BMRB Entry 26855
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26855
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kacirova, Miroslava; Novacek, Jiri; Man, Petr; Obsilova, Veronika; Obsil, Tomas. "Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function" Biophys. J. 112, 1339-1349 (2017).
PubMed: 28402877
Assembly members:
PDC, polymer, 265 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b
Entity Sequences (FASTA):
PDC: GSSHHHHHHSSGLVPRGSHM
EEAASQSLEEDFEGQATHTG
PKGVINDWRKFKLESEDGDS
IPPSKKEILRKMSSPQSRDD
KDSKERMSRKMSIQEYELIH
QDKEDEGCLRKYRRQCMQDM
HQKLSFGPRYGFVYELETGE
QFLETIEKEQKVTTIVVNIY
EDGVRGCDALNSSLECLAAE
YPMVKFCKIRASNTGAGDRF
SSDVLPTLLVYKGGELISNF
ISVAEQFAEDFFAADVESFL
NEYGLLPEREIHDLGQTNTE
DEDIE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 402 |
| 15N chemical shifts | 155 |
| 1H chemical shifts | 197 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | phosducin | 1 |
Entities:
Entity 1, phosducin 265 residues - Formula weight is not available
| 1 | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | SER | ||||
| 2 | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | MET | ||||
| 3 | GLU | GLU | ALA | ALA | SER | GLN | SER | LEU | GLU | GLU | ||||
| 4 | ASP | PHE | GLU | GLY | GLN | ALA | THR | HIS | THR | GLY | ||||
| 5 | PRO | LYS | GLY | VAL | ILE | ASN | ASP | TRP | ARG | LYS | ||||
| 6 | PHE | LYS | LEU | GLU | SER | GLU | ASP | GLY | ASP | SER | ||||
| 7 | ILE | PRO | PRO | SER | LYS | LYS | GLU | ILE | LEU | ARG | ||||
| 8 | LYS | MET | SER | SER | PRO | GLN | SER | ARG | ASP | ASP | ||||
| 9 | LYS | ASP | SER | LYS | GLU | ARG | MET | SER | ARG | LYS | ||||
| 10 | MET | SER | ILE | GLN | GLU | TYR | GLU | LEU | ILE | HIS | ||||
| 11 | GLN | ASP | LYS | GLU | ASP | GLU | GLY | CYS | LEU | ARG | ||||
| 12 | LYS | TYR | ARG | ARG | GLN | CYS | MET | GLN | ASP | MET | ||||
| 13 | HIS | GLN | LYS | LEU | SER | PHE | GLY | PRO | ARG | TYR | ||||
| 14 | GLY | PHE | VAL | TYR | GLU | LEU | GLU | THR | GLY | GLU | ||||
| 15 | GLN | PHE | LEU | GLU | THR | ILE | GLU | LYS | GLU | GLN | ||||
| 16 | LYS | VAL | THR | THR | ILE | VAL | VAL | ASN | ILE | TYR | ||||
| 17 | GLU | ASP | GLY | VAL | ARG | GLY | CYS | ASP | ALA | LEU | ||||
| 18 | ASN | SER | SER | LEU | GLU | CYS | LEU | ALA | ALA | GLU | ||||
| 19 | TYR | PRO | MET | VAL | LYS | PHE | CYS | LYS | ILE | ARG | ||||
| 20 | ALA | SER | ASN | THR | GLY | ALA | GLY | ASP | ARG | PHE | ||||
| 21 | SER | SER | ASP | VAL | LEU | PRO | THR | LEU | LEU | VAL | ||||
| 22 | TYR | LYS | GLY | GLY | GLU | LEU | ILE | SER | ASN | PHE | ||||
| 23 | ILE | SER | VAL | ALA | GLU | GLN | PHE | ALA | GLU | ASP | ||||
| 24 | PHE | PHE | ALA | ALA | ASP | VAL | GLU | SER | PHE | LEU | ||||
| 25 | ASN | GLU | TYR | GLY | LEU | LEU | PRO | GLU | ARG | GLU | ||||
| 26 | ILE | HIS | ASP | LEU | GLY | GLN | THR | ASN | THR | GLU | ||||
| 27 | ASP | GLU | ASP | ILE | GLU |
Samples:
sample_1: PDC, [U-100% 13C; U-100% 15N], 0.2 mM; MES 50 mM; sodium chloride 100 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 5D HN(CA)CONH | sample_1 | isotropic | sample_conditions_1 |
| 5D HabCabCONH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 850 MHz
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks