BMRB Entry 6927
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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/BMR6927
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kelker, Matthew; Peti, Wolfgang. "NMR assignment of the Spinophilin PDZ domain (493-602)" J. Biomol. NMR 36, 24-24 (2006).
PubMed: 16607467
Assembly members:
spinophilin, polymer, 113 residues, 11668 Da.
Natural source: Common Name: rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
spinophilin: GHMELFPVELEKDSEGLGIS
IIGMGAGADMGLEKLGIFVK
TVTEGGAAHRDGRIQVNDLL
VEVDGTSLVGVTQSFAASVL
RNTKGRVRFMIGRERPGEQS
EVAQLIQQTLEQE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 447 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 755 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | spinophlin PDZ domain | 1 |
Entities:
Entity 1, spinