data_17471 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for p38 alpha MAPK ; _BMRB_accession_number 17471 _BMRB_flat_file_name bmr17471.str _Entry_type original _Submission_date 2011-02-15 _Accession_date 2011-02-15 _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 Francis Dana M. . 2 Peti Wolfgang . . 3 Page Rebecca . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 273 "13C chemical shifts" 585 "15N chemical shifts" 273 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-12-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6468 'p38 mitogen-activated protein kinase' stop_ _Original_release_date 2011-12-12 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis of p38 regulation by hematopoietic tyrosine phosphatase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22057126 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Francis Dana M. . 2 Roycki Bartosz . . 3 Koveal Dorothy . . 4 Hummer Gerhard . . 5 Page Rebecca . . 6 Peti Wolfgang . . stop_ _Journal_abbreviation 'Nat. Chem. Biol.' _Journal_name_full 'Nature chemical biology' _Journal_volume 7 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 916 _Page_last 924 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name p38_alpha _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'p38 alpha' $p38_alpha stop_ _System_molecular_weight 40290 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'protein kinase' stop_ _Database_query_date . _Details 'monomer, no ligand bound' save_ ######################## # Monomeric polymers # ######################## save_p38_alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p38_alpha _Molecular_mass 40290 _Mol_thiol_state 'all free' loop_ _Biological_function 'mitogen-activated protein kinase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 352 _Mol_residue_sequence ; GHMGSQERPTFYRQELNKTI WEVPERYQNLSPVGSGAYGS VCAAFDTKTGLRVAVKKLSR PFQSIIHAKRTYRELRLLKH MKHENVIGLLDVFTPARSLE EFNDVYLVTHLMGADLNNIV KCQKLTDDHVQFLIYQILRG LKYIHSADIIHRDLKPSNLA VNEDCELKILDFGLARHTDD EMTGYVATRWYRAPEIMLNW MHYNQTVDIWSVGCIMAELL TGRTLFPGTDHIDQLKLILR LVGTPGAELLKKISSESARN YIQSLTQMPKMNFANVFIGA NPLAVDLLEKMLVLDSDKRI TAAQALAHAYFAQYHDPDDE PVADPYDQSFESRDLLIDEW KSLTYDEVISFV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 GLY 5 SER 6 GLN 7 GLU 8 ARG 9 PRO 10 THR 11 PHE 12 TYR 13 ARG 14 GLN 15 GLU 16 LEU 17 ASN 18 LYS 19 THR 20 ILE 21 TRP 22 GLU 23 VAL 24 PRO 25 GLU 26 ARG 27 TYR 28 GLN 29 ASN 30 LEU 31 SER 32 PRO 33 VAL 34 GLY 35 SER 36 GLY 37 ALA 38 TYR 39 GLY 40 SER 41 VAL 42 CYS 43 ALA 44 ALA 45 PHE 46 ASP 47 THR 48 LYS 49 THR 50 GLY 51 LEU 52 ARG 53 VAL 54 ALA 55 VAL 56 LYS 57 LYS 58 LEU 59 SER 60 ARG 61 PRO 62 PHE 63 GLN 64 SER 65 ILE 66 ILE 67 HIS 68 ALA 69 LYS 70 ARG 71 THR 72 TYR 73 ARG 74 GLU 75 LEU 76 ARG 77 LEU 78 LEU 79 LYS 80 HIS 81 MET 82 LYS 83 HIS 84 GLU 85 ASN 86 VAL 87 ILE 88 GLY 89 LEU 90 LEU 91 ASP 92 VAL 93 PHE 94 THR 95 PRO 96 ALA 97 ARG 98 SER 99 LEU 100 GLU 101 GLU 102 PHE 103 ASN 104 ASP 105 VAL 106 TYR 107 LEU 108 VAL 109 THR 110 HIS 111 LEU 112 MET 113 GLY 114 ALA 115 ASP 116 LEU 117 ASN 118 ASN 119 ILE 120 VAL 121 LYS 122 CYS 123 GLN 124 LYS 125 LEU 126 THR 127 ASP 128 ASP 129 HIS 130 VAL 131 GLN 132 PHE 133 LEU 134 ILE 135 TYR 136 GLN 137 ILE 138 LEU 139 ARG 140 GLY 141 LEU 142 LYS 143 TYR 144 ILE 145 HIS 146 SER 147 ALA 148 ASP 149 ILE 150 ILE 151 HIS 152 ARG 153 ASP 154 LEU 155 LYS 156 PRO 157 SER 158 ASN 159 LEU 160 ALA 161 VAL 162 ASN 163 GLU 164 ASP 165 CYS 166 GLU 167 LEU 168 LYS 169 ILE 170 LEU 171 ASP 172 PHE 173 GLY 174 LEU 175 ALA 176 ARG 177 HIS 178 THR 179 ASP 180 ASP 181 GLU 182 MET 183 THR 184 GLY 185 TYR 186 VAL 187 ALA 188 THR 189 ARG 190 TRP 191 TYR 192 ARG 193 ALA 194 PRO 195 GLU 196 ILE 197 MET 198 LEU 199 ASN 200 TRP 201 MET 202 HIS 203 TYR 204 ASN 205 GLN 206 THR 207 VAL 208 ASP 209 ILE 210 TRP 211 SER 212 VAL 213 GLY 214 CYS 215 ILE 216 MET 217 ALA 218 GLU 219 LEU 220 LEU 221 THR 222 GLY 223 ARG 224 THR 225 LEU 226 PHE 227 PRO 228 GLY 229 THR 230 ASP 231 HIS 232 ILE 233 ASP 234 GLN 235 LEU 236 LYS 237 LEU 238 ILE 239 LEU 240 ARG 241 LEU 242 VAL 243 GLY 244 THR 245 PRO 246 GLY 247 ALA 248 GLU 249 LEU 250 LEU 251 LYS 252 LYS 253 ILE 254 SER 255 SER 256 GLU 257 SER 258 ALA 259 ARG 260 ASN 261 TYR 262 ILE 263 GLN 264 SER 265 LEU 266 THR 267 GLN 268 MET 269 PRO 270 LYS 271 MET 272 ASN 273 PHE 274 ALA 275 ASN 276 VAL 277 PHE 278 ILE 279 GLY 280 ALA 281 ASN 282 PRO 283 LEU 284 ALA 285 VAL 286 ASP 287 LEU 288 LEU 289 GLU 290 LYS 291 MET 292 LEU 293 VAL 294 LEU 295 ASP 296 SER 297 ASP 298 LYS 299 ARG 300 ILE 301 THR 302 ALA 303 ALA 304 GLN 305 ALA 306 LEU 307 ALA 308 HIS 309 ALA 310 TYR 311 PHE 312 ALA 313 GLN 314 TYR 315 HIS 316 ASP 317 PRO 318 ASP 319 ASP 320 GLU 321 PRO 322 VAL 323 ALA 324 ASP 325 PRO 326 TYR 327 ASP 328 GLN 329 SER 330 PHE 331 GLU 332 SER 333 ARG 334 ASP 335 LEU 336 LEU 337 ILE 338 ASP 339 GLU 340 TRP 341 LYS 342 SER 343 LEU 344 THR 345 TYR 346 ASP 347 GLU 348 VAL 349 ILE 350 SER 351 PHE 352 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-29 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 17940 p38alpha 99.15 349 99.14 99.14 0.00e+00 BMRB 19930 Non-phosphorylated_human_p38_alpha_(apo) 99.72 367 99.43 99.43 0.00e+00 BMRB 19934 Dual-phosphorylated_human_p38_alpha_(apo) 99.72 367 98.86 98.86 0.00e+00 BMRB 19935 Dual-phosphorylated_human_p38_alpha 99.72 367 98.86 98.86 0.00e+00 BMRB 19936 dual-phosphorylated_human_p38_alpha_(apo) 99.72 367 98.86 98.86 0.00e+00 BMRB 19937 dual-phosphorylated_human_p38_alpha_(apo) 99.72 367 98.86 98.86 0.00e+00 PDB 1A9U "The Complex Structure Of The Map Kinase P38SB203580" 100.00 379 99.43 99.43 0.00e+00 PDB 1BL6 "The Complex Structure Of The Map Kinase P38SB216995" 100.00 379 99.43 99.43 0.00e+00 PDB 1BL7 "The Complex Structure Of The Map Kinase P38SB220025" 100.00 379 99.43 99.43 0.00e+00 PDB 1BMK "The Complex Structure Of The Map Kinase P38SB218655" 100.00 379 98.86 98.86 0.00e+00 PDB 1DI9 "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" 98.86 360 100.00 100.00 0.00e+00 PDB 1IAN "Human P38 Map Kinase Inhibitor Complex" 99.72 366 99.43 99.43 0.00e+00 PDB 1KV1 "P38 Map Kinase In Complex With Inhibitor 1" 98.86 360 100.00 100.00 0.00e+00 PDB 1KV2 "Human P38 Map Kinase In Complex With Birb 796" 98.86 360 100.00 100.00 0.00e+00 PDB 1LEW "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" 98.86 360 99.43 99.43 0.00e+00 PDB 1LEZ "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" 98.86 360 99.43 99.43 0.00e+00 PDB 1M7Q "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 1OUK "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 1OUY "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 1OVE "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" 98.86 366 99.71 99.71 0.00e+00 PDB 1OZ1 "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" 98.86 372 100.00 100.00 0.00e+00 PDB 1P38 "The Structure Of The Map Kinase P38 At 2.1 Angstoms Resolution" 100.00 379 98.86 98.86 0.00e+00 PDB 1R39 "The Structure Of P38alpha" 98.86 366 100.00 100.00 0.00e+00 PDB 1R3C "The Structure Of P38alpha C162s Mutant" 98.86 366 99.71 99.71 0.00e+00 PDB 1W7H "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 1W82 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 1W83 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 1W84 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 1WBN "Fragment Based P38 Inhibitors" 98.86 360 100.00 100.00 0.00e+00 PDB 1WBO "Fragment Based P38 Inhibitors" 98.86 360 100.00 100.00 0.00e+00 PDB 1WBS "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 98.86 360 100.00 100.00 0.00e+00 PDB 1WBT "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." 98.86 360 100.00 100.00 0.00e+00 PDB 1WBV "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 98.86 360 100.00 100.00 0.00e+00 PDB 1WBW "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 98.86 360 100.00 100.00 0.00e+00 PDB 1WFC "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" 98.86 366 100.00 100.00 0.00e+00 PDB 1YQJ "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 1YW2 "Mutated Mus Musculus P38 Kinase (Mp38)" 98.86 360 98.85 99.14 0.00e+00 PDB 1YWR "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" 98.86 360 99.14 99.43 0.00e+00 PDB 1ZYJ "Human P38 Map Kinase In Complex With Inhibitor 1a" 98.86 360 100.00 100.00 0.00e+00 PDB 1ZZ2 "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" 98.86 360 100.00 100.00 0.00e+00 PDB 1ZZL "Crystal Structure Of P38 With Triazolopyridine" 98.30 351 100.00 100.00 0.00e+00 PDB 2BAJ "P38alpha Bound To Pyrazolourea" 99.72 365 99.43 99.43 0.00e+00 PDB 2BAK "P38alpha Map Kinase Bound To Mpaq" 99.72 365 99.43 99.43 0.00e+00 PDB 2BAL "P38alpha Map Kinase Bound To Pyrazoloamine" 99.72 365 99.15 99.15 0.00e+00 PDB 2BAQ "P38alpha Bound To Ro3201195" 99.72 365 98.86 99.15 0.00e+00 PDB 2EWA "Dual Binding Mode Of Pyridinylimidazole To Map Kinase P38" 100.00 379 99.43 99.43 0.00e+00 PDB 2FSL "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" 99.72 367 98.86 98.86 0.00e+00 PDB 2FSM "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" 99.72 367 98.86 98.86 0.00e+00 PDB 2FSO "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" 99.72 367 99.15 99.15 0.00e+00 PDB 2FST "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" 99.72 367 98.86 98.86 0.00e+00 PDB 2GFS "P38 Kinase Crystal Structure In Complex With Ro3201195" 98.86 372 100.00 100.00 0.00e+00 PDB 2GHL "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" 98.01 348 98.84 99.13 0.00e+00 PDB 2GHM "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" 98.01 348 98.84 99.13 0.00e+00 PDB 2GTM "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" 98.01 348 99.42 99.42 0.00e+00 PDB 2GTN "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" 98.01 348 99.42 99.42 0.00e+00 PDB 2I0H "The Structure Of P38alpha In Complex With An Arylpyridazinone" 98.86 366 99.71 99.71 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" 98.86 359 100.00 100.00 0.00e+00 PDB 2NPQ "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" 99.72 367 99.43 99.43 0.00e+00 PDB 2OKR "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 98.86 366 100.00 100.00 0.00e+00 PDB 2ONL "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 98.86 366 100.00 100.00 0.00e+00 PDB 2OZA "Structure Of P38alpha Complex" 99.72 366 98.86 98.86 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" 98.01 348 98.84 98.84 0.00e+00 PDB 2QD9 "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" 99.72 366 99.43 99.43 0.00e+00 PDB 2RG5 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" 99.72 366 99.43 99.43 0.00e+00 PDB 2RG6 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" 99.72 366 99.43 99.43 0.00e+00 PDB 2Y8O "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" 98.86 362 99.71 99.71 0.00e+00 PDB 2YIS "Triazolopyridine Inhibitors Of P38 Kinase." 98.86 359 100.00 100.00 0.00e+00 PDB 2YIW "Triazolopyridine Inhibitors Of P38 Kinase" 98.86 359 100.00 100.00 0.00e+00 PDB 2YIX "Triazolopyridine Inhibitors Of P38" 98.30 351 100.00 100.00 0.00e+00 PDB 2ZAZ "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 2ZB0 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 2ZB1 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 3BV2 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" 99.72 366 99.43 99.43 0.00e+00 PDB 3BV3 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" 99.72 366 99.43 99.43 0.00e+00 PDB 3BX5 "P38 Alpha Map Kinase Complexed With Bms-640994" 99.72 366 99.43 99.43 0.00e+00 PDB 3C5U "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" 99.72 366 99.43 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" 98.01 348 98.84 98.84 0.00e+00 PDB 3D7Z "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 98.86 360 99.71 99.71 0.00e+00 PDB 3D83 "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 98.86 360 99.43 99.43 0.00e+00 PDB 3DS6 "P38 Complex With A Phthalazine Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 3DT1 "P38 Complexed With A Quinazoline Inhibitor" 98.86 383 100.00 100.00 0.00e+00 PDB 3E92 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 99.72 371 99.15 99.15 0.00e+00 PDB 3E93 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 99.72 371 99.15 99.15 0.00e+00 PDB 3FC1 "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 3FI4 "P38 Kinase Crystal Structure In Complex With Ro4499" 98.86 372 99.71 100.00 0.00e+00 PDB 3FKL "P38 Kinase Crystal Structure In Complex With Ro9552" 98.86 372 100.00 100.00 0.00e+00 PDB 3FKN "P38 Kinase Crystal Structure In Complex With Ro7125" 98.86 372 100.00 100.00 0.00e+00 PDB 3FKO "P38 Kinase Crystal Structure In Complex With Ro3668" 98.86 372 99.71 100.00 0.00e+00 PDB 3FL4 "P38 Kinase Crystal Structure In Complex With Ro5634" 98.86 372 100.00 100.00 0.00e+00 PDB 3FLN "P38 Kinase Crystal Structure In Complex With R1487" 98.86 372 99.71 100.00 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-" 98.86 372 100.00 100.00 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-" 98.86 372 100.00 100.00 0.00e+00 PDB 3FLW "P38 Kinase Crystal Structure In Complex With Pamapimod" 98.86 372 100.00 100.00 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" 98.86 372 100.00 100.00 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" 98.86 372 100.00 100.00 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-" 98.86 372 100.00 100.00 0.00e+00 PDB 3FMJ "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" 98.86 372 100.00 100.00 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-" 98.86 372 100.00 100.00 0.00e+00 PDB 3FML "P38 Kinase Crystal Structure In Complex With Ro6224" 98.86 372 100.00 100.00 0.00e+00 PDB 3FMM "P38 Kinase Crystal Structure In Complex With Ro6226" 98.86 372 100.00 100.00 0.00e+00 PDB 3FMN "P38 Kinase Crystal Structure In Complex With Ro2530" 98.86 372 100.00 100.00 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" 98.86 372 100.00 100.00 0.00e+00 PDB 3FSK "P38 Kinase Crystal Structure In Complex With Ro6257" 98.86 372 100.00 100.00 0.00e+00 PDB 3GC7 "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" 98.86 366 99.71 99.71 0.00e+00 PDB 3GCP "Human P38 Map Kinase In Complex With Sb203580" 99.15 360 98.85 98.85 0.00e+00 PDB 3GCQ "Human P38 Map Kinase In Complex With Rl45" 99.15 360 98.85 98.85 0.00e+00 PDB 3GCS "Human P38 Map Kinase In Complex With Sorafenib" 99.15 360 98.85 98.85 0.00e+00 PDB 3GCU "Human P38 Map Kinase In Complex With Rl48" 99.15 360 100.00 100.00 0.00e+00 PDB 3GCV "Human P38 Map Kinase In Complex With Rl62" 99.15 360 98.85 98.85 0.00e+00 PDB 3GFE "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 3GI3 "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" 98.86 360 99.43 99.43 0.00e+00 PDB 3HA8 "The Complex Structure Of The Map Kinase P38COMPOUND 14B" 100.00 379 99.43 99.43 0.00e+00 PDB 3HEC "P38 In Complex With Imatinib" 98.01 348 100.00 100.00 0.00e+00 PDB 3HEG "P38 In Complex With Sorafenib" 98.01 348 100.00 100.00 0.00e+00 PDB 3HL7 "Crystal Structure Of Human P38alpha Complexed With Sd-0006" 98.86 360 100.00 100.00 0.00e+00 PDB 3HLL "Crystal Structure Of Human P38alpha Complexed With Ph-797804" 98.86 360 100.00 100.00 0.00e+00 PDB 3HP2 "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" 98.86 360 100.00 100.00 0.00e+00 PDB 3HP5 "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" 98.86 360 100.00 100.00 0.00e+00 PDB 3HRB "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 359 100.00 100.00 0.00e+00 PDB 3HUB "Human P38 Map Kinase In Complex With Scios-469" 99.15 360 98.85 98.85 0.00e+00 PDB 3HUC "Human P38 Map Kinase In Complex With Rl40" 99.15 360 100.00 100.00 0.00e+00 PDB 3HV3 "Human P38 Map Kinase In Complex With Rl49" 99.15 360 98.85 98.85 0.00e+00 PDB 3HV4 "Human P38 Map Kinase In Complex With Rl51" 99.15 360 100.00 100.00 0.00e+00 PDB 3HV5 "Human P38 Map Kinase In Complex With Rl24" 99.15 360 100.00 100.00 0.00e+00 PDB 3HV6 "Human P38 Map Kinase In Complex With Rl39" 99.15 360 100.00 100.00 0.00e+00 PDB 3HV7 "Human P38 Map Kinase In Complex With Rl38" 99.15 360 100.00 100.00 0.00e+00 PDB 3HVC "Crystal Structure Of Human P38alpha Map Kinase" 98.86 362 100.00 100.00 0.00e+00 PDB 3IPH "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" 98.86 360 99.43 99.43 0.00e+00 PDB 3ITZ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 3IW5 "Human P38 Map Kinase In Complex With An Indole Derivative" 99.15 360 98.85 98.85 0.00e+00 PDB 3IW6 "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" 99.15 360 98.85 98.85 0.00e+00 PDB 3IW7 "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" 99.15 360 98.85 98.85 0.00e+00 PDB 3IW8 "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" 99.15 360 98.85 98.85 0.00e+00 PDB 3K3I "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" 98.01 350 100.00 100.00 0.00e+00 PDB 3K3J "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" 98.86 362 100.00 100.00 0.00e+00 PDB 3KF7 "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" 98.86 360 100.00 100.00 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" 100.00 380 99.43 99.43 0.00e+00 PDB 3L8S "Human P38 Map Kinase In Complex With Cp-547632" 99.15 360 98.85 98.85 0.00e+00 PDB 3L8X "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" 99.72 366 99.43 99.43 0.00e+00 PDB 3LFA "Human P38 Map Kinase In Complex With Dasatinib" 99.15 360 100.00 100.00 0.00e+00 PDB 3LFB "Human P38 Map Kinase In Complex With Rl98" 99.15 360 98.85 98.85 0.00e+00 PDB 3LFC "Human P38 Map Kinase In Complex With Rl99" 99.15 360 98.85 98.85 0.00e+00 PDB 3LFD "Human P38 Map Kinase In Complex With Rl113" 99.15 360 98.85 98.85 0.00e+00 PDB 3LFE "Human P38 Map Kinase In Complex With Rl116" 99.15 360 98.85 98.85 0.00e+00 PDB 3LFF "Human P38 Map Kinase In Complex With Rl166" 99.15 360 98.85 98.85 0.00e+00 PDB 3LHJ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." 