data_6468
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H, 13C and 15N backbone resonance assignment of p38 mitogen-activated protein
kinase
;
_BMRB_accession_number 6468
_BMRB_flat_file_name bmr6468.str
_Entry_type original
_Submission_date 2005-01-21
_Accession_date 2005-01-21
_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 Vogtherr Martin . .
2 Saxena Krishna . .
3 Grimme Susanne . .
4 Betz Marco . .
5 Schieborr Ulrich . .
6 Pescatore Barbara . .
7 Langer Thomas . .
8 Schwalbe Harald . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 219
"13C chemical shifts" 684
"15N chemical shifts" 219
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2006-01-06 original author .
stop_
_Original_release_date 2006-01-06
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Vogtherr Martin . .
2 Saxena Krishna . .
3 Grimme Susanne . .
4 Betz Marco . .
5 Schieborr Ulrich . .
6 Pescatore Barbara . .
7 Langer Thomas . .
8 Schwalbe Harald . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 32
_Journal_issue 2
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 175
_Page_last 175
_Year 2005
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_p38
_Saveframe_category molecular_system
_Mol_system_name 'mitogen-activated protein kinase p38 alpha'
_Abbreviation_common p38
_Enzyme_commission_number 2.7.1.-
loop_
_Mol_system_component_name
_Mol_label
'p38 alpha' $p38
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Biological_function
'protein kinase'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_p38
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'mitogen-activated protein kinase p38 alpha'
_Abbreviation_common p38
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 351
_Mol_residue_sequence
;
GHNSQERPTFYRQELNKTIW
EVPERYQNLSPVGSGAYGSV
CAAFDTKTGHRVAVKKLSRP
FQSIIHAKRTYRELRLLKHM
KHENVIGLLDVFTPARSLEE
FNDVYLVTHLMGADLNNIVK
CQKLTDDHVQFLIYQILRGL
KYIHSADIIHRDLKPSNLAV
NEDCELKILDFGLARHTDDE
MTGYVATRWYRAPEIMLNWM
HYNQTVDIWSVGCIMAELLT
GRTLFPGTDHIDQLKLILRL
VGTPGAELLKKISSESARNY
IQSLAQMPKMNFANVFIGAN
PLAVDLLEKMLVLDSDKRIT
AAQALAHAYFAQYHDPDDEP
VADPYDQSFESRDLLIDEWK
SLTYDEVISFV
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 -2 GLY 2 -1 HIS 3 1 ASN 4 2 SER 5 3 GLN
6 4 GLU 7 5 ARG 8 6 PRO 9 7 THR 10 8 PHE
11 9 TYR 12 10 ARG 13 11 GLN 14 12 GLU 15 13 LEU
16 14 ASN 17 15 LYS 18 16 THR 19 17 ILE 20 18 TRP
21 19 GLU 22 20 VAL 23 21 PRO 24 22 GLU 25 23 ARG
26 24 TYR 27 25 GLN 28 26 ASN 29 27 LEU 30 28 SER
31 29 PRO 32 30 VAL 33 31 GLY 34 32 SER 35 33 GLY
36 34 ALA 37 35 TYR 38 36 GLY 39 37 SER 40 38 VAL
41 39 CYS 42 40 ALA 43 41 ALA 44 42 PHE 45 43 ASP
46 44 THR 47 45 LYS 48 46 THR 49 47 GLY 50 48 HIS
51 49 ARG 52 50 VAL 53 51 ALA 54 52 VAL 55 53 LYS
56 54 LYS 57 55 LEU 58 56 SER 59 57 ARG 60 58 PRO
61 59 PHE 62 60 GLN 63 61 SER 64 62 ILE 65 63 ILE
66 64 HIS 67 65 ALA 68 66 LYS 69 67 ARG 70 68 THR
71 69 TYR 72 70 ARG 73 71 GLU 74 72 LEU 75 73 ARG
76 74 LEU 77 75 LEU 78 76 LYS 79 77 HIS 80 78 MET
81 79 LYS 82 80 HIS 83 81 GLU 84 82 ASN 85 83 VAL
86 84 ILE 87 85 GLY 88 86 LEU 89 87 LEU 90 88 ASP
91 89 VAL 92 90 PHE 93 91 THR 94 92 PRO 95 93 ALA
96 94 ARG 97 95 SER 98 96 LEU 99 97 GLU 100 98 GLU
101 99 PHE 102 100 ASN 103 101 ASP 104 102 VAL 105 103 TYR
106 104 LEU 107 105 VAL 108 106 THR 109 107 HIS 110 108 LEU
111 109 MET 112 110 GLY 113 111 ALA 114 112 ASP 115 113 LEU
116 114 ASN 117 115 ASN 118 116 ILE 119 117 VAL 120 118 LYS
121 119 CYS 122 120 GLN 123 121 LYS 124 122 LEU 125 123 THR
126 124 ASP 127 125 ASP 128 126 HIS 129 127 VAL 130 128 GLN
131 129 PHE 132 130 LEU 133 131 ILE 134 132 TYR 135 133 GLN
136 134 ILE 137 135 LEU 138 136 ARG 139 137 GLY 140 138 LEU
141 139 LYS 142 140 TYR 143 141 ILE 144 142 HIS 145 143 SER
146 144 ALA 147 145 ASP 148 146 ILE 149 147 ILE 150 148 HIS
151 149 ARG 152 150 ASP 153 151 LEU 154 152 LYS 155 153 PRO
156 154 SER 157 155 ASN 158 156 LEU 159 157 ALA 160 158 VAL
161 159 ASN 162 160 GLU 163 161 ASP 164 162 CYS 165 163 GLU
166 164 LEU 167 165 LYS 168 166 ILE 169 167 LEU 170 168 ASP
171 169 PHE 172 170 GLY 173 171 LEU 174 172 ALA 175 173 ARG
176 174 HIS 177 175 THR 178 176 ASP 179 177 ASP 180 178 GLU
181 179 MET 182 180 THR 183 181 GLY 184 182 TYR 185 183 VAL
186 184 ALA 187 185 THR 188 186 ARG 189 187 TRP 190 188 TYR
191 189 ARG 192 190 ALA 193 191 PRO 194 192 GLU 195 193 ILE
196 194 MET 197 195 LEU 198 196 ASN 199 197 TRP 200 198 MET
201 199 HIS 202 200 TYR 203 201 ASN 204 202 GLN 205 203 THR
206 204 VAL 207 205 ASP 208 206 ILE 209 207 TRP 210 208 SER
211 209 VAL 212 210 GLY 213 211 CYS 214 212 ILE 215 213 MET
216 214 ALA 217 215 GLU 218 216 LEU 219 217 LEU 220 218 THR
221 219 GLY 222 220 ARG 223 221 THR 224 222 LEU 225 223 PHE
226 224 PRO 227 225 GLY 228 226 THR 229 227 ASP 230 228 HIS
231 229 ILE 232 230 ASP 233 231 GLN 234 232 LEU 235 233 LYS
236 234 LEU 237 235 ILE 238 236 LEU 239 237 ARG 240 238 LEU
241 239 VAL 242 240 GLY 243 241 THR 244 242 PRO 245 243 GLY
246 244 ALA 247 245 GLU 248 246 LEU 249 247 LEU 250 248 LYS
251 249 LYS 252 250 ILE 253 251 SER 254 252 SER 255 253 GLU
256 254 SER 257 255 ALA 258 256 ARG 259 257 ASN 260 258 TYR
261 259 ILE 262 260 GLN 263 261 SER 264 262 LEU 265 263 ALA
266 264 GLN 267 265 MET 268 266 PRO 269 267 LYS 270 268 MET
271 269 ASN 272 270 PHE 273 271 ALA 274 272 ASN 275 273 VAL
276 274 PHE 277 275 ILE 278 276 GLY 279 277 ALA 280 278 ASN
281 279 PRO 282 280 LEU 283 281 ALA 284 282 VAL 285 283 ASP
286 284 LEU 287 285 LEU 288 286 GLU 289 287 LYS 290 288 MET
291 289 LEU 292 290 VAL 293 291 LEU 294 292 ASP 295 293 SER
296 294 ASP 297 295 LYS 298 296 ARG 299 297 ILE 300 298 THR
301 299 ALA 302 300 ALA 303 301 GLN 304 302 ALA 305 303 LEU
306 304 ALA 307 305 HIS 308 306 ALA 309 307 TYR 310 308 PHE
311 309 ALA 312 310 GLN 313 311 TYR 314 312 HIS 315 313 ASP
316 314 PRO 317 315 ASP 318 316 ASP 319 317 GLU 320 318 PRO
321 319 VAL 322 320 ALA 323 321 ASP 324 322 PRO 325 323 TYR
326 324 ASP 327 325 GLN 328 326 SER 329 327 PHE 330 328 GLU
331 329 SER 332 330 ARG 333 331 ASP 334 332 LEU 335 333 LEU
336 334 ILE 337 335 ASP 338 336 GLU 339 337 TRP 340 338 LYS
341 339 SER 342 340 LEU 343 341 THR 344 342 TYR 345 343 ASP
346 344 GLU 347 345 VAL 348 346 ILE 349 347 SER 350 348 PHE
351 349 VAL
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-29
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 17471 p38_alpha 100.28 352 98.86 98.86 0.00e+00
BMRB 17940 p38alpha 99.43 349 100.00 100.00 0.00e+00
BMRB 19930 Non-phosphorylated_human_p38_alpha_(apo) 99.72 367 99.14 99.43 0.00e+00
BMRB 19934 Dual-phosphorylated_human_p38_alpha_(apo) 99.72 367 98.57 98.86 0.00e+00
BMRB 19935 Dual-phosphorylated_human_p38_alpha 99.72 367 98.57 98.86 0.00e+00
BMRB 19936 dual-phosphorylated_human_p38_alpha_(apo) 99.72 367 98.57 98.86 0.00e+00
BMRB 19937 dual-phosphorylated_human_p38_alpha_(apo) 99.72 367 98.57 98.86 0.00e+00
PDB 1A9U "The Complex Structure Of The Map Kinase P38SB203580" 100.00 379 98.86 98.86 0.00e+00
PDB 1BL6 "The Complex Structure Of The Map Kinase P38SB216995" 100.00 379 98.86 98.86 0.00e+00
PDB 1BL7 "The Complex Structure Of The Map Kinase P38SB220025" 100.00 379 98.86 98.86 0.00e+00
PDB 1BMK "The Complex Structure Of The Map Kinase P38SB218655" 100.00 379 99.43 99.43 0.00e+00
PDB 1DI9 "The Structure Of P38 Mitogen-Activated Protein Kinase In Complex With 4-[3-Methylsulfanylanilino]-6,7- Dimethoxyquinazoline" 99.15 360 99.43 99.43 0.00e+00
PDB 1IAN "Human P38 Map Kinase Inhibitor Complex" 99.72 366 99.14 99.43 0.00e+00
PDB 1KV1 "P38 Map Kinase In Complex With Inhibitor 1" 99.15 360 99.43 99.43 0.00e+00
PDB 1KV2 "Human P38 Map Kinase In Complex With Birb 796" 99.15 360 99.43 99.43 0.00e+00
PDB 1LEW "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Nuclear Substrate Mef2a" 99.15 360 100.00 100.00 0.00e+00
PDB 1LEZ "Crystal Structure Of Map Kinase P38 Complexed To The Docking Site On Its Activator Mkk3b" 99.15 360 100.00 100.00 0.00e+00
PDB 1M7Q "Crystal Structure Of P38 Map Kinase In Complex With A Dihydroquinazolinone Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 1OUK "The Structure Of P38 Alpha In Complex With A Pyridinylimidazole Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 1OUY "The Structure Of P38 Alpha In Complex With A Dihydropyrido- Pyrimidine Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 1OVE "The Structure Of P38 Alpha In Complex With A Dihydroquinolinone" 99.15 366 99.14 99.14 0.00e+00
PDB 1OZ1 "P38 Mitogen-Activated Kinase In Complex With 4-Azaindole Inhibitor" 100.00 372 98.86 98.86 0.00e+00
PDB 1P38 "The Structure Of The Map Kinase P38 At 2.1 Angstoms Resolution" 100.00 379 99.43 99.43 0.00e+00
PDB 1R39 "The Structure Of P38alpha" 99.15 366 99.43 99.43 0.00e+00
PDB 1R3C "The Structure Of P38alpha C162s Mutant" 99.15 366 99.14 99.14 0.00e+00
PDB 1W7H "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 1W82 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 1W83 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 1W84 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 1WBN "Fragment Based P38 Inhibitors" 99.15 360 99.43 99.43 0.00e+00
PDB 1WBO "Fragment Based P38 Inhibitors" 99.15 360 99.43 99.43 0.00e+00
PDB 1WBS "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 99.15 360 99.43 99.43 0.00e+00
PDB 1WBT "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-based Lead Generation." 99.15 360 99.43 99.43 0.00e+00
PDB 1WBV "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 99.15 360 99.43 99.43 0.00e+00
PDB 1WBW "Identification Of Novel P38 Alpha Map Kinase Inhibitors Using Fragment-Based Lead Generation." 99.15 360 99.43 99.43 0.00e+00
PDB 1WFC "Structure Of Apo, Unphosphorylated, P38 Mitogen Activated Protein Kinase P38 (P38 Map Kinase) The Mammalian Homologue Of The Ye" 99.15 366 99.43 99.43 0.00e+00
PDB 1YQJ "Crystal Structure Of P38 Alpha In Complex With A Selective Pyridazine Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 1YW2 "Mutated Mus Musculus P38 Kinase (Mp38)" 99.15 360 99.43 99.71 0.00e+00
PDB 1YWR "Crystal Structure Analysis Of Inactive P38 Kinase Domain In Complex With A Monocyclic Pyrazolone Inhibitor" 99.15 360 99.14 99.43 0.00e+00
PDB 1ZYJ "Human P38 Map Kinase In Complex With Inhibitor 1a" 99.15 360 99.43 99.43 0.00e+00
PDB 1ZZ2 "Two Classes Of P38alpha Map Kinase Inhibitors Having A Common Diphenylether Core But Exhibiting Divergent Binding Modes" 99.15 360 99.43 99.43 0.00e+00
PDB 1ZZL "Crystal Structure Of P38 With Triazolopyridine" 98.58 351 99.42 99.42 0.00e+00
PDB 2BAJ "P38alpha Bound To Pyrazolourea" 99.72 365 99.14 99.43 0.00e+00
PDB 2BAK "P38alpha Map Kinase Bound To Mpaq" 99.72 365 99.14 99.43 0.00e+00
PDB 2BAL "P38alpha Map Kinase Bound To Pyrazoloamine" 99.72 365 98.86 99.14 0.00e+00
PDB 2BAQ "P38alpha Bound To Ro3201195" 99.72 365 98.57 99.14 0.00e+00
PDB 2EWA "Dual Binding Mode Of Pyridinylimidazole To Map Kinase P38" 100.00 379 98.86 98.86 0.00e+00
PDB 2FSL "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-A" 99.72 367 98.57 98.86 0.00e+00
PDB 2FSM "Mitogen Activated Protein Kinase P38alpha (D176a+f327s) Activating Mutant Form-B" 99.72 367 98.57 98.86 0.00e+00
PDB 2FSO "Mitogen Activated Protein Kinase P38alpha (D176a) Activating Mutant" 99.72 367 98.86 99.14 0.00e+00
PDB 2FST "Mitogen Activated Protein Kinase P38alpha (d176a+f327l) Activating Mutant" 99.72 367 98.57 98.86 0.00e+00
PDB 2GFS "P38 Kinase Crystal Structure In Complex With Ro3201195" 100.00 372 98.86 98.86 0.00e+00
PDB 2GHL "Mutant Mus Musculus P38 Kinase Domain In Complex With Inhibitor Pg-874743" 98.29 348 99.42 99.71 0.00e+00
PDB 2GHM "Mutated Map Kinase P38 (Mus Musculus) In Complex With Inhbitor Pg-895449" 98.29 348 99.42 99.71 0.00e+00
PDB 2GTM "Mutated Mouse P38 Map Kinase Domain In Complex With Inhibitor Pg-892579" 98.29 348 100.00 100.00 0.00e+00
PDB 2GTN "Mutated Map Kinase P38 (mus Musculus) In Complex With Inhbitor Pg-951717" 98.29 348 100.00 100.00 0.00e+00
PDB 2I0H "The Structure Of P38alpha In Complex With An Arylpyridazinone" 99.15 366 99.14 99.14 0.00e+00
PDB 2LGC "Joint Nmr And X-Ray Refinement Reveals The Structure Of A Novel Dibenzo[a,D]cycloheptenone InhibitorP38 MAP KINASE COMPLEX IN S" 99.15 359 99.43 99.43 0.00e+00
PDB 2NPQ "A Novel Lipid Binding Site In The P38 Alpha Map Kinase" 99.72 367 99.14 99.43 0.00e+00
PDB 2OKR "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 99.15 366 99.43 99.43 0.00e+00
PDB 2ONL "Crystal Structure Of The P38a-Mapkap Kinase 2 Heterodimer" 99.15 366 99.43 99.43 0.00e+00
PDB 2OZA "Structure Of P38alpha Complex" 99.72 366 99.71 100.00 0.00e+00
PDB 2PUU "Crystal Structure Of P38 Complex With 1-(5-Tert-Butyl-2-P- Tolyl-2h-Pyrazol-3-Yl)-3-[4-(6-Morpholin-4-Ylmethyl- Pyridin-3-Yl)na" 98.29 348 99.42 99.42 0.00e+00
PDB 2QD9 "P38 Alpha Map Kinase Inhibitor Based On Heterobicyclic Scaffolds" 99.72 366 99.14 99.43 0.00e+00
PDB 2RG5 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11b" 99.72 366 99.14 99.43 0.00e+00
PDB 2RG6 "Phenylalanine Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 11j" 99.72 366 99.14 99.43 0.00e+00
PDB 2Y8O "Crystal Structure Of Human P38alpha Complexed With A Mapk Docking Peptide" 100.00 362 98.58 98.58 0.00e+00
PDB 2YIS "Triazolopyridine Inhibitors Of P38 Kinase." 99.15 359 99.43 99.43 0.00e+00
PDB 2YIW "Triazolopyridine Inhibitors Of P38 Kinase" 99.15 359 99.43 99.43 0.00e+00
PDB 2YIX "Triazolopyridine Inhibitors Of P38" 98.58 351 99.42 99.42 0.00e+00
PDB 2ZAZ "Crystal Structure Of P38 In Complex With 4-Anilino Quinoline Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 2ZB0 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 2ZB1 "Crystal Structure Of P38 In Complex With Biphenyl Amide Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 3BV2 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 30" 99.72 366 99.14 99.43 0.00e+00
PDB 3BV3 "Morpholino Pyrrolotriazine P38 Alpha Map Kinase Inhibitor Compound 2" 99.72 366 99.14 99.43 0.00e+00
PDB 3BX5 "P38 Alpha Map Kinase Complexed With Bms-640994" 99.72 366 99.14 99.43 0.00e+00
PDB 3C5U "P38 Alpha Map Kinase Complexed With A Benzothiazole Based Inhibitor" 99.72 366 99.14 99.43 0.00e+00
PDB 3CTQ "Structure Of Map Kinase P38 In Complex With A 1-O-Tolyl-1,2, 3-Triazole-4-Carboxamide" 98.29 348 99.42 99.42 0.00e+00
PDB 3D7Z "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 99.15 360 99.14 99.14 0.00e+00
PDB 3D83 "Crystal Structure Of P38 Kinase In Complex With A Biphenyl Amide Inhibitor" 99.15 360 98.85 98.85 0.00e+00
PDB 3DS6 "P38 Complex With A Phthalazine Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 3DT1 "P38 Complexed With A Quinazoline Inhibitor" 99.15 383 99.43 99.43 0.00e+00
PDB 3E92 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 99.15 371 99.14 99.14 0.00e+00
PDB 3E93 "Crystal Structure Of P38 Kinase In Complex With A Biaryl Amide Inhibitor" 99.15 371 99.14 99.14 0.00e+00
PDB 3FC1 "Crystal Structure Of P38 Kinase Bound To Pyrimido-Pyridazinone Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 3FI4 "P38 Kinase Crystal Structure In Complex With Ro4499" 100.00 372 98.58 98.86 0.00e+00
PDB 3FKL "P38 Kinase Crystal Structure In Complex With Ro9552" 100.00 372 98.86 98.86 0.00e+00
PDB 3FKN "P38 Kinase Crystal Structure In Complex With Ro7125" 100.00 372 98.86 98.86 0.00e+00
PDB 3FKO "P38 Kinase Crystal Structure In Complex With Ro3668" 100.00 372 98.58 98.86 0.00e+00
PDB 3FL4 "P38 Kinase Crystal Structure In Complex With Ro5634" 100.00 372 98.86 98.86 0.00e+00
PDB 3FLN "P38 Kinase Crystal Structure In Complex With R1487" 100.00 372 98.58 98.86 0.00e+00
PDB 3FLQ "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((S)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" 100.00 372 98.86 98.86 0.00e+00
PDB 3FLS "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-((R)-2-Methanesulfonyl-1-Methyl- Ethylamino)-8-Methyl-" 100.00 372 98.86 98.86 0.00e+00
PDB 3FLW "P38 Kinase Crystal Structure In Complex With Pamapimod" 100.00 372 98.86 98.86 0.00e+00
PDB 3FLY "P38 Kinase Crystal Structure In Complex With 6-(2,4- Difluoro-Phenoxy)-2-Isopropylamino-8-Methyl-8h-Pyrido[2,3- D]pyrimidin-7-O" 100.00 372 98.86 98.86 0.00e+00
PDB 3FLZ "P38 Kinase Crystal Structure In Complex With 8-Methyl-6-Phenoxy-2- (Tetrahydro-Pyran-4-Ylamino)-8h-Pyrido[2,3-D]pyrimidin-7-One" 100.00 372 98.86 98.86 0.00e+00
PDB 3FMH "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((R)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" 100.00 372 98.86 98.86 0.00e+00
PDB 3FMJ "P38 Kinase Crystal Structure In Complex With 4-(5-Methyl-3-Phenyl- Isoxazol-4-Yl)-Pyrimidin-2-Ylamine" 100.00 372 98.86 98.86 0.00e+00
PDB 3FMK "P38 Kinase Crystal Structure In Complex With 6-(2,4-Difluoro-Phenoxy)- 8-Methyl-2-((S)-1-Methyl-2-Tetrazol-2-Yl-Ethylamino)-8h-" 100.00 372 98.86 98.86 0.00e+00
PDB 3FML "P38 Kinase Crystal Structure In Complex With Ro6224" 100.00 372 98.86 98.86 0.00e+00
PDB 3FMM "P38 Kinase Crystal Structure In Complex With Ro6226" 100.00 372 98.86 98.86 0.00e+00
PDB 3FMN "P38 Kinase Crystal Structure In Complex With Ro2530" 100.00 372 98.86 98.86 0.00e+00
PDB 3FSF "P38 Kinase Crystal Structure In Complex With 3-(2,6- Dichloro-Phenyl)-7-[4-(2-Diethylamino-Ethoxy)-Phenylamino]- 1-Methyl-3,4-D" 100.00 372 98.86 98.86 0.00e+00
PDB 3FSK "P38 Kinase Crystal Structure In Complex With Ro6257" 100.00 372 98.86 98.86 0.00e+00
PDB 3GC7 "The Structure Of P38alpha In Complex With A Dihydroquinazolinone" 99.15 366 99.14 99.14 0.00e+00
PDB 3GCP "Human P38 Map Kinase In Complex With Sb203580" 99.43 360 97.99 97.99 0.00e+00
PDB 3GCQ "Human P38 Map Kinase In Complex With Rl45" 99.43 360 97.99 97.99 0.00e+00
PDB 3GCS "Human P38 Map Kinase In Complex With Sorafenib" 99.43 360 97.99 97.99 0.00e+00
PDB 3GCU "Human P38 Map Kinase In Complex With Rl48" 99.43 360 99.14 99.14 0.00e+00
PDB 3GCV "Human P38 Map Kinase In Complex With Rl62" 99.43 360 97.99 97.99 0.00e+00
PDB 3GFE "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 3GI3 "Crystal Structure Of A N-Phenyl-N'-Naphthylurea Analog In Complex With P38 Map Kinase" 99.15 360 99.43 99.43 0.00e+00
PDB 3HA8 "The Complex Structure Of The Map Kinase P38COMPOUND 14B" 100.00 379 98.86 98.86 0.00e+00
PDB 3HEC "P38 In Complex With Imatinib" 98.29 348 99.42 99.42 0.00e+00
PDB 3HEG "P38 In Complex With Sorafenib" 98.29 348 99.42 99.42 0.00e+00
PDB 3HL7 "Crystal Structure Of Human P38alpha Complexed With Sd-0006" 99.15 360 99.43 99.43 0.00e+00
PDB 3HLL "Crystal Structure Of Human P38alpha Complexed With Ph-797804" 99.15 360 99.43 99.43 0.00e+00
PDB 3HP2 "Crystal Structure Of Human P38alpha Complexed With A Pyridinone Compound" 99.15 360 99.43 99.43 0.00e+00
PDB 3HP5 "Crystal Structure Of Human P38alpha Complexed With A Pyrimidopyridazinone Compound" 99.15 360 99.43 99.43 0.00e+00
PDB 3HRB "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 359 99.43 99.43 0.00e+00
PDB 3HUB "Human P38 Map Kinase In Complex With Scios-469" 99.43 360 97.99 97.99 0.00e+00
PDB 3HUC "Human P38 Map Kinase In Complex With Rl40" 99.43 360 99.14 99.14 0.00e+00
PDB 3HV3 "Human P38 Map Kinase In Complex With Rl49" 99.43 360 97.99 97.99 0.00e+00
PDB 3HV4 "Human P38 Map Kinase In Complex With Rl51" 99.43 360 99.14 99.14 0.00e+00
PDB 3HV5 "Human P38 Map Kinase In Complex With Rl24" 99.43 360 99.14 99.14 0.00e+00
PDB 3HV6 "Human P38 Map Kinase In Complex With Rl39" 99.43 360 99.14 99.14 0.00e+00
PDB 3HV7 "Human P38 Map Kinase In Complex With Rl38" 99.43 360 99.14 99.14 0.00e+00
PDB 3HVC "Crystal Structure Of Human P38alpha Map Kinase" 100.00 362 98.86 98.86 0.00e+00
PDB 3IPH "Crystal Structure Of P38 In Complex With A Biphenylamide Inhibitor" 99.15 360 98.85 98.85 0.00e+00
PDB 3ITZ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridazine Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 3IW5 "Human P38 Map Kinase In Complex With An Indole Derivative" 99.43 360 97.99 97.99 0.00e+00
PDB 3IW6 "Human P38 Map Kinase In Complex With A Benzylpiperazin- Pyrrol" 99.43 360 97.99 97.99 0.00e+00
PDB 3IW7 "Human P38 Map Kinase In Complex With An Imidazo-Pyridine" 99.43 360 97.99 97.99 0.00e+00
PDB 3IW8 "Structure Of Inactive Human P38 Map Kinase In Complex With A Thiazole-Urea" 99.43 360 97.99 97.99 0.00e+00
PDB 3K3I "P38alpha Bound To Novel Dgf-Out Compound Pf-00215955" 98.29 350 99.42 99.42 0.00e+00
PDB 3K3J "P38alpha Bound To Novel Dfg-Out Compound Pf-00416121" 100.00 362 98.86 98.86 0.00e+00
PDB 3KF7 "Crystal Structure Of Human P38alpha Complexed With A Triazolopyrimidine Compound" 99.15 360 99.43 99.43 0.00e+00
PDB 3KQ7 "Structure Of Human P38alpha With N-[4-Methyl-3-(6-{[2-(1- Methylpyrrolidin-2-Yl)ethyl]amino}pyridine-3-Amido)phenyl]- 2-(Morpho" 100.00 380 98.86 98.86 0.00e+00
PDB 3L8S "Human P38 Map Kinase In Complex With Cp-547632" 99.43 360 97.99 97.99 0.00e+00
PDB 3L8X "P38 Alpha Kinase Complexed With A Pyrazolo-Pyrimidine Based Inhibitor" 99.72 366 99.14 99.43 0.00e+00
PDB 3LFA "Human P38 Map Kinase In Complex With Dasatinib" 99.43 360 99.14 99.14 0.00e+00
PDB 3LFB "Human P38 Map Kinase In Complex With Rl98" 99.43 360 97.99 97.99 0.00e+00
PDB 3LFC "Human P38 Map Kinase In Complex With Rl99" 99.43 360 97.99 97.99 0.00e+00
PDB 3LFD "Human P38 Map Kinase In Complex With Rl113" 99.43 360 97.99 97.99 0.00e+00
PDB 3LFE "Human P38 Map Kinase In Complex With Rl116" 99.43 360 97.99 97.99 0.00e+00
PDB 3LFF "Human P38 Map Kinase In Complex With Rl166" 99.43 360 97.99 97.99 0.00e+00
PDB 3LHJ "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Pyrazolopyridinone Inhibitor." 99.15 366 99.43 99.43 0.00e+00
PDB 3MGY "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " 99.15 360 99.43 99.43 0.00e+00
PDB 3MH0 "Mutagenesis Of P38 Map Kinase Eshtablishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out " 99.15 360 99.14 99.14 0.00e+00
PDB 3MH1 "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" 99.15 360 99.14 99.14 0.00e+00
