BMRB Entry 18927

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18927

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Title:
Solution NMR assignments of V5 domain from Protein Kinase C alpha
Deposition date:
2013-01-02
Original release date:
2014-02-14
Authors:
Yang, Yuan; Igumenova, Tatyana
Citation:

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).
PubMed: 23762412

Assembly members:

Assembly members:
V5_domain,_residue_606-672, polymer, 68 residues, 7596.5 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET31b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
V5_domain,_residue_606-672: ENREIQPPFKPKVSGKGAEN FDKFFTRGQPVLTPPDQLVI ANIDQSDFEGFSYVNPQFVH PILQSAVX

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

Additional metadata:

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

Assembly:

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

Entities:

Entity 1, V5 domain of Protein Kinase C alpha 68 residues - 7596.5 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   VALLEUTHRPROPROASPGLNLEUVALILE
5   ALAASNILEASPGLNSERASPPHEGLUGLY
6   PHESERTYRVALASNPROGLNPHEVALHIS
7   PROILELEUGLNSERALAVALHSL

Samples:

sample_1: 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 VNMRS 600 MHz

Related Database Links:

BMRB 18928 18929 18930
PDB
DBJ BAE27664 BAE37546 BAG70072 BAG70197 BAI45848
EMBL CAA30266 CAA36718 CAA36907 CAA36908
GB AAA30706 AAA39934 AAH96493 AAI09274 AAI09275
PRF 1602247A
REF NP_001099183 NP_001247662 NP_002728 NP_035231 NP_776860
SP P04409 P05696 P17252 P20444
AlphaFold P04409 P05696 P17252 P20444

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