BMRB Entry 27273

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments of phosphorylated (T183 and Y185) p38 alpha
Deposition date:
2017-10-04
Original release date:
2018-05-22
Authors:
Ganesan, Senthil Kumar; Page, Rebecca; Peti, Wolfgang
Citation:

Citation: Kumar, Ganesan Senthil; Clarkson, Michael; Kunze, Micha; Granata, Daniele; Wand, A Joshua; Lindorff-Larsen, Kresten; Page, Rebecca; Peti, Wolfgang. "Dynamic activation and regulation of the mitogen-activated protein kinase p38"  Proc. Natl. Acad. Sci. U.S.A. 115, 4655-4660 (2018).
PubMed: 29666261

Assembly members:

Assembly members:
dp-p38_alpha, polymer, 352 residues, 40450 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: RP1B

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts268
1H chemical shifts268

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1dp-p38 alpha1

Entities:

Entity 1, dp-p38 alpha 352 residues - 40450 Da.

Residues 1-3 are products of a non-native cloning artifact; Native Residue 183 is phosphorylated threonine and native residue 185 is phosphorylated tyrosine.

1   GLYHISMETGLYSERGLNGLUARGPROTHR
2   PHETYRARGGLNGLULEUASNLYSTHRILE
3   TRPGLUVALPROGLUARGTYRGLNASNLEU
4   SERPROVALGLYSERGLYALATYRGLYSER
5   VALCYSALAALAPHEASPTHRLYSTHRGLY
6   LEUARGVALALAVALLYSLYSLEUSERARG
7   PROPHEGLNSERILEILEHISALALYSARG
8   THRTYRARGGLULEUARGLEULEULYSHIS
9   METLYSHISGLUASNVALILEGLYLEULEU
10   ASPVALPHETHRPROALAARGSERLEUGLU
11   GLUPHEASNASPVALTYRLEUVALTHRHIS
12   LEUMETGLYALAASPLEUASNASNILEVAL
13   LYSCYSGLNLYSLEUTHRASPASPHISVAL
14   GLNPHELEUILETYRGLNILELEUARGGLY
15   LEULYSTYRILEHISSERALAASPILEILE
16   HISARGASPLEULYSPROSERASNLEUALA
17   VALASNGLUASPCYSGLULEULYSILELEU
18   ASPPHEGLYLEUALAARGHISTHRASPASP
19   GLUMETTPOGLYPTRVALALATHRARGTRP
20   TYRARGALAPROGLUILEMETLEUASNTRP
21   METHISTYRASNGLNTHRVALASPILETRP
22   SERVALGLYCYSILEMETALAGLULEULEU
23   THRGLYARGTHRLEUPHEPROGLYTHRASP
24   HISILEASPGLNLEULYSLEUILELEUARG
25   LEUVALGLYTHRPROGLYALAGLULEULEU
26   LYSLYSILESERSERGLUSERALAARGASN
27   TYRILEGLNSERLEUTHRGLNMETPROLYS
28   METASNPHEALAASNVALPHEILEGLYALA
29   ASNPROLEUALAVALASPLEULEUGLULYS
30   METLEUVALLEUASPSERASPLYSARGILE
31   THRALAALAGLNALALEUALAHISALATYR
32   PHEALAGLNTYRHISASPPROASPASPGLU
33   PROVALALAASPPROTYRASPGLNSERPHE
34   GLUSERARGASPLEULEUILEASPGLUTRP
35   LYSSERLEUTHRTYRASPGLUVALILESER
36   PHEVAL

Samples:

sample_1: dp-p38_alpha, [U-2H; U-13C; U-15N], 0.35 mM; HEPES 10 mM; sodium chloride 150 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

Sparky vNMRFAM, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

BMRB 17471
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks