BMRB Entry 18929

Name: Solution NMR assignments 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/BMR18929

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR assignments of V5 domain from Protein Kinase C alpha, in complex with DPC micelles 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:
V5_domain,_residue_606-672, polymer, 68 residues, 7596.5 Da.
dodecyl 2-(trimethylammonio)ethyl phosphate, non-polymer, 351.462 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 Vector: pET31b(+)

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	176
15N chemical shifts	55
1H chemical shifts	55

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	V5 domain of Protein Kinase C alpha	1

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

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

THR

PRO

ASP

GLN

LEU

VAL

ILE

5

ALA

ASN

ILE

ASP

GLN

SER

ASP

PHE

GLU

GLY

6

PHE

SER

TYR

VAL

ASN

PRO

GLN

PHE

VAL

HIS

7

PRO

ILE

LEU

GLN

SER

ALA

VAL

HSL

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%; n-dodecylphosphocholine 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 18930
PDB	4RA4
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	P17252 P04409 P05696 P20444

Biological Magnetic Resonance Data Bank