data_17748 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR Insights into Docking Interactions Involving Inactive ERK2 ; _BMRB_accession_number 17748 _BMRB_flat_file_name bmr17748.str _Entry_type original _Submission_date 2011-06-29 _Accession_date 2011-06-29 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Partial assignment of inactive ERK2 with no ligands' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Piserchio Andrea . . 2 Ghose Ranajeet . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 186 "13C chemical shifts" 569 "15N chemical shifts" 186 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-07-18 original author . stop_ _Original_release_date 2011-07-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR Insights into Docking Interactions Involving Inactive ERK2.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21449613 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Piserchio Andrea . . 2 Warthaka Mangalika . . 3 Devkota Ashwini K. . 4 Kaoud Tamer S. . 5 Lee Sunbae . . 6 Abramczyk Olga . . 7 Ren Pengyu . . 8 Dalby Kevin N. . 9 Ghose Ranajeet . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 50 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3660 _Page_last 3672 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ERK2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ERK2 $ERK2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ERK2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ERK2 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Ser/Thr kinase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 361 _Mol_residue_sequence ; GSHMAAAAAAGPEMVRGQVF DVGPRYTNLSYIGEGAYGMV CSAYDNLNKVRVAIKKISPF EHQTYCQRTLREIKILLRFR HENIIGINDIIRAPTIEQMK DVYIVQDLMETDLYKLLKTQ HLSNDHICYFLYQILRGLKY IHSANVLHRDLKPSNLLLNT TCDLKICDFGLARVADPDHD HTGFLTEYVATRWYRAPEIM LNSKGYTKSIDIWSVGCILA EMLSNRPIFPGKHYLDQLNH ILGILGSPSQEDLNCIINLK ARNYLLSLPHKNKVPWNRLF PNADSKALDLLDKMLTFNPH KRIEVEQALAHPYLEQYYDP SDEPIAEAPFKFDMELDDLP KEKLKELIFEETARFQPGYR S ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 ALA 6 ALA 7 ALA 8 ALA 9 ALA 10 ALA 11 GLY 12 PRO 13 GLU 14 MET 15 VAL 16 ARG 17 GLY 18 GLN 19 VAL 20 PHE 21 ASP 22 VAL 23 GLY 24 PRO 25 ARG 26 TYR 27 THR 28 ASN 29 LEU 30 SER 31 TYR 32 ILE 33 GLY 34 GLU 35 GLY 36 ALA 37 TYR 38 GLY 39 MET 40 VAL 41 CYS 42 SER 43 ALA 44 TYR 45 ASP 46 ASN 47 LEU 48 ASN 49 LYS 50 VAL 51 ARG 52 VAL 53 ALA 54 ILE 55 LYS 56 LYS 57 ILE 58 SER 59 PRO 60 PHE 61 GLU 62 HIS 63 GLN 64 THR 65 TYR 66 CYS 67 GLN 68 ARG 69 THR 70 LEU 71 ARG 72 GLU 73 ILE 74 LYS 75 ILE 76 LEU 77 LEU 78 ARG 79 PHE 80 ARG 81 HIS 82 GLU 83 ASN 84 ILE 85 ILE 86 GLY 87 ILE 88 ASN 89 ASP 90 ILE 91 ILE 92 ARG 93 ALA 94 PRO 95 THR 96 ILE 97 GLU 98 GLN 99 MET 100 LYS 101 ASP 102 VAL 103 TYR 104 ILE 105 VAL 106 GLN 107 ASP 108 LEU 109 MET 110 GLU 111 THR 112 ASP 113 LEU 114 TYR 115 LYS 116 LEU 117 LEU 118 LYS 119 THR 120 GLN 121 HIS 122 LEU 123 SER 124 ASN 125 ASP 126 HIS 127 ILE 128 CYS 129 TYR 130 PHE 131 LEU 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 ASN 146 VAL 147 LEU 148 HIS 149 ARG 150 ASP 151 LEU 152 LYS 153 PRO 154 SER 155 ASN 156 LEU 157 LEU 158 LEU 159 ASN 160 THR 161 THR 162 CYS 163 ASP 164 LEU 165 LYS 166 ILE 167 CYS 168 ASP 169 PHE 170 GLY 171 LEU 172 ALA 173 ARG 174 VAL 175 ALA 176 ASP 177 PRO 178 ASP 179 HIS 180 ASP 181 HIS 182 THR 183 GLY 184 PHE 185 LEU 186 THR 187 GLU 188 TYR 189 VAL 190 ALA 191 THR 192 ARG 193 TRP 194 TYR 195 ARG 196 ALA 197 PRO 198 GLU 199 ILE 200 MET 201 LEU 202 ASN 203 SER 204 LYS 205 GLY 206 TYR 207 THR 208 LYS 209 SER 210 ILE 211 ASP 212 ILE 213 TRP 214 SER 215 VAL 216 GLY 217 CYS 218 ILE 219 LEU 220 ALA 221 GLU 222 MET 223 LEU 224 SER 225 ASN 226 ARG 227 PRO 228 ILE 229 PHE 230 PRO 231 GLY 232 LYS 233 HIS 234 TYR 235 LEU 236 ASP 237 GLN 238 LEU 239 ASN 240 HIS 241 ILE 242 LEU 243 GLY 244 ILE 245 LEU 246 GLY 247 SER 248 PRO 249 SER 250 GLN 251 GLU 252 ASP 253 LEU 254 ASN 255 CYS 256 ILE 257 ILE 258 ASN 259 LEU 260 LYS 261 ALA 262 ARG 263 ASN 264 TYR 265 LEU 266 LEU 267 SER 268 LEU 269 PRO 270 HIS 271 LYS 272 ASN 273 LYS 274 VAL 275 PRO 276 TRP 277 ASN 278 ARG 279 LEU 280 PHE 281 PRO 282 ASN 283 ALA 284 ASP 285 SER 286 LYS 287 ALA 288 LEU 289 ASP 290 LEU 291 LEU 292 ASP 293 LYS 294 MET 295 LEU 296 THR 297 PHE 298 ASN 299 PRO 300 HIS 301 LYS 302 ARG 303 ILE 304 GLU 305 VAL 306 GLU 307 GLN 308 ALA 309 LEU 310 ALA 311 HIS 312 PRO 313 TYR 314 LEU 315 GLU 316 GLN 317 TYR 318 TYR 319 ASP 320 PRO 321 SER 322 ASP 323 GLU 324 PRO 325 ILE 326 ALA 327 GLU 328 ALA 329 PRO 330 PHE 331 LYS 332 PHE 333 ASP 334 MET 335 GLU 336 LEU 337 ASP 338 ASP 339 LEU 340 PRO 341 LYS 342 GLU 343 LYS 344 LEU 345 LYS 346 GLU 347 LEU 348 ILE 349 PHE 350 GLU 351 GLU 352 THR 353 ALA 354 ARG 355 PHE 356 GLN 357 PRO 358 GLY 359 TYR 360 ARG 361 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1ERK "Structure Of Signal-Regulated Kinase" 99.45 364 100.00 100.00 0.00e+00 PDB 1GOL "Coordinates Of Rat Map Kinase Erk2 With An Arginine Mutation At Position 52" 99.45 364 99.72 100.00 0.00e+00 PDB 1PME "Structure Of Penta Mutant Human Erk2 Map Kinase Complexed With A Specific Inhibitor Of Human P38 Map Kinase" 100.55 380 97.52 98.07 0.00e+00 PDB 1TVO "The Structure Of Erk2 In Complex With A Small Molecule Inhibitor" 98.89 368 99.44 99.72 0.00e+00 PDB 1WZY "Crystal Structure Of Human Erk2 Complexed With A Pyrazolopyridazine Derivative" 98.89 368 99.44 99.72 0.00e+00 PDB 2ERK "Phosphorylated Map Kinase Erk2" 99.45 365 99.44 99.44 0.00e+00 PDB 2FYS "Crystal Structure Of Erk2 Complex With Kim Peptide Derived From Mkp3" 99.45 364 100.00 100.00 0.00e+00 PDB 2GPH "Docking Motif Interactions In The Map Kinase Erk2" 99.45 364 99.72 99.72 0.00e+00 PDB 2OJG "Crystal Structure Of Erk2 In Complex With N,n-dimethyl-4-(4- Phenyl-1h-pyrazol-3-yl)-1h-pyrrole-2-carboxamide" 100.55 380 99.17 99.45 0.00e+00 PDB 2OJI "Crystal Structure Of Erk2 In Complex With N-Benzyl-4-(4-(3- Chlorophenyl)-1h-Pyrazol-3-Yl)-1h-Pyrrole-2-Carboxamide" 100.55 380 99.17 99.45 0.00e+00 PDB 2OJJ "Crystal Structure Of Erk2 In Complex With (S)-N-(1-(3- Chloro-4-Fluorophenyl)-2-Hydroxyethyl)-4-(4-(3- Chlorophenyl)-1h-Pyrazol" 100.55 380 99.17 99.45 0.00e+00 PDB 2Y9Q "Crystal Structure Of Human Erk2 Complexed With A Mapk Docking Peptide" 98.89 362 99.44 99.72 0.00e+00 PDB 2Z7L "Unphosphorylated Mitogen Activated Protein Kinase Erk2 In Complex With (4-{[5-Carbamoyl-4-(3-Methylanilino)pyrimidin 2-Yl]amino" 99.45 366 100.00 100.00 0.00e+00 PDB 3C9W "Crystal Structure Of Erk-2 With Hypothemycin Covalently Bound" 98.89 357 100.00 100.00 0.00e+00 PDB 3ERK "The Complex Structure Of The Map Kinase Erk2SB220025" 99.45 364 100.00 100.00 0.00e+00 PDB 3I5Z "Crystal Structure Of Erk2 Bound To (S)-N-(2-Hydroxy-1-Phenylethyl)-4- (5-Methyl-2-(Phenylamino)pyrimidin-4-Yl)-1h-Pyrrole-2-Car" 100.55 380 99.17 99.45 0.00e+00 PDB 3I60 "Crystal Structure Of Erk2 Bound To (s)-4-(2-(2-chlorophenylamino)-5- Methylpyrimidin-4-yl)-n-(2-hydroxy-1-phenylethyl)-1h-pyrro" 100.55 380 99.17 99.45 0.00e+00 PDB 3O71 "Crystal Structure Of Erk2DCC PEPTIDE COMPLEX" 99.17 358 100.00 100.00 0.00e+00 PDB 3QYW "Crystal Structure Of Erk2 In Complex With An Inhibitor" 99.45 364 99.72 99.72 0.00e+00 PDB 3QYZ "Crystal Structure Of Erk2 In Complex With An Inhibitor" 99.45 364 99.72 99.72 0.00e+00 PDB 3R63 "Structure Of Erk2 (Spe) Mutant (S246e)" 99.17 358 99.72 99.72 0.00e+00 PDB 3SA0 "Complex Of Erk2 With Norathyriol" 98.89 360 98.60 98.88 0.00e+00 PDB 3TEI "Crystal Structure Of Human Erk2 Complexed With A Mapk Docking Peptide" 98.89 362 98.88 99.16 0.00e+00 PDB 3W55 "The Structure Of Erk2 In Complex With Fr148083" 98.89 368 99.44 99.72 0.00e+00 PDB 3ZU7 "Crystal Structure Of A Designed Selected Ankyrin Repeat Protein In Complex With The Map Kinase Erk2" 99.45 365 99.44 99.44 0.00e+00 PDB 3ZUV "Crystal Structure Of A Designed Selected Ankyrin Repeat Protein In Complex With The Phosphorylated Map Kinase Erk2" 99.45 364 98.89 98.89 0.00e+00 PDB 4ERK "The Complex Structure Of The Map Kinase Erk2OLOMOUCINE" 99.45 364 100.00 100.00 0.00e+00 PDB 4FMQ "Crystal Structure Of Human Erk2 Complexed With A Mapk Docking Peptide" 98.89 362 99.44 99.72 0.00e+00 PDB 4FUX "Crystal Structure Of The Erk2 Complexed With E75" 98.89 360 99.16 99.44 0.00e+00 PDB 4FUY "Crystal Structure Of The Erk2 Complexed With Ek2" 98.89 360 98.60 98.88 0.00e+00 PDB 4FV0 "Crystal Structure Of The Erk2 Complexed With Ek3" 98.89 360 98.60 98.88 0.00e+00 PDB 4FV1 "Crystal Structure Of The Erk2 Complexed With Ek4" 98.89 360 99.16 99.44 0.00e+00 PDB 4FV2 "Crystal Structure Of The Erk2 Complexed With Ek5" 98.89 360 99.16 99.44 0.00e+00 PDB 4FV3 "Crystal Structure Of The Erk2 Complexed With Ek6" 98.89 360 99.16 99.44 0.00e+00 PDB 4FV4 "Crystal Structure Of The Erk2 Complexed With Ek7" 98.89 360 99.16 99.44 0.00e+00 PDB 4FV5 "Crystal Structure Of The Erk2 Complexed With Ek9" 98.89 360 99.16 99.44 0.00e+00 PDB 4FV6 "Crystal Structure Of The Erk2 Complexed With E57" 98.89 360 99.44 99.72 0.00e+00 PDB 4FV7 "Crystal Structure Of The Erk2 Complexed With E94" 98.89 360 98.88 99.16 0.00e+00 PDB 4FV8 "Crystal Structure Of The Erk2 Complexed With E63" 98.89 360 99.16 99.44 0.00e+00 PDB 4FV9 "Crystal Structure Of The Erk2 Complexed With E71" 98.89 360 99.16 99.44 0.00e+00 PDB 4G6N "Crystal Structure Of The Erk2" 98.89 360 99.16 99.44 0.00e+00 PDB 4G6O "Crystal Structure Of The Erk2" 98.89 360 98.88 99.16 0.00e+00 PDB 4GSB "Monoclinic Crystal Form Of The Apo-Erk2" 99.45 364 99.44 99.44 0.00e+00 PDB 4GT3 "Atp-Bound Form Of The Erk2 Kinase" 99.45 364 99.72 99.72 0.00e+00 PDB 4GVA "Adp-Bound Form Of The Erk2 Kinase" 99.45 364 99.72 99.72 0.00e+00 PDB 4H3P "Crystal Structure Of Human Erk2 Complexed With A Mapk Docking Peptide" 98.89 362 98.88 99.16 0.00e+00 PDB 4H3Q "Crystal Structure Of Human Erk2 Complexed With A Mapk Docking Peptide" 98.89 362 98.32 98.60 0.00e+00 PDB 4I5H "Crystal Structure Of A Double Mutant Rat Erk2 Complexed With A Type Ii Quinazoline Inhibitor" 98.89 359 99.44 99.44 0.00e+00 PDB 4IZ5 "Structure Of The Complex Between Erk2 Phosphomimetic Mutant And Pea-15" 98.61 356 98.31 98.60 0.00e+00 PDB 4IZ7 "Structure Of Non-phosphorylated Erk2 Bound To The Pea-15 Death Effector Domain" 98.61 356 98.60 98.88 0.00e+00 PDB 4IZA "Structure Of Dually Phosphorylated Erk2 Bound To The Pea-15 Death Effector Domain" 98.61 356 98.03 98.31 0.00e+00 PDB 4N0S "Complex Of Erk2 With Caffeic Acid" 98.89 360 98.32 98.60 0.00e+00 PDB 4N4S "A Double Mutant Rat Erk2 In Complex With A Pyrazolo[3,4-d]pyrimidine Inhibitor" 98.89 359 99.44 99.44 0.00e+00 PDB 4NIF "Heterodimeric Structure Of Erk2 And Rsk1" 98.89 362 99.44 99.72 0.00e+00 PDB 4O6E "Discovery Of 5,6,7,8-tetrahydropyrido[3,4-d]pyrimidine Inhibitors Of Erk2" 99.45 368 97.21 97.77 0.00e+00 PDB 4QP1 "Crystal Structure Of Erk2 In Complex With N-cyclohexyl-9h-purin-6- Amine" 100.00 369 98.89 99.17 0.00e+00 PDB 4QP2 "Crystal Structure Of Erks In Complex With 5-chlorobenzo[d]oxazol-2- Amine" 100.00 369 98.89 99.17 0.00e+00 PDB 4QP3 "Crystal Structure Of Erk2 In Complex With (s)-2-((9h-purin-6-yl) Amino)-3-phenylpropan-1-ol" 100.00 369 98.89 99.17 0.00e+00 PDB 4QP4 "Crystal Structure Of Erk2 In Complex With N-cyclohexyl-9h-purin-6- Amine" 100.00 369 99.17 99.45 0.00e+00 PDB 4QP6 "Crystal Structure Of Erk2 In Complex With 5h-pyrrolo[2,3-b]pyrazine" 100.00 369 98.89 99.17 0.00e+00 PDB 4QP7 "Crystal Structure Of Erk2 In Complex With 2-(1h-pyrazol-4-yl)-5h- Pyrrolo[2,3-b]pyrazine" 100.00 369 99.17 99.45 0.00e+00 PDB 4QP8 "Crystal Structure Of Erk2 In Complex With 2-(1h-pyrazol-4-yl)-7- (pyridin-3-yl)-5h-pyrrolo[2,3-b]pyrazine" 100.00 369 99.17 99.45 0.00e+00 PDB 4QP9 "Crystal Structure Of Erk2 In Complex With 7-(1-propyl-1h-pyrazol-4- Yl)-2-(pyridin-4-yl)-5h-pyrrolo[2,3-b]pyrazine" 100.00 369 99.17 99.45 0.00e+00 PDB 4QPA "Crystal Structure Of Erk2 In Complex With 7-(1-benzyl-1h-pyrazol-4- Yl)-2-(pyridin-4-yl)-5h-pyrrolo[2,3-b]pyrazine" 100.00 369 98.89 99.17 0.00e+00 PDB 4QTA "Structure Of Human Erk2 In Complex With Sch772984 Revealing A Novel Inhibitor-induced Binding Pocket" 98.89 361 99.44 99.72 0.00e+00 PDB 4QTE "Structure Of Erk2 In Complex With Vtx-11e, 4-{2-[(2-chloro-4- Fluorophenyl)amino]-5-methylpyrimidin-4-yl}-n-[(1s)-1-(3- Chlorop" 98.89 361 99.44 99.72 0.00e+00 PDB 4QYY "Discovery Of Novel, Dual Mechanism Erk Inhibitors By Affinity Selection Screening Of An Inactive Kinase State" 99.45 365 100.00 100.00 0.00e+00 PDB 4XJ0 "Crystal