Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18929
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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:
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 type | Count |
13C chemical shifts | 176 |
15N chemical shifts | 55 |
1H chemical shifts | 55 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | V5 domain of Protein Kinase C alpha | 1 |
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 | PRO | PHE | LYS | ||||
2 | PRO | LYS | VAL | SER | GLY | LYS | GLY | ALA | GLU | ASN | ||||
3 | PHE | ASP | LYS | PHE | PHE | THR | ARG | GLY | GLN | PRO | ||||
4 | VAL | LEU | THR | PRO | 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 |
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
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 |
SPARKY, Goddard - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
BMRB | 18927 18928 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