BMRB Entry 19935

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19935

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Title:
Dual-phosphorylated human p38 alpha ILVM methyl resonance assignments in ADP-bound state
Deposition date:
2014-04-24
Original release date:
2014-08-05
Authors:
Tokunaga, Yuji; Takeuchi, Koh; Takahashi, Hideo; Shimada, Ichio
Citation:

Citation: Tokunaga, Yuji; Takeuchi, Koh; Takahashi, Hideo; Shimada, Ichio. "Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions."  Nat. Struct. Mol. Biol. 21, 704-711 (2014).
PubMed: 25038803

Assembly members:

Assembly members:
Dual-phosphorylated_human_p38_alpha, polymer, 367 residues, Formula weight is not available
ADENOSINE-5'-DIPHOSPHATE, non-polymer, 427.201 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dual-phosphorylated_human_p38_alpha: MAHHHHHHSQERPTFYRQEL NKTIWEVPERYQNLSPVGSG AYGSVCAAFDTKTGLRVAVK KLSRPFQSIIHAKRTYRELR LLKHMKHENVIGLLDVFTPA RSLEEFNDVYLVTHLMGADL NNIVKCQKLTDDHVQFLIYQ ILRGLKYIHSADIIHRDLKP SNLAVNEDCELKILDFGLAR HTDDEMXGXVATRWYRAPEI MLNWMHYNQTVDIWSVGCIM AELLTGRTLFPGTDHIDQLK LILRLVGTPGAELLKKISSE SARNYIQSLTQMPKMNFANV FIGANPLAVDLLEKMLVLDS DKRITAAQALAHAYFAQYHD PDDEPVADPYDQSFESRDLL IDEWKSLTYDEVISFVPPPL DQEEMES

Data sets:
Data typeCount
1H chemical shifts378
13C chemical shifts126

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1dual-phosphorylated human p38 alpha (apo)1
2ADP2

Entities:

Entity 1, dual-phosphorylated human p38 alpha (apo) 367 residues - Formula weight is not available

Residues 2-8 represent a non-native affinity tag. Thr-180 and Tyr-182 in native sequence are phosphorylated.

1   METALAHISHISHISHISHISHISSERGLN
2   GLUARGPROTHRPHETYRARGGLNGLULEU
3   ASNLYSTHRILETRPGLUVALPROGLUARG
4   TYRGLNASNLEUSERPROVALGLYSERGLY
5   ALATYRGLYSERVALCYSALAALAPHEASP
6   THRLYSTHRGLYLEUARGVALALAVALLYS
7   LYSLEUSERARGPROPHEGLNSERILEILE
8   HISALALYSARGTHRTYRARGGLULEUARG
9   LEULEULYSHISMETLYSHISGLUASNVAL
10   ILEGLYLEULEUASPVALPHETHRPROALA
11   ARGSERLEUGLUGLUPHEASNASPVALTYR
12   LEUVALTHRHISLEUMETGLYALAASPLEU
13   ASNASNILEVALLYSCYSGLNLYSLEUTHR
14   ASPASPHISVALGLNPHELEUILETYRGLN
15   ILELEUARGGLYLEULYSTYRILEHISSER
16   ALAASPILEILEHISARGASPLEULYSPRO
17   SERASNLEUALAVALASNGLUASPCYSGLU
18   LEULYSILELEUASPPHEGLYLEUALAARG
19   HISTHRASPASPGLUMETTPOGLYPTRVAL
20   ALATHRARGTRPTYRARGALAPROGLUILE
21   METLEUASNTRPMETHISTYRASNGLNTHR
22   VALASPILETRPSERVALGLYCYSILEMET
23   ALAGLULEULEUTHRGLYARGTHRLEUPHE
24   PROGLYTHRASPHISILEASPGLNLEULYS
25   LEUILELEUARGLEUVALGLYTHRPROGLY
26   ALAGLULEULEULYSLYSILESERSERGLU
27   SERALAARGASNTYRILEGLNSERLEUTHR
28   GLNMETPROLYSMETASNPHEALAASNVAL
29   PHEILEGLYALAASNPROLEUALAVALASP
30   LEULEUGLULYSMETLEUVALLEUASPSER
31   ASPLYSARGILETHRALAALAGLNALALEU
32   ALAHISALATYRPHEALAGLNTYRHISASP
33   PROASPASPGLUPROVALALAASPPROTYR
34   ASPGLNSERPHEGLUSERARGASPLEULEU
35   ILEASPGLUTRPLYSSERLEUTHRTYRASP
36   GLUVALILESERPHEVALPROPROPROLEU
37   ASPGLNGLUGLUMETGLUSER

Entity 2, ADP - 427.201 Da.

1   ADP

Samples:

sample_3: dual-phosphorylated human p38 alpha (apo), U-2H15N13C, ILVM-methyl-1H13C], 0.2 mM; TRIS, [U-100% 2H], 25 mM; potassium chloride 150 mM; DTT, [U-2H], 5 mM; ADP 5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: temperature: 298 K; pH: 7.5; pressure: 1 atm; ionic strength: 150 mM

Experiments:

NameSampleSample stateSample conditions
(H)CC(CO)NHsample_3isotropicsample_conditions_1
H(CCCO)NHsample_3isotropicsample_conditions_1
HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

CARA, Keller, R. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17471 17940 19930 19934 19936 19937
PDB
DBJ BAB85654 BAE21782 BAE30324 BAE31659 BAF84398
EMBL CAG38743
GB AAA20888 AAA57456 AAA74301 AAB51285 AAC36131
PRF 2111247A 2124426A
REF NP_001003206 NP_001136366 NP_001161985 NP_001161986 NP_036081
SP O02812 P47811 P70618 Q16539
AlphaFold O02812 P47811 P70618 Q16539