 295 295 LYS C C 176.283 0.1 1 742 295 295 LYS CA C 54.282 0.1 1 743 295 295 LYS CB C 32.651 0.1 1 744 295 295 LYS N N 117.449 0.1 1 745 296 296 ARG H H 7.07 0.02 1 746 296 296 ARG C C 174.64 0.1 1 747 296 296 ARG CA C 56.791 0.1 1 748 296 296 ARG CB C 29.534 0.1 1 749 296 296 ARG N N 122.488 0.1 1 750 297 297 ILE H H 7.102 0.02 1 751 297 297 ILE C C 172.023 0.1 1 752 297 297 ILE N N 125.047 0.1 1 753 298 298 THR H H 7.392 0.02 1 754 298 298 THR C C 175.94 0.1 1 755 298 298 THR CA C 59.565 0.1 1 756 298 298 THR CB C 70.819 0.1 1 757 298 298 THR N N 109.234 0.1 1 758 299 299 ALA H H 9.529 0.02 1 759 299 299 ALA C C 178.774 0.1 1 760 299 299 ALA CA C 55.836 0.1 1 761 299 299 ALA CB C 15.656 0.1 1 762 299 299 ALA N N 122.251 0.1 1 763 300 300 ALA H H 8.653 0.02 1 764 300 300 ALA C C 180.633 0.1 1 765 300 300 ALA CA C 54.477 0.1 1 766 300 300 ALA CB C 17.436 0.1 1 767 300 300 ALA N N 116.194 0.1 1 768 301 301 GLN H H 7.445 0.02 1 769 301 301 GLN C C 179.55 0.1 1 770 301 301 GLN CA C 57.377 0.1 1 771 301 301 GLN CB C 28.01 0.1 1 772 301 301 GLN N N 116.039 0.1 1 773 302 302 ALA H H 8.711 0.02 1 774 302 302 ALA C C 178.936 0.1 1 775 302 302 ALA CA C 54.307 0.1 1 776 302 302 ALA CB C 18.424 0.1 1 777 302 302 ALA N N 123.83 0.1 1 778 303 303 LEU H H 7.679 0.02 1 779 303 303 LEU C C 175.814 0.1 1 780 303 303 LEU CA C 57.01 0.1 1 781 303 303 LEU CB C 40.904 0.1 1 782 303 303 LEU N N 116.261 0.1 1 783 304 304 ALA H H 6.661 0.02 1 784 304 304 ALA C C 176.734 0.1 1 785 304 304 ALA CA C 50.411 0.1 1 786 304 304 ALA CB C 17.983 0.1 1 787 304 304 ALA N N 115.372 0.1 1 788 305 305 HIS H H 7.988 0.02 1 789 305 305 HIS C C 177.33 0.1 1 790 305 305 HIS CA C 58.25 0.1 1 791 305 305 HIS CB C 32.117 0.1 1 792 305 305 HIS N N 122.726 0.1 1 793 306 306 ALA H H 8.35 0.02 1 794 306 306 ALA C C 179.333 0.1 1 795 306 306 ALA CA C 54.727 0.1 1 796 306 306 ALA CB C 18.055 0.1 1 797 306 306 ALA N N 132.765 0.1 1 798 307 307 TYR H H 11.672 0.02 1 799 307 307 TYR C C 176.211 0.1 1 800 307 307 TYR CA C 59.591 0.1 1 801 307 307 TYR CB C 37.733 0.1 1 802 307 307 TYR N N 125.113 0.1 1 803 308 308 PHE H H 7.696 0.02 1 804 308 308 PHE C C 176.915 0.1 1 805 308 308 PHE CA C 55.179 0.1 1 806 308 308 PHE CB C 37.979 0.1 1 807 308 308 PHE N N 110.604 0.1 1 808 309 309 ALA H H 7.561 0.02 1 809 309 309 ALA C C 179.045 0.1 1 810 309 309 ALA CA C 54.998 0.1 1 811 309 309 ALA CB C 18.078 0.1 1 812 309 309 ALA N N 123.686 0.1 1 813 310 310 GLN H H 8.671 0.02 1 814 310 310 GLN C C 175.344 0.1 1 815 310 310 GLN CA C 56.438 0.1 1 816 310 310 GLN CB C 27.322 0.1 1 817 310 310 GLN N N 114.054 0.1 1 818 311 311 TYR H H 7.478 0.02 1 819 311 311 TYR C C 177.98 0.1 1 820 311 311 TYR CA C 57.792 0.1 1 821 311 311 TYR CB C 39.585 0.1 1 822 311 311 TYR N N 115.945 0.1 1 823 314 314 PRO C C 177.98 0.1 1 824 314 314 PRO CA C 63.254 0.1 1 825 314 314 PRO CB C 30.935 0.1 1 826 315 315 ASP H H 7.99 0.02 1 827 315 315 ASP C C 175.832 0.1 1 828 315 315 ASP CA C 54.687 0.1 1 829 315 315 ASP CB C 39.945 0.1 1 830 315 315 ASP N N 117.456 0.1 1 831 316 316 ASP H H 8.03 0.02 1 832 316 316 ASP C C 175.868 0.1 1 833 316 316 ASP CA C 52.061 0.1 1 834 316 316 ASP CB C 41.675 0.1 1 835 316 316 ASP N N 121.204 0.1 1 836 317 317 GLU H H 7.792 0.02 1 837 317 317 GLU CA C 53.007 0.1 1 838 317 317 GLU CB C 28.863 0.1 1 839 317 317 GLU N N 121.453 0.1 1 840 318 318 PRO C C 177.131 0.1 1 841 318 318 PRO CA C 62.838 0.1 1 842 318 318 PRO CB C 32.718 0.1 1 843 319 319 VAL H H 7.87 0.02 1 844 319 319 VAL C C 175.073 0.1 1 845 319 319 VAL CA C 58.813 0.1 1 846 319 319 VAL CB C 33.131 0.1 1 847 319 319 VAL N N 109.286 0.1 1 848 320 320 ALA H H 8.47 0.02 1 849 320 320 ALA C C 178.611 0.1 1 850 320 320 ALA CA C 50.075 0.1 1 851 320 320 ALA CB C 19.329 0.1 1 852 320 320 ALA N N 123.674 0.1 1 853 321 321 ASP H H 8.063 0.02 1 854 321 321 ASP CA C 53.445 0.1 1 855 321 321 ASP CB C 38.767 0.1 1 856 321 321 ASP N N 120.833 0.1 1 857 326 326 SER C C 176.842 0.1 1 858 326 326 SER CA C 63.023 0.1 1 859 326 326 SER CB C 66.147 0.1 1 860 327 327 PHE H H 7.815 0.02 1 861 327 327 PHE CA C 58.652 0.1 1 862 327 327 PHE N N 118.994 0.1 1 863 328 328 GLU C C 178.611 0.1 1 864 329 329 SER H H 7.465 0.02 1 865 329 329 SER C C 174.37 0.1 1 866 329 329 SER CA C 57.314 0.1 1 867 329 329 SER CB C 63.105 0.1 1 868 329 329 SER N N 111.88 0.1 1 869 330 330 ARG H H 7.634 0.02 1 870 330 330 ARG C C 175.073 0.1 1 871 330 330 ARG CA C 55.392 0.1 1 872 330 330 ARG CB C 30.226 0.1 1 873 330 330 ARG N N 121.918 0.1 1 874 331 331 ASP H H 8.561 0.02 1 875 331 331 ASP C C 174.37 0.1 1 876 331 331 ASP CA C 52.088 0.1 1 877 331 331 ASP CB C 40.527 0.1 1 878 331 331 ASP N N 124.757 0.1 1 879 332 332 LEU H H 7.833 0.02 1 880 332 332 LEU C C 177.005 0.1 1 881 332 332 LEU CA C 52.328 0.1 1 882 332 332 LEU CB C 41.234 0.1 1 883 332 332 LEU N N 123.212 0.1 1 884 333 333 LEU H H 8.796 0.02 1 885 333 333 LEU C C 179.785 0.1 1 886 333 333 LEU CA C 53.394 0.1 1 887 333 333 LEU CB C 41.46 0.1 1 888 333 333 LEU N N 119.962 0.1 1 889 334 334 ILE H H 8.989 0.02 1 890 334 334 ILE C C 177.366 0.1 1 891 334 334 ILE CA C 66.415 0.1 1 892 334 334 ILE CB C 37.068 0.1 1 893 334 334 ILE N N 121.824 0.1 1 894 335 335 ASP H H 8.386 0.02 1 895 335 335 ASP C C 178.954 0.1 1 896 335 335 ASP CA C 56.651 0.1 1 897 335 335 ASP CB C 39.299 0.1 1 898 335 335 ASP N N 116.044 0.1 1 899 336 336 GLU H H 7.146 0.02 1 900 336 336 GLU C C 179.063 0.1 1 901 336 336 GLU CA C 58.014 0.1 1 902 336 336 GLU CB C 28.938 0.1 1 903 336 336 GLU N N 120.648 0.1 1 904 337 337 TRP H H 7.753 0.02 1 905 337 337 TRP C C 180.705 0.1 1 906 337 337 TRP CA C 59.427 0.1 1 907 337 337 TRP CB C 30.184 0.1 1 908 337 337 TRP N N 119.77 0.1 1 909 338 338 LYS H H 8.778 0.02 1 910 338 338 LYS C C 177.438 0.1 1 911 338 338 LYS CA C 59.909 0.1 1 912 338 338 LYS CB C 31.444 0.1 1 913 338 338 LYS N N 121.418 0.1 1 914 339 339 SER H H 7.662 0.02 1 915 339 339 SER C C 176.644 0.1 1 916 339 339 SER CA C 60.701 0.1 1 917 339 339 SER CB C 61.965 0.1 1 918 339 339 SER N N 114.588 0.1 1 919 340 340 LEU H H 7.97 0.02 1 920 340 340 LEU C C 180.687 0.1 1 921 340 340 LEU CA C 57.262 0.1 1 922 340 340 LEU CB C 41.304 0.1 1 923 340 340 LEU N N 120.453 0.1 1 924 341 341 THR H H 8.182 0.02 1 925 341 341 THR C C 175.796 0.1 1 926 341 341 THR CA C 67.93 0.1 1 927 341 341 THR CB C 67.473 0.1 1 928 341 341 THR N N 116.213 0.1 1 929 342 342 TYR H H 8.846 0.02 1 930 342 342 TYR C C 177.221 0.1 1 931 342 342 TYR CA C 61.263 0.1 1 932 342 342 TYR CB C 37.232 0.1 1 933 342 342 TYR N N 124.824 0.1 1 934 343 343 ASP H H 8.084 0.02 1 935 343 343 ASP C C 179.821 0.1 1 936 343 343 ASP CA C 56.711 0.1 1 937 343 343 ASP CB C 39.535 0.1 1 938 343 343 ASP N N 117.358 0.1 1 939 344 344 GLU H H 7.545 0.02 1 940 344 344 GLU C C 178.774 0.1 1 941 344 344 GLU CA C 57.51 0.1 1 942 344 344 GLU CB C 28.964 0.1 1 943 344 344 GLU N N 118.326 0.1 1 944 345 345 VAL H H 8.106 0.02 1 945 345 345 VAL C C 178.684 0.1 1 946 345 345 VAL CA C 65.444 0.1 1 947 345 345 VAL CB C 30.593 0.1 1 948 345 345 VAL N N 121.218 0.1 1 949 346 346 ILE H H 8.125 0.02 1 950 346 346 ILE C C 177.619 0.1 1 951 346 346 ILE CA C 62.634 0.1 1 952 346 346 ILE CB C 36.019 0.1 1 953 346 346 ILE N N 114.601 0.1 1 954 347 347 SER H H 7.434 0.02 1 955 347 347 SER C C 174.57 0.1 1 956 347 347 SER CA C 57.583 0.1 1 957 347 347 SER CB C 63.18 0.1 1 958 347 347 SER N N 113.416 0.1 1 959 348 348 PHE H H 7.321 0.02 1 960 348 348 PHE C C 173.956 0.1 1 961 348 348 PHE CA C 59.744 0.1 1 962 348 348 PHE CB C 38.852 0.1 1 963 348 348 PHE N N 124.96 0.1 1 964 349 349 VAL H H 6.933 0.02 1 965 349 349 VAL CA C 63.116 0.1 1 966 349 349 VAL CB C 32.888 0.1 1 967 349 349 VAL N N 130.008 0.1 1 stop_ save_