Structure Of Erk2 In Complex With An Inhibitor 14k" 96.68 349 99.43 99.71 0.00e+00 PDB 4XNE "Crystal Structure Of Erk2 In Complex With An Inhibitor" 95.84 346 99.42 99.42 0.00e+00 PDB 4XOY "Crystal Structure Of Erk2 In Complex With An Inhibitor" 97.23 351 98.86 98.86 0.00e+00 PDB 4XOZ "Crystal Structure Of Erk2 In Complex With An Inhibitor" 97.23 351 99.72 99.72 0.00e+00 PDB 4XP0 "Crystal Structure Of Erk2 In Complex With An Inhibitor" 97.23 351 98.86 98.86 0.00e+00 PDB 4XP2 "Crystal Structure Of Erk2 In Complex With An Inhibitor" 97.23 351 99.43 99.43 0.00e+00 PDB 4XP3 "Crystal Structure Of Erk2 In Complex With An Inhibitor" 97.23 351 99.43 99.43 0.00e+00 PDB 4XRJ "Crystal Structure Of Erk2 In Complex With An Inhibitor" 95.84 346 99.42 99.42 0.00e+00 PDB 4ZZM "Human Erk2 In Complex With An Irreversible Inhibitor" 96.95 350 99.71 99.71 0.00e+00 PDB 4ZZN "Human Erk2 In Complex With An Inhibitor" 96.95 350 99.71 99.71 0.00e+00 PDB 4ZZO "Human Erk2 In Complex With An Irreversible Inhibitor" 96.95 350 99.71 99.71 0.00e+00 PDB 5BUE "Erk2 Complexed With N-benzylpyridone Tetrahydroazaindazole" 100.00 361 98.61 98.89 0.00e+00 PDB 5BUI "Erk2 Complexed With 2-pyridiyl Tetrahydroazaindazole" 100.00 361 98.61 98.89 0.00e+00 PDB 5BUJ "Erk2 Complexed With A N-h Tetrahydroazaindazole" 100.00 361 98.61 98.89 0.00e+00 PDB 5BVD "Tetrahydropyrrolo-diazepenones As Inhibitors Of Erk2 Kinase" 100.00 361 98.61 98.89 0.00e+00 PDB 5BVE "Tetrahydropyrrolo-diazepenones As Inhibitors Of Erk2 Kinase" 100.00 361 98.61 98.89 0.00e+00 PDB 5BVF "Tetrahydropyrrolo-diazepenones As Inhibitors Of Erk2 Kinase" 100.00 361 98.61 98.89 0.00e+00 DBJ BAA01733 "ERK2 [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 DBJ BAA22620 "ERK2 [Mus musculus]" 76.45 291 97.10 97.10 0.00e+00 DBJ BAC29053 "unnamed protein product [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 DBJ BAC33251 "unnamed protein product [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 DBJ BAC40044 "unnamed protein product [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 EMBL CAA41548 "mitogen-activated protein kinase (p42) [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 EMBL CAA77752 "41kD protein kinase [Homo sapiens]" 98.89 360 99.16 99.72 0.00e+00 EMBL CAA77753 "40kDa protein kinase [Homo sapiens]" 96.40 348 99.71 100.00 0.00e+00 EMBL CAA78467 "extracellular signal-regulated kinase (ERK2) [Bos taurus]" 98.89 360 99.16 99.72 0.00e+00 EMBL CAI29602 "hypothetical protein [Pongo abelii]" 98.89 358 99.16 99.44 0.00e+00 GB AAA41124 "extracellular signal-related kinase 2 [Rattus norvegicus]" 99.17 358 100.00 100.00 0.00e+00 GB AAA58459 "protein kinase 2 [Homo sapiens]" 98.89 360 99.44 99.72 0.00e+00 GB AAH17832 "Mitogen-activated protein kinase 1 [Homo sapiens]" 98.89 360 99.44 99.72 0.00e+00 GB AAH58258 "Mitogen-activated protein kinase 1 [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 GB AAH99905 "Mitogen-activated protein kinase 1 [Homo sapiens]" 98.89 360 98.88 99.44 0.00e+00 PRF 1813206A "mitogen-activated protein kinase" 98.89 360 99.16 99.72 0.00e+00 PRF 1813206B "mitogen-activated protein kinase" 96.40 348 99.71 100.00 0.00e+00 REF NP_001033752 "mitogen-activated protein kinase 1 [Mus musculus]" 99.17 358 100.00 100.00 0.00e+00 REF NP_001104270 "mitogen-activated protein kinase 1 [Canis lupus familiaris]" 98.89 360 99.44 99.72 0.00e+00 REF NP_001185851 "mitogen-activated protein kinase 1 [Sus scrofa]" 98.89 359 99.16 99.72 0.00e+00 REF NP_001297736 "mitogen-activated protein kinase 1 [Anas platyrhynchos]" 98.89 368 97.76 98.60 0.00e+00 REF NP_001301131 "mitogen-activated protein kinase 1 [Capra hircus]" 98.89 360 99.16 99.72 0.00e+00 SP P28482 "RecName: Full=Mitogen-activated protein kinase 1; Short=MAP kinase 1; Short=MAPK 1; AltName: Full=ERT1; AltName: Full=Extracell" 98.89 360 99.44 99.72 0.00e+00 SP P46196 "RecName: Full=Mitogen-activated protein kinase 1; Short=MAP kinase 1; Short=MAPK 1; AltName: Full=ERT1; AltName: Full=Extracell" 98.89 360 99.16 99.72 0.00e+00 SP P63085 "RecName: Full=Mitogen-activated protein kinase 1; Short=MAP kinase 1; Short=MAPK 1; AltName: Full=ERT1; AltName: Full=Extracell" 99.17 358 100.00 100.00 0.00e+00 SP P63086 "RecName: Full=Mitogen-activated protein kinase 1; Short=MAP kinase 1; Short=MAPK 1; AltName: Full=ERT1; AltName: Full=Extracell" 99.17 358 100.00 100.00 0.00e+00 TPG DAA20381 "TPA: mitogen-activated protein kinase 1 [Bos taurus]" 88.09 321 99.37 99.69 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 $ERK2 Rat 10116 Eukaryota Metazoa Rattus norvegicus 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 $ERK2 'recombinant technology' . Escherichia coli . pET28 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details pH=6.8 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ERK2 0.2 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' DTT 2 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . 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 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 200 . mM 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 internal indirect . . . 0.25144953 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal 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' '3D HNCO' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ERK2 _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 4 4 MET C C 175.786 0.25 1 2 4 4 MET CA C 55.086 0.25 1 3 4 4 MET CB C 32.056 0.25 1 4 5 5 ALA H H 8.263 0.05 1 5 5 5 ALA CA C 52.116 0.25 1 6 5 5 ALA CB C 18.326 0.25 1 7 5 5 ALA N N 125.997 0.14 1 8 6 6 ALA H H 8.178 0.05 1 9 6 6 ALA N N 123.797 0.14 1 10 9 9 ALA H H 8.193 0.05 1 11 9 9 ALA N N 123.997 0.14 1 12 10 10 ALA C C 177.786 0.25 1 13 10 10 ALA CA C 51.876 0.25 1 14 10 10 ALA CB C 18.776 0.25 1 15 11 11 GLY H H 8.005 0.10 1 16 11 11 GLY CA C 44.006 0.25 1 17 11 11 GLY N N 108.797 0.14 1 18 12 12 PRO C C 176.786 0.25 1 19 12 12 PRO CA C 62.276 0.25 1 20 12 12 PRO CB C 31.596 0.25 1 21 13 13 GLU H H 8.480 0.05 1 22 13 13 GLU C C 174.886 0.25 1 23 13 13 GLU CA C 56.596 0.25 1 24 13 13 GLU CB C 30.166 0.25 1 25 13 13 GLU N N 121.497 0.14 1 26 14 14 MET H H 8.255 0.05 1 27 14 14 MET C C 176.186 0.25 1 28 14 14 MET CA C 