PDB 3MH2 "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" 99.15 360 99.14 99.43 0.00e+00
PDB 3MH3 "Mutagenesis Of P38 Map Kinase Establishes Key Roles Of Phe169 In Function And Structural Dynamics And Reveals A Novel Dfg-Out S" 99.15 360 99.14 99.14 0.00e+00
PDB 3MPA "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.14 0.00e+00
PDB 3MPT "Crystal Structure Of P38 Kinase In Complex With A Pyrrole-2- Carboxamide Inhibitor" 99.15 371 99.43 99.43 0.00e+00
PDB 3MVL "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7k" 99.72 366 99.14 99.43 0.00e+00
PDB 3MVM "P38 Alpha Map Kinase Complexed With Pyrrolotriazine Inhibitor 7v" 99.72 366 99.14 99.43 0.00e+00
PDB 3MW1 "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 359 99.43 99.43 0.00e+00
PDB 3NEW "P38-Alpha Complexed With Compound 10" 99.15 366 99.14 99.14 0.00e+00
PDB 3NNU "Crystal Structure Of P38 Alpha In Complex With Dp1376" 99.15 354 99.43 99.43 0.00e+00
PDB 3NNV "Crystal Structure Of P38 Alpha In Complex With Dp437" 99.15 354 99.43 99.43 0.00e+00
PDB 3NNW "Crystal Structure Of P38 Alpha In Complex With Dp802" 99.15 354 99.43 99.43 0.00e+00
PDB 3NNX "Crystal Structure Of Phosphorylated P38 Alpha In Complex With Dp802" 99.15 354 99.14 99.14 0.00e+00
PDB 3NWW "P38 Alpha Kinase Complexed With A 2-aminothiazol-5-yl-pyrimidine Based Inhibitor" 99.72 366 99.14 99.43 0.00e+00
PDB 3O8P "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.14 0.00e+00
PDB 3O8T "Conformational Plasticity Of P38 Map Kinase Dfg-Motif Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.14 0.00e+00
PDB 3O8U "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.43 0.00e+00
PDB 3OBG "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.14 0.00e+00
PDB 3OBJ "Conformational Plasticity Of P38 Map Kinase Dfg Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.14 0.00e+00
PDB 3OC1 "Conformational Plasticity Of P38 Map Kinase Dfg Motif Mutants In Response To Inhibitor Binding" 99.15 360 99.14 99.14 0.00e+00
PDB 3OCG "P38 Alpha Kinase Complexed With A 5-Amino-Pyrazole Based Inhibitor" 99.72 366 99.14 99.43 0.00e+00
PDB 3OD6 "Crystal Structure Of P38alpha Y323t Active Mutant" 99.15 360 99.14 99.14 0.00e+00
PDB 3ODY "Crystal Structure Of P38alpha Y323q Active Mutant" 99.15 360 99.14 99.14 0.00e+00
PDB 3ODZ "Crystal Structure Of P38alpha Y323r Active Mutant" 99.15 360 99.14 99.14 0.00e+00
PDB 3OEF "Crystal Structure Of Y323f Inactive Mutant Of P38alpha Map Kinase" 99.15 360 99.14 99.43 0.00e+00
PDB 3P4K "The Third Conformation Of P38a Map Kinase Observed In Phosphorylated P38a And In Solution" 99.15 370 99.71 100.00 0.00e+00
PDB 3P5K "P38 Inhibitor-Bound" 99.72 366 99.71 100.00 0.00e+00
PDB 3P78 "P38 Inhibitor-Bound" 99.72 366 99.71 100.00 0.00e+00
PDB 3P79 "P38 Inhibitor-Bound" 99.72 366 99.71 100.00 0.00e+00
PDB 3P7A "P38 Inhibitor-Bound" 99.72 366 99.71 100.00 0.00e+00
PDB 3P7B "P38 Inhibitor-Bound" 99.72 366 99.71 100.00 0.00e+00
PDB 3P7C "P38 Inhibitor-Bound" 99.72 366 99.71 100.00 0.00e+00
PDB 3PG3 "Human P38 Map Kinase In Complex With Rl182" 99.43 360 97.99 97.99 0.00e+00
PDB 3PY3 "Crystal Structure Of Phosphorylated P38alpha Map Kinase" 100.00 380 98.86 98.86 0.00e+00
PDB 3QUD "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino-Benzophenone" 99.43 360 99.14 99.14 0.00e+00
PDB 3QUE "Human P38 Map Kinase In Complex With Skepinone-l" 99.43 360 99.14 99.14 0.00e+00
PDB 3RIN "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 99.15 360 99.43 99.43 0.00e+00
PDB 3ROC "Crystal Structure Of Human P38 Alpha Complexed With A Pyrimidinone Compound" 99.15 360 99.43 99.43 0.00e+00
PDB 3S3I "P38 Kinase Crystal Structure In Complex With Small Molecule Inhibitor" 98.58 349 99.42 99.42 0.00e+00
PDB 3S4Q "P38 Alpha Kinase Complexed With A Pyrazolo-Triazine Based Inhibitor" 99.72 366 99.14 99.43 0.00e+00
PDB 3TG1 "Crystal Structure Of P38alpha In Complex With A Mapk Docking Partner" 100.00 380 99.43 99.43 0.00e+00
PDB 3U8W "Crystal Structure Of P38a Mitogen-Activated Protein Kinase In Complex With A Triazolopyridazinone Inhibitor" 99.15 366 99.43 99.43 0.00e+00
PDB 3UVP "Human P38 Map Kinase In Complex With A Benzamide Substituted Benzosuberone" 99.43 360 99.14 99.14 0.00e+00
PDB 3UVQ "Human P38 Map Kinase In Complex With A Dibenzosuberone Derivative" 99.43 360 99.14 99.14 0.00e+00
PDB 3UVR "Human P38 Map Kinase In Complex With Km064" 99.43 360 99.14 99.14 0.00e+00
PDB 3ZS5 "Structural Basis For Kinase Selectivity Of Three Clinical P38alpha Inhibitors" 100.00 362 98.86 99.15 0.00e+00
PDB 3ZSG "X-Ray Structure Of P38alpha Bound To Tak-715" 100.00 362 98.86 99.15 0.00e+00
PDB 3ZSH "X-Ray Structure Of P38alpha Bound To Scio-469" 100.00 362 98.86 99.15 0.00e+00
PDB 3ZSI "X-Ray Structure Of P38alpha Bound To Vx-745" 100.00 362 98.86 99.15 0.00e+00
PDB 3ZYA "Human P38 Map Kinase In Complex With 2-Amino-Phenylamino- Dibenzosuberone" 99.15 366 99.43 99.43 0.00e+00
PDB 4A9Y "P38alpha Map Kinase Bound To Cmpd 8" 99.72 365 99.14 99.43 0.00e+00
PDB 4AA0 "P38alpha Map Kinase Bound To Cmpd 2" 99.72 365 99.14 99.43 0.00e+00
PDB 4AA4 "P38alpha Map Kinase Bound To Cmpd 22" 99.72 365 99.14 99.43 0.00e+00
PDB 4AA5 "P38alpha Map Kinase Bound To Cmpd 33" 99.72 365 98.86 99.14 0.00e+00
PDB 4AAC "P38alpha Map Kinase Bound To Cmpd 29" 99.72 365 99.14 99.43 0.00e+00
PDB 4DLI "Human P38 Map Kinase In Complex With Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4DLJ "Human P38 Map Kinase In Complex With Rl163" 99.43 360 99.14 99.14 0.00e+00
PDB 4E5A "The W197a Mutant Of P38a Map Kinase" 99.15 360 99.14 99.14 0.00e+00
PDB 4E5B "Structure Of P38a Map Kinase Without Bog" 99.15 360 99.43 99.43 0.00e+00
PDB 4E6A "P38a-pia23 Complex" 99.15 360 99.43 99.43 0.00e+00
PDB 4E6C "P38a-perifosine Complex" 99.15 360 99.43 99.43 0.00e+00
PDB 4E8A "The Crystal Structure Of P38a Map Kinase In Complex With Pia24" 99.15 360 99.43 99.43 0.00e+00
PDB 4EH2 "Human P38 Map Kinase In Complex With Np-F1 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH3 "Human P38 Map Kinase In Complex With Np-F2 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH4 "Human P38 Map Kinase In Complex With Np-F3 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH5 "Human P38 Map Kinase In Complex With Np-F4 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH6 "Human P38 Map Kinase In Complex With Np-F5 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH7 "Human P38 Map Kinase In Complex With Np-F6 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH8 "Human P38 Map Kinase In Complex With Np-F7 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EH9 "Human P38 Map Kinase In Complex With Np-F11 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EHV "Human P38 Map Kinase In Complex With Np-F10 And Rl87" 99.43 360 99.14 99.14 0.00e+00
PDB 4EWQ "Human P38 Alpha Mapk In Complex With A Pyridazine Based Inhibitor" 99.15 383 99.14 99.14 0.00e+00
PDB 4F9W "Human P38alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" 99.15 383 99.43 99.43 0.00e+00
PDB 4F9Y "Human P38 Alpha Mapk In Complex With A Novel And Selective Small Molecule Inhibitor" 99.15 383 99.43 99.43 0.00e+00
PDB 4FA2 "Human P38 Alpha Mitogen-activated Kinase In Complex With Sb239063" 99.15 383 99.43 99.43 0.00e+00
PDB 4GEO "P38a Map Kinase Def-pocket Penta Mutant (m194a, L195a, H228a, I229a, Y258a)" 99.72 367 97.71 97.71 0.00e+00
PDB 4KA3 "Structure Of Map Kinase In Complex With A Docking Peptide" 99.15 360 100.00 100.00 0.00e+00
PDB 4KIN "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 5-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 99.72 366 99.14 99.43 0.00e+00
PDB 4KIP "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With 2-(2-chlorophenyl)-n-(5-(cyclopropylcarbamoyl)-2" 99.72 366 99.14 99.43 0.00e+00
PDB 4KIQ "Crystal Structure Of Mitogen-activated Protein Kinase 14 (p38-h5) Complex With Ethyl 6-((5-(cyclopropylcarbamoyl)-2-methylpheny" 99.72 366 99.14 99.43 0.00e+00
PDB 4L8M "Human P38 Map Kinase In Complex With A Dibenzoxepinone" 99.43 360 99.14 99.14 0.00e+00
PDB 4LOO "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (monoclinic Crystal Form)" 99.15 361 100.00 100.00 0.00e+00
PDB 4LOP "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form)" 99.15 361 100.00 100.00 0.00e+00
PDB 4LOQ "Structural Basis Of Autoactivation Of P38 Alpha Induced By Tab1 (tetragonal Crystal Form With Bound Sulphate)" 99.15 361 100.00 100.00 0.00e+00
DBJ BAB85654 "Alternative spliced variant of p38alpha EXIP [Homo sapiens]" 72.08 307 99.60 99.60 0.00e+00
DBJ BAE21782 "unnamed protein product [Mus musculus]" 99.15 360 100.00 100.00 0.00e+00
DBJ BAE30324 "unnamed protein product [Mus musculus]" 77.49 283 100.00 100.00 0.00e+00
DBJ BAE31659 "unnamed protein product [Mus musculus]" 77.49 283 100.00 100.00 0.00e+00
DBJ BAF84398 "unnamed protein product [Homo sapiens]" 99.15 360 99.14 99.14 0.00e+00
EMBL CAG38743 "MAPK14 [Homo sapiens]" 99.15 360 99.43 99.43 0.00e+00
GB AAA20888 "MAP kinase [Mus musculus]" 99.15 360 100.00 100.00 0.00e+00
GB AAA57456 "CSaids binding protein [Homo sapiens]" 99.15 360 99.43 99.43 0.00e+00
GB AAA74301 "MAP kinase [Homo sapiens]" 99.15 360 99.43 99.43 0.00e+00
GB AAB51285 "p38 mitogen activated protein kinase [Rattus norvegicus]" 99.15 360 98.85 99.43 0.00e+00
GB AAC36131 "p38 mitogen activated protein kinase [Canis lupus familiaris]" 99.15 360 98.85 99.43 0.00e+00
PRF 2111247A "p38 mitogen-activated protein kinase" 99.15 360 99.43 99.43 0.00e+00
PRF 2124426A "Mxi2 protein" 79.77 297 98.93 98.93 0.00e+00
REF NP_001003206 "mitogen-activated protein kinase 14 [Canis lupus familiaris]" 99.15 360 98.85 99.43 0.00e+00
REF NP_001136366 "mitogen-activated protein kinase 14 [Ovis aries]" 99.15 360 99.43 99.43 0.00e+00
REF NP_001161985 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.49 283 100.00 100.00 0.00e+00
REF NP_001161986 "mitogen-activated protein kinase 14 isoform 3 [Mus musculus]" 77.49 283 100.00 100.00 0.00e+00
REF NP_036081 "mitogen-activated protein kinase 14 isoform 1 [Mus musculus]" 99.15 360 100.00 100.00 0.00e+00
SP O02812 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Mitogen-activated protein " 99.15 360 98.85 99.43 0.00e+00
SP P47811 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" 99.15 360 100.00 100.00 0.00e+00
SP P70618 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=CRK1; AltName: Full=Mitoge" 99.15 360 99.14 99.71 0.00e+00
SP Q16539 "RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; AltName: Full=Cytokine suppressive anti-" 99.15 360 99.43 99.43 0.00e+00
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$p38 Mouse 10090 Eukaryota Metazoa Mus musculus
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_name
$p38 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_triple_labeled
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$p38 0.7 mM '[U-2H; U-13C; U-15N]'
NaCl 150 mM .
