BMRB Entry 17471

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for p38 alpha MAPK   PubMed: 22057126
Deposition date:
2011-02-15
Original release date:
2011-12-12
Authors:
Francis, Dana; Peti, Wolfgang; Page, Rebecca
Citation:

Citation: Francis, Dana; Roycki, Bartosz; Koveal, Dorothy; Hummer, Gerhard; Page, Rebecca; Peti, Wolfgang. "Structural basis of p38 regulation by hematopoietic tyrosine phosphatase."  Nat. Chem. Biol. 7, 916-924 (2011).

Assembly members:

Assembly members:
p38_alpha, polymer, 352 residues, 40290 Da.

Natural source:

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

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

Experimental source:

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

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

Data sets:
Data typeCount
13C chemical shifts585
15N chemical shifts273
1H chemical shifts273

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p38 alpha1

Entities:

Entity 1, p38 alpha 352 residues - 40290 Da.

Residues 1-3 are products of a non-native cloning artifact.

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   GLUMETTHRGLYTYRVALALATHRARGTRP
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: p38_alpha, [U-13C; U-15N; U-2H], 0.58 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_2: p38 alpha, [U-2H;U-15N], 0.2 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v1.3 and 2.1, Bruker Biospin - collection, processing

CARA v1.8, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17940 19930 19934 19935 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 P70618

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