53.426 0.25 1 29 14 14 MET CB C 34.366 0.25 1 30 14 14 MET N N 119.997 0.14 1 31 15 15 VAL H H 9.053 0.05 1 32 15 15 VAL C C 174.886 0.25 1 33 15 15 VAL CA C 61.206 0.25 1 34 15 15 VAL CB C 33.276 0.25 1 35 15 15 VAL N N 124.197 0.14 1 36 16 16 ARG H H 9.203 0.05 1 37 16 16 ARG C C 176.586 0.25 1 38 16 16 ARG CA C 56.266 0.25 1 39 16 16 ARG CB C 27.056 0.25 1 40 16 16 ARG N N 125.397 0.14 1 41 17 17 GLY H H 8.464 0.05 1 42 17 17 GLY C C 173.886 0.25 1 43 17 17 GLY CA C 45.046 0.25 1 44 17 17 GLY N N 103.597 0.14 1 45 18 18 GLN H H 8.139 0.05 1 46 18 18 GLN C C 175.186 0.25 1 47 18 18 GLN CA C 53.256 0.25 1 48 18 18 GLN CB C 30.296 0.25 1 49 18 18 GLN N N 119.897 0.14 1 50 19 19 VAL H H 8.682 0.05 1 51 19 19 VAL C C 175.886 0.25 1 52 19 19 VAL CA C 63.006 0.25 1 53 19 19 VAL CB C 31.596 0.25 1 54 19 19 VAL N N 123.597 0.14 1 55 20 20 PHE H H 8.986 0.05 1 56 20 20 PHE C C 174.786 0.25 1 57 20 20 PHE CA C 56.756 0.25 1 58 20 20 PHE CB C 40.176 0.25 1 59 20 20 PHE N N 130.997 0.14 1 60 21 21 ASP H H 7.918 0.05 1 61 21 21 ASP C C 174.486 0.25 1 62 21 21 ASP CA C 53.026 0.25 1 63 21 21 ASP CB C 38.946 0.25 1 64 21 21 ASP N N 124.497 0.14 1 65 22 22 VAL H H 7.448 0.05 1 66 22 22 VAL C C 176.186 0.25 1 67 22 22 VAL CA C 59.706 0.25 1 68 22 22 VAL CB C 31.196 0.25 1 69 22 22 VAL N N 110.297 0.14 1 70 23 23 GLY H H 8.712 0.05 1 71 23 23 GLY CA C 44.286 0.25 1 72 23 23 GLY N N 112.497 0.14 1 73 24 24 PRO C C 177.486 0.25 1 74 24 24 PRO CA C 62.386 0.25 1 75 24 24 PRO CB C 33.806 0.25 1 76 25 25 ARG H H 8.540 0.05 1 77 25 25 ARG C C 175.586 0.25 1 78 25 25 ARG CA C 60.036 0.25 1 79 25 25 ARG CB C 28.866 0.25 1 80 25 25 ARG N N 123.497 0.14 1 81 26 26 TYR H H 7.259 0.05 1 82 26 26 TYR C C 175.486 0.25 1 83 26 26 TYR CA C 55.146 0.25 1 84 26 26 TYR N N 117.297 0.14 1 85 27 27 THR H H 8.742 0.05 1 86 27 27 THR C C 174.086 0.25 1 87 27 27 THR CA C 59.366 0.25 1 88 27 27 THR CB C 72.756 0.25 1 89 27 27 THR N N 112.397 0.14 1 90 28 28 ASN H H 9.652 0.05 1 91 28 28 ASN C C 174.686 0.25 1 92 28 28 ASN CA C 53.626 0.25 1 93 28 28 ASN CB C 35.676 0.25 1 94 28 28 ASN N N 119.097 0.14 1 95 29 29 LEU H H 8.643 0.05 1 96 29 29 LEU C C 178.986 0.25 1 97 29 29 LEU CA C 54.836 0.25 1 98 29 29 LEU CB C 41.456 0.25 1 99 29 29 LEU N N 121.697 0.14 1 100 30 30 SER H H 8.466 0.05 1 101 30 30 SER C C 173.386 0.25 1 102 30 30 SER CA C 56.596 0.25 1 103 30 30 SER CB C 64.336 0.25 1 104 30 30 SER N N 114.697 0.14 1 105 31 31 TYR H H 8.971 0.05 1 106 31 31 TYR C C 175.686 0.25 1 107 31 31 TYR CA C 60.016 0.25 1 108 31 31 TYR CB C 38.476 0.25 1 109 31 31 TYR N N 127.997 0.14 1 110 32 32 ILE H H 8.278 0.05 1 111 32 32 ILE C C 175.486 0.25 1 112 32 32 ILE CA C 62.346 0.25 1 113 32 32 ILE CB C 38.526 0.25 1 114 32 32 ILE N N 126.997 0.14 1 115 33 33 GLY H H 7.141 0.05 1 116 33 33 GLY C C 182.286 0.25 1 117 33 33 GLY CA C 45.456 0.25 1 118 33 33 GLY N N 106.597 0.14 1 119 34 34 GLU H H 8.300 0.05 1 120 34 34 GLU C C 175.586 0.25 1 121 34 34 GLU CA C 54.916 0.25 1 122 34 34 GLU CB C 31.806 0.25 1 123 34 34 GLU N N 116.897 0.14 1 124 35 35 GLY H H 8.076 0.05 1 125 35 35 GLY CA C 43.506 0.25 1 126 35 35 GLY N N 110.597 0.14 1 127 36 36 ALA C C 178.286 0.25 1 128 36 36 ALA CA C 54.146 0.25 1 129 37 37 TYR H H 8.000 0.05 1 130 37 37 TYR C C 174.686 0.25 1 131 37 37 TYR CA C 55.446 0.25 1 132 37 37 TYR CB C 36.656 0.25 1 133 37 37 TYR N N 112.997 0.14 1 134 38 38 GLY H H 6.956 0.05 1 135 38 38 GLY C C 172.686 0.25 1 136 38 38 GLY CA C 44.916 0.25 1 137 38 38 GLY N N 106.997 0.14 1 138 39 39 MET H H 8.270 0.05 1 139 39 39 MET C C 173.786 0.25 1 140 39 39 MET CA C 55.756 0.25 1 141 39 39 MET CB C 35.546 0.25 1 142 39 39 MET N N 121.497 0.14 1 143 40 40 VAL H H 9.005 0.10 1 144 40 40 VAL C C 175.486 0.25 1 145 40 40 VAL CA C 60.636 0.25 1 146 40 40 VAL CB C 32.776 0.25 1 147 40 40 VAL N N 125.497 0.14 1 148 41 41 CYS H H 8.983 0.05 1 149 41 41 CYS C C 173.786 0.25 1 150 41 41 CYS CA C 56.436 0.25 1 151 41 41 CYS CB C 32.256 0.25 1 152 41 41 CYS N N 123.497 0.14 1 153 42 42 SER H H 9.412 0.05 1 154 42 42 SER CA C 55.526 0.25 1 155 42 42 SER CB C 65.376 0.25 1 156 42 42 SER N N 115.497 0.14 1 157 43 43 ALA C C 174.386 0.25 1 158 43 43 ALA CA C 50.396 0.25 1 159 43 43 ALA CB C 23.926 0.25 1 160 44 44 TYR H H 9.668 0.05 1 161 44 44 TYR CA C 57.936 0.25 1 162 44 44 TYR CB C 38.716 0.25 1 163 44 44 TYR N N 122.597 0.14 1 164 46 46 ASN C C 175.386 0.25 1 165 46 46 ASN CB C 39.186 0.25 1 166 47 47 LEU H H 8.363 0.05 1 167 47 47 LEU C C 177.586 0.25 1 168 47 47 LEU CA C 56.606 0.25 1 169 47 47 LEU CB C 40.776 0.25 1 170 47 47 LEU N N 120.897 0.14 1 171 48 48 ASN H H 6.661 0.05 1 172 48 48 ASN C C 174.186 0.25 1 173 48 48 ASN CA C 52.596 0.25 1 174 48 48 ASN CB C 38.556 0.25 1 175 48 48 ASN N N 115.197 0.14 1 176 49 49 LYS H H 8.013 0.05 1 177 49 49 LYS C C 175.186 0.25 1 178 49 49 LYS CA C 56.396 0.25 1 179 49 49 LYS CB C 27.116 0.25 1 180 49 49 LYS N N 118.097 0.14 1 181 50 50 VAL H H 6.716 0.05 1 182 50 50 VAL C C 173.986 0.25 1 183 50 50 VAL CA C 58.486 0.25 1 184 50 50 VAL CB C 35.206 0.25 1 185 50 50 VAL N N 112.497 0.14 1 186 51 51 ARG H H 8.474 0.05 1 187 51 51 ARG CA C 55.766 0.25 1 188 51 51 ARG CB C 30.046 0.25 1 189 51 51 ARG N N 122.597 0.14 1 190 55 55 LYS C C 174.886 0.25 1 191 55 55 LYS CA C 53.656 0.25 1 192 56 56 LYS H H 8.972 0.05 1 193 56 56 LYS CA C 55.096 0.25 1 194 56 56 LYS N N 127.297 0.14 1 195 59 59 PRO C C 177.186 0.25 1 196 59 59 PRO CA C 63.386 0.25 1 197 59 59 PRO CB C 32.706 0.25 1 198 60 60 PHE H H 7.925 0.05 1 199 60 60 PHE C C 176.186 0.25 1 200 60 60 PHE CA C 61.426 0.25 1 201 60 60 PHE CB C 36.736 0.25 1 202 60 60 PHE N N 115.497 0.14 1 203 61 61 GLU H H 8.607 0.05 1 204 61 61 GLU C C 175.986 0.25 1 205 61 61 GLU CA C 56.496 0.25 1 206 61 61 GLU CB C 28.586 0.25 1 207 61 61 GLU N N 116.797 0.14 1 208 62 62 HIS H H 7.737 0.05 1 209 62 62 HIS CA C 54.586 0.25 1 210 62 62 HIS CB C 32.576 0.25 1 211 62 62 HIS N N 116.997 0.14 1 212 65 65 TYR C C 180.186 0.25 1 213 65 65 TYR CA C 57.436 0.25 1 214 66 66 CYS H H 8.290 0.05 1 215 66 66 CYS C C 176.186 0.25 1 216 66 66 CYS CA C 64.646 0.25 1 217 66 66 CYS CB C 27.626 0.25 1 218 66 66 CYS N N 121.197 0.14 1 219 67 67 GLN H H 8.405 0.05 1 220 67 67 GLN C C 177.186 0.25 1 221 67 67 GLN CA C 59.876 0.25 1 222 67 67 GLN CB C 27.946 0.25 1 223 67 67 GLN N N 119.897 0.14 1 224 68 68 ARG H H 7.819 0.05 1 225 68 68 ARG C C 178.786 0.25 1 226 68 68 ARG CA C 58.896 0.25 1 227 68 68 ARG N N 117.697 0.14 1 228 69 69 THR H H 7.688 0.05 1 229 69 69 THR C C 175.186 0.25 1 230 69 69 THR CA C 66.696 0.25 1 231 69 69 THR CB C 68.006 0.25 1 232 69 69 THR N N 115.097 0.14 1 233 70 70 LEU H H 7.984 0.05 1 234 70 70 LEU C C 177.386 0.25 1 235 70 70 LEU CA C 57.546 0.25 1 236 70 70 LEU CB C 40.006 0.25 1 237 70 70 LEU N N 120.397 0.14 1 238 71 71 ARG H H 8.260 0.05 1 239 71 71 ARG CA C 60.496 0.25 1 240 71 71 ARG CB C 29.716 0.25 1 241 71 71 ARG N N 117.797 0.14 1 242 76 76 LEU C C 180.686 0.25 1 243 77 77 LEU H H 7.909 0.05 1 244 77 77 LEU C C 178.886 0.25 1 245 77 77 LEU CA C 56.406 0.25 1 246 77 77 LEU N N 115.397 0.14 1 247 78 78 ARG H H 7.285 0.05 1 248 78 78 ARG C C 176.686 0.25 1 249 78 78 ARG CA C 55.866 0.25 1 250 78 78 ARG CB C 29.886 0.25 1 251 78 78 ARG N N 119.297 0.14 1 252 79 79 PHE H H 7.946 0.05 1 253 79 79 PHE C C 175.286 0.25 1 254 79 79 PHE CA C 53.866 0.25 1 255 79 79 PHE CB C 38.506 0.25 1 256 79 79 PHE N N 120.997 0.14 1 257 80 80 ARG H H 7.635 0.05 1 258 80 80 ARG C C 173.386 0.25 1 259 80 80 ARG CA C 55.206 0.25 1 260 80 80 ARG CB C 30.386 0.25 1 261 80 80 ARG N N 119.697 0.14 1 262 81 81 HIS H H 9.008 0.05 1 263 81 81 HIS C C 175.286 0.25 1 264 81 81 HIS CA C 57.496 0.25 1 265 81 81 HIS CB C 32.826 0.25 1 266 81 81 HIS N N 126.797 0.14 1 267 82 82 GLU H H 8.120 0.05 1 268 82 82 GLU C C 177.786 0.25 1 269 82 82 GLU CA C 59.126 0.25 1 270 82 82 GLU CB C 29.406 0.25 1 271 82 82 GLU N N 126.097 0.14 1 272 83 83 ASN H H 11.554 0.05 1 273 83 83 ASN C C 173.786 0.25 1 274 83 83 ASN CA C 53.776 0.25 1 275 83 83 ASN CB C 39.816 0.25 1 276 83 83 ASN N N 118.897 0.14 1 277 84 84 ILE H H 7.807 0.05 1 278 84 84 ILE CA C 60.516 0.25 1 279 84 84 ILE CB C 40.016 0.25 1 280 84 84 ILE N N 120.897 0.14 1 281 86 86 GLY C C 174.686 0.25 1 282 86 86 GLY CA C 43.486 0.25 1 283 87 87 ILE H H 8.549 0.05 1 284 87 87 ILE C C 174.586 0.25 1 285 87 87 ILE CA C 61.796 0.25 1 286 87 87 ILE CB C 39.376 0.25 1 287 87 87 ILE N N 119.297 0.14 1 288 88 88 ASN H H 8.873 0.05 1 289 88 88 ASN C C 174.686 0.25 1 290 88 88 ASN CA C 53.256 0.25 1 291 88 88 ASN N N 125.297 0.14 1 292 89 89 ASP H H 7.474 0.05 1 293 89 89 ASP C C 173.486 0.25 1 294 89 89 ASP CA C 52.456 0.25 1 295 89 89 ASP CB C 41.106 0.25 1 296 89 89 ASP N N 117.297 0.14 1 297 90 90 ILE H H 7.337 0.05 1 298 90 90 ILE CA C 60.646 0.25 1 299 90 90 ILE CB C 40.506 0.25 1 300 90 90 ILE N N 121.197 0.14 1 301 91 91 ILE C C 175.386 0.25 1 302 91 91 ILE CA C 59.696 0.25 1 303 91 91 ILE CB C 40.136 0.25 1 304 92 92 ARG H H 7.960 0.05 1 305 92 92 ARG C C 175.286 0.25 1 306 92 92 ARG CA C 54.296 0.25 1 307 92 92 ARG CB C 31.926 0.25 1 308 92 92 ARG N N 117.597 0.14 1 309 93 93 ALA H H 8.824 0.05 1 310 93 93 ALA CA C 50.966 0.25 1 311 93 93 ALA CB C 18.076 0.25 1 312 93 93 ALA N N 122.497 0.14 1 313 94 94 PRO C C 177.386 0.25 1 314 94 94 PRO CA C 64.476 0.25 1 315 95 95 THR H H 6.855 0.05 1 316 95 95 THR C C 174.786 0.25 1 317 95 95 THR CA C 58.206 0.25 1 318 95 95 THR CB C 71.386 0.25 1 319 95 95 THR N N 104.697 0.14 1 320 96 96 ILE H H 8.250 0.05 1 321 96 96 ILE C C 177.286 0.25 1 322 96 96 ILE CA C 64.996 0.25 1 323 96 96 ILE CB C 36.266 0.25 1 324 96 96 ILE N N 124.497 0.14 1 325 97 97 GLU H H 8.581 0.05 1 326 97 97 GLU C C 178.486 0.25 1 327 97 97 GLU CA C 58.706 0.25 1 328 97 97 GLU CB C 27.266 0.25 1 329 97 97 GLU N N 120.197 0.14 1 330 98 98 GLN H H 6.989 0.05 1 331 98 98 GLN C C 175.386 0.25 1 332 98 98 GLN CA C 55.156 0.25 1 333 98 98 GLN CB C 30.076 0.25 1 334 98 98 GLN N N 114.797 0.14 1 335 99 99 MET H H 7.250 0.05 1 336 99 99 MET CA C 55.736 0.25 1 337 99 99 MET CB C 31.476 0.25 1 338 99 99 MET N N 121.597 0.14 1 339 100 100 LYS C C 174.886 0.25 1 340 101 101 ASP H H 7.641 0.05 1 341 101 101 ASP C C 174.586 0.25 1 342 101 101 ASP CA C 51.476 0.25 1 343 101 101 ASP CB C 45.156 0.25 1 344 101 101 ASP N N 116.197 0.14 1 345 102 102 VAL H H 9.052 0.05 1 346 102 102 VAL CA C 60.506 0.25 1 347 102 102 VAL CB C 34.116 0.25 1 348 102 102 VAL N N 118.997 0.14 1 349 105 105 VAL C C 175.486 0.25 1 350 105 105 VAL CA C 60.946 0.25 1 351 106 106 GLN H H 9.434 0.05 1 352 106 106 GLN C C 173.586 0.25 1 353 106 106 GLN CA C 53.146 0.25 1 354 106 106 GLN N N 126.597 0.14 1 355 107 107 ASP H H 8.647 0.05 1 356 107 107 ASP CA C 54.736 0.25 1 357 107 107 ASP CB C 40.106 0.25 1 358 107 107 ASP N N 120.397 0.14 1 359 109 109 MET C C 176.286 0.25 1 360 109 109 MET CA C 52.456 0.25 1 361 110 110 GLU H H 8.943 0.05 1 362 110 110 GLU C C 176.386 0.25 1 363 110 110 GLU CA C 59.616 0.25 1 364 110 110 GLU CB C 30.006 0.25 1 365 110 110 GLU N N 123.397 0.14 1 366 111 111 THR H H 8.390 0.05 1 367 111 111 THR C C 172.986 0.25 1 368 111 111 THR CA C 58.966 0.25 1 369 111 111 THR CB C 68.606 0.25 1 370 111 111 THR N N 112.997 0.14 1 371 112 112 ASP H H 8.870 0.05 1 372 112 112 ASP CA C 53.076 0.25 1 373 112 112 ASP CB C 43.966 0.25 1 374 112 112 ASP N N 119.597 0.14 1 375 114 114 TYR C C 177.586 0.25 1 376 114 114 TYR CA C 60.376 0.25 1 377 115 115 LYS H H 8.780 0.1 1 378 115 115 LYS C C 180.786 0.25 1 379 115 115 LYS CA C 59.226 0.25 1 380 115 115 LYS CB C 31.576 0.25 1 381 115 115 LYS N N 120.997 0.14 1 382 116 116 LEU H H 8.309 0.05 1 383 116 116 LEU C C 179.386 0.25 1 384 116 116 LEU CA C 58.076 0.25 1 385 116 116 LEU CB C 41.676 0.25 1 386 116 116 LEU N N 121.797 0.14 1 387 117 117 LEU H H 7.987 0.1 1 388 117 117 LEU C C 179.086 0.25 1 389 117 117 LEU CA C 55.856 0.25 1 390 117 117 LEU CB C 40.366 0.25 1 391 117 117 LEU N N 116.497 0.14 1 392 118 118 LYS H H 7.280 0.05 1 393 118 118 LYS C C 178.186 0.25 1 394 118 118 LYS CA C 57.166 0.25 1 395 118 118 LYS CB C 31.496 0.25 1 396 118 118 LYS N N 116.597 0.14 1 397 119 119 THR H H 7.464 0.1 1 398 119 119 THR C C 174.286 0.25 1 399 119 119 THR CA C 61.786 0.25 1 400 119 119 THR CB C 70.946 0.25 1 401 119 119 THR N N 106.997 0.14 1 402 120 120 GLN H H 8.195 0.05 1 403 120 120 GLN C C 173.786 0.25 1 404 120 120 GLN CA C 54.676 0.25 1 405 120 120 GLN CB C 31.196 0.25 1 406 120 120 GLN N N 121.097 0.14 1 407 121 121 HIS H H 8.424 0.1 1 408 121 121 HIS C C 175.286 0.25 1 409 121 121 HIS CA C 54.186 0.25 1 410 121 121 HIS CB C 28.546 0.25 1 411 121 121 HIS N N 119.997 0.14 1 412 122 122 LEU H H 9.421 0.05 1 413 122 122 LEU C C 177.086 0.25 1 414 122 122 LEU CA C 54.056 0.25 1 415 122 122 LEU CB C 42.366 0.25 1 416 122 122 LEU N N 126.997 0.14 1 417 123 123 SER H H 8.862 0.05 1 418 123 123 SER CA C 56.786 0.25 1 419 123 123 SER CB C 64.196 0.25 1 420 123 123 SER N N 118.397 0.14 1 421 124 124 ASN C C 176.786 0.25 1 422 124 124 ASN CA C 56.956 0.25 1 423 124 124 ASN CB C 38.486 0.25 1 424 125 125 ASP H H 8.222 0.05 1 425 125 125 ASP C C 178.886 0.25 1 426 125 125 ASP CA C 56.676 0.25 1 427 125 125 ASP CB C 39.646 0.25 1 428 125 125 ASP N N 115.997 0.14 1 429 126 126 HIS H H 7.595 0.05 1 430 126 126 HIS C C 176.386 0.25 1 431 126 126 HIS CA C 58.956 0.25 1 432 126 126 HIS CB C 30.336 0.25 1 433 126 126 HIS N N 120.397 0.14 1 434 127 127 ILE H H 8.097 0.05 1 435 127 127 ILE C C 177.086 0.25 1 436 127 127 ILE CA C 66.026 0.25 1 437 127 127 ILE CB C 37.296 0.25 1 438 127 127 ILE N N 119.997 0.14 1 439 128 128 CYS H H 7.965 0.05 1 440 128 128 CYS C C 175.586 0.25 1 441 128 128 CYS CA C 62.686 0.25 1 442 128 128 CYS CB C 26.686 0.25 1 443 128 128 CYS N N 118.397 0.14 1 444 129 129 TYR H H 7.478 0.05 1 445 129 129 TYR CA C 58.676 0.25 1 446 129 129 TYR CB C 37.606 0.25 1 447 129 129 TYR N N 116.697 0.14 1 448 143 143 SER C C 175.386 0.25 1 449 143 143 SER CA C 61.206 0.25 1 450 144 144 ALA H H 7.462 0.05 1 451 144 144 ALA C C 176.086 0.25 1 452 144 144 ALA CA C 51.186 0.25 1 453 144 144 ALA CB C 17.786 0.25 1 454 144 144 ALA N N 126.397 0.14 1 455 145 145 ASN H H 8.469 0.05 1 456 145 145 ASN C C 173.086 0.25 1 457 145 145 ASN CA C 53.636 0.25 1 458 145 145 ASN CB C 37.286 0.25 1 459 145 145 ASN N N 115.697 0.14 1 460 146 146 VAL H H 7.563 0.05 1 461 146 146 VAL C C 172.386 0.25 1 462 146 146 VAL CA C 61.036 0.25 1 463 146 146 VAL CB C 33.506 0.25 1 464 146 146 VAL N N 118.997 0.14 1 465 147 147 LEU H H 8.677 0.05 1 466 147 147 LEU CA C 51.906 0.25 1 467 147 147 LEU N N 121.697 0.14 1 468 153 153 PRO C C 176.386 0.25 1 469 153 153 PRO CA C 66.696 0.25 1 470 154 154 SER H H 8.384 0.05 1 471 154 154 SER C C 173.586 0.25 1 472 154 154 SER CA C 60.496 0.25 1 473 154 154 SER CB C 61.626 0.25 1 474 154 154 SER N N 109.297 0.14 1 475 155 155 ASN H H 7.422 0.05 1 476 155 155 ASN CA C 52.006 0.25 1 477 155 155 ASN N N 117.997 0.14 1 478 156 156 LEU C C 174.886 0.25 1 479 157 157 LEU H H 8.547 0.05 1 480 157 157 LEU C C 173.786 0.25 1 481 157 157 LEU CA C 54.686 0.25 1 482 157 157 LEU N N 122.197 0.14 1 483 158 158 LEU H H 8.052 0.05 1 484 158 158 LEU C C 176.486 0.25 1 485 158 158 LEU CA C 53.086 0.25 1 486 158 158 LEU N N 124.097 0.14 1 487 159 159 ASN H H 7.498 0.05 1 488 159 159 ASN CA C 50.316 0.25 1 489 159 159 ASN CB C 40.376 0.25 1 490 159 159 ASN N N 117.497 0.14 1 491 160 160 THR C C 175.586 0.25 1 492 160 160 THR CA C 64.716 0.25 1 493 161 161 THR H H 7.437 0.05 1 494 161 161 THR C C 173.986 0.25 1 495 161 161 THR CA C 60.876 0.25 1 496 161 161 THR CB C 67.646 0.25 1 497 161 161 THR N N 110.697 0.14 1 498 162 162 CYS H H 8.189 0.05 1 499 162 162 CYS C C 172.386 0.25 1 500 162 162 CYS CA C 61.976 0.25 1 501 162 162 CYS CB C 24.166 0.25 1 502 162 162 CYS N N 111.797 0.14 1 503 163 163 ASP H H 8.309 0.05 1 504 163 163 ASP CA C 54.746 0.25 1 505 163 163 ASP CB C 39.716 0.25 1 506 163 163 ASP N N 119.197 0.14 1 507 166 166 ILE C C 175.486 0.25 1 508 166 166 ILE CA C 61.936 0.25 1 509 167 167 CYS H H 8.727 0.05 1 510 167 167 CYS C C 172.286 0.25 1 511 167 167 CYS CA C 55.196 0.25 1 512 167 167 CYS CB C 31.996 0.25 1 513 167 167 CYS N N 124.797 0.14 1 514 168 168 ASP H H 8.601 0.05 1 515 168 168 ASP CA C 55.136 0.25 1 516 168 168 ASP CB C 38.016 0.25 1 517 168 168 ASP N N 116.497 0.14 1 518 223 223 LEU C C 178.986 0.25 1 519 223 223 LEU CA C 56.386 0.25 1 520 224 224 SER H H 7.475 0.05 1 521 224 224 SER C C 174.286 0.25 1 522 224 224 SER CA C 58.336 0.25 1 523 224 224 SER CB C 66.526 0.25 1 524 224 224 SER N N 109.897 0.14 1 525 225 225 ASN H H 8.879 0.05 1 526 225 225 ASN C C 173.286 0.25 1 527 225 225 ASN CA C 56.186 0.25 1 528 225 225 ASN CB C 35.846 0.25 1 529 225 225 ASN N N 118.297 0.14 1 530 226 226 ARG H H 7.822 0.05 1 531 226 226 ARG CA C 53.116 0.25 1 532 226 226 ARG CB C 30.596 0.25 1 533 226 226 ARG N N 116.997 0.14 1 534 242 242 LEU C C 178.386 0.25 1 535 242 242 LEU CA C 56.886 0.25 1 536 243 243 GLY H H 7.736 0.05 1 537 243 243 GLY C C 174.086 0.25 1 538 243 243 GLY CA C 45.666 0.25 1 539 243 243 GLY N N 103.697 0.14 1 540 244 244 ILE H H 7.158 0.05 1 541 244 244 ILE C C 175.286 0.25 1 542 244 244 ILE CA C 61.866 0.25 1 543 244 244 ILE N N 119.397 0.14 1 544 245 245 LEU H H 8.594 0.05 1 545 245 245 LEU C C 178.986 0.25 1 546 245 245 LEU CA C 56.506 0.25 1 547 245 245 LEU N N 115.697 0.14 1 548 246 246 GLY H H 7.555 0.05 1 549 246 246 GLY C C 171.986 0.25 1 550 246 246 GLY CA C 42.596 0.25 1 551 246 246 GLY N N 106.897 0.14 1 552 247 247 SER H H 8.084 0.05 1 553 247 247 SER CA C 58.296 0.25 1 554 247 247 SER CB C 61.606 0.25 1 555 247 247 SER N N 114.897 0.14 1 556 248 248 PRO C C 176.186 0.25 1 557 248 248 PRO CA C 61.466 0.25 1 558 249 249 SER H H 8.917 0.05 1 559 249 249 SER C C 174.586 0.25 1 560 249 249 SER CA C 56.616 0.25 1 561 249 249 SER CB C 64.526 0.25 1 562 249 249 SER N N 118.297 0.14 1 563 250 250 GLN H H 8.844 0.05 1 564 250 250 GLN C C 178.486 0.25 1 565 250 250 GLN CA C 59.216 0.25 1 566 250 250 GLN CB C 27.236 0.25 1 567 250 250 GLN N N 120.697 0.14 1 568 251 251 GLU H H 8.413 0.05 1 569 251 251 GLU C C 178.986 0.25 1 570 251 251 GLU CA C 58.966 0.25 1 571 251 251 GLU CB C 28.356 0.25 1 572 251 251 GLU N N 118.397 0.14 1 573 252 252 ASP H H 7.722 0.05 1 574 252 252 ASP C C 179.086 0.25 1 575 252 252 ASP CA C 56.826 0.25 1 576 252 252 ASP CB C 39.976 0.25 1 577 252 252 ASP N N 121.397 0.14 1 578 253 253 LEU H H 8.218 0.05 1 579 253 253 LEU C C 178.986 0.25 1 580 253 253 LEU CA C 56.936 0.25 1 581 253 253 LEU N N 120.797 0.14 1 582 254 254 ASN H H 7.790 0.05 1 583 254 254 ASN C C 176.386 0.25 1 584 254 254 ASN CA C 54.426 0.25 