98.86 366 100.00 100.00 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 " 98.86 360 100.00 100.00 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 " 98.86 360 99.71 99.71 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" 98.86 360 99.71 99.71 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" 98.86 360 99.71 100.00 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" 98.86 360 99.71 99.71 0.00e+00 PDB 3MPA "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 98.86 360 99.71 99.71 0.00e+00 PDB 3MPT "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" 99.72 371 99.43 99.43 0.00e+00 PDB 3MVL "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" 99.72 366 99.43 99.43 0.00e+00 PDB 3MVM "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" 99.72 366 99.43 99.43 0.00e+00 PDB 3MW1 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 359 100.00 100.00 0.00e+00 PDB 3NEW "P38-Alpha Complexed With Compound 10" 98.86 366 99.71 99.71 0.00e+00 PDB 3NNU "Crystal Structure Of P38 Alpha In Complex With Dp1376" 98.86 354 100.00 100.00 0.00e+00 PDB 3NNV "Crystal Structure Of P38 Alpha In Complex With Dp437" 98.86 354 100.00 100.00 0.00e+00 PDB 3NNW "Crystal Structure Of P38 Alpha In Complex With Dp802" 98.86 354 100.00 100.00 0.00e+00 PDB 3NNX "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" 98.86 354 99.71 99.71 0.00e+00 PDB 3NWW "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" 99.72 366 99.43 99.43 0.00e+00 PDB 3O8P "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 98.86 360 99.71 99.71 0.00e+00 PDB 3O8T "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" 98.86 360 99.71 99.71 0.00e+00 PDB 3O8U "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 98.86 360 99.71 100.00 0.00e+00 PDB 3OBG "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 98.86 360 99.71 99.71 0.00e+00 PDB 3OBJ "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 98.86 360 99.71 99.71 0.00e+00 PDB 3OC1 "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 98.86 360 99.71 99.71 0.00e+00 PDB 3OCG "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" 99.72 366 99.43 99.43 0.00e+00 PDB 3OD6 "Crystal Structure Of P38alpha Y323t Active Mutant" 98.86 360 99.71 99.71 0.00e+00 PDB 3ODY "Crystal Structure Of P38alpha Y323q Active Mutant" 98.86 360 99.71 99.71 0.00e+00 PDB 3ODZ "Crystal Structure Of P38alpha Y323r Active Mutant" 98.86 360 99.71 99.71 0.00e+00 PDB 3OEF "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" 98.86 360 99.71 100.00 0.00e+00 PDB 3P4K "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" 99.43 370 98.86 99.14 0.00e+00 PDB 3P5K "P38 Inhibitor-Bound" 99.72 366 98.86 98.86 0.00e+00 PDB 3P78 "P38 Inhibitor-Bound" 99.72 366 98.86 98.86 0.00e+00 PDB 3P79 "P38 Inhibitor-Bound" 99.72 366 98.86 98.86 0.00e+00 PDB 3P7A "P38 Inhibitor-Bound" 99.72 366 98.86 98.86 0.00e+00 PDB 3P7B "P38 Inhibitor-Bound" 99.72 366 98.86 98.86 0.00e+00 PDB 3P7C "P38 Inhibitor-Bound" 99.72 366 98.86 98.86 0.00e+00 PDB 3PG3 "Human P38 Map Kinase In Complex With Rl182" 99.15 360 98.85 98.85 0.00e+00 PDB 3PY3 "Crystal Structure Of Phosphorylated P38alpha Map Kinase" 100.00 380 98.01 98.01 0.00e+00 PDB 3QUD "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" 99.15 360 100.00 100.00 0.00e+00 PDB 3QUE "Human P38 Map Kinase In Complex With Skepinone-l" 99.15 360 100.00 100.00 0.00e+00 PDB 3RIN "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.86 360 100.00 100.00 0.00e+00 PDB 3ROC "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" 98.86 360 100.00 100.00 0.00e+00 PDB 3S3I "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.30 349 100.00 100.00 0.00e+00 PDB 3S4Q "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" 99.72 366 99.43 99.43 0.00e+00 PDB 3TG1 "Crystal Structure Of P38alpha In Complex With A Mapk Docking Partner" 100.00 380 98.58 98.58 0.00e+00 PDB 3U8W "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" 98.86 366 100.00 100.00 0.00e+00 PDB 3UVP "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" 99.15 360 100.00 100.00 0.00e+00 PDB 3UVQ "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" 99.15 360 100.00 100.00 0.00e+00 PDB 3UVR "Human P38 Map Kinase In Complex With Km064" 99.15 360 100.00 100.00 0.00e+00 PDB 3ZS5 "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" 98.86 362 100.00 100.00 0.00e+00 PDB 3ZSG "X-Ray Structure Of P38alpha Bound To Tak-715" 98.86 362 100.00 100.00 0.00e+00 PDB 3ZSH "X-Ray Structure Of P38alpha Bound To Scio-469" 98.86 362 100.00 100.00 0.00e+00 PDB 3ZSI "X-Ray Structure Of P38alpha Bound To Vx-745" 98.86 362 100.00 100.00 0.00e+00 PDB 3ZYA "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" 98.86 366 100.00 100.00 0.00e+00 PDB 4A9Y "P38alpha Map Kinase Bound To Cmpd 8" 99.72 365 99.43 99.43 0.00e+00 PDB 4AA0 "P38alpha Map Kinase Bound To Cmpd 2" 99.72 365 99.43 99.43 0.00e+00 PDB 4AA4 "P38alpha Map Kinase Bound To Cmpd 22" 99.72 365 99.43 99.43 0.00e+00 PDB 4AA5 "P38alpha Map Kinase Bound To Cmpd 33" 99.72 365 99.15 99.15 0.00e+00 PDB 4AAC "P38alpha Map Kinase Bound To Cmpd 29" 99.72 365 99.43 99.43 0.00e+00 PDB 4DLI "Human P38 Map Kinase In Complex With Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4DLJ "Human P38 Map Kinase In Complex With Rl163" 99.15 360 100.00 100.00 0.00e+00 PDB 4E5A "The W197a Mutant Of P38a Map Kinase" 98.86 360 99.71 99.71 0.00e+00 PDB 4E5B "Structure Of P38a Map Kinase Without Bog" 98.86 360 100.00 100.00 0.00e+00 PDB 4E6A "P38a-pia23 Complex" 98.86 360 100.00 100.00 0.00e+00 PDB 4E6C "P38a-perifosine Complex" 98.86 360 100.00 100.00 0.00e+00 PDB 4E8A "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" 98.86 360 100.00 100.00 0.00e+00 PDB 4EH2 "Human P38 Map Kinase In Complex With Np-F1 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH3 "Human P38 Map Kinase In Complex With Np-F2 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH4 "Human P38 Map Kinase In Complex With Np-F3 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH5 "Human P38 Map Kinase In Complex With Np-F4 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH6 "Human P38 Map Kinase In Complex With Np-F5 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH7 "Human P38 Map Kinase In Complex With Np-F6 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH8 "Human P38 Map Kinase In Complex With Np-F7 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EH9 "Human P38 Map Kinase In Complex With Np-F11 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EHV "Human P38 Map Kinase In Complex With Np-F10 And Rl87" 99.15 360 100.00 100.00 0.00e+00 PDB 4EWQ "Human P38 Alpha Mapk In Complex With A Pyridazine Based Inhibitor" 99.15 383 99.43 99.43 0.00e+00 PDB 4F9W "Human P38alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" 99.15 383 99.71 99.71 0.00e+00 PDB 4F9Y "Human P38 Alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" 99.15 383 99.71 99.71 0.00e+00 PDB 4FA2 "Human P38 Alpha Mitogen-activated Kinase In Complex With Sb239063" 99.15 383 99.71 99.71 0.00e+00 PDB 4GEO "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" 99.72 367 98.01 98.01 0.00e+00 PDB 4KA3 "Structure Of Map Kinase In Complex With A Docking Peptide" 98.86 360 99.43 99.43 0.00e+00 PDB 4KIN "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 99.72 366 99.43 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" 99.72 366 99.43 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" 99.72 366 99.43 99.43 0.00e+00 PDB 4L8M "Human P38 Map Kinase In Complex With A Dibenzoxepinone" 99.15 360 100.00 100.00 0.00e+00 PDB 4LOO "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" 98.86 361 99.43 99.43 0.00e+00 PDB 4LOP "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" 98.86 361 99.43 99.43 0.00e+00 PDB 4LOQ "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" 98.86 361 99.43 99.43 0.00e+00 PDB 4R3C "Crystal Structure Of P38 Alpha Map