BMRB Entry 18930

Name: Solution NMR assignments of the phosphorylation-mimicking mutant of V5 domain from Protein Kinase C alpha, in complex with DPC micelles
Published: 2014-02-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18930

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR assignments of the phosphorylation-mimicking mutant of V5 domain from Protein Kinase C alpha, in complex with DPC micelles

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:
T638E/S657E_V5_domain,_residue_606-672, polymer, 68 residues, 7666.6 Da.
dodecyl 2-(trimethylammonio)ethyl phosphate, non-polymer, 351.462 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):
T638E/S657E_V5_domain,_residue_606-672: ENREIQPPFKPKVSGKGAEN FDKFFTRGQPVLEPPDQLVI ANIDQSDFEGFEYVNPQFVH PILQSAVX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	162
15N chemical shifts	52
1H chemical shifts	52

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	T638E/S657E V5 domain of Protein Kinase C alpha	1
2	DPV	2

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

GLU

ASN

ARG

GLU

ILE

GLN

PRO

PHE

LYS

2

PRO

LYS

VAL

SER

GLY

LYS

GLY

ALA

GLU

ASN

3

PHE

ASP

LYS

PHE

THR

ARG

GLY

GLN

PRO

4

VAL

LEU

GLU

PRO

ASP

GLN

LEU

VAL

ILE

5

ALA

ASN

ILE

ASP

GLN

SER

ASP

PHE

GLU

GLY

6

PHE

GLU

TYR

VAL

ASN

PRO

GLN

PHE

VAL

HIS

7

PRO

ILE

LEU

GLN

SER

ALA

VAL

HSL

Entity 2, DPV - C17 H38 N O4 P - 351.462 Da.

1

DPV

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%; n-dodecylphosphocholine-D38, [U-2H], 100 mM

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

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_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

BMRB	18927 18928 18929
PDB	4RA4