BMRB Entry 27338
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27338
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NMR-STAR v3 text file.
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Citation: Zhao, Yu; Cushing, Patrick; Smithson, David; Pellegrini, Maria; Pletnev, Alexandre; Al-Ayyoubi, Sahar; Grassetti, Andrew; Gerber, Scott; Guy, R Kiplin; Madden, Dean. "Cysteine modification reveals an allosteric inhibitory site on the CAL PDZ domain" Biosci. Rep. 38, BSR20180231-BSR20180231 (2018).
PubMed: 29472314
Assembly members:
CAL_PDZ, polymer, 87 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: pet16B
Entity Sequences (FASTA):
CAL_PDZ: GPIRKVLLLKEDHEGLGISI
TGGKEHGVPILISEIHPGQP
ADRCGGLHVGDAILAVNGVN
LRDTKHKEAVTILSQQRGEI
EFEVVYV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 80 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 81 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CAL PDZ | 1 |
Entities:
Entity 1, CAL PDZ 87 residues - Formula weight is not available
| 1 | GLY | PRO | ILE | ARG | LYS | VAL | LEU | LEU | LEU | LYS | ||||
| 2 | GLU | ASP | HIS | GLU | GLY | LEU | GLY | ILE | SER | ILE | ||||
| 3 | THR | GLY | GLY | LYS | GLU | HIS | GLY | VAL | PRO | ILE | ||||
| 4 | LEU | ILE | SER | GLU | ILE | HIS | PRO | GLY | GLN | PRO | ||||
| 5 | ALA | ASP | ARG | CYS | GLY | GLY | LEU | HIS | VAL | GLY | ||||
| 6 | ASP | ALA | ILE | LEU | ALA | VAL | ASN | GLY | VAL | ASN | ||||
| 7 | LEU | ARG | ASP | THR | LYS | HIS | LYS | GLU | ALA | VAL | ||||
| 8 | THR | ILE | LEU | SER | GLN | GLN | ARG | GLY | GLU | ILE | ||||
| 9 | GLU | PHE | GLU | VAL | VAL | TYR | VAL |
Samples:
sample_1: CAL PDZ, [U-100% 13C; U-100% 15N], 755 uM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks