BMRB Entry 15430
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15430
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Title: The chemical shift assignment of gamma subunit of phosphodiesterase PubMed: 18230733
Deposition date: 2007-08-14 Original release date: 2007-08-20
Authors: Song, Jikui; Guo, Lian-Wang; Ruoho, Arnold; Markley, John
Citation: Song, Jikui; Guo, Lian-Wang; Muradov, Hakim; Artemyev, Nikolai; Ruoho, Arnold; Markley, John. "Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure" Proc. Natl. Acad. Sci. U. S. A. 105, 1505-1510 (2008).
Assembly members:
PDEgamma, polymer, 87 residues, 13286.163 Da.
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
Entity Sequences (FASTA):
PDEgamma: MNLEPPKAEIRSATRVMGGP
VTPRKGPPKFKQRQTRQFKS
KPPKKGVQGFGDDIPGMEGL
GTDITVIAPWEAFNHLELHE
LAQYGII
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 325 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 443 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDEgamma | 1 |
Entities:
Entity 1, PDEgamma 87 residues - 13286.163 Da.
| 1 | MET | ASN | LEU | GLU | PRO | PRO | LYS | ALA | GLU | ILE | ||||
| 2 | ARG | SER | ALA | THR | ARG | VAL | MET | GLY | GLY | PRO | ||||
| 3 | VAL | THR | PRO | ARG | LYS | GLY | PRO | PRO | LYS | PHE | ||||
| 4 | LYS | GLN | ARG | GLN | THR | ARG | GLN | PHE | LYS | SER | ||||
| 5 | LYS | PRO | PRO | LYS | LYS | GLY | VAL | GLN | GLY | PHE | ||||
| 6 | GLY | ASP | ASP | ILE | PRO | GLY | MET | GLU | GLY | LEU | ||||
| 7 | GLY | THR | ASP | ILE | THR | VAL | ILE | ALA | PRO | TRP | ||||
| 8 | GLU | ALA | PHE | ASN | HIS | LEU | GLU | LEU | HIS | GLU | ||||
| 9 | LEU | ALA | GLN | TYR | GLY | ILE | ILE |
Samples:
sample_1: PDEgamma, [U-100% 15N], 0.05 mM
sample_2: PDEgamma, [U-100% 13C; U-100% 15N], 0.09 mM
sample_3: PROXYL-PDEgamma, [U-15N], 0.05 mM
sample_4: PROXYL-PDEgamma, [U-100% 15N], 0.05 mM; Ascorbic Acid 5 mM
sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR, Varian - collection
SPARKY, Goddard - processing
NMR spectrometers:
- Bruker DMX 600 MHz
- Bruker DMX 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts