BMRB Entry 26733

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26733

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for MAPK p38g
Deposition date:
2016-01-15
Original release date:
2016-07-14
Authors:
Aoto, Phillip; Wright, Peter
Citation:

Citation: Aoto, Phillip; Martin, Bryan; Wright, Peter. "NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38\u03b3"  Sci. Rep. 6, 28655-28655 (2016).
PubMed: 27353957

Assembly members:

Assembly members:
MAPK_p38g, polymer, 367 residues, Formula weight is not available

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):
MAPK_p38g: MSSPPPARSGFYRQEVTKTA WEVRAVYRDLQPVGSGAYGA VCSAVDGRTGAKVAIKKLYR PFQSELFAKRAYRELRLLKH MRHENVIGLLDVFTPDETLD DFTDFYLVMPFMGTDLGKLM KHEKLGEDRIQFLVYQMLKG LRYIHAAGIIHRDLKPGNLA VNEDCELKILDFGLARQADS EMTGYVVTRWYRAPEVILNW MRYTQTVDIWSVGCIMAEMI TGKTLFKGSDHLDQLKEIMK VTGTPPAEFVQRLQSDEAKN YMKGLPELEKKDFASILTNA SPLAVNLLEKMLVLDAEQRV TAGEALAHPYFESLHDTEDE PQVQKYDDSFDDVDRTLDEW KRVTYKEVLSFKPPRQLGAR VSKETPL

Data sets:
Data typeCount
13C chemical shifts769
15N chemical shifts281
1H chemical shifts267

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p38g monomer1

Entities:

Entity 1, p38g monomer 367 residues - Formula weight is not available

1   METSERSERPROPROPROALAARGSERGLY
2   PHETYRARGGLNGLUVALTHRLYSTHRALA
3   TRPGLUVALARGALAVALTYRARGASPLEU
4   GLNPROVALGLYSERGLYALATYRGLYALA
5   VALCYSSERALAVALASPGLYARGTHRGLY
6   ALALYSVALALAILELYSLYSLEUTYRARG
7   PROPHEGLNSERGLULEUPHEALALYSARG
8   ALATYRARGGLULEUARGLEULEULYSHIS
9   METARGHISGLUASNVALILEGLYLEULEU
10   ASPVALPHETHRPROASPGLUTHRLEUASP
11   ASPPHETHRASPPHETYRLEUVALMETPRO
12   PHEMETGLYTHRASPLEUGLYLYSLEUMET
13   LYSHISGLULYSLEUGLYGLUASPARGILE
14   GLNPHELEUVALTYRGLNMETLEULYSGLY
15   LEUARGTYRILEHISALAALAGLYILEILE
16   HISARGASPLEULYSPROGLYASNLEUALA
17   VALASNGLUASPCYSGLULEULYSILELEU
18   ASPPHEGLYLEUALAARGGLNALAASPSER
19   GLUMETTHRGLYTYRVALVALTHRARGTRP
20   TYRARGALAPROGLUVALILELEUASNTRP
21   METARGTYRTHRGLNTHRVALASPILETRP
22   SERVALGLYCYSILEMETALAGLUMETILE
23   THRGLYLYSTHRLEUPHELYSGLYSERASP
24   HISLEUASPGLNLEULYSGLUILEMETLYS
25   VALTHRGLYTHRPROPROALAGLUPHEVAL
26   GLNARGLEUGLNSERASPGLUALALYSASN
27   TYRMETLYSGLYLEUPROGLULEUGLULYS
28   LYSASPPHEALASERILELEUTHRASNALA
29   SERPROLEUALAVALASNLEULEUGLULYS
30   METLEUVALLEUASPALAGLUGLNARGVAL
31   THRALAGLYGLUALALEUALAHISPROTYR
32   PHEGLUSERLEUHISASPTHRGLUASPGLU
33   PROGLNVALGLNLYSTYRASPASPSERPHE
34   ASPASPVALASPARGTHRLEUASPGLUTRP
35   LYSARGVALTHRTYRLYSGLUVALLEUSER
36   PHELYSPROPROARGGLNLEUGLYALAARG
37   VALSERLYSGLUTHRPROLEU

Samples:

sample_1: MAPK p38g, [U-100% 13C; U-100% 15N; U-80% 2H], 400 uM; HEPES, [U-2H], 25 mM; sodium chloride 250 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

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