1 585 254 254 ASN CB C 37.326 0.25 1 586 254 254 ASN N N 116.297 0.14 1 587 255 255 CYS H H 7.480 0.05 1 588 255 255 CYS C C 174.486 0.25 1 589 255 255 CYS CA C 58.916 0.25 1 590 255 255 CYS CB C 27.026 0.25 1 591 255 255 CYS N N 114.897 0.14 1 592 256 256 ILE H H 7.694 0.05 1 593 256 256 ILE CA C 59.576 0.25 1 594 256 256 ILE N N 123.997 0.14 1 595 262 262 ARG C C 177.886 0.25 1 596 262 262 ARG CA C 60.296 0.25 1 597 263 263 ASN H H 8.473 0.05 1 598 263 263 ASN C C 178.386 0.25 1 599 263 263 ASN CA C 55.396 0.25 1 600 263 263 ASN CB C 37.286 0.25 1 601 263 263 ASN N N 115.997 0.14 1 602 264 264 TYR H H 7.923 0.05 1 603 264 264 TYR C C 178.886 0.25 1 604 264 264 TYR CA C 61.016 0.25 1 605 264 264 TYR N N 122.197 0.14 1 606 265 265 LEU H H 8.183 0.05 1 607 265 265 LEU C C 180.186 0.25 1 608 265 265 LEU CA C 57.606 0.25 1 609 265 265 LEU N N 120.797 0.14 1 610 266 266 LEU H H 8.165 0.05 1 611 266 266 LEU C C 177.686 0.25 1 612 266 266 LEU CA C 56.576 0.25 1 613 266 266 LEU CB C 41.306 0.25 1 614 266 266 LEU N N 118.797 0.14 1 615 267 267 SER H H 7.442 0.05 1 616 267 267 SER C C 174.086 0.25 1 617 267 267 SER CA C 58.736 0.25 1 618 267 267 SER CB C 63.596 0.25 1 619 267 267 SER N N 114.297 0.14 1 620 268 268 LEU H H 6.836 0.05 1 621 268 268 LEU CA C 52.766 0.25 1 622 268 268 LEU CB C 39.946 0.25 1 623 268 268 LEU N N 124.097 0.14 1 624 269 269 PRO C C 176.086 0.25 1 625 269 269 PRO CA C 62.266 0.25 1 626 270 270 HIS H H 8.487 0.05 1 627 270 270 HIS C C 175.186 0.25 1 628 270 270 HIS CA C 57.446 0.25 1 629 270 270 HIS CB C 29.136 0.25 1 630 270 270 HIS N N 121.297 0.14 1 631 271 271 LYS H H 8.308 0.05 1 632 271 271 LYS C C 175.786 0.25 1 633 271 271 LYS CA C 53.366 0.25 1 634 271 271 LYS CB C 34.176 0.25 1 635 271 271 LYS N N 126.797 0.14 1 636 272 272 ASN H H 8.606 0.05 1 637 272 272 ASN C C 174.386 0.25 1 638 272 272 ASN CA C 51.786 0.25 1 639 272 272 ASN CB C 39.126 0.25 1 640 272 272 ASN N N 121.797 0.14 1 641 273 273 LYS H H 8.317 0.05 1 642 273 273 LYS C C 176.686 0.25 1 643 273 273 LYS CA C 56.086 0.25 1 644 273 273 LYS CB C 33.146 0.25 1 645 273 273 LYS N N 121.997 0.14 1 646 274 274 VAL H H 8.819 0.05 1 647 274 274 VAL CA C 59.316 0.25 1 648 274 274 VAL CB C 32.476 0.25 1 649 274 274 VAL N N 131.597 0.14 1 650 275 275 PRO C C 178.886 0.25 1 651 275 275 PRO CA C 61.946 0.25 1 652 275 275 PRO CB C 31.326 0.25 1 653 276 276 TRP H H 7.718 0.05 1 654 276 276 TRP C C 178.086 0.25 1 655 276 276 TRP CA C 59.366 0.25 1 656 276 276 TRP CB C 29.966 0.25 1 657 276 276 TRP N N 123.097 0.14 1 658 277 277 ASN H H 8.704 0.05 1 659 277 277 ASN C C 175.886 0.25 1 660 277 277 ASN CA C 54.366 0.25 1 661 277 277 ASN CB C 36.106 0.25 1 662 277 277 ASN N N 113.897 0.14 1 663 278 278 ARG H H 7.536 0.05 1 664 278 278 ARG C C 177.786 0.25 1 665 278 278 ARG CA C 56.636 0.25 1 666 278 278 ARG CB C 29.086 0.25 1 667 278 278 ARG N N 118.597 0.14 1 668 279 279 LEU H H 6.837 0.05 1 669 279 279 LEU C C 177.086 0.25 1 670 279 279 LEU CA C 56.096 0.25 1 671 279 279 LEU CB C 41.666 0.25 1 672 279 279 LEU N N 119.797 0.14 1 673 280 280 PHE H H 7.844 0.05 1 674 280 280 PHE CA C 53.546 0.25 1 675 280 280 PHE CB C 38.766 0.25 1 676 280 280 PHE N N 115.997 0.14 1 677 281 281 PRO C C 177.686 0.25 1 678 281 281 PRO CA C 64.416 0.25 1 679 281 281 PRO CB C 31.306 0.25 1 680 282 282 ASN H H 8.759 0.05 1 681 282 282 ASN C C 174.886 0.25 1 682 282 282 ASN CA C 52.166 0.25 1 683 282 282 ASN CB C 38.746 0.25 1 684 282 282 ASN N N 115.297 0.14 1 685 283 283 ALA H H 7.162 0.05 1 686 283 283 ALA C C 176.686 0.25 1 687 283 283 ALA CA C 51.146 0.25 1 688 283 283 ALA CB C 20.796 0.25 1 689 283 283 ALA N N 122.997 0.14 1 690 284 284 ASP H H 8.595 0.05 1 691 284 284 ASP C C 177.686 0.25 1 692 284 284 ASP CA C 54.426 0.25 1 693 284 284 ASP CB C 42.666 0.25 1 694 284 284 ASP N N 122.297 0.14 1 695 285 285 SER H H 8.916 0.05 1 696 285 285 SER C C 177.786 0.25 1 697 285 285 SER CA C 61.996 0.25 1 698 285 285 SER N N 122.997 0.14 1 699 286 286 LYS H H 8.968 0.05 1 700 286 286 LYS C C 178.786 0.25 1 701 286 286 LYS CA C 59.276 0.25 1 702 286 286 LYS CB C 31.316 0.25 1 703 286 286 LYS N N 123.597 0.14 1 704 287 287 ALA H H 7.139 0.05 1 705 287 287 ALA C C 179.386 0.25 1 706 287 287 ALA CA C 54.476 0.25 1 707 287 287 ALA CB C 16.156 0.25 1 708 287 287 ALA N N 122.297 0.14 1 709 288 288 LEU H H 7.270 0.05 1 710 288 288 LEU C C 178.686 0.25 1 711 288 288 LEU CA C 56.106 0.25 1 712 288 288 LEU CB C 39.706 0.25 1 713 288 288 LEU N N 112.797 0.14 1 714 289 289 ASP H H 7.499 0.05 1 715 289 289 ASP CA C 57.496 0.25 1 716 289 289 ASP CB C 42.536 0.25 1 717 289 289 ASP N N 120.797 0.14 1 718 296 296 THR C C 174.786 0.25 1 719 296 296 THR CA C 60.986 0.25 1 720 296 296 THR CB C 70.446 0.25 1 721 297 297 PHE H H 9.641 0.05 1 722 297 297 PHE C C 174.586 0.25 1 723 297 297 PHE CA C 62.446 0.25 1 724 297 297 PHE CB C 39.266 0.25 1 725 297 297 PHE N N 129.997 0.14 1 726 298 298 ASN H H 8.743 0.05 1 727 298 298 ASN CA C 50.116 0.25 1 728 298 298 ASN CB C 38.486 0.25 1 729 298 298 ASN N N 117.097 0.14 1 730 299 299 PRO C C 178.286 0.25 1 731 299 299 PRO CA C 64.066 0.25 1 732 300 300 HIS H H 8.217 0.05 1 733 300 300 HIS C C 176.386 0.25 1 734 300 300 HIS CA C 57.116 0.25 1 735 300 300 HIS CB C 28.836 0.25 1 736 300 300 HIS N N 116.597 0.14 1 737 301 301 LYS H H 7.310 0.05 1 738 301 301 LYS C C 175.586 0.25 1 739 301 301 LYS CA C 55.076 0.25 1 740 301 301 LYS CB C 33.176 0.25 1 741 301 301 LYS N N 116.897 0.14 1 742 302 302 ARG H H 6.980 0.05 1 743 302 302 ARG C C 175.786 0.25 1 744 302 302 ARG CA C 56.676 0.25 1 745 302 302 ARG CB C 30.556 0.25 1 746 302 302 ARG N N 123.197 0.14 1 747 303 303 ILE H H 7.358 0.05 1 748 303 303 ILE C C 173.486 0.25 1 749 303 303 ILE CA C 62.286 0.25 1 750 303 303 ILE N N 127.297 0.14 1 751 304 304 GLU H H 8.118 0.05 1 752 304 304 GLU C C 179.186 0.25 1 753 304 304 GLU CA C 55.216 0.25 1 754 304 304 GLU N N 123.597 0.14 1 755 305 305 VAL H H 8.820 0.05 1 756 305 305 VAL C C 175.686 0.25 1 757 305 305 VAL CA C 66.726 0.25 1 758 305 305 VAL CB C 30.376 0.25 1 759 305 305 VAL N N 121.497 0.14 1 760 306 306 GLU H H 8.985 0.05 1 761 306 306 GLU C C 179.086 0.25 1 762 306 306 GLU CA C 60.206 0.25 1 763 306 306 GLU CB C 