Hepes*HCl 50 mM .
DTT 5 mM .
TSP 1 mM .
stop_
save_
save_selectively_labeled
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$p38 0.2 mM 'selectively labeled'
stop_
save_
############################
# Computer software used #
############################
save_XEASY
_Saveframe_category software
_Name XEASY
_Version .
loop_
_Task
assignment
stop_
_Details 'C. Bartels et al., J. Biomol. NMR 5, 1-10 (1995)'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_Deuterium-decoupled_TROSY_variants_of_HNCO_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 'Deuterium-decoupled TROSY variants of HNCO'
_Sample_label .
save_
save_HN(CA)CO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_Sample_label .
save_
save_HNCA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label .
save_
save_HNCACB_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_HN(CO)CACB_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CACB
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 'Deuterium-decoupled TROSY variants of HNCO'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.8 0.2 pH
temperature 298 0.1 K
'ionic strength' 0.3 . M
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$triple_labeled
stop_
_Sample_conditions_label $Ex-cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_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 . 8 PRO CA C 61.769 0.1 1
2 . 8 PRO CB C 31.237 0.1 1
3 . 8 PRO C C 175.558 0.1 1
4 . 9 THR N N 116.925 0.1 1
5 . 9 THR H H 8.479 0.02 1
6 . 9 THR CA C 62.173 0.1 1
7 . 9 THR CB C 68.754 0.1 1
8 . 9 THR C C 173.716 0.1 1
9 . 10 PHE N N 126.754 0.1 1
10 . 10 PHE H H 8.776 0.02 1
11 . 10 PHE CA C 56.304 0.1 1
12 . 10 PHE CB C 40.97 0.1 1
13 . 10 PHE C C 175.722 0.1 1
14 . 11 TYR N N 119.578 0.1 1
15 . 11 TYR H H 9.138 0.02 1
16 . 11 TYR CA C 55.391 0.1 1
17 . 11 TYR CB C 40.106 0.1 1
18 . 11 TYR C C 172.385 0.1 1
19 . 12 ARG N N 119.476 0.1 1
20 . 12 ARG H H 8.436 0.02 1
21 . 12 ARG CA C 53.957 0.1 1
22 . 12 ARG CB C 32.729 0.1 1
23 . 12 ARG C C 175.908 0.1 1
24 . 13 GLN N N 122.07 0.1 1
25 . 13 GLN H H 8.985 0.02 1
26 . 13 GLN CA C 54.283 0.1 1
27 . 13 GLN CB C 32.258 0.1 1
28 . 13 GLN C C 172.815 0.1 1
29 . 14 GLU N N 125.474 0.1 1
30 . 14 GLU H H 8.847 0.02 1
31 . 14 GLU CA C 54.805 0.1 1
32 . 14 GLU CB C 29.589 0.1 1
33 . 14 GLU C C 175.582 0.1 1
34 . 15 LEU N N 128.053 0.1 1
35 . 15 LEU H H 8.999 0.02 1
36 . 15 LEU CA C 53.37 0.1 1
37 . 15 LEU CB C 43.324 0.1 1
38 . 15 LEU C C 175.444 0.1 1
39 . 16 ASN CA C 53.841 0.1 1
40 . 16 ASN CB C 36.339 0.1 1
41 . 16 ASN C C 174.952 0.1 1
42 . 17 LYS N N 109.536 0.1 1
43 . 17 LYS H H 8.884 0.02 1
44 . 17 LYS CA C 56.956 0.1 1
45 . 17 LYS CB C 28.647 0.1 1
46 . 17 LYS C C 175.349 0.1 1
47 . 18 THR N N 115.299 0.1 1
48 . 18 THR H H 7.853 0.02 1
49 . 18 THR CA C 60.608 0.1 1
50 . 18 THR CB C 70.638 0.1 1
51 . 18 THR C C 172.387 0.1 1
52 . 19 ILE N N 125.144 0.1 1
53 . 19 ILE H H 8.614 0.02 1
54 . 19 ILE CA C 59.63 0.1 1
55 . 19 ILE CB C 35.711 0.1 1
56 . 19 ILE C C 175.489 0.1 1
57 . 20 TRP N N 130.528 0.1 1
58 . 20 TRP H H 9.293 0.02 1
59 . 20 TRP CA C 56.37 0.1 1
60 . 20 TRP CB C 28.333 0.1 1
61 . 20 TRP C C 174.532 0.1 1
62 . 21 GLU N N 127.643 0.1 1
63 . 21 GLU H H 8.3 0.02 1
64 . 21 GLU CA C 54.283 0.1 1
65 . 21 GLU CB C 30.452 0.1 1
66 . 21 GLU C C 173.04 0.1 1
67 . 22 VAL N N 111.964 0.1 1
68 . 22 VAL H H 7.644 0.02 1
69 . 22 VAL CA C 55.652 0.1 1
70 . 22 VAL CB C 32.964 0.1 1
71 . 23 PRO CA C 60.984 0.1 1
72 . 23 PRO CB C 31.237 0.1 1
73 . 24 GLU N N 118.485 0.1 1
74 . 24 GLU H H 8.128 0.02 1
75 . 24 GLU CA C 57.82 0.1 1
76 . 24 GLU CB C 28.647 0.1 1
77 . 25 ARG N N 117.114 0.1 1
78 . 25 ARG H H 7.433 0.02 1
79 . 25 ARG CA C 57.217 0.1 1
80 . 25 ARG CB C 29.746 0.1 1
81 . 25 ARG C C 174.304 0.1 1
82 . 26 TYR N N 116.889 0.1 1
83 . 26 TYR H H 7.81 0.02 1
84 . 26 TYR CA C 56.591 0.1 1
85 . 26 TYR CB C 36.967 0.1 1
86 . 26 TYR C C 174.346 0.1 1
87 . 27 GLN N N 121.815 0.1 1
88 . 27 GLN H H 9.13 0.02 1
89 . 27 GLN CA C 52.914 0.1 1
90 . 27 GLN CB C 32.493 0.1 1
91 . 27 GLN C C 174.718 0.1 1
92 . 28 ASN N N 117.001 0.1 1
93 . 28 ASN H H 8.84 0.02 1
94 . 28 ASN CA C 53.174 0.1 1
95 . 28 ASN CB C 35.947 0.1 1
96 . 28 ASN C C 174.066 0.1 1
97 . 29 LEU N N 119.747 0.1 1
98 . 29 LEU H H 8.567 0.02 1
99 . 29 LEU CA C 56.37 0.1 1
100 . 29 LEU CB C 40.42 0.1 1
101 . 29 LEU C C 178.986 0.1 1
102 . 30 SER N N 115.523 0.1 1
103 . 30 SER H H 8.745 0.02 1
104 . 30 SER CA C 54.087 0.1 1
105 . 30 SER CB C 63.966 0.1 1
106 . 30 SER C C 171.823 0.1 1
107 . 31 PRO CA C 63.731 0.1 1
108 . 31 PRO CB C 31.394 0.1 1
109 . 31 PRO C C 176.923 0.1 1
110 . 32 VAL N N 120.389 0.1 1
111 . 32 VAL H H 8.646 0.02 1
112 . 32 VAL CA C 61.325 0.1 1
113 . 32 VAL CB C 32.886 0.1 1
114 . 32 VAL C C 175.932 0.1 1
115 . 33 GLY N N 107.936 0.1 1
116 . 33 GLY H H 7.79 0.02 1
117 . 33 GLY CA C 45.024 0.1 1
118 . 34 SER N N 115.389 0.1 1
119 . 34 SER H H 8.129 0.02 1
120 . 34 SER CA C 57.152 0.1 1
121 . 34 SER CB C 64.437 0.1 1
122 . 34 SER C C 173.39 0.1 1
123 . 35 GLY N N 109.949 0.1 1
124 . 35 GLY H H 8.171 0.02 1
125 . 35 GLY CA C 44.111 0.1 1
126 . 35 GLY C C 173.661 0.1 1
127 . 36 ALA CA C 53.135 0.1 1
128 . 36 ALA CB C 17.267 0.1 1
129 . 36 ALA C C 178.077 0.1 1
130 . 37 TYR N N 113.178 0.1 1
131 . 37 TYR H H 8.075 0.02 1
132 . 37 TYR CA C 56.63 0.1 1
133 . 37 TYR CB C 37.045 0.1 1
134 . 37 TYR C C 176.048 0.1 1
135 . 38 GLY N N 107.983 0.1 1
136 . 38 GLY H H 7.338 0.02 1
137 . 38 GLY CA C 44.893 0.1 1
138 . 38 GLY C C 171.828 0.1 1
139 . 39 SER N N 115.499 0.1 1
140 . 39 SER H H 8.152 0.02 1
141 . 39 SER CA C 57.152 0.1 1
142 . 39 SER CB C 64.359 0.1 1
143 . 39 SER C C 171.967 0.1 1
144 . 40 VAL N N 121.985 0.1 1
145 . 40 VAL H H 8.685 0.02 1
146 . 40 VAL CA C 60.738 0.1 1
147 . 40 VAL CB C 34.063 0.1 1
148 . 40 VAL C C 176.281 0.1 1
149 . 41 CYS N N 124.965 0.1 1
150 . 41 CYS H H 9.327 0.02 1
151 . 41 CYS CA C 57.217 0.1 1
152 . 41 CYS CB C 30.295 0.1 1
153 . 41 CYS C C 173.227 0.1 1
154 . 42 ALA N N 124.934 0.1 1
155 . 42 ALA H H 8.803 0.02 1
156 . 42 ALA CA C 50.045 0.1 1
157 . 42 ALA CB C 19.7 0.1 1
158 . 42 ALA C C 176.294 0.1 1
159 . 43 ALA N N 120.389 0.1 1
160 . 43 ALA H H 8.99 0.02 1
161 . 43 ALA CA C 50.045 0.1 1
162 . 43 ALA CB C 22.29 0.1 1
163 . 43 ALA C C 175.115 0.1 1
164 . 44 PHE N N 121.612 0.1 1
165 . 44 PHE H H 9.308 0.02 1
166 . 44 PHE CA C 57.022 0.1 1
167 . 44 PHE CB C 39.871 0.1 1
168 . 44 PHE C C 173.88 0.1 1
169 . 45 ASP N N 125.645 0.1 1
170 . 45 ASP H H 8.121 0.02 1
171 . 45 ASP CA C 51.414 0.1 1
172 . 45 ASP CB C 40.42 0.1 1
173 . 45 ASP C C 176.317 0.1 1
174 . 46 THR N N 116.639 0.1 1
175 . 46 THR H H 8.867 0.02 1
176 . 46 THR CA C 62.955 0.1 1
177 . 46 THR CB C 68.597 0.1 1
178 . 46 THR C C 176.281 0.1 1
179 . 47 LYS N N 121.406 0.1 1
180 . 47 LYS H H 7.973 0.02 1
181 . 47 LYS CA C 58.065 0.1 1
182 . 47 LYS CB C 31.551 0.1 1
183 . 47 LYS C C 177.587 0.1 1
184 . 48 THR N N 104.425 0.1 1
185 . 48 THR H H 6.596 0.02 1
186 . 48 THR CA C 61.064 0.1 1
187 . 48 THR CB C 69.696 0.1 1
188 . 48 THR C C 175.675 0.1 1
189 . 49 GLY N N 110.774 0.1 1
190 . 49 GLY H H 8.31 0.02 1
191 . 49 GLY CA C 45.415 0.1 1
192 . 49 GLY C C 173.506 0.1 1
193 . 50 HIS N N 116.442 0.1 1
194 . 50 HIS H H 7.127 0.02 1
195 . 50 HIS CA C 53.566 0.1 1
196 . 50 HIS CB C 31.473 0.1 1
197 . 50 HIS C C 174.089 0.1 1
198 . 51 ARG N N 120.265 0.1 1
199 . 51 ARG H H 8.659 0.02 1
200 . 51 ARG CA C 55.522 0.1 1
201 . 51 ARG CB C 29.982 0.1 1
202 . 51 ARG C C 177.34 0.1 1
203 . 52 VAL N N 115.639 0.1 1
204 . 52 VAL H H 8.997 0.02 1
205 . 52 VAL CA C 59.209 0.1 1
206 . 52 VAL CB C 34.534 0.1 1
207 . 52 VAL C C 172.704 0.1 1
208 . 53 ALA N N 121.889 0.1 1
209 . 53 ALA H H 8.754 0.02 1
210 . 53 ALA CA C 49.641 0.1 1
211 . 53 ALA CB C 19.307 0.1 1
212 . 53 ALA C C 175.65 0.1 1
213 . 54 VAL N N 121.639 0.1 1
214 . 54 VAL H H 9.24 0.02 1
215 . 54 VAL CA C 60.021 0.1 1
216 . 54 VAL CB C 31.787 0.1 1
217 . 54 VAL C C 173.553 0.1 1
218 . 55 LYS N N 128.717 0.1 1
219 . 55 LYS H H 9.594 0.02 1
220 . 55 LYS CA C 53.474 0.1 1
221 . 55 LYS CB C 34.141 0.1 1
222 . 55 LYS C C 174.276 0.1 1
223 . 56 LYS N N 127.804 0.1 1
224 . 56 LYS H H 8.6 0.02 1
225 . 56 LYS CA C 53.567 0.1 1
226 . 56 LYS CB C 32.807 0.1 1
227 . 56 LYS C C 176.748 0.1 1
228 . 57 LEU N N 128.174 0.1 1
229 . 57 LEU H H 8.01 0.02 1
230 . 57 LEU CA C 54.348 0.1 1
231 . 57 LEU CB C 38.929 0.1 1
232 . 57 LEU C C 176.235 0.1 1
233 . 58 SER N N 117.467 0.1 1
234 . 58 SER H H 8.03 0.02 1
235 . 58 SER CA C 56.565 0.1 1
236 . 58 SER CB C 62.383 0.1 1
237 . 58 SER C C 173.6 0.1 1
238 . 59 ARG N N 122.459 0.1 1
239 . 59 ARG H H 8.73 0.02 1
240 . 59 ARG CA C 55.913 0.1 1
241 . 59 ARG CB C 28.453 0.1 1
242 . 59 ARG C C 174.076 0.1 1
243 . 60 PRO CA C 61.2 0.1 1
244 . 60 PRO CB C 28.6 0.1 1
245 . 60 PRO C C 175.139 0.1 1
246 . 61 PHE N N 111.746 0.1 1
247 . 61 PHE H H 7.887 0.02 1
248 . 61 PHE CA C 54.087 0.1 1
249 . 61 PHE CB C 37.053 0.1 1
250 . 61 PHE C C 176.538 0.1 1
251 . 62 GLN N N 115.063 0.1 1
252 . 62 GLN H H 7.08 0.02 1
253 . 62 GLN CA C 56.861 0.1 1
254 . 62 GLN CB C 28.453 0.1 1
255 . 62 GLN C C 174.276 0.1 1
256 . 63 SER N N 110.102 0.1 1
257 . 63 SER H H 7.446 0.02 1
258 . 63 SER CA C 56.187 0.1 1
259 . 63 SER CB C 65.588 0.1 1
260 . 65 ILE CA C 63.712 0.1 1
261 . 65 ILE CB C 40.18 0.1 1
262 . 65 ILE C C 178.986 0.1 1
263 . 66 HIS N N 119.489 0.1 1
264 . 66 HIS H H 7.674 0.02 1
265 . 66 HIS CA C 60.604 0.1 1
266 . 66 HIS CB C 34.707 0.1 1
267 . 66 HIS C C 177.051 0.1 1
268 . 67 ALA N N 122.934 0.1 1
269 . 67 ALA H H 8.6 0.02 1
270 . 67 ALA CA C 54.609 0.1 1
271 . 67 ALA CB C 18.368 0.1 1
272 . 67 ALA C C 178.59 0.1 1
273 . 68 LYS N N 117.644 0.1 1
274 . 68 LYS H H 7.83 0.02 1
275 . 68 LYS CA C 58.732 0.1 1
276 . 68 LYS CB C 31.189 0.1 1
277 . 68 LYS C C 177.727 0.1 1
278 . 69 ARG N N 118.628 0.1 1
279 . 69 ARG H H 7.477 0.02 1
280 . 69 ARG CA C 58.807 0.1 1
281 . 69 ARG CB C 28.531 0.1 1
282 . 69 ARG C C 178.361 0.1 1
283 . 80 MET CA C 55.112 0.1 1
284 . 80 MET CB C 32.909 0.1 1
285 . 81 LYS N N 128.058 0.1 1
286 . 81 LYS H H 8.486 0.02 1
287 . 81 LYS CA C 54.615 0.1 1
288 . 81 LYS CB C 31.971 0.1 1
289 . 81 LYS C C 172.97 0.1 1
290 . 82 HIS N N 123.4 0.1 1
291 . 82 HIS H H 8.675 0.02 1
292 . 82 HIS CA C 56.778 0.1 1
293 . 82 HIS CB C 32.518 0.1 1
294 . 82 HIS C C 175.162 0.1 1
295 . 83 GLU N N 125.002 0.1 1
296 . 83 GLU H H 8.066 0.02 1
297 . 83 GLU CA C 59.032 0.1 1
298 . 83 GLU CB C 29.078 0.1 1
299 . 83 GLU C C 177.634 0.1 1
300 . 84 ASN N N 117.684 0.1 1
301 . 84 ASN H H 11.348 0.02 1
302 . 84 ASN CA C 52.979 0.1 1
303 . 84 ASN CB C 40.258 0.1 1
304 . 85 VAL N N 118.967 0.1 1
305 . 85 VAL H H 7.674 0.02 1
306 . 85 VAL CA C 60.753 0.1 1
307 . 85 VAL CB C 34.864 0.1 1
308 . 85 VAL C C 174.591 0.1 1
309 . 86 ILE N N 128.624 0.1 1
310 . 86 ILE H H 8.316 0.02 1
311 . 86 ILE CA C 60.903 0.1 1
312 . 86 ILE CB C 37.756 0.1 1
313 . 86 ILE C C 171.758 0.1 1
314 . 87 GLY N N 108.926 0.1 1
315 . 87 GLY H H 7.734 0.02 1
316 . 87 GLY CA C 43.237 0.1 1
317 . 87 GLY C C 172.563 0.1 1
318 . 88 LEU N N 120.389 0.1 1
319 . 88 LEU H H 8.22 0.02 1
320 . 88 LEU CA C 53.693 0.1 1
321 . 88 LEU CB C 42.056 0.1 1
322 . 88 LEU C C 176.188 0.1 1
323 . 89 LEU N N 126.175 0.1 1
324 . 89 LEU H H 9.034 0.02 1
325 . 89 LEU CA C 55 0.1 1
326 . 89 LEU CB C 41.822 0.1 1
327 . 90 ASP CA C 52.376 0.1 1
328 . 90 ASP CB C 41.509 0.1 1
329 . 90 ASP C C 172.504 0.1 1
330 . 91 VAL N N 119.789 0.1 1
331 . 91 VAL H H 7.882 0.02 1
332 . 91 VAL CA C 58.882 0.1 1
333 . 91 VAL CB C 32.44 0.1 1
334 . 91 VAL C C 171.493 0.1 1
335 . 92 PHE N N 118.389 0.1 1
336 . 92 PHE H H 8.243 0.02 1
337 . 92 PHE CA C 55.427 0.1 1
338 . 92 PHE CB C 40.877 0.1 1
339 . 92 PHE C C 172.597 0.1 1
340 . 93 THR N N 113.048 0.1 1
341 . 93 THR H H 8.956 0.02 1
342 . 93 THR CA C 56.761 0.1 1
343 . 93 THR CB C 71.558 0.1 1
344 . 93 THR C C 184.431 0.1 1
345 . 94 PRO CA C 61.746 0.1 1
346 . 94 PRO CB C 29.975 0.1 1
347 . 94 PRO C C 176.445 0.1 1
348 . 95 ALA N N 121.798 0.1 1
349 . 95 ALA H H 7.713 0.02 1
350 . 95 ALA CA C 52.131 0.1 1
351 . 95 ALA CB C 19.774 0.1 1
352 . 95 ALA C C 178.357 0.1 1
353 . 96 ARG N N 120.687 0.1 1
354 . 96 ARG H H 9.265 0.02 1
355 . 96 ARG CA C 55.326 0.1 1
356 . 96 ARG CB C 29.508 0.1 1
357 . 96 ARG C C 174.929 0.1 1
358 . 97 SER N N 110.856 0.1 1
359 . 97 SER H H 7.385 0.02 1
360 . 97 SER CA C 56.109 0.1 1
361 . 97 SER CB C 64.939 0.1 1
362 . 97 SER C C 173.53 0.1 1
363 . 98 LEU N N 121.974 0.1 1
364 . 98 LEU H H 8.465 0.02 1
365 . 98 LEU CA C 56.565 0.1 1
366 . 98 LEU CB C 40.098 0.1 1
367 . 98 LEU C C 178.706 0.1 1
368 . 99 GLU N N 116.819 0.1 1
369 . 99 GLU H H 8.306 0.02 1
370 . 99 GLU CA C 58.717 0.1 1
371 . 99 GLU CB C 27.873 0.1 1
372 . 99 GLU C C 177.354 0.1 1
373 . 100 GLU N N 114.798 0.1 1
374 . 100 GLU H H 7.025 0.02 1
375 . 100 GLU CA C 54.153 0.1 1
376 . 100 GLU CB C 29.975 0.1 1
377 . 100 GLU C C 175.209 0.1 1
378 . 101 PHE N N 121.692 0.1 1
379 . 101 PHE H H 7.299 0.02 1
380 . 101 PHE CA C 56.239 0.1 1
381 . 101 PHE CB C 37.84 0.1 1
382 . 101 PHE C C 172.9 0.1 1
383 . 102 ASN N N 124.934 0.1 1
384 . 102 ASN H H 8.556 0.02 1
385 . 102 ASN CA C 53.892 0.1 1
386 . 102 ASN CB C 41.57 0.1 1
387 . 102 ASN C C 172.364 0.1 1
388 . 103 ASP N N 115.238 0.1 1
389 . 103 ASP H H 7.608 0.02 1
390 . 103 ASP CA C 52.819 0.1 1
391 . 103 ASP CB C 43.587 0.1 1
392 . 103 ASP C C 174.113 0.1 1
393 . 104 VAL N N 120.607 0.1 1
394 . 104 VAL H H 8.448 0.02 1
395 . 104 VAL CA C 60.934 0.1 1
396 . 104 VAL CB C 34.512 0.1 1
397 . 104 VAL C C 177.282 0.1 1
398 . 105 TYR N N 123.89 0.1 1
399 . 105 TYR H H 8.089 0.02 1
400 . 105 TYR CA C 54.36 0.1 1
401 . 105 TYR CB C 39.398 0.1 1
402 . 105 TYR C C 174.408 0.1 1
403 . 106 LEU N N 118.889 0.1 1
404 . 106 LEU H H 8.843 0.02 1
405 . 106 LEU CA C 52.712 0.1 1
406 . 106 LEU CB C 43.276 0.1 1
407 . 106 LEU C C 175.057 0.1 1
408 . 107 VAL N N 123.139 0.1 1
409 . 107 VAL H H 8.449 0.02 1
410 . 107 VAL CA C 60.08 0.1 1
411 . 107 VAL CB C 31.642 0.1 1
412 . 107 VAL C C 175.395 0.1 1
413 . 108 THR N N 117.658 0.1 1
414 . 108 THR H H 9.089 0.02 1
415 . 108 THR CA C 59.043 0.1 1
416 . 108 THR CB C 72.595 0.1 1
417 . 108 THR C C 173.6 0.1 1
418 . 109 HIS N N 117.916 0.1 1
419 . 109 HIS H H 8.625 0.02 1
420 . 109 HIS CA C 58.391 0.1 1
421 . 109 HIS CB C 30.711 0.1 1
422 . 109 HIS C C 174.999 0.1 1
423 . 110 LEU N N 123.917 0.1 1
424 . 110 LEU H H 8.225 0.02 1
425 . 110 LEU CA C 53.761 0.1 1
426 . 110 LEU CB C 41.492 0.1 1
427 . 110 LEU C C 175.722 0.1 1
428 . 111 MET N N 125.409 0.1 1
429 . 111 MET H H 8.752 0.02 1
430 . 111 MET CA C 54.218 0.1 1
431 . 111 MET CB C 30.866 0.1 1
432 . 111 MET C C 176.095 0.1 1
433 . 112 GLY N N 108.525 0.1 1
434 . 112 GLY H H 8.158 0.02 1