Kinase In Complex With A Novel Isoform Selective Drug Candidate" 99.15 383 99.43 99.43 0.00e+00 PDB 4TYH "Ternary Complex Of P38 And Mk2 With A P38 Inhibitor" 97.73 348 99.42 99.42 0.00e+00 DBJ BAB85654 "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" 71.88 307 100.00 100.00 0.00e+00 DBJ BAE21782 "unnamed protein product [Mus musculus]" 98.86 360 99.43 99.43 0.00e+00 DBJ BAE30324 "unnamed protein product [Mus musculus]" 77.27 283 99.63 99.63 0.00e+00 DBJ BAE31659 "unnamed protein product [Mus musculus]" 77.27 283 99.63 99.63 0.00e+00 DBJ BAF84398 "unnamed protein product [Homo sapiens]" 98.86 360 99.71 99.71 0.00e+00 EMBL CAG38743 "MAPK14 [Homo sapiens]" 98.86 360 100.00 100.00 0.00e+00 GB AAA20888 "MAP kinase [Mus musculus]" 98.86 360 99.43 99.43 0.00e+00 GB AAA57456 "CSaids binding protein [Homo sapiens]" 98.86 360 100.00 100.00 0.00e+00 GB AAA74301 "MAP kinase [Homo sapiens]" 98.86 360 100.00 100.00 0.00e+00 GB AAB51285 "p38 mitogen activated protein kinase [Rattus norvegicus]" 98.86 360 98.28 98.85 0.00e+00 GB AAC36131 "p38 mitogen activated protein kinase [Canis lupus familiaris]" 98.86 360 99.43 100.00 0.00e+00 PRF 2111247A "p38 mitogen-activated protein kinase" 98.86 360 100.00 100.00 0.00e+00 PRF 2124426A "Mxi2 protein" 79.55 297 99.64 99.64 0.00e+00 REF NP_001003206 "mitogen-activated protein kinase 14 [Canis lupus familiaris]" 98.86 360 99.43 100.00 0.00e+00 REF NP_001136366 "mitogen-activated protein kinase 14 [Ovis aries]" 98.86 360 100.00 100.00 0.00e+00 REF NP_001161985 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.27 283 99.63 99.63 0.00e+00 REF NP_001161986 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.27 283 99.63 99.63 0.00e+00 REF NP_036081 "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" 98.86 360 99.43 99.43 0.00e+00 SP O02812 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " 98.86 360 99.43 100.00 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" 98.86 360 99.43 99.43 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" 98.86 360 98.56 99.14 0.00e+00 SP Q16539 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" 98.86 360 100.00 100.00 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 $p38_alpha 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 $p38_alpha 'recombinant technology' 'Escherichia coli' Escherichia coli . pRPIB stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p38_alpha 0.58 mM '[U-13C; U-15N; U-2H]' HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' DTT 5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p38_alpha 0.2 mM [U-2H;U-15N] HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' DTT 5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version '1.3 and 2.1' loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.8 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . 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 800 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_1 $citation_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(COCA)CB' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'p38 alpha' _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 3 3 MET CA C 55.190 0.250 1 2 3 3 MET CB C 31.685 0.250 1 3 4 4 GLY H H 8.346 0.010 1 4 4 4 GLY CA C 44.812 0.250 1 5 4 4 GLY N N 110.960 0.070 1 6 5 5 SER H H 8.138 0.010 1 7 5 5 SER CA C 58.001 0.250 1 8 5 5 SER CB C 63.163 0.250 1 9 5 5 SER N N 116.267 0.070 1 10 6 6 GLN H H 8.389 0.010 1 11 6 6 GLN CA C 55.404 0.250 1 12 6 6 GLN CB C 28.614 0.250 1 13 6 6 GLN N N 122.413 0.070 1 14 7 7 GLU H H 8.276 0.010 1 15 7 7 GLU CA C 55.779 0.250 1 16 7 7 GLU CB C 29.365 0.250 1 17 7 7 GLU N N 122.700 0.070 1 18 8 8 ARG H H 8.332 0.010 1 19 8 8 ARG CA C 53.717 0.250 1 20 8 8 ARG CB C 29.698 0.250 1 21 8 8 ARG N N 125.403 0.070 1 22 9 9 PRO CA C 62.205 0.250 1 23 9 9 PRO CB C 31.480 0.250 1 24 10 10 THR H H 8.418 0.010 1 25 10 10 THR CA C 62.660 0.250 1 26 10 10 THR CB C 68.880 0.250 1 27 10 10 THR N N 117.617 0.070 1 28 11 11 PHE H H 8.729 0.010 1 29 11 11 PHE CA C 56.555 0.250 1 30 11 11 PHE CB C 41.172 0.250 1 31 11 11 PHE N N 127.438 0.070 1 32 12 12 TYR H H 9.089 0.010 1 33 12 12 TYR CA C 55.538 0.250 1 34 12 12 TYR CB C 40.148 0.250 1 35 12 12 TYR N N 120.358 0.070 1 36 13 13 ARG H H 8.385 0.010 1 37 13 13 ARG CA C 54.092 0.250 1 38 13 13 ARG CB C 32.914 0.250 1 39 13 13 ARG N N 120.323 0.070 1 40 14 14 GLN H H 8.934 0.010 1 41 14 14 GLN CA C 54.494 0.250 1 42 14 14 GLN CB C 32.368 0.250 1 43 14 14 GLN N N 122.785 0.070 1 44 15 15 GLU H H 8.790 0.010 1 45 15 15 GLU CA C 55.110 0.250 1 46 15 15 GLU CB C 29.706 0.250 1 47 15 15 GLU N N 125.887 0.070 1 48 16 16 LEU H H 8.942 0.010 1 49 16 16 LEU CA C 53.557 0.250 1 50 16 16 LEU CB C 43.492 0.250 1 51 16 16 LEU N N 128.790 0.070 1 52 17 17 ASN H H 7.250 0.010 1 53 17 17 ASN CA C 53.664 0.250 1 54 17 17 ASN CB C 36.715 0.250 1 55 17 17 ASN N N 116.253 0.070 1 56 18 18 LYS H H 8.830 0.010 1 57 18 18 LYS CA C 57.363 0.250 1 58 18 18 LYS CB C 28.887 0.250 1 59 18 18 LYS N N 110.200 0.070 1 60 19 19 THR H H 7.806 0.010 1 61 19 19 THR CA C 60.946 0.250 1 62 19 19 THR CB C 70.723 0.250 1 63 19 19 THR N N 115.941 0.070 1 64 20 20 ILE H H 8.553 0.010 1 65 20 20 ILE CA C 59.742 0.250 1 66 20 20 ILE CB C 35.917 0.250 1 67 20 20 ILE N N 125.788 0.070 1 68 21 21 TRP H H 9.227 0.010 1 69 21 21 TRP CA C 56.529 0.250 1 70 21 21 TRP CB C 28.546 0.250 1 71 21 21 TRP N N 131.308 0.070 1 72 22 22 GLU H H 8.222 0.010 1 73 22 22 GLU CA C 54.547 0.250 1 74 22 22 GLU CB C 30.525 0.250 1 75 22 22 GLU N N 128.263 0.070 1 76 23 23 VAL H H 7.608 0.010 1 77 23 23 VAL CA C 55.886 0.250 1 78 23 23 VAL CB C 33.187 0.250 1 79 23 23 VAL N N 112.747 0.070 1 80 24 24 PRO CA C 61.509 0.250 1 81 24 24 PRO CB C 31.412 0.250 1 82 25 25 GLU H H 8.068 0.010 1 83 25 25 GLU CA C 58.162 0.250 1 84 25 25 GLU CB C 28.955 0.250 1 85 25 25 GLU N N 119.212 0.070 1 86 26 26 ARG H H 7.407 0.010 1 87 26 26 ARG CA C 57.385 0.250 1 88 26 26 ARG CB C 29.706 0.250 1 89 26 26 ARG N N 117.646 0.070 1 90 27 27 TYR H H 7.742 0.010 1 91 27 27 TYR CA C 56.930 0.250 1 92 27 27 TYR CB C 37.008 0.250 1 93 27 27 TYR N N 118.387 0.070 1 94 28 28 GLN H H 9.138 0.010 1 95 28 28 GLN CA C 53.262 0.250 1 96 28 28 GLN CB C 32.504 0.250 1 97 28 28 GLN N N 122.815 0.070 1 98 29 29 ASN H H 8.775 0.010 1 99 29 29 ASN CA C 53.209 0.250 1 100 29 29 ASN CB C 36.258 0.250 1 101 29 29 ASN N N 117.790 0.070 1 102 30 30 LEU H H 8.484 0.010 1 103 30 30 LEU CA C 56.582 0.250 1 104 30 30 LEU CB C 40.557 0.250 1 105 30 30 LEU N N 120.480 0.070 1 106 31 31 SER H H 8.709 0.010 1 107 31 31 SER CA C 54.226 0.250 1 108 31 31 SER CB C 64.171 0.250 1 109 31 31 SER N N 116.358 0.070 1 110 32 32 PRO CA C 64.106 0.250 1 111 32 32 PRO CB C 31.412 0.250 1 112 33 33 VAL H H 8.564 0.010 1 113 33 33 VAL CA C 61.669 0.250 1 114 33 33 VAL CB C 33.114 0.250 1 115 33 33 VAL N N 121.177 0.070 1 116 34 34 GLY H H 7.766 0.010 1 117 34 34 GLY CA C 45.176 0.250 1 118 34 34 GLY N N 108.805 0.070 1 119 35 35 SER H H 8.347 0.010 1 120 35 35 SER CA C 57.600 0.250 1 121 35 35 SER CB C 64.376 0.250 1 122 35 35 SER N N 115.586 0.070 1 123 36 36 GLY H H 8.121 0.010 1 124 36 36 GLY CA C 44.406 0.250 1 125 36 36 GLY N N 110.707 0.070 1 126 37 37 ALA H H 8.431 0.010 1 127 37 37 ALA CA C 53.557 0.250 1 128 37 37 ALA CB C 17.558 0.250 1 129 37 37 ALA N N 124.397 0.070 1 130 38 38 TYR H H 7.999 0.010 1 131 38 38 TYR CA C 56.770 0.250 1 132 38 38 TYR CB C 37.213 0.250 1 133 38 38 TYR N N 114.004 0.070 1 134 39 39 GLY H H 7.298 0.010 1 135 39 39 GLY CA C 45.149 0.250 1 136 39 39 GLY N N 108.673 0.070 1 137 40 40 SER H H 8.096 0.010 1 138 40 40 SER CA C 57.573 0.250 1 139 40 40 SER CB C 64.739 0.250 1 140 40 40 SER N N 116.281 0.070 1 141 41 41 VAL H H 8.609 0.010 1 142 41 41 VAL CA C 60.973 0.250 1 143 41 41 VAL CB C 34.210 0.250 1 144 41 41 VAL N N 122.728 0.070 1 145 42 42 CYS H H 9.208 0.010 1 146 42 42 CYS CA C 57.573 0.250 1 147 42 42 CYS CB C 30.593 0.250 1 148 42 42 CYS N N 125.560 0.070 1 149 43 43 ALA H H 8.758 0.010 1 150 43 43 ALA CA C 50.263 0.250 1 151 43 43 ALA CB C 19.810 0.250 1 152 43 43 ALA N N 125.873 0.070 1 153 44 44 ALA H H 8.985 0.010 1 154 44 44 ALA CA C 50.263 0.250 1 155 44 44 ALA CB C 22.327 0.250 1 156 44 44 ALA N N 120.878 0.070 1 157 45 45 PHE H H 9.166 0.010 1 158 45 45 PHE CA C 56.743 0.250 1 159 45 45 PHE CB C 40.353 0.250 1 160 45 45 PHE N N 122.529 0.070 1 161 46 46 ASP H H 8.278 0.010 1 162 46 46 ASP CA C 51.549 0.250 1 163 46 46 ASP CB C 40.694 0.250 1 164 46 46 ASP N N 126.243 0.070 1 165 47 47 THR H H 8.883 0.010 1 166 47 47 THR CA C 63.383 0.250 1 167 47 47 THR CB C 68.676 0.250 1 168 47 47 THR N N 117.609 0.070 1 169 48 48 LYS H H 7.852 0.010 1 170 48 48 LYS CA C 58.215 0.250 1 171 48 48 LYS CB C 31.685 0.250 1 172 48 48 LYS N N 121.988 0.070 1 173 49 49 THR H H 6.545 0.010 1 174 49 49 THR CA C 61.348 0.250 1 175 49 49 THR CB C 70.450 0.250 1 176 49 49 THR N N 105.262 0.070 1 177 50 50 GLY H H 8.321 0.010 1 178 50 50 GLY CA C 45.566 0.250 1 179 50 50 GLY N N 112.515 0.070 1 180 51 51 LEU H H 7.063 0.010 1 181 51 51 LEU CA C 53.289 0.250 1 182 51 51 LEU CB C 43.083 0.250 1 183 51 51 LEU N N 119.897 0.070 1 184 52 52 ARG H H 8.172 0.010 1 185 52 52 ARG CA C 55.565 0.250 1 186 52 52 ARG CB C 29.501 0.250 1 187 52 52 ARG N N 119.982 0.070 1 188 53 53 VAL H H 8.765 0.010 1 189 53 53 VAL CA C 59.019 0.250 1 190 53 53 VAL CB C 34.347 0.250 1 191 53 53 VAL N N 116.742 0.070 1 192 54 54 ALA H H 8.764 0.010 1 193 54 54 ALA CA C 49.674 0.250 1 194 54 54 ALA CB C 19.537 0.250 1 195 54 54 ALA N N 122.915 0.070 1 196 55 55 VAL H H 9.200 0.010 1 197 55 55 VAL CA C 60.224 0.250 1 198 55 55 VAL CB C 31.753 0.250 1 199 55 55 VAL N N 122.763 0.070 1 200 56 56 LYS H H 9.521 0.010 1 201 56 56 LYS CA C 53.717 0.250 1 202 56 56 LYS CB C 34.142 0.250 1 203 56 56 LYS N N 129.428 0.070 1 204 57 57 LYS H H 8.561 0.010 1 205 57 57 LYS CA C 53.985 0.250 1 206 57 57 LYS CB C 32.914 0.250 1 207 57 57 LYS N N 128.633 0.070 1 208 58 58 LEU H H 7.961 0.010 1 209 58 58 LEU CA C 54.869 0.250 1 210 58 58 LEU CB C 39.192 0.250 1 211 58 58 LEU N N 128.760 0.070 1 212 59 59 SER H H 7.980 0.010 1 213 59 59 SER CA C 56.779 0.250 1 214 59 59 SER CB C 62.602 0.250 1 215 59 59 SER N N 118.104 0.070 1 216 60 60 ARG H H 8.689 0.010 1 217 60 60 ARG CA C 55.672 0.250 1 218 60 60 ARG CB C 28.614 0.250 1 219 60 60 ARG N N 123.240 0.070 1 220 61 61 PRO CA C 63.811 0.250 1 221 61 61 PRO CB C 30.866 0.250 1 222 62 62 PHE H H 7.852 0.010 1 223 62 62 PHE CA C 54.146 0.250 1 224 62 62 PHE CB C 37.281 0.250 1 225 62 62 PHE N N 112.453 0.070 1 226 63 63 GLN H H 7.032 0.010 1 227 63 63 GLN CA C 57.184 0.250 1 228 63 63 GLN CB C 28.682 0.250 1 229 63 63 GLN N N 115.844 0.070 1 230 64 64 SER H H 7.382 0.010 1 231 64 64 SER CA C 56.154 0.250 1 232 64 64 SER CB C 65.946 0.250 1 233 64 64 SER N N 110.593 0.070 1 234 65 65 ILE H H 9.131 0.010 1 235 65 65 ILE CA C 65.257 0.250 1 236 65 65 ILE CB C 36.872 0.250 1 237 65 65 ILE N N 123.454 0.070 1 238 66 66 ILE H H 7.559 0.010 1 239 66 66 ILE CA C 63.811 0.250 1 240 66 66 ILE CB C 36.736 0.250 1 241 66 66 ILE N N 119.012 0.070 1 242 67 67 HIS CA C 60.491 0.250 1 243 67 67 HIS CB C 29.453 0.250 1 244 68 68 ALA H H 8.558 0.010 1 245 68 68 ALA CA C 54.761 0.250 1 246 68 68 ALA CB C 18.513 0.250 1 247 68 68 ALA N N 123.952 0.070 1 248 69 69 LYS H H 7.801 0.010 1 249 69 69 LYS CA C 59.153 0.250 1 250 69 69 LYS CB C 31.412 0.250 1 251 69 69 LYS N N 118.448 0.070 1 252 70 70 ARG H H 7.432 0.010 1 253 70 70 ARG CA C 58.809 0.250 1 254 70 70 ARG CB C 28.630 0.250 1 255 70 70 ARG N N 119.357 0.070 1 256 71 71 THR H H 8.346 0.010 1 257 71 71 THR CA C 66.246 0.250 1 258 71 71 THR CB C 67.480 0.250 1 259 71 71 THR N N 119.966 0.070 1 260 72 72 TYR H H 7.554 0.010 1 261 72 72 TYR CA C 62.205 0.250 1 262 72 72 TYR CB C 37.469 0.250 1 263 72 72 TYR N N 121.675 0.070 1 264 81 81 MET CA C 55.190 0.250 1 265 81 81 MET CB C 33.187 0.250 1 266 82 82 LYS H H 8.448 0.010 1 267 82 82 LYS CA C 54.119 0.250 1 268 82 82 LYS CB C 31.753 0.250 1 269 82 82 LYS N N 128.850 0.070 1 270 83 83 HIS H H 8.657 0.010 1 271 83 83 HIS CA C 56.957 0.250 1 272 83 83 HIS CB C 32.641 0.250 1 273 83 83 HIS N N 124.208 0.070 1 274 84 84 GLU H H 8.009 0.010 1 275 84 84 GLU CA C 59.179 0.250 1 276 84 84 GLU CB C 29.365 0.250 1 277 84 84 GLU N N 125.802 0.070 1 278 85 85 ASN H H 11.288 0.010 1 279 85 85 ASN CA C 53.236 0.250 1 280 85 85 ASN CB C 40.507 0.250 1 281 85 85 ASN N N 118.168 0.070 1 282 86 86 VAL H H 7.644 0.010 1 283 86 86 VAL CA C 61.134 0.250 1 284 86 86 VAL CB C 35.071 0.250 1 285 86 86 VAL N N 119.943 0.070 1 286 87 87 ILE H H 8.311 0.010 1 287 87 87 ILE CA C 61.134 0.250 1 288 87 87 ILE CB C 37.880 0.250 1 289 87 87 ILE N N 129.638 0.070 1 290 88 88 GLY H H 7.590 0.010 1 291 88 88 GLY CA C 43.088 0.250 1 292 88 88 GLY N N 109.828 0.070 1 293 89 89 LEU H H 8.183 0.010 1 294 89 89 LEU CA C 54.226 0.250 1 295 89 89 LEU CB C 42.265 0.250 1 296 89 89 LEU N N 121.321 0.070 1 297 90 90 LEU H H 8.925 0.010 1 298 90 90 LEU CA C 55.431 0.250 1 299 90 90 LEU CB C 42.167 0.250 1 300 90 90 LEU N N 126.816 0.070 1 301 91 91 ASP CA C 52.619 0.250 1 302 91 91 ASP CB C 41.717 0.250 1 303 92 92 VAL H H 7.797 0.010 1 304 92 92 VAL CA C 59.153 0.250 1 305 92 92 VAL CB C 32.504 0.250 1 306 92 92 VAL N N 120.603 0.070 1 307 93 93 PHE H H 8.203 0.010 1 308 93 93 PHE CA C 55.565 0.250 1 309 93 93 PHE CB C 40.964 0.250 1 310 93 93 PHE N N 119.140 0.070 1 311 94 94 THR H H 8.891 0.010 1 312 94 94 THR CA C 56.957 0.250 1 313 94 94 THR CB C 71.679 0.250 1 314 94 94 THR N N 113.768 0.070 1 315 95 95 PRO CA C 62.151 0.250 1 316 95 95 PRO CB C 30.320 0.250 1 317 96 96 ALA H H 7.658 0.010 1 318 96 96 ALA CA C 52.405 0.250 1 319 96 96 ALA CB C 19.878 0.250 1 320 96 96 ALA N N 122.543 0.070 1 321 97 97 ARG H H 9.219 0.010 1 322 97 97 ARG CA C 55.591 0.250 1 323 97 97 ARG CB C 29.706 0.250 1 324 97 97 ARG N N 121.436 0.070 1 325 98 98 SER H H 7.335 0.010 1 326 98 98 SER CA C 56.207 0.250 1 327 98 98 SER CB C 65.127 0.250 1 328 98 98 SER N N 111.570 0.070 1 329 99 99 LEU H H 8.411 0.010 1 330 99 99 LEU CA C 56.582 0.250 1 331 99 99 LEU CB C 40.278 0.250 1 332 99 99 LEU N N 122.712 0.070 1 333 100 100 GLU H H 8.256 0.010 1 334 100 100 GLU CA C 58.992 0.250 1 335 100 100 GLU CB C 28.068 0.250 1 336 100 100 GLU N N 117.561 0.070 1 337 101 101 GLU H H 6.979 0.010 1 338 101 101 GLU CA C 54.467 0.250 1 339 101 101 GLU CB C 30.115 0.250 1 340 101 101 GLU N N 115.634 0.070 1 341 102 102 PHE H H 7.248 0.010 1 342 102 102 PHE CA C 56.540 0.250 1 343 102 102 PHE CB C 37.964 0.250 1 344 102 102 PHE N N 122.415 0.070 1 345 103 103 ASN H H 8.490 0.010 1 346 103 103 ASN CA C 53.776 0.250 1 347 103 103 ASN CB C 41.581 0.250 1 348 103 103 ASN N N 125.658 0.070 1 349 104 104 ASP H H 7.575 0.010 1 350 104 104 ASP CA C 52.860 0.250 1 351 104 104 ASP CB C 43.833 0.250 1 352 104 104 ASP N N 116.118 0.070 1 353 105 105 VAL H H 8.412 0.010 1 354 105 105 VAL CA C 61.214 0.250 1 355 105 105 VAL CB C 34.620 0.250 1 356 105 105 VAL N N 121.405 0.070 1 357 106 106 TYR H H 8.047 0.010 1 358 106 106 TYR CA C 54.595 0.250 1 359 106 106 TYR CB C 39.182 0.250 1 360 106 106 TYR N N 124.881 0.070 1 361 107 107 LEU H H 8.790 0.010 1 362 107 107 LEU CA C 53.101 0.250 1 363 107 107 LEU CB C 43.560 0.250 1 364 107 107 LEU N N 119.729 0.070 1 365 108 108 VAL CA C 60.518 0.250 1 366 108 108 VAL CB C 31.753 0.250 1 367 109 109 THR H H 8.970 0.010 1 368 109 109 THR CA C 59.153 0.250 1 369 109 109 THR CB C 72.839 0.250 1 370 109 109 THR N N 118.292 0.070 1 371 110 110 HIS H H 8.849 0.010 1 372 110 110 HIS CA C 58.537 0.250 1 373 110 110 HIS CB C 31.029 0.250 1 374 110 110 HIS N N 119.612 0.070 1 375 111 111 LEU H H 8.153 0.010 1 376 111 111 LEU CA C 54.119 0.250 1 377 111 111 LEU CB C 41.376 0.250 1 378 111 111 LEU N N 125.617 0.070 1 379 112 112 MET H H 8.633 0.010 1 380 112 112 MET CA C 54.949 0.250 1 381 112 112 MET CB C 31.440 0.250 1 382 112 112 MET N N 126.200 0.070 1 383 113 113 GLY H H 8.075 0.010 1 384 113 113 GLY CA C 45.417 0.250 1 385 113 113 GLY N N 108.863 0.070 1 386 114 114 ALA H H 7.825 0.010 1 387 114 114 ALA CA C 51.013 0.250 1 388 114 114 ALA CB C 20.203 0.250 1 389 114 114 ALA N N 124.052 0.070 1 390 115 115 ASP H H 7.932 0.010 1 391 115 115 ASP CA C 52.030 0.250 1 392 115 115 ASP CB C 41.854 0.250 1 393 115 115 ASP N N 118.747 0.070 1 394 116 116 LEU H H 7.769 0.010 1 395 116 116 LEU CA C 56.850 0.250 1 396 116 116 LEU CB C 41.240 0.250 1 397 116 116 LEU N N 117.746 0.070 1 398 117 117 ASN H H 7.634 0.010 1 399 117 117 ASN CA C 55.565 0.250 1 400 117 117 ASN CB C 37.554 0.250 1 401 117 117 ASN N N 115.928 0.070 1 402 118 118 ASN H H 7.927 0.010 1 403 118 118 ASN CA C 55.966 0.250 1 404 118 118 ASN CB C 39.056 0.250 1 405 118 118 ASN N N 118.374 0.070 1 406 119 119 ILE H H 7.449 0.010 1 407 119 119 ILE CA C 62.847 0.250 1 408 119 119 ILE CB C 36.190 0.250 1 409 119 119 ILE N N 118.978 0.070 1 410 120 120 VAL H H 7.482 0.010 1 411 120 120 VAL CA C 64.106 0.250 1 412 120 120 VAL CB C 30.661 0.250 1 413 120 120 VAL N N 116.779 0.070 1 414 121 121 LYS H H 7.343 0.010 1 415 121 121 LYS CA C 57.359 0.250 1 416 121 121 LYS CB C 31.753 0.250 1 417 121 121 LYS N N 117.668 0.070 1 418 122 122 CYS H H 7.612 0.010 1 419 122 122 CYS CA C 59.340 0.250 1 420 122 122 CYS CB C 28.614 0.250 1 421 122 122 CYS N N 114.705 0.070 1 422 123 123 GLN H H 7.948 0.010 1 423 123 123 GLN CA C 54.547 0.250 1 424 123 123 GLN CB C 30.115 0.250 1 425 123 123 GLN N N 119.718 0.070 1 426 124 124 LYS H H 8.169 0.010 1 427 124 124 LYS CA C 54.815 0.250 1 428 124 124 LYS CB C 30.934 0.250 1 429 124 124 LYS N N 122.116 0.070 1 430 125 125 LEU H H 8.508 0.010 1 431 125 125 LEU CA C 54.039 0.250 1 432 125 125 LEU CB C 41.649 0.250 1 433 125 125 LEU N N 127.011 0.070 1 434 126 126 THR CA C 60.170 0.250 1 435 126 126 THR CB C 70.928 0.250 1 436 127 127 ASP H H 8.910 0.010 1 437 127 127 ASP CA C 58.055 0.250 1 438 127 127 ASP CB C 42.127 0.250 1 439 127 127 ASP N N 121.220 0.070 1 440 128 128 ASP H H 7.987 0.010 1 441 128 128 ASP CA C 56.957 0.250 1 442 128 128 ASP CB C 39.807 0.250 1 443 128 128 ASP N N 115.626 0.070 1 444 129 129 HIS H H 7.477 0.010 1 445 129 129 HIS CA C 59.527 0.250 1 446 129 129 HIS CB C 31.207 0.250 1 447 129 129 HIS N N 119.357 0.070 1 448 130 130 VAL H H 8.115 0.010 1 449 130 130 VAL CA C 68.023 0.250 1 450 130 130 VAL CB C 29.842 0.250 1 451 130 130 VAL N N 120.595 0.070 1 452 131 131 GLN H H 8.365 0.010 1 453 131 131 GLN CA C 58.965 0.250 1 454 131 131 GLN CB C 29.365 0.250 1 455 131 131 GLN N N 118.481 0.070 1 456 132 132 PHE H H 7.398 0.010 1 457 132 132 PHE CA C 58.135 0.250 1 458 132 132 PHE CB C 38.988 0.250 1 459 132 132 PHE N N 116.511 0.070 1 460 133 133 LEU H H 8.705 0.010 1 461 133 133 LEU CA C 58.165 0.250 1 462 133 133 LEU CB C 41.581 0.250 1 463 133 133 LEU N N 120.915 0.070 1 464 134 134 ILE CA C 55.645 0.250 1 465 135 135 TYR H H 8.862 0.010 1 466 135 135 TYR CA C 51.388 0.250 1 467 135 135 TYR CB C 39.124 0.250 1 468 135 135 TYR N N 120.118 0.070 1 469 136 136 GLN H H 8.519 0.010 1 470 136 136 GLN CA C 51.388 0.250 1 471 136 136 GLN CB C 25.890 0.250 1 472 136 136 GLN N N 116.659 0.070 1 473 139 139 ARG CA C 59.956 0.250 1 474 140 140 GLY H H 8.089 0.010 1 475 140 140 GLY CA C 46.595 0.250 1 476 140 140 GLY N N 107.443 0.070 1 477 141 141 LEU H H 8.633 0.010 1 478 141 141 LEU CA C 56.368 0.250 1 479 141 141 LEU CB C 40.347 0.250 1 480 141 141 LEU N N 121.832 0.070 1 481 142 142 LYS H H 8.625 0.010 1 482 142 142 LYS CA C 59.447 0.250 1 483 142 142 LYS CB C 31.412 0.250 1 484 142 142 LYS N N 119.584 0.070 1 485 143 143 TYR H H 6.781 0.010 1 486 143 143 TYR CA C 61.428 0.250 1 487 143 143 TYR CB C 37.350 0.250 1 488 143 143 TYR N N 118.435 0.070 1 489 144 144 ILE H H 8.398 0.010 1 490 144 144 ILE CA C 66.315 0.250 1 491 144 144 ILE CB C 37.469 0.250 1 492 144 144 ILE N N 120.323 0.070 1 493 145 145 HIS H H 9.463 0.010 1 494 145 145 HIS CA C 56.850 0.250 1 495 145 145 HIS CB C 30.184 0.250 1 496 145 145 HIS N N 119.879 0.070 1 497 146 146 SER H H 7.824 0.010 1 498 146 146 SER CA C 60.920 0.250 1 499 146 146 SER CB C 61.861 0.250 1 500 146 146 SER N N 116.726 0.070 1 501 147 147 ALA H H 7.364 0.010 1 502 147 147 ALA CA C 51.013 0.250 1 503 147 147 ALA CB C 17.257 0.250 1 504 147 147 ALA N N 126.542 0.070 1 505 148 148 ASP H H 8.147 0.010 1 506 148 148 ASP CA C 55.190 0.250 1 507 148 148 ASP CB C 38.510 0.250 1 508 148 148 ASP N N 115.457 0.070 1 509 149 149 ILE H H 7.192 0.010 1 510 149 149 ILE CA C 58.965 0.250 1 511 149 149 ILE CB C 38.419 0.250 1 512 149 149 ILE N N 119.258 0.070 1 513 150 150 ILE H H 7.792 0.010 1 514 150 150 ILE CA C 59.688 0.250 1 515 150 150 ILE CB C 39.730 0.250 1 516 150 150 ILE N N 123.300 0.070 1 517 151 151 HIS H H 7.360 0.010 1 518 151 151 HIS CA C 62.473 0.250 1 519 151 151 HIS CB C 35.423 0.250 1 520 151 151 HIS N N 121.123 0.070 1 521 157 157 SER H H 7.484 0.010 1 522 157 157 SER CA C 59.313 0.250 1 523 157 157 SER CB C 62.125 0.250 1 524 157 157 SER N N 106.345 0.070 1 525 158 158 ASN H H 7.742 0.010 1 526 158 158 ASN CA C 52.352 0.250 1 527 158 158 ASN CB C 37.829 0.250 1 528 158 158 ASN N N 119.241 0.070 1 529 159 159 LEU H H 7.010 0.010 1 530 159 159 LEU CA C 52.566 0.250 1 531 159 159 LEU CB C 42.059 0.250 1 532 159 159 LEU N N 119.484 0.070 1 533 160 160 ALA H H 8.497 0.010 1 534 160 160 ALA CA C 50.290 0.250 1 535 160 160 ALA CB C 20.834 0.250 1 536 160 160 ALA N N 125.759 0.070 1 537 161 161 VAL H H 8.123 0.010 1 538 161 161 VAL CA C 59.045 0.250 1 539 161 161 VAL CB C 34.961 0.250 1 540 161 161 VAL N N 118.135 0.070 1 541 162 162 ASN H H 7.844 0.010 1 542 162 162 ASN CA C 50.129 0.250 1 543 162 162 ASN CB C 39.261 0.250 1 544 162 162 ASN N N 122.501 0.070 1 545 163 163 GLU H H 8.798 0.010 1 546 163 163 GLU CA C 58.762 0.250 1 547 163 163 GLU CB C 28.136 0.250 1 548 163 163 GLU N N 117.831 0.070 1 549 164 164 ASP H H 7.470 0.010 1 550 164 164 ASP CA C 53.985 0.250 1 551 164 164 ASP CB C 40.557 0.250 1 552 164 164 ASP N N 118.914 0.070 1 553 165 165 CYS H H 8.248 0.010 1 554 165 165 CYS CA C 62.125 0.250 1 555 165 165 CYS CB C 24.382 0.250 1 556 165 165 CYS N N 111.527 0.070 1 557 166 166 GLU H H 7.622 0.010 1 558 166 166 GLU CA C 55.806 0.250 1 559 166 166 GLU CB C 28.273 0.250 1 560 166 166 GLU N N 117.983 0.070 1 561 167 167 LEU H H 7.924 0.010 1 562 167 167 LEU CA C 53.289 0.250 1 563 167 167 LEU CB C 45.335 0.250 1 564 167 167 LEU N N 125.603 0.070 1 565 168 168 LYS H H 8.931 0.010 1 566 168 168 LYS CB C 37.213 0.250 1 567 168 168 LYS N N 122.956 0.070 1 568 169 169 ILE H H 8.167 0.010 1 569 169 169 ILE CA C 62.124 0.250 1 570 169 169 ILE CB C 38.908 0.250 1 571 169 169 ILE N N 122.261 0.070 1 572 170 170 LEU H H 8.403 0.010 1 573 170 170 LEU CA C 54.146 0.250 1 574 170 170 LEU CB C 43.156 0.250 1 575 170 170 LEU N N 125.543 0.070 1 576 174 174 LEU CA C 54.440 0.250 1 577 174 174 LEU CB C 40.484 0.250 1 578 175 175 ALA H H 8.028 0.010 1 579 175 175 ALA CA C 59.665 0.250 1 580 175 175 ALA CB C 18.010 0.250 1 581 175 175 ALA N N 119.416 0.070 1 582 176 176 ARG H H 8.348 0.010 1 583 176 176 ARG CA C 55.270 0.250 1 584 176 176 ARG CB C 37.264 0.250 1 585 176 176 ARG N N 117.319 0.070 1 586 177 177 HIS CA C 59.340 0.250 1 587 177 177 HIS CB C 27.277 0.250 1 588 178 178 THR H H 7.248 0.010 1 589 178 178 THR CA C 55.940 0.250 1 590 178 178 THR CB C 62.942 0.250 1 591 178 178 THR N N 115.565 0.070 1 592 179 179 ASP CA C 54.654 0.250 1 593 179 179 ASP CB C 40.284 0.250 1 594 180 180 ASP H H 8.043 0.010 1 595 180 180 ASP CA C 54.547 0.250 1 596 180 180 ASP CB C 40.454 0.250 1 597 180 180 ASP N N 120.257 0.070 1 598 181 181 GLU H H 8.083 0.010 1 599 181 181 GLU CA C 56.745 0.250 1 600 181 181 GLU CB C 29.160 0.250 1 601 181 181 GLU N N 120.550 0.070 1 602 182 182 MET H H 8.108 0.010 1 603 182 182 MET CA C 55.511 0.250 1 604 182 182 MET CB C 31.549 0.250 1 605 182 182 MET N N 120.172 0.070 1 606 183 183 THR H H 7.878 0.010 1 607 183 183 THR CA C 62.151 0.250 1 608 183 183 THR CB C 69.017 0.250 1 609 183 183 THR N N 114.220 0.070 1 610 184 184 GLY H H 8.208 0.010 1 611 184 184 GLY CA C 44.908 0.250 1 612 184 184 GLY N N 111.449 0.070 1 613 185 185 TYR H H 7.809 0.010 1 614 185 185 TYR CA C 57.733 0.250 1 615 185 185 TYR CB C 37.812 0.250 1 616 185 185 TYR N N 121.106 0.070 1 617 186 186 VAL H H 7.726 0.010 1 618 186 186 VAL CA C 61.937 0.250 1 619 186 186 VAL CB C 31.420 0.250 1 620 186 186 VAL N N 123.303 0.070 1 621 191 191 TYR CA C 56.743 0.250 1 622 191 191 TYR CB C 37.896 0.250 1 623 192 192 ARG H H 7.292 0.010 1 624 192 192 ARG CA C 55.431 0.250 1 625 192 192 ARG CB C 30.798 0.250 1 626 192 192 ARG N N 122.671 0.070 1 627 193 193 ALA H H 8.794 0.010 1 628 193 193 ALA CA C 49.674 0.250 1 629 193 193 ALA CB C 16.777 0.250 1 630 193 193 ALA N N 126.460 0.070 1 631 197 197 MET CA C 59.286 0.250 1 632 197 197 MET CB C 33.733 0.250 1 633 198 198 LEU H H 9.162 0.010 1 634 198 198 LEU CA C 57.707 0.250 1 635 198 198 LEU CB C 41.240 0.250 1 636 198 198 LEU N N 126.842 0.070 1 637 199 199 ASN H H 7.819 0.010 1 638 199 199 ASN CA C 53.342 0.250 1 639 199 199 ASN CB C 40.284 0.250 1 640 199 199 ASN N N 115.457 0.070 1 641 200 200 TRP H H 8.500 0.010 1 642 200 200 TRP CA C 54.226 0.250 1 643 200 200 TRP CB C 27.727 0.250 1 644 200 200 TRP N N 125.361 0.070 1 645 201 201 MET H H 8.619 0.010 1 646 201 201 MET CA C 61.803 0.250 1 647 201 201 MET CB C 36.990 0.250 1 648 201 201 MET N N 120.188 0.070 1 649 202 202 HIS H H 7.172 0.010 1 650 202 202 HIS CA C 59.260 0.250 1 651 202 202 HIS CB C 32.380 0.250 1 652 202 202 HIS N N 115.369 0.070 1 653 203 203 TYR H H 10.038 0.010 1 654 203 203 TYR CA C 52.539 0.250 1 655 203 203 TYR CB C 41.376 0.250 1 656 203 203 TYR N N 127.109 0.070 1 657 204 204 ASN H H 8.718 0.010 1 658 204 204 ASN CA C 56.100 0.250 1 659 204 204 ASN CB C 41.376 0.250 1 660 204 204 ASN N N 125.076 0.070 1 661 205 205 GLN H H 7.150 0.010 1 662 205 205 GLN CA C 57.252 0.250 1 663 205 205 GLN CB C 28.151 0.250 1 664 205 205 GLN N N 118.612 0.070 1 665 206 206 THR H H 8.296 0.010 1 666 206 206 THR CA C 58.965 0.250 1 667 206 206 THR CB C 64.328 0.250 1 668 206 206 THR N N 115.664 0.070 1 669 208 208 ASP CA C 56.448 0.250 1 670 209 209 ILE H H 7.227 0.010 1 671 209 209 ILE CA C 60.679 0.250 1 672 209 209 ILE CB C 34.210 0.250 1 673 209 209 ILE N N 119.502 0.070 1 674 210 210 TRP H H 7.476 0.010 1 675 210 210 TRP CA C 61.054 0.250 1 676 210 210 TRP CB C 27.931 0.250 1 677 210 210 TRP N N 121.120 0.070 1 678 211 211 SER H H 7.554 0.010 1 679 211 211 SER CA C 61.995 0.250 1 680 211 211 SER CB C 62.752 0.250 1 681 211 211 SER N N 112.846 0.070 1 682 212 212 VAL H H 7.952 0.010 1 683 212 212 VAL CA C 67.206 0.250 1 684 212 212 VAL CB C 29.453 0.250 1 685 212 212 VAL N N 120.112 0.070 1 686 213 213 GLY H H 8.473 0.010 1 687 213 213 GLY CA C 47.666 0.250 1 688 213 213 GLY N N 110.547 0.070 1 689 214 214 CYS H H 7.846 0.010 1 690 214 214 CYS CA C 63.624 0.250 1 691 214 214 CYS CB C 27.329 0.250 1 692 214 214 CYS N N 119.526 0.070 1 693 215 215 ILE H H 8.390 0.010 1 694 215 215 ILE CA C 65.471 0.250 1 695 215 215 ILE CB C 37.691 0.250 1 696 215 215 ILE N N 124.407 0.070 1 697 216 216 MET H H 9.256 0.010 1 698 216 216 MET CA C 60.036 0.250 1 699 216 216 MET CB C 30.934 0.250 1 700 216 216 MET N N 120.794 0.070 1 701 217 217 ALA H H 8.104 0.010 1 702 217 217 ALA CA C 55.136 0.250 1 703 217 217 ALA CB C 19.537 0.250 1 704 217 217 ALA N N 118.722 0.070 1 705 218 218 GLU H H 7.090 0.010 1 706 218 218 GLU CA C 57.760 0.250 1 707 218 218 GLU CB C 29.160 0.250 1 708 218 218 GLU N N 120.110 0.070 1 709 219 219 LEU H H 7.245 0.010 1 710 219 219 LEU CA C 56.850 0.250 1 711 219 219 LEU CB C 42.127 0.250 1 712 219 219 LEU N N 116.669 0.070 1 713 220 220 LEU H H 8.456 0.010 1 714 220 220 LEU CA C 56.770 0.250 1 715 220 220 LEU CB C 39.875 0.250 1 716 220 220 LEU N N 118.670 0.070 1 717 221 221 THR H H 7.913 0.010 1 718 221 221 THR CA C 61.803 0.250 1 719 221 221 THR CB C 71.201 0.250 1 720 221 221 THR N N 106.254 0.070 1 721 222 222 GLY H H 8.377 0.010 1 722 222 222 GLY CA C 45.203 0.250 1 723 222 222 GLY N N 112.899 0.070 1 724 223 223 ARG H H 7.962 0.010 1 725 223 223 ARG CA C 53.610 0.250 1 726 223 223 ARG CB C 32.056 0.250 1 727 223 223 ARG N N 119.277 0.070 1 728 224 224 THR H H 7.889 0.010 1 729 224 224 THR CA C 63.142 0.250 1 730 224 224 THR CB C 68.471 0.250 1 731 224 224 THR N N 120.136 0.070 1 732 225 225 LEU H H 7.808 0.010 1 733 225 225 LEU CA C 52.673 0.250 1 734 225 225 LEU CB C 40.626 0.250 1 735 225 225 LEU N N 118.038 0.070 1 736 227 227 PRO CA C 60.625 0.250 1 737 227 227 PRO CB C 26.157 0.250 1 738 228 228 GLY H H 8.300 0.010 1 739 228 228 GLY CA C 45.116 0.250 1 740 228 228 GLY N N 113.787 0.070 1 741 229 229 THR H H 10.053 0.010 1 742 229 229 THR CA C 63.276 0.250 1 743 229 229 THR CB C 68.644 0.250 1 744 229 229 THR N N 116.820 0.070 1 745 230 230 ASP H H 8.590 0.010 1 746 230 230 ASP CA C 57.653 0.250 1 747 230 230 ASP CB C 39.730 0.250 1 748 230 230 ASP N N 130.939 0.070 1 749 231 231 HIS H H 8.516 0.010 1 750 231 231 HIS CA C 51.789 0.250 1 751 231 231 HIS CB C 39.807 0.250 1 752 231 231 HIS N N 114.572 0.070 1 753 239 239 LEU CA C 57.252 0.250 1 754 239 239 LEU CB C 41.308 0.250 1 755 240 240 ARG H H 8.174 0.010 1 756 240 240 ARG CA C 58.938 0.250 1 757 240 240 ARG CB C 31.958 0.250 1 758 240 240 ARG N N 117.568 0.070 1 759 241 241 LEU H H 7.556 0.010 1 760 241 241 LEU CA C 57.225 0.250 1 761 241 241 LEU CB C 40.278 0.250 1 762 241 241 LEU N N 117.984 0.070 1 763 242 242 VAL H H 8.532 0.010 1 764 242 242 VAL CA C 59.956 0.250 1 765 242 242 VAL CB C 40.284 0.250 1 766 242 242 VAL N N 122.708 0.070 1 767 243 243 GLY CA C 44.775 0.250 1 768 244 244 THR H H 7.756 0.010 1 769 244 244 THR CA C 59.554 0.250 1 770 244 244 THR CB C 64.122 0.250 1 771 244 244 THR N N 121.804 0.070 1 772 245 245 PRO CA C 62.339 0.250 1 773 245 245 PRO CB C 32.026 0.250 1 774 246 246 GLY H H 8.218 0.010 1 775 246 246 GLY CA C 43.347 0.250 1 776 246 246 GLY N N 108.873 0.070 1 777 247 247 ALA H H 8.313 0.010 1 778 247 247 ALA CA C 55.029 0.250 1 779 247 247 ALA CB C 18.010 0.250 1 780 247 247 ALA N N 121.547 0.070 1 781 248 248 GLU H H 8.521 0.010 1 782 248 248 GLU CA C 58.778 0.250 1 783 248 248 GLU CB C 27.931 0.250 1 784 248 248 GLU N N 116.456 0.070 1 785 249 249 LEU H H 7.410 0.010 1 786 249 249 LEU CA C 56.395 0.250 1 787 249 249 LEU CB C 40.353 0.250 1 788 249 249 LEU N N 120.565 0.070 1 789 250 250 LEU H H 7.826 0.010 1 790 250 250 LEU CA C 57.588 0.250 1 791 250 250 LEU CB C 41.308 0.250 1 792 250 250 LEU N N 118.242 0.070 1 793 251 251 LYS H H 7.572 0.010 1 794 251 251 LYS CA C 55.601 0.250 1 795 251 251 LYS CB C 36.326 0.250 1 796 251 251 LYS N N 120.278 0.070 1 797 252 252 LYS H H 7.408 0.010 1 798 252 252 LYS CA C 55.538 0.250 1 799 252 252 LYS CB C 38.840 0.250 1 800 252 252 LYS N N 120.693 0.070 1 801 256 256 GLU CA C 59.286 0.250 1 802 257 257 SER H H 8.312 0.010 1 803 257 257 SER CA C 60.526 0.250 1 804 257 257 SER CB C 61.450 0.250 1 805 257 257 SER N N 114.084 0.070 1 806 258 258 ALA H H 7.642 0.010 1 807 258 258 ALA CA C 54.387 0.250 1 808 258 258 ALA CB C 17.914 0.250 1 809 258 258 ALA N N 126.001 0.070 1 810 259 259 ARG H H 8.792 0.010 1 811 259 259 ARG CA C 55.163 0.250 1 812 259 259 ARG CB C 29.658 0.250 1 813 259 259 ARG N N 126.420 0.070 1 814 262 262 ILE CA C 63.329 0.250 1 815 263 263 GLN H H 7.966 0.010 1 816 263 263 GLN CA C 57.733 0.250 1 817 263 263 GLN CB C 28.204 0.250 1 818 263 263 GLN N N 118.349 0.070 1 819 264 264 SER H H 7.371 0.010 1 820 264 264 SER CA C 58.848 0.250 1 821 264 264 SER CB C 63.421 0.250 1 822 264 264 SER N N 113.958 0.070 1 823 265 265 LEU H H 6.815 0.010 1 824 265 265 LEU CA C 54.039 0.250 1 825 265 265 LEU CB C 41.376 0.250 1 826 265 265 LEU N N 123.112 0.070 1 827 266 266 THR H H 9.158 0.010 1 828 266 266 THR CA C 63.356 0.250 1 829 266 266 THR CB C 71.522 0.250 1 830 266 266 THR N N 122.017 0.070 1 831 267 267 GLN H H 8.436 0.010 1 832 267 267 GLN CA C 56.261 0.250 1 833 267 267 GLN CB C 27.658 0.250 1 834 267 267 GLN N N 127.025 0.070 1 835 268 268 MET H H 8.673 0.010 1 836 268 268 MET CA C 51.709 0.250 1 837 268 268 MET N N 124.057 0.070 1 838 269 269 PRO CA C 61.187 0.250 1 839 269 269 PRO CB C 31.207 0.250 1 840 270 270 LYS H H 8.209 0.010 1 841 270 270 LYS CA C 56.395 0.250 1 842 270 270 LYS CB C 32.026 0.250 1 843 270 270 LYS N N 120.637 0.070 1 844 271 271 MET H H 8.342 0.010 1 845 271 271 MET CA C 55.538 0.250 1 846 271 271 MET CB C 32.504 0.250 1 847 271 271 MET N N 126.456 0.070 1 848 272 272 ASN H H 8.518 0.010 1 849 272 272 ASN CA C 52.432 0.250 1 850 272 272 ASN CB C 37.418 0.250 1 851 272 272 ASN N N 120.679 0.070 1 852 273 273 PHE H H 9.355 0.010 1 853 273 273 PHE CA C 59.420 0.250 1 854 273 273 PHE CB C 36.667 0.250 1 855 273 273 PHE N N 130.170 0.070 1 856 274 274 ALA H H 8.505 0.010 1 857 274 274 ALA CA C 54.280 0.250 1 858 274 274 ALA CB C 17.012 0.250 1 859 274 274 ALA N N 122.572 0.070 1 860 275 275 ASN H H 7.417 0.010 1 861 275 275 ASN CA C 53.316 0.250 1 862 275 275 ASN CB C 38.017 0.250 1 863 275 275 ASN N N 113.227 0.070 1 864 276 276 VAL H H 7.157 0.010 1 865 276 276 VAL CA C 63.892 0.250 1 866 276 276 VAL CB C 32.163 0.250 1 867 276 276 VAL N N 120.181 0.070 1 868 277 277 PHE H H 7.570 0.010 1 869 277 277 PHE CA C 55.672 0.250 1 870 277 277 PHE CB C 36.190 0.250 1 871 277 277 PHE N N 120.992 0.070 1 872 278 278 ILE H H 6.842 0.010 1 873 278 278 ILE CA C 61.964 0.250 1 874 278 278 ILE CB C 36.463 0.250 1 875 278 278 ILE N N 121.106 0.070 1 876 279 279 GLY H H 8.944 0.010 1 877 279 279 GLY CA C 44.614 0.250 1 878 279 279 GLY N N 116.481 0.070 1 879 280 280 ALA H H 7.348 0.010 1 880 280 280 ALA CA C 50.780 0.250 1 881 280 280 ALA CB C 18.970 0.250 1 882 280 280 ALA N N 122.202 0.070 1 883 281 281 ASN H H 9.033 0.010 1 884 281 281 ASN CA C 50.959 0.250 1 885 281 281 ASN CB C 38.578 0.250 1 886 281 281 ASN N N 122.728 0.070 1 887 282 282 PRO CA C 64.775 0.250 1 888 283 283 LEU H H 8.378 0.010 1 889 283 283 LEU CA C 56.770 0.250 1 890 283 283 LEU CB C 41.718 0.250 1 891 283 283 LEU N N 117.304 0.070 1 892 284 284 ALA H H 7.067 0.010 1 893 284 284 ALA CA C 53.591 0.250 1 894 284 284 ALA CB C 17.148 0.250 1 895 284 284 ALA N N 121.254 0.070 1 