27.956 0.25 1 764 306 306 GLU N N 120.197 0.14 1 765 307 307 GLN H H 6.905 0.05 1 766 307 307 GLN CA C 57.466 0.25 1 767 307 307 GLN CB C 27.556 0.25 1 768 307 307 GLN N N 116.097 0.14 1 769 314 314 LEU C C 177.686 0.25 1 770 314 314 LEU CA C 53.376 0.25 1 771 315 315 GLU H H 7.172 0.05 1 772 315 315 GLU C C 177.386 0.25 1 773 315 315 GLU CA C 58.936 0.25 1 774 315 315 GLU CB C 28.986 0.25 1 775 315 315 GLU N N 120.997 0.14 1 776 316 316 GLN H H 8.864 0.05 1 777 316 316 GLN C C 175.586 0.25 1 778 316 316 GLN CA C 57.146 0.25 1 779 316 316 GLN CB C 27.546 0.25 1 780 316 316 GLN N N 117.497 0.14 1 781 317 317 TYR H H 7.428 0.05 1 782 317 317 TYR C C 174.886 0.25 1 783 317 317 TYR CA C 57.976 0.25 1 784 317 317 TYR N N 116.497 0.14 1 785 318 318 TYR H H 7.254 0.05 1 786 318 318 TYR C C 176.486 0.25 1 787 318 318 TYR CA C 57.426 0.25 1 788 318 318 TYR CB C 38.186 0.25 1 789 318 318 TYR N N 117.797 0.14 1 790 319 319 ASP H H 9.254 0.05 1 791 319 319 ASP CA C 50.956 0.25 1 792 319 319 ASP CB C 39.476 0.25 1 793 319 319 ASP N N 127.397 0.14 1 794 320 320 PRO C C 178.586 0.25 1 795 320 320 PRO CA C 63.976 0.25 1 796 321 321 SER H H 7.911 0.05 1 797 321 321 SER C C 174.286 0.25 1 798 321 321 SER CA C 59.935 0.25 1 799 321 321 SER CB C 62.696 0.25 1 800 321 321 SER N N 114.097 0.14 1 801 322 322 ASP H H 8.269 0.05 1 802 322 322 ASP C C 175.786 0.25 1 803 322 322 ASP CA C 52.436 0.25 1 804 322 322 ASP CB C 42.626 0.25 1 805 322 322 ASP N N 123.597 0.14 1 806 323 323 GLU H H 7.299 0.05 1 807 323 323 GLU CA C 53.446 0.25 1 808 323 323 GLU CB C 29.256 0.25 1 809 323 323 GLU N N 121.297 0.14 1 810 324 324 PRO C C 176.686 0.25 1 811 324 324 PRO CA C 63.146 0.25 1 812 325 325 ILE H H 7.916 0.05 1 813 325 325 ILE C C 175.686 0.25 1 814 325 325 ILE CA C 59.106 0.25 1 815 325 325 ILE CB C 40.986 0.25 1 816 325 325 ILE N N 111.597 0.14 1 817 326 326 ALA H H 8.460 0.05 1 818 326 326 ALA C C 178.086 0.25 1 819 326 326 ALA CA C 51.406 0.25 1 820 326 326 ALA CB C 17.446 0.25 1 821 326 326 ALA N N 124.697 0.14 1 822 327 327 GLU H H 8.758 0.05 1 823 327 327 GLU C C 175.786 0.25 1 824 327 327 GLU CA C 57.696 0.25 1 825 327 327 GLU CB C 28.966 0.25 1 826 327 327 GLU N N 121.497 0.14 1 827 328 328 ALA H H 7.586 0.05 1 828 328 328 ALA CA C 49.386 0.25 1 829 328 328 ALA CB C 19.086 0.25 1 830 328 328 ALA N N 119.997 0.14 1 831 336 336 LEU C C 178.386 0.25 1 832 336 336 LEU CA C 55.506 0.25 1 833 337 337 ASP H H 8.173 0.05 1 834 337 337 ASP C C 176.386 0.25 1 835 337 337 ASP CA C 56.916 0.25 1 836 337 337 ASP N N 116.597 0.14 1 837 338 338 ASP H H 8.072 0.05 1 838 338 338 ASP C C 176.286 0.25 1 839 338 338 ASP CA C 53.256 0.25 1 840 338 338 ASP CB C 40.596 0.25 1 841 338 338 ASP N N 115.397 0.14 1 842 339 339 LEU H H 7.105 0.05 1 843 339 339 LEU CA C 52.386 0.25 1 844 339 339 LEU CB C 41.226 0.25 1 845 339 339 LEU N N 121.497 0.14 1 846 340 340 PRO C C 178.886 0.25 1 847 340 340 PRO CA C 61.536 0.25 1 848 341 341 LYS H H 9.398 0.05 1 849 341 341 LYS C C 178.086 0.25 1 850 341 341 LYS CA C 59.736 0.25 1 851 341 341 LYS CB C 31.066 0.25 1 852 341 341 LYS N N 121.897 0.14 1 853 342 342 GLU H H 9.602 0.05 1 854 342 342 GLU C C 178.886 0.25 1 855 342 342 GLU CA C 60.566 0.25 1 856 342 342 GLU CB C 27.376 0.25 1 857 342 342 GLU N N 122.397 0.14 1 858 343 343 LYS H H 6.924 0.05 1 859 343 343 LYS C C 178.986 0.25 1 860 343 343 LYS CA C 56.356 0.25 1 861 343 343 LYS CB C 30.446 0.25 1 862 343 343 LYS N N 120.397 0.14 1 863 344 344 LEU H H 7.947 0.05 1 864 344 344 LEU C C 178.886 0.25 1 865 344 344 LEU CA C 57.906 0.25 1 866 344 344 LEU CB C 41.586 0.25 1 867 344 344 LEU N N 118.797 0.14 1 868 345 345 LYS H H 8.292 0.05 1 869 345 345 LYS C C 177.986 0.25 1 870 345 345 LYS CA C 60.766 0.25 1 871 345 345 LYS CB C 30.326 0.25 1 872 345 345 LYS N N 119.497 0.14 1 873 346 346 GLU H H 7.203 0.05 1 874 346 346 GLU C C 179.186 0.25 1 875 346 346 GLU CA C 59.366 0.25 1 876 346 346 GLU CB C 28.696 0.25 1 877 346 346 GLU N N 119.497 0.14 1 878 347 347 LEU H H 8.196 0.05 1 879 347 347 LEU C C 180.586 0.25 1 880 347 347 LEU CA C 57.616 0.25 1 881 347 347 LEU CB C 40.936 0.25 1 882 347 347 LEU N N 119.797 0.14 1 883 348 348 ILE H H 8.729 0.05 1 884 348 348 ILE C C 178.486 0.25 1 885 348 348 ILE CA C 65.676 0.25 1 886 348 348 ILE CB C 37.486 0.25 1 887 348 348 ILE N N 121.597 0.14 1 888 349 349 PHE H H 8.822 0.05 1 889 349 349 PHE C C 177.386 0.25 1 890 349 349 PHE CA C 62.936 0.25 1 891 349 349 PHE CB C 38.666 0.25 1 892 349 349 PHE N N 124.797 0.14 1 893 350 350 GLU H H 8.467 0.05 1 894 350 350 GLU C C 179.986 0.25 1 895 350 350 GLU CA C 59.096 0.25 1 896 350 350 GLU CB C 28.816 0.25 1 897 350 350 GLU N N 119.297 0.14 1 898 351 351 GLU H H 8.551 0.05 1 899 351 351 GLU CA C 57.946 0.25 1 900 351 351 GLU CB C 29.246 0.25 1 901 351 351 GLU N N 119.397 0.14 1 902 352 352 THR C C 175.886 0.25 1 903 352 352 THR CA C 61.266 0.25 1 904 353 353 ALA H H 7.360 0.05 1 905 353 353 ALA C C 179.086 0.25 1 906 353 353 ALA CA C 55.116 0.25 1 907 353 353 ALA CB C 16.866 0.25 1 908 353 353 ALA N N 128.597 0.14 1 909 354 354 ARG H H 7.646 0.05 1 910 354 354 ARG C C 175.586 0.25 1 911 354 354 ARG CA C 56.276 0.25 1 912 354 354 ARG N N 113.797 0.14 1 913 355 355 PHE H H 6.880 0.05 1 914 355 355 PHE C C 176.086 0.25 1 915 355 355 PHE CA C 57.986 0.25 1 916 355 355 PHE CB C 39.636 0.25 1 917 355 355 PHE N N 116.597 0.14 1 918 356 356 GLN H H 7.753 0.05 1 919 356 356 GLN CA C 53.256 0.25 1 920 356 356 GLN CB C 27.416 0.25 1 921 356 356 GLN N N 120.797 0.14 1 922 357 357 PRO C C 178.086 0.25 1 923 357 357 PRO CA C 63.526 0.25 1 924 358 358 GLY H H 8.681 0.05 1 925 358 358 GLY C C 174.286 0.25 1 926 358 358 GLY CA C 44.836 0.25 1 927 358 358 GLY N N 110.697 0.14 1 928 359 359 TYR H H 7.596 0.05 1 929 359 359 TYR C C 175.786 0.25 1 930 359 359 TYR CA C 58.936 0.25 1 931 359 359 TYR CB C 38.056 0.25 1 932 359 359 TYR N N 121.597 0.14 1 933 360 360 ARG H H 7.892 0.05 1 934 360 360 ARG C C 174.586 0.25 1 935 360 360 ARG CA C 55.096 0.25 1 936 360 360 ARG CB C 30.156 0.25 1 937 360 360 ARG N N 125.597 0.14 1 938 361 361 SER H H 7.692 0.05 1 939 361 361 SER CA C 59.636 0.25 1 940 361 361 SER CB C 64.136 0.25 1 941 361 361 SER N N 122.997 0.14 1 stop_ save_