435 . 112 GLY CA C 45.285 0.1 1
436 . 112 GLY C C 172.807 0.1 1
437 . 113 ALA N N 123.472 0.1 1
438 . 113 ALA H H 7.877 0.02 1
439 . 113 ALA CA C 50.958 0.1 1
440 . 113 ALA CB C 19.775 0.1 1
441 . 113 ALA C C 176.771 0.1 1
442 . 114 ASP N N 117.75 0.1 1
443 . 114 ASP H H 7.981 0.02 1
444 . 114 ASP CA C 51.682 0.1 1
445 . 114 ASP CB C 41.803 0.1 1
446 . 114 ASP C C 177.261 0.1 1
447 . 115 LEU N N 116.902 0.1 1
448 . 115 LEU H H 7.801 0.02 1
449 . 115 LEU CA C 56.642 0.1 1
450 . 115 LEU CB C 41.027 0.1 1
451 . 115 LEU C C 178.123 0.1 1
452 . 116 ASN N N 115.157 0.1 1
453 . 116 ASN H H 7.665 0.02 1
454 . 116 ASN CB C 37.381 0.1 1
455 . 116 ASN C C 176.913 0.1 1
456 . 117 ASN CA C 57.005 0.1 1
457 . 117 ASN CB C 40.174 0.1 1
458 . 117 ASN C C 176.812 0.1 1
459 . 118 ILE N N 118.139 0.1 1
460 . 118 ILE H H 7.511 0.02 1
461 . 118 ILE CA C 62.482 0.1 1
462 . 118 ILE CB C 36.14 0.1 1
463 . 118 ILE C C 177.284 0.1 1
464 . 119 VAL N N 116.1 0.1 1
465 . 119 VAL H H 7.523 0.02 1
466 . 119 VAL CA C 63.673 0.1 1
467 . 119 VAL CB C 30.478 0.1 1
468 . 119 VAL C C 177.284 0.1 1
469 . 120 LYS N N 116.937 0.1 1
470 . 120 LYS H H 7.388 0.02 1
471 . 120 LYS CA C 57.011 0.1 1
472 . 120 LYS CB C 31.642 0.1 1
473 . 120 LYS C C 177.914 0.1 1
474 . 121 CYS N N 114.003 0.1 1
475 . 121 CYS H H 7.653 0.02 1
476 . 121 CYS CB C 28.384 0.1 1
477 . 121 CYS C C 173.996 0.1 1
478 . 122 GLN N N 119.073 0.1 1
479 . 122 GLN H H 8.013 0.02 1
480 . 122 GLN CA C 54.294 0.1 1
481 . 122 GLN CB C 29.858 0.1 1
482 . 122 GLN C C 173.505 0.1 1
483 . 125 THR C C 181.26 0.1 1
484 . 126 ASP N N 120.139 0.1 1
485 . 126 ASP H H 8.961 0.02 1
486 . 126 ASP CA C 57.935 0.1 1
487 . 126 ASP CB C 42.113 0.1 1
488 . 126 ASP C C 177.54 0.1 1
489 . 127 ASP N N 114.934 0.1 1
490 . 127 ASP H H 7.977 0.02 1
491 . 127 ASP CA C 56.761 0.1 1
492 . 127 ASP CB C 39.863 0.1 1
493 . 127 ASP C C 178.683 0.1 1
494 . 128 HIS N N 118.842 0.1 1
495 . 128 HIS H H 7.522 0.02 1
496 . 128 HIS CA C 59.406 0.1 1
497 . 128 HIS CB C 39.941 0.1 1
498 . 128 HIS C C 178.884 0.1 1
499 . 129 VAL N N 119.645 0.1 1
500 . 129 VAL H H 8.146 0.02 1
501 . 129 VAL CA C 67.715 0.1 1
502 . 129 VAL CB C 29.642 0.1 1
503 . 129 VAL C C 177.401 0.1 1
504 . 130 GLN N N 117.779 0.1 1
505 . 130 GLN H H 8.403 0.02 1
506 . 130 GLN CA C 58.717 0.1 1
507 . 130 GLN CB C 29.315 0.1 1
508 . 130 GLN C C 177.797 0.1 1
509 . 131 PHE N N 115.806 0.1 1
510 . 131 PHE H H 7.441 0.02 1
511 . 131 PHE CA C 58.208 0.1 1
512 . 131 PHE CB C 38.7 0.1 1
513 . 131 PHE C C 179.429 0.1 1
514 . 132 LEU N N 120.086 0.1 1
515 . 132 LEU H H 8.774 0.02 1
516 . 132 LEU CA C 58.065 0.1 1
517 . 132 LEU CB C 41.647 0.1 1
518 . 132 LEU C C 179.51 0.1 1
519 . 133 ILE N N 115.639 0.1 1
520 . 133 ILE H H 8.672 0.02 1
521 . 133 ILE CA C 61.216 0.1 1
522 . 133 ILE C C 178.573 0.1 1
523 . 138 ARG CA C 59.565 0.1 1
524 . 138 ARG CB C 29.082 0.1 1
525 . 138 ARG C C 179.639 0.1 1
526 . 139 GLY N N 106.651 0.1 1
527 . 139 GLY H H 8.123 0.02 1
528 . 139 GLY CA C 46.458 0.1 1
529 . 139 GLY C C 174.766 0.1 1
530 . 140 LEU N N 121.035 0.1 1
531 . 140 LEU H H 8.674 0.02 1
532 . 140 LEU CA C 55.978 0.1 1
533 . 140 LEU CB C 40.174 0.1 1
534 . 140 LEU C C 177.284 0.1 1
535 . 141 LYS N N 118.828 0.1 1
536 . 141 LYS H H 8.676 0.02 1
537 . 141 LYS CA C 59.304 0.1 1
538 . 141 LYS CB C 31.409 0.1 1
539 . 141 LYS C C 179.289 0.1 1
540 . 142 TYR N N 117.577 0.1 1
541 . 142 TYR H H 6.829 0.02 1
542 . 142 TYR CA C 61.053 0.1 1
543 . 142 TYR CB C 37.381 0.1 1
544 . 142 TYR C C 178.07 0.1 1
545 . 143 ILE N N 119.594 0.1 1
546 . 143 ILE H H 8.433 0.02 1
547 . 143 ILE CA C 66.095 0.1 1
548 . 143 ILE CB C 37.149 0.1 1
549 . 143 ILE C C 177.937 0.1 1
550 . 144 HIS N N 119.267 0.1 1
551 . 144 HIS H H 9.506 0.02 1
552 . 144 HIS CA C 56.63 0.1 1
553 . 144 HIS CB C 30.09 0.1 1
554 . 144 HIS C C 180.898 0.1 1
555 . 145 SER N N 115.912 0.1 1
556 . 145 SER H H 7.856 0.02 1
557 . 145 SER CA C 60.608 0.1 1
558 . 145 SER CB C 62.124 0.1 1
559 . 145 SER C C 174.532 0.1 1
560 . 146 ALA N N 125.714 0.1 1
561 . 146 ALA H H 7.415 0.02 1
562 . 146 ALA CA C 48.74 0.1 1
563 . 146 ALA CB C 14.67 0.1 1
564 . 146 ALA C C 175.512 0.1 1
565 . 147 ASP N N 114.686 0.1 1
566 . 147 ASP H H 8.198 0.02 1
567 . 147 ASP CA C 55.131 0.1 1
568 . 147 ASP CB C 38.39 0.1 1
569 . 147 ASP C C 174.183 0.1 1
570 . 148 ILE N N 118.715 0.1 1
571 . 148 ILE H H 7.262 0.02 1
572 . 148 ILE CA C 58.657 0.1 1
573 . 148 ILE CB C 37.924 0.1 1
574 . 148 ILE C C 173.695 0.1 1
575 . 149 ILE N N 122.639 0.1 1
576 . 149 ILE H H 7.832 0.02 1
577 . 149 ILE CA C 59.194 0.1 1
578 . 149 ILE CB C 39.863 0.1 1
579 . 155 PRO C C 176.375 0.1 1
580 . 156 SER N N 105.461 0.1 1
581 . 156 SER H H 7.505 0.02 1
582 . 156 SER CA C 59.406 0.1 1
583 . 156 SER CB C 61.65 0.1 1
584 . 156 SER C C 174.638 0.1 1
585 . 157 ASN N N 118.389 0.1 1
586 . 157 ASN H H 7.801 0.02 1
587 . 157 ASN CA C 52.264 0.1 1
588 . 157 ASN CB C 37.546 0.1 1
589 . 157 ASN C C 171.291 0.1 1
590 . 158 LEU N N 118.628 0.1 1
591 . 158 LEU H H 7.059 0.02 1
592 . 158 LEU CA C 52.444 0.1 1
593 . 158 LEU CB C 41.795 0.1 1
594 . 158 LEU C C 173.623 0.1 1
595 . 159 ALA N N 124.866 0.1 1
596 . 159 ALA H H 8.523 0.02 1
597 . 159 ALA CA C 50.11 0.1 1
598 . 159 ALA CB C 20.55 0.1 1
599 . 159 ALA C C 176.445 0.1 1
600 . 160 VAL N N 117.432 0.1 1
601 . 160 VAL H H 8.163 0.02 1
602 . 160 VAL CA C 59.032 0.1 1
603 . 160 VAL CB C 34.962 0.1 1
604 . 160 VAL C C 175.279 0.1 1
605 . 161 ASN N N 121.74 0.1 1
606 . 161 ASN H H 7.873 0.02 1
607 . 161 ASN CA C 49.899 0.1 1
608 . 161 ASN CB C 39.254 0.1 1
609 . 161 ASN C C 177.349 0.1 1
610 . 162 GLU N N 117.263 0.1 1
611 . 162 GLU H H 8.856 0.02 1
612 . 162 GLU CA C 58.391 0.1 1
613 . 162 GLU CB C 27.911 0.1 1
614 . 162 GLU C C 176.934 0.1 1
615 . 163 ASP N N 118.254 0.1 1
616 . 163 ASP H H 7.521 0.02 1
617 . 163 ASP CA C 53.792 0.1 1
618 . 163 ASP CB C 40.48 0.1 1
619 . 163 ASP C C 174.591 0.1 1
620 . 164 CYS N N 110.888 0.1 1
621 . 164 CYS H H 8.298 0.02 1
622 . 164 CYS CA C 61.847 0.1 1
623 . 164 CYS CB C 24.156 0.1 1
624 . 164 CYS C C 172.574 0.1 1
625 . 165 GLU N N 117.208 0.1 1
626 . 165 GLU H H 7.668 0.02 1
627 . 165 GLU CA C 55.588 0.1 1
628 . 165 GLU CB C 28.065 0.1 1
629 . 165 GLU C C 175.792 0.1 1
630 . 166 LEU N N 125.056 0.1 1
631 . 166 LEU H H 7.981 0.02 1
632 . 166 LEU CA C 53.101 0.1 1
633 . 166 LEU CB C 45.061 0.1 1
634 . 166 LEU C C 175.578 0.1 1
635 . 167 LYS N N 122.139 0.1 1
636 . 167 LYS H H 8.97 0.02 1
637 . 167 LYS CA C 53.359 0.1 1
638 . 167 LYS CB C 37.123 0.1 1
639 . 167 LYS C C 174.168 0.1 1
640 . 168 ILE N N 121.389 0.1 1
641 . 168 ILE H H 8.198 0.02 1
642 . 168 ILE CA C 61.772 0.1 1
643 . 168 ILE CB C 38.726 0.1 1
644 . 168 ILE C C 174.766 0.1 1
645 . 169 LEU N N 124.595 0.1 1
646 . 169 LEU H H 8.459 0.02 1
647 . 169 LEU CA C 53.914 0.1 1
648 . 169 LEU CB C 42.619 0.1 1
649 . 180 GLU CA C 56.817 0.1 1
650 . 180 GLU C C 174.766 0.1 1
651 . 181 MET N N 119.535 0.1 1
652 . 181 MET H H 8.146 0.02 1
653 . 181 MET CA C 55.466 0.1 1
654 . 181 MET CB C 31.398 0.1 1
655 . 181 MET C C 176.561 0.1 1
656 . 182 THR N N 113.484 0.1 1
657 . 182 THR H H 7.927 0.02 1
658 . 182 THR CA C 61.726 0.1 1
659 . 182 THR CB C 68.877 0.1 1
660 . 182 THR C C 175.232 0.1 1
661 . 183 GLY N N 110.726 0.1 1
662 . 183 GLY H H 8.253 0.02 1
663 . 183 GLY CA C 44.698 0.1 1
664 . 183 GLY C C 173.74 0.1 1
665 . 184 TYR N N 120.401 0.1 1
666 . 184 TYR H H 7.858 0.02 1
667 . 184 TYR CA C 57.478 0.1 1
668 . 184 TYR CB C 37.581 0.1 1
669 . 185 VAL N N 122.618 0.1 1
670 . 185 VAL H H 7.787 0.02 1
671 . 185 VAL CA C 61.651 0.1 1
672 . 185 VAL CB C 40.711 0.1 1
673 . 185 VAL C C 176.536 0.1 1
674 . 207 ASP C C 177.564 0.1 1
675 . 208 ILE N N 118.779 0.1 1
676 . 208 ILE H H 7.305 0.02 1
677 . 208 ILE CA C 60.529 0.1 1
678 . 208 ILE CB C 34.146 0.1 1
679 . 208 ILE C C 177.797 0.1 1
680 . 209 TRP N N 120.459 0.1 1
681 . 209 TRP H H 7.513 0.02 1
682 . 209 TRP CB C 27.581 0.1 1
683 . 209 TRP C C 179.815 0.1 1
684 . 210 SER N N 112.138 0.1 1
685 . 210 SER H H 7.591 0.02 1
686 . 210 SER CA C 60.999 0.1 1
687 . 210 SER CB C 62.771 0.1 1
688 . 210 SER C C 176.27 0.1 1
689 . 211 VAL N N 119.389 0.1 1
690 . 211 VAL H H 8.004 0.02 1
691 . 211 VAL CA C 66.802 0.1 1
692 . 211 VAL CB C 29.642 0.1 1
693 . 211 VAL C C 176.911 0.1 1
694 . 212 GLY N N 109.772 0.1 1
695 . 212 GLY H H 8.515 0.02 1
696 . 212 GLY CA C 47.502 0.1 1
697 . 212 GLY C C 174.276 0.1 1
698 . 213 CYS N N 118.866 0.1 1
699 . 213 CYS H H 7.894 0.02 1
700 . 213 CYS CA C 63.216 0.1 1
701 . 213 CYS CB C 27.2 0.1 1
702 . 213 CYS C C 179.01 0.1 1
703 . 214 ILE N N 123.718 0.1 1
704 . 214 ILE H H 8.44 0.02 1
705 . 214 ILE CA C 65.238 0.1 1
706 . 214 ILE CB C 37.505 0.1 1
707 . 214 ILE C C 176.165 0.1 1
708 . 215 MET N N 120.101 0.1 1
709 . 215 MET H H 9.308 0.02 1
710 . 215 MET CA C 59.695 0.1 1
711 . 215 MET CB C 31.016 0.1 1
712 . 215 MET C C 176.841 0.1 1
713 . 216 ALA N N 117.903 0.1 1
714 . 216 ALA H H 8.159 0.02 1
715 . 216 ALA CA C 54.935 0.1 1
716 . 216 ALA CB C 19.49 0.1 1
717 . 216 ALA C C 178.683 0.1 1
718 . 217 GLU N N 119.396 0.1 1
719 . 217 GLU H H 7.135 0.02 1
720 . 217 GLU CA C 57.152 0.1 1
721 . 217 GLU CB C 28.879 0.1 1
722 . 217 GLU C C 178.742 0.1 1
723 . 218 LEU N N 115.389 0.1 1
724 . 218 LEU H H 7.825 0.02 1
725 . 218 LEU CA C 55.719 0.1 1
726 . 218 LEU CB C 42.161 0.1 1
727 . 218 LEU C C 174.454 0.1 1
728 . 219 LEU C C 179.383 0.1 1
729 . 220 THR N N 105.449 0.1 1
730 . 220 THR H H 7.949 0.02 1
731 . 220 THR CA C 61.726 0.1 1
732 . 220 THR CB C 71.014 0.1 1
733 . 220 THR C C 176.375 0.1 1
734 . 221 GLY N N 112.119 0.1 1
735 . 221 GLY H H 8.434 0.02 1
736 . 221 GLY CA C 44.959 0.1 1
737 . 221 GLY C C 173.309 0.1 1
738 . 222 ARG N N 118.389 0.1 1
739 . 222 ARG H H 8.014 0.02 1
740 . 222 ARG CA C 53.268 0.1 1
741 . 222 ARG CB C 32.045 0.1 1
742 . 222 ARG C C 174.253 0.1 1
743 . 223 THR N N 119.431 0.1 1
744 . 223 THR H H 7.945 0.02 1
745 . 223 THR CA C 62.774 0.1 1
746 . 223 THR CB C 68.233 0.1 1
747 . 223 THR C C 174.299 0.1 1
748 . 224 LEU N N 117.272 0.1 1
749 . 224 LEU H H 7.85 0.02 1
750 . 224 LEU CA C 52.594 0.1 1
751 . 224 LEU CB C 40.56 0.1 1
752 . 224 LEU C C 177.564 0.1 1
753 . 225 PHE N N 129.516 0.1 1
754 . 225 PHE H H 9.417 0.02 1
755 . 225 PHE CA C 62.27 0.1 1
756 . 225 PHE CB C 36.911 0.1 1
757 . 226 PRO C C 176.048 0.1 1
758 . 227 GLY N N 112.977 0.1 1
759 . 227 GLY H H 8.352 0.02 1
760 . 227 GLY CA C 44.763 0.1 1
761 . 227 GLY C C 176.141 0.1 1
762 . 228 THR N N 116.233 0.1 1
763 . 228 THR H H 10.11 0.02 1
764 . 228 THR CA C 63.533 0.1 1
765 . 228 THR CB C 64.052 0.1 1
766 . 256 SER C C 177.331 0.1 1
767 . 257 ALA N N 124.968 0.1 1
768 . 257 ALA H H 7.698 0.02 1
769 . 257 ALA CA C 54.241 0.1 1
770 . 257 ALA CB C 17.981 0.1 1
771 . 257 ALA C C 179.383 0.1 1
772 . 260 TYR CA C 64.812 0.1 1
773 . 260 TYR CB C 37.443 0.1 1
774 . 260 TYR C C 176.421 0.1 1
775 . 261 ILE N N 118.427 0.1 1
776 . 261 ILE H H 7.575 0.02 1
777 . 261 ILE CA C 63.523 0.1 1
778 . 261 ILE CB C 36.607 0.1 1
779 . 261 ILE C C 178.31 0.1 1
780 . 262 GLN N N 117.656 0.1 1
781 . 262 GLN H H 8.111 0.02 1
782 . 262 GLN CA C 57.759 0.1 1
783 . 262 GLN CB C 28.016 0.1 1
784 . 262 GLN C C 176.095 0.1 1
785 . 263 SER N N 113.519 0.1 1
786 . 263 SER H H 7.44 0.02 1
787 . 263 SER CA C 58.657 0.1 1
788 . 263 SER CB C 62.9 0.1 1
789 . 263 SER C C 173.973 0.1 1
790 . 264 LEU N N 122.623 0.1 1
791 . 264 LEU H H 6.962 0.02 1
792 . 264 LEU CA C 53.567 0.1 1
793 . 264 LEU CB C 41.018 0.1 1
794 . 264 LEU C C 177.097 0.1 1
795 . 265 ALA N N 123.726 0.1 1
796 . 265 ALA H H 8.043 0.02 1
797 . 265 ALA CA C 51.846 0.1 1
798 . 265 ALA CB C 17.546 0.1 1
799 . 265 ALA C C 177.261 0.1 1
800 . 266 GLN N N 119.789 0.1 1
801 . 266 GLN H H 8.212 0.02 1
802 . 266 GLN CA C 56.112 0.1 1
803 . 266 GLN CB C 27.162 0.1 1
804 . 266 GLN C C 176.235 0.1 1
805 . 267 MET N N 123.917 0.1 1
806 . 267 MET H H 8.717 0.02 1
807 . 267 MET CA C 51.878 0.1 1
808 . 268 PRO CA C 57.464 0.1 1
809 . 268 PRO CB C 29.185 0.1 1
810 . 268 PRO C C 175.465 0.1 1
811 . 269 LYS N N 120.065 0.1 1
812 . 269 LYS H H 8.268 0.02 1
813 . 269 LYS CA C 56.304 0.1 1
814 . 269 LYS CB C 31.402 0.1 1
815 . 269 LYS C C 177.587 0.1 1
816 . 270 MET N N 125.51 0.1 1
817 . 270 MET H H 8.411 0.02 1
818 . 270 MET CA C 55.522 0.1 1
819 . 270 MET C C 174.183 0.1 1
820 . 271 ASN N N 130.206 0.1 1
821 . 271 ASN H H 8.636 0.02 1
822 . 271 ASN CA C 57.385 0.1 1
823 . 271 ASN CB C 39.958 0.1 1
824 . 271 ASN C C 175.838 0.1 1
825 . 272 PHE N N 113.679 0.1 1
826 . 272 PHE H H 8.564 0.02 1
827 . 272 PHE CA C 51.675 0.1 1
828 . 272 PHE CB C 39.503 0.1 1
829 . 272 PHE C C 177.75 0.1 1
830 . 273 ALA N N 121.809 0.1 1
831 . 273 ALA H H 8.548 0.02 1
832 . 273 ALA CA C 54.087 0.1 1
833 . 273 ALA CB C 16.814 0.1 1
834 . 273 ALA C C 178.322 0.1 1
835 . 274 ASN N N 112.388 0.1 1
836 . 274 ASN H H 7.466 0.02 1
837 . 274 ASN CA C 53.268 0.1 1
838 . 274 ASN CB C 38.004 0.1 1
839 . 274 ASN C C 175.209 0.1 1
840 . 275 VAL N N 119.566 0.1 1
841 . 275 VAL H H 7.207 0.02 1
842 . 275 VAL CA C 63.523 0.1 1
843 . 275 VAL CB C 31.896 0.1 1
844 . 275 VAL C C 176.584 0.1 1
845 . 276 PHE N N 120.239 0.1 1
846 . 276 PHE H H 7.621 0.02 1
847 . 276 PHE CA C 55.391 0.1 1
848 . 276 PHE CB C 36.043 0.1 1
849 . 276 PHE C C 175.349 0.1 1
850 . 277 ILE N N 120.416 0.1 1
851 . 277 ILE H H 6.876 0.02 1
852 . 277 ILE CA C 61.782 0.1 1
853 . 277 ILE CB C 36.345 0.1 1
854 . 277 ILE C C 177.797 0.1 1
855 . 278 GLY N N 115.679 0.1 1
856 . 278 GLY H H 8.992 0.02 1
857 . 278 GLY CA C 44.502 0.1 1
858 . 278 GLY C C 173.833 0.1 1
859 . 279 ALA N N 121.521 0.1 1
860 . 279 ALA H H 7.411 0.02 1
861 . 279 ALA CA C 50.501 0.1 1
862 . 279 ALA CB C 18.775 0.1 1
863 . 279 ALA C C 176.748 0.1 1
864 . 280 ASN N N 121.951 0.1 1
865 . 280 ASN H H 9.091 0.02 1
866 . 280 ASN CA C 50.762 0.1 1
867 . 280 ASN CB C 38.23 0.1 1
868 . 280 ASN C C 176.613 0.1 1
869 . 281 PRO C C 179.919 0.1 1
870 . 282 LEU N N 116.631 0.1 1
871 . 282 LEU H H 8.435 0.02 1
872 . 282 LEU CA C 56.5 0.1 1
873 . 282 LEU CB C 41.699 0.1 1
874 . 282 LEU C C 178.543 0.1 1
875 . 283 ALA N N 120.572 0.1 1
876 . 283 ALA H H 7.114 0.02 1
877 . 283 ALA CB C 16.814 0.1 1
878 . 283 ALA C C 178.796 0.1 1
879 . 284 VAL N N 115.841 0.1 1
880 . 284 VAL H H 7.087 0.02 1
881 . 284 VAL CA C 65.993 0.1 1
882 . 284 VAL CB C 30.661 0.1 1
883 . 295 SER CA C 60.701 0.1 1
884 . 295 SER CB C 62.578 0.1 1
885 . 295 SER C C 176.06 0.1 1
886 . 296 ASP N N 120.389 0.1 1
887 . 296 ASP H H 8.461 0.02 1
888 . 296 ASP CA C 55.76 0.1 1
889 . 296 ASP CB C 39.973 0.1 1
890 . 296 ASP C C 177.144 0.1 1
891 . 297 LYS N N 117.008 0.1 1
892 . 297 LYS H H 7.628 0.02 1
893 . 297 LYS CA C 54.54 0.1 1
894 . 297 LYS CB C 32.838 0.1 1
895 . 297 LYS C C 176.165 0.1 1
896 . 298 ARG N N 122.127 0.1 1
897 . 298 ARG H H 7.063 0.02 1
898 . 298 ARG CA C 56.786 0.1 1
899 . 298 ARG CB C 29.534 0.1 1
900 . 298 ARG C C 174.463 0.1 1
901 . 299 ILE N N 124.579 0.1 1
902 . 299 ILE H H 7.063 0.02 1
903 . 299 ILE CA C 61.586 0.1 1
904 . 299 ILE CB C 38.922 0.1 1
905 . 299 ILE C C 171.828 0.1 1
906 . 300 THR N N 108.773 0.1 1
907 . 300 THR H H 7.376 0.02 1
908 . 300 THR CA C 59.565 0.1 1
909 . 300 THR CB C 70.464 0.1 1
910 . 300 THR C C 175.792 0.1 1
911 . 301 ALA N N 121.649 0.1 1
912 . 301 ALA H H 9.5 0.02 1
913 . 301 ALA CA C 55.652 0.1 1
914 . 301 ALA CB C 15.791 0.1 1
915 . 301 ALA C C 178.59 0.1 1
916 . 302 ALA N N 115.711 0.1 1
917 . 302 ALA H H 8.623 0.02 1
918 . 302 ALA CA C 54.544 0.1 1
919 . 302 ALA CB C 17.593 0.1 1
920 . 302 ALA C C 180.433 0.1 1
921 . 303 GLN N N 115.639 0.1 1
922 . 303 GLN H H 7.413 0.02 1
923 . 303 GLN CA C 57.804 0.1 1
924 . 303 GLN CB C 27.732 0.1 1
925 . 303 GLN C C 179.465 0.1 1
926 . 304 ALA N N 123.389 0.1 1
927 . 304 ALA H H 8.679 0.02 1
928 . 304 ALA CA C 54.348 0.1 1
929 . 304 ALA CB C 18.367 0.1 1
930 . 304 ALA C C 178.8 0.1 1
931 . 305 LEU N N 115.841 0.1 1
932 . 305 LEU H H 7.656 0.02 1
933 . 305 LEU CA C 56.956 0.1 1
934 . 305 LEU CB C 40.88 0.1 1
935 . 305 LEU C C 175.582 0.1 1
936 . 306 ALA N N 114.595 0.1 1
937 . 306 ALA H H 6.603 0.02 1
938 . 306 ALA CA C 50.566 0.1 1
939 . 306 ALA CB C 17.919 0.1 1
940 . 306 ALA C C 176.678 0.1 1
941 . 307 HIS N N 122.225 0.1 1
942 . 307 HIS H H 7.964 0.02 1
943 . 307 HIS CA C 58.195 0.1 1
944 . 307 HIS CB C 31.98 0.1 1
945 . 307 HIS C C 177.191 0.1 1
946 . 308 ALA N N 132.02 0.1 1
947 . 308 ALA H H 8.328 0.02 1
948 . 308 ALA CA C 54.674 0.1 1
949 . 308 ALA CB C 17.919 0.1 1
950 . 308 ALA C C 179.099 0.1 1
951 . 309 TYR N N 124.614 0.1 1
952 . 309 TYR H H 11.641 0.02 1
953 . 309 TYR CA C 59.499 0.1 1
954 . 309 TYR CB C 37.963 0.1 1
955 . 309 TYR C C 179.23 0.1 1
956 . 310 PHE N N 109.984 0.1 1
957 . 310 PHE H H 7.669 0.02 1
958 . 310 PHE CA C 55.391 0.1 1
959 . 310 PHE CB C 37.963 0.1 1
960 . 310 PHE C C 176.771 0.1 1
961 . 311 ALA N N 123.091 0.1 1
962 . 311 ALA H H 7.533 0.02 1
963 . 311 ALA CA C 55.326 0.1 1
964 . 311 ALA CB C 17.993 0.1 1
965 . 311 ALA C C 178.893 0.1 1
966 . 312 GLN N N 113.508 0.1 1
967 . 312 GLN H H 8.658 0.02 1
968 . 312 GLN CA C 56.63 0.1 1
969 . 312 GLN CB C 27.343 0.1 1
970 . 312 GLN C C 175.209 0.1 1
971 . 313 TYR N N 115.476 0.1 1
972 . 313 TYR H H 7.476 0.02 1
973 . 313 TYR CA C 57.984 0.1 1
974 . 313 TYR CB C 39.459 0.1 1
975 . 314 HIS CA C 59.062 0.1 1
976 . 314 HIS CB C 29.491 0.1 1
977 . 314 HIS C C 176.071 0.1 1
978 . 315 ASP N N 126.371 0.1 1
979 . 315 ASP H H 10.091 0.02 1
980 . 315 ASP CA C 52.196 0.1 1
981 . 315 ASP CB C 41.334 0.1 1
982 . 316 PRO CA C 63.456 0.1 1
983 . 316 PRO CB C 31.055 0.1 1
984 . 316 PRO C C 177.914 0.1 1
985 . 317 ASP N N 116.949 0.1 1
986 . 317 ASP H H 7.963 0.02 1
987 . 317 ASP CA C 54.989 0.1 1
988 . 317 ASP CB C 39.844 0.1 1
989 . 317 ASP C C 175.698 0.1 1
990 . 318 ASP N N 120.678 0.1 1
991 . 318 ASP H H 8.014 0.02 1
992 . 318 ASP CA C 52.22 0.1 1
993 . 318 ASP CB C 41.483 0.1 1
994 . 318 ASP C C 175.652 0.1 1
995 . 319 GLU N N 120.863 0.1 1
996 . 319 GLU H H 7.755 0.02 1
997 . 319 GLU CA C 52.894 0.1 1
998 . 319 GLU CB C 28.746 0.1 1
999 . 319 GLU C C 172.733 0.1 1
1000 . 320 PRO CA C 62.711 0.1 1
1001 . 320 PRO CB C 33.215 0.1 1
1002 . 320 PRO C C 177.051 0.1 1
1003 . 321 VAL N N 108.69 0.1 1
1004 . 321 VAL H H 7.847 0.02 1
1005 . 321 VAL CA C 58.874 0.1 1
1006 . 321 VAL CB C 32.992 0.1 1
1007 . 321 VAL C C 174.906 0.1 1
1008 . 322 ALA N N 123.07 0.1 1
1009 . 322 ALA H H 8.44 0.02 1
1010 . 322 ALA CA C 50.371 0.1 1
1011 . 322 ALA C C 178.095 0.1 1
1012 . 323 ASP N N 120.389 0.1 1
1013 . 323 ASP H H 8.067 0.02 1
1014 . 323 ASP CA C 52.692 0.1 1
1015 . 323 ASP CB C 38.727 0.1 1
1016 . 323 ASP C C 174.067 0.1 1
1017 . 328 SER C C 176.654 0.1 1
1018 . 329 PHE N N 118.438 0.1 1
1019 . 329 PHE H H 7.822 0.02 1
1020 . 329 PHE CA C 58.957 0.1 1
1021 . 329 PHE CB C 37.759 0.1 1
1022 . 330 GLU C C 178.357 0.1 1
1023 . 331 SER N N 111.422 0.1 1
1024 . 331 SER H H 7.448 0.02 1
1025 . 331 SER CA C 57.478 0.1 1
1026 . 331 SER CB C 62.935 0.1 1
1027 . 331 SER C C 174.206 0.1 1
1028 . 332 ARG N N 121.325 0.1 1
1029 . 332 ARG H H 7.6 0.02 1
1030 . 332 ARG CA C 55.652 0.1 1
1031 . 332 ARG CB C 30.236 0.1 1
1032 . 332 ARG C C 174.976 0.1 1
1033 . 333 ASP N N 124.225 0.1 1
1034 . 333 ASP H H 8.569 0.02 1
1035 . 333 ASP CA C 52.588 0.1 1
1036 . 333 ASP CB C 40.142 0.1 1
1037 . 333 ASP C C 174.159 0.1 1
1038 . 334 LEU N N 122.56 0.1 1
1039 . 334 LEU H H 7.805 0.02 1
1040 . 334 LEU CA C 52.327 0.1 1
1041 . 334 LEU CB C 40.962 0.1 1
1042 . 334 LEU C C 176.841 0.1 1
1043 . 335 LEU N N 119.306 0.1 1
1044 . 335 LEU H H 8.778 0.02 1
1045 . 335 LEU CA C 53.566 0.1 1
1046 . 335 LEU CB C 41.26 0.1 1
1047 . 335 LEU C C 179.616 0.1 1
1048 . 336 ILE N N 121.171 0.1 1
1049 . 336 ILE H H 8.968 0.02 1
1050 . 336 ILE CA C 66.15 0.1 1
1051 . 336 ILE CB C 36.939 0.1 1
1052 . 336 ILE C C 177.307 0.1 1
1053 . 337 ASP N N 115.238 0.1 1
1054 . 337 ASP H H 8.385 0.02 1
1055 . 337 ASP CA C 56.761 0.1 1
1056 . 337 ASP CB C 39.249 0.1 1
1057 . 337 ASP C C 178.753 0.1 1
1058 . 338 GLU N N 119.998 0.1 1
1059 . 338 GLU H H 7.112 0.02 1
1060 . 338 GLU CA C 58 0.1 1
1061 . 338 GLU CB C 29.118 0.1 1
1062 . 338 GLU C C 178.986 0.1 1
1063 . 339 TRP N N 119.2 0.1 1
1064 . 339 TRP H H 7.713 0.02 1
1065 . 339 TRP CA C 59.481 0.1 1
1066 . 339 TRP CB C 30.14 0.1 1
1067 . 339 TRP C C 180.502 0.1 1
1068 . 340 LYS N N 120.913 0.1 1
1069 . 340 LYS H H 8.747 0.02 1
1070 . 340 LYS CA C 59.695 0.1 1
1071 . 340 LYS CB C 31.401 0.1 1
1072 . 340 LYS C C 177.377 0.1 1
1073 . 341 SER N N 114.061 0.1 1
1074 . 341 SER H H 7.63 0.02 1
1075 . 341 SER CA C 60.304 0.1 1
1076 . 341 SER CB C 61.888 0.1 1
1077 . 341 SER C C 177.996 0.1 1
1078 . 342 LEU N N 119.889 0.1 1
1079 . 342 LEU H H 7.939 0.02 1
1080 . 342 LEU CA C 57.253 0.1 1
1081 . 342 LEU CB C 41.192 0.1 1
1082 . 343 THR C C 175.512 0.1 1
1083 . 344 TYR N N 124.222 0.1 1
1084 . 344 TYR H H 8.819 0.02 1
1085 . 344 TYR CA C 61.39 0.1 1
1086 . 344 TYR CB C 37.112 0.1 1
1087 . 344 TYR C C 181.3 0.1 1
1088 . 345 ASP N N 116.639 0.1 1
1089 . 345 ASP H H 8.068 0.02 1
1090 . 345 ASP CA C 56.636 0.1 1
1091 . 345 ASP CB C 39.354 0.1 1
1092 . 345 ASP C C 179.709 0.1 1
1093 . 346 GLU N N 117.679 0.1 1
1094 . 346 GLU H H 7.491 0.02 1
1095 . 346 GLU CA C 57.348 0.1 1
1096 . 346 GLU CB C 28.643 0.1 1
1097 . 346 GLU C C 178.79 0.1 1
1098 . 347 VAL N N 120.323 0.1 1
1099 . 347 VAL H H 8.077 0.02 1
1100 . 347 VAL CA C 65.433 0.1 1
1101 . 347 VAL CB C 30.637 0.1 1
1102 . 347 VAL C C 178.543 0.1 1
1103 . 348 ILE N N 113.955 0.1 1
1104 . 348 ILE H H 8.087 0.02 1
1105 . 348 ILE CA C 62.27 0.1 1
1106 . 348 ILE CB C 36.03 0.1 1
1107 . 348 ILE C C 177.494 0.1 1
1108 . 349 SER N N 112.848 0.1 1
1109 . 349 SER H H 7.402 0.02 1
1110 . 349 SER CA C 57.608 0.1 1
1111 . 349 SER CB C 63.14 0.1 1
1112 . 349 SER C C 176.89 0.1 1
1113 . 350 PHE N N 124.358 0.1 1
1114 . 350 PHE H H 7.29 0.02 1
1115 . 350 PHE CA C 59.825 0.1 1
1116 . 350 PHE CB C 38.984 0.1 1
1117 . 350 PHE C C 173.833 0.1 1
1118 . 351 VAL N N 129.601 0.1 1
1119 . 351 VAL H H 6.899 0.02 1
1120 . 351 VAL CA C 62.955 0.1 1
1121 . 351 VAL CB C 32.927 0.1 1
1122 . 351 VAL C C 179.328 0.1 1
stop_
save_