896 285 285 VAL H H 7.040 0.010 1 897 285 285 VAL CA C 66.383 0.250 1 898 285 285 VAL CB C 30.388 0.250 1 899 285 285 VAL N N 116.679 0.070 1 900 286 286 ASP H H 7.441 0.010 1 901 286 286 ASP CA C 57.530 0.250 1 902 286 286 ASP CB C 42.676 0.250 1 903 286 286 ASP N N 118.168 0.070 1 904 287 287 LEU H H 7.060 0.010 1 905 287 287 LEU CA C 57.385 0.250 1 906 287 287 LEU CB C 38.988 0.250 1 907 287 287 LEU N N 117.793 0.070 1 908 288 288 LEU H H 8.083 0.010 1 909 288 288 LEU CA C 58.483 0.250 1 910 288 288 LEU CB C 40.537 0.250 1 911 288 288 LEU N N 120.497 0.070 1 912 289 289 GLU H H 7.929 0.010 1 913 289 289 GLU CA C 58.349 0.250 1 914 289 289 GLU CB C 28.356 0.250 1 915 289 289 GLU N N 117.728 0.070 1 916 290 290 LYS H H 7.290 0.010 1 917 290 290 LYS CA C 56.930 0.250 1 918 290 290 LYS CB C 31.958 0.250 1 919 290 290 LYS N N 116.504 0.070 1 920 291 291 MET H H 7.520 0.010 1 921 291 291 MET CA C 58.269 0.250 1 922 291 291 MET CB C 34.112 0.250 1 923 291 291 MET N N 118.499 0.070 1 924 292 292 LEU H H 7.795 0.010 1 925 292 292 LEU CA C 59.208 0.250 1 926 292 292 LEU CB C 38.154 0.250 1 927 292 292 LEU N N 119.026 0.070 1 928 296 296 SER CA C 60.946 0.250 1 929 296 296 SER CB C 62.192 0.250 1 930 297 297 ASP H H 8.414 0.010 1 931 297 297 ASP CA C 56.073 0.250 1 932 297 297 ASP CB C 40.216 0.250 1 933 297 297 ASP N N 121.163 0.070 1 934 298 298 LYS H H 7.584 0.010 1 935 298 298 LYS CA C 54.521 0.250 1 936 298 298 LYS CB C 32.845 0.250 1 937 298 298 LYS N N 117.606 0.070 1 938 299 299 ARG H H 7.013 0.010 1 939 299 299 ARG CA C 56.955 0.250 1 940 299 299 ARG CB C 29.638 0.250 1 941 299 299 ARG N N 122.742 0.070 1 942 300 300 ILE H H 7.047 0.010 1 943 300 300 ILE CA C 61.937 0.250 1 944 300 300 ILE CB C 38.988 0.250 1 945 300 300 ILE N N 125.275 0.070 1 946 301 301 THR H H 7.321 0.010 1 947 301 301 THR CA C 59.929 0.250 1 948 301 301 THR CB C 70.723 0.250 1 949 301 301 THR N N 109.543 0.070 1 950 302 302 ALA H H 9.459 0.010 1 951 302 302 ALA CA C 55.940 0.250 1 952 302 302 ALA CB C 15.920 0.250 1 953 302 302 ALA N N 122.372 0.070 1 954 303 303 ALA H H 8.582 0.010 1 955 303 303 ALA CA C 54.869 0.250 1 956 303 303 ALA CB C 17.558 0.250 1 957 303 303 ALA N N 116.407 0.070 1 958 304 304 GLN H H 7.371 0.010 1 959 304 304 GLN CA C 57.747 0.250 1 960 304 304 GLN CB C 27.863 0.250 1 961 304 304 GLN N N 116.005 0.070 1 962 305 305 ALA H H 8.647 0.010 1 963 305 305 ALA CA C 54.708 0.250 1 964 305 305 ALA CB C 18.513 0.250 1 965 305 305 ALA N N 124.028 0.070 1 966 306 306 LEU H H 7.606 0.010 1 967 306 306 LEU CA C 57.359 0.250 1 968 306 306 LEU CB C 41.035 0.250 1 969 306 306 LEU N N 116.445 0.070 1 970 307 307 ALA H H 6.617 0.010 1 971 307 307 ALA CA C 50.611 0.250 1 972 307 307 ALA CB C 18.079 0.250 1 973 307 307 ALA N N 115.594 0.070 1 974 308 308 HIS H H 7.919 0.010 1 975 308 308 HIS CA C 58.483 0.250 1 976 308 308 HIS CB C 32.163 0.250 1 977 308 308 HIS N N 122.927 0.070 1 978 309 309 ALA H H 8.292 0.010 1 979 309 309 ALA CA C 54.865 0.250 1 980 309 309 ALA CB C 18.151 0.250 1 981 309 309 ALA N N 132.975 0.070 1 982 310 310 TYR H H 11.592 0.010 1 983 310 310 TYR CA C 59.962 0.250 1 984 310 310 TYR CB C 38.075 0.250 1 985 310 310 TYR N N 125.286 0.070 1 986 311 311 PHE H H 7.617 0.010 1 987 311 311 PHE CA C 55.832 0.250 1 988 311 311 PHE CB C 38.100 0.250 1 989 311 311 PHE N N 110.659 0.070 1 990 312 312 ALA H H 7.487 0.010 1 991 312 312 ALA CA C 55.565 0.250 1 992 312 312 ALA CB C 18.104 0.250 1 993 312 312 ALA N N 123.854 0.070 1 994 313 313 GLN H H 8.606 0.010 1 995 313 313 GLN CA C 56.957 0.250 1 996 313 313 GLN CB C 27.522 0.250 1 997 313 313 GLN N N 114.214 0.070 1 998 314 314 TYR H H 7.395 0.010 1 999 314 314 TYR CA C 58.172 0.250 1 1000 314 314 TYR CB C 39.134 0.250 1 1001 314 314 TYR N N 116.170 0.070 1 1002 315 315 HIS H H 7.780 0.010 1 1003 315 315 HIS CA C 55.719 0.250 1 1004 315 315 HIS CB C 28.819 0.250 1 1005 315 315 HIS N N 115.759 0.070 1 1006 316 316 ASP H H 7.367 0.010 1 1007 316 316 ASP CA C 50.611 0.250 1 1008 316 316 ASP CB C 41.103 0.250 1 1009 316 316 ASP N N 125.289 0.070 1 1010 317 317 PRO CA C 63.702 0.250 1 1011 317 317 PRO CB C 31.029 0.250 1 1012 318 318 ASP H H 7.924 0.010 1 1013 318 318 ASP CA C 54.963 0.250 1 1014 318 318 ASP CB C 40.013 0.250 1 1015 318 318 ASP N N 117.625 0.070 1 1016 319 319 ASP H H 7.940 0.010 1 1017 319 319 ASP CA C 52.379 0.250 1 1018 319 319 ASP CB C 41.581 0.250 1 1019 319 319 ASP N N 121.362 0.070 1 1020 320 320 GLU H H 7.743 0.010 1 1021 320 320 GLU CA C 53.262 0.250 1 1022 320 320 GLU CB C 28.905 0.250 1 1023 320 320 GLU N N 121.547 0.070 1 1024 321 321 PRO CA C 63.169 0.250 1 1025 321 321 PRO CB C 32.777 0.250 1 1026 322 322 VAL H H 7.793 0.010 1 1027 322 322 VAL CA C 59.206 0.250 1 1028 322 322 VAL CB C 33.118 0.250 1 1029 322 322 VAL N N 109.357 0.070 1 1030 323 323 ALA H H 8.393 0.010 1 1031 323 323 ALA CA C 50.585 0.250 1 1032 323 323 ALA CB C 19.381 0.250 1 1033 323 323 ALA N N 123.753 0.070 1 1034 324 324 ASP H H 8.027 0.010 1 1035 324 324 ASP CA C 52.780 0.250 1 1036 324 324 ASP CB C 38.988 0.250 1 1037 324 324 ASP N N 121.100 0.070 1 1038 326 326 TYR CA C 59.153 0.250 1 1039 327 327 ASP H H 6.931 0.010 1 1040 327 327 ASP CA C 54.039 0.250 1 1041 327 327 ASP CB C 41.033 0.250 1 1042 327 327 ASP N N 123.144 0.070 1 1043 328 328 GLN H H 8.076 0.010 1 1044 328 328 GLN CA C 55.940 0.250 1 1045 328 328 GLN CB C 31.685 0.250 1 1046 328 328 GLN N N 121.360 0.070 1 1047 330 330 PHE CA C 63.945 0.250 1 1048 331 331 GLU H H 9.845 0.010 1 1049 331 331 GLU CA C 58.215 0.250 1 1050 331 331 GLU CB C 27.181 0.250 1 1051 331 331 GLU N N 115.089 0.070 1 1052 332 332 SER H H 7.405 0.010 1 1053 332 332 SER CA C 57.760 0.250 1 1054 332 332 SER CB C 62.958 0.250 1 1055 332 332 SER N N 112.114 0.070 1 1056 333 333 ARG H H 7.556 0.010 1 1057 333 333 ARG CA C 55.832 0.250 1 1058 333 333 ARG CB C 30.388 0.250 1 1059 333 333 ARG N N 122.059 0.070 1 1060 334 334 ASP H H 8.505 0.010 1 1061 334 334 ASP CA C 53.128 0.250 1 1062 334 334 ASP CB C 40.353 0.250 1 1063 334 334 ASP N N 124.848 0.070 1 1064 335 335 LEU H H 7.761 0.010 1 1065 335 335 LEU CA C 52.512 0.250 1 1066 335 335 LEU CB C 41.172 0.250 1 1067 335 335 LEU N N 123.340 0.070 1 1068 336 336 LEU H H 8.718 0.010 1 1069 336 336 LEU CA C 53.717 0.250 1 1070 336 336 LEU CB C 41.358 0.250 1 1071 336 336 LEU N N 120.110 0.070 1 1072 337 337 ILE H H 8.912 0.010 1 1073 337 337 ILE CA C 66.452 0.250 1 1074 337 337 ILE CB C 37.350 0.250 1 1075 337 337 ILE N N 121.975 0.070 1 1076 338 338 ASP H H 8.333 0.010 1 1077 338 338 ASP CA C 56.903 0.250 1 1078 338 338 ASP CB C 39.319 0.250 1 1079 338 338 ASP N N 116.168 0.070 1 1080 339 339 GLU H H 7.065 0.010 1 1081 339 339 GLU CA C 58.323 0.250 1 1082 339 339 GLU CB C 29.110 0.250 1 1083 339 339 GLU N N 120.722 0.070 1 1084 340 340 TRP H H 7.658 0.010 1 1085 340 340 TRP CA C 59.742 0.250 1 1086 340 340 TRP CB C 30.252 0.250 1 1087 340 340 TRP N N 119.775 0.070 1 1088 341 341 LYS H H 8.705 0.010 1 1089 341 341 LYS CA C 60.009 0.250 1 1090 341 341 LYS CB C 31.412 0.250 1 1091 341 341 LYS N N 121.618 0.070 1 1092 342 342 SER H H 7.583 0.010 1 1093 342 342 SER CA C 60.902 0.250 1 1094 342 342 SER CB C 61.987 0.250 1 1095 342 342 SER N N 114.776 0.070 1 1096 343 343 LEU H H 7.887 0.010 1 1097 343 343 LEU CA C 57.439 0.250 1 1098 343 343 LEU CB C 41.392 0.250 1 1099 343 343 LEU N N 120.634 0.070 1 1100 345 345 TYR H H 8.774 0.010 1 1101 345 345 TYR CA C 61.643 0.250 1 1102 345 345 TYR CB C 37.332 0.250 1 1103 345 345 TYR N N 125.005 0.070 1 1104 346 346 ASP H H 8.011 0.010 1 1105 346 346 ASP CA C 56.930 0.250 1 1106 346 346 ASP CB C 39.534 0.250 1 1107 346 346 ASP N N 117.510 0.070 1 1108 347 347 GLU H H 7.454 0.010 1 1109 347 347 GLU CA C 57.690 0.250 1 1110 347 347 GLU CB C 28.887 0.250 1 1111 347 347 GLU N N 118.513 0.070 1 1112 348 348 VAL H H 8.028 0.010 1 1113 348 348 VAL CA C 65.739 0.250 1 1114 348 348 VAL CB C 30.661 0.250 1 1115 348 348 VAL N N 121.295 0.070 1 1116 349 349 ILE H H 8.058 0.010 1 1117 349 349 ILE CA C 62.874 0.250 1 1118 349 349 ILE CB C 36.053 0.250 1 1119 349 349 ILE N N 114.770 0.070 1 1120 350 350 SER H H 7.349 0.010 1 1121 350 350 SER CA C 57.841 0.250 1 1122 350 350 SER CB C 63.284 0.250 1 1123 350 350 SER N N 113.552 0.070 1 1124 351 351 PHE H H 7.252 0.010 1 1125 351 351 PHE CA C 60.170 0.250 1 1126 351 351 PHE CB C 39.056 0.250 1 1127 351 351 PHE N N 125.133 0.070 1 1128 352 352 VAL H H 6.862 0.010 1 1129 352 352 VAL CA C 63.225 0.250 1 1130 352 352 VAL CB C 33.136 0.250 1 1131 352 352 VAL N N 130.112 0.070 1 stop_ save_