BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18928

Title: Solution NMR assignments of the phosphorylation-mimicking mutant of V5 domain from Protein Kinase C alpha   PubMed: 23762412

Deposition date: 2013-01-02 Original release date: 2014-02-14

Authors: Yang, Yuan; Igumenova, Tatyana

Citation: Yang, Yuan; Igumenova, Tatyana. "The C-terminal V5 domain of Protein Kinase C is intrinsically disordered, with propensity to associate with a membrane mimetic."  PLoS ONE 8, e65699-e65699 (2013).

Assembly members:
T638E/S657E_V5_domain,_residue_606-672, polymer, 68 residues, 7666.6 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
T638E/S657E_V5_domain,_residue_606-672: ENREIQPPFKPKVSGKGAEN FDKFFTRGQPVLEPPDQLVI ANIDQSDFEGFEYVNPQFVH PILQSAVX

Data sets:
Data typeCount
13C chemical shifts188
15N chemical shifts57
1H chemical shifts57

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1T638E/S657E V5 domain of Protein Kinase C alpha1

Entities:

Entity 1, T638E/S657E V5 domain of Protein Kinase C alpha 68 residues - 7666.6 Da.

Residue 673 (HSL) is a non-standard Homoserine-lactone that resulted from CNBr cleavage at Methionine residue

1   GLUASNARGGLUILEGLNPROPROPHELYS
2   PROLYSVALSERGLYLYSGLYALAGLUASN
3   PHEASPLYSPHEPHETHRARGGLYGLNPRO
4   VALLEUGLUPROPROASPGLNLEUVALILE
5   ALAASNILEASPGLNSERASPPHEGLUGLY
6   PHEGLUTYRVALASNPROGLNPHEVALHIS
7   PROILELEUGLNSERALAVALHSL

Samples:

sample_1: T638E/S657E V5 domain, residue 606-672, [U-95% 13C; U-95% 15N], 0.25 mM; MES 20 mM; potassium chloride 100 mM; sodium azide 0.02%; H2O 92%; D2O, [U-2H], 8%

sample_conditions_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18927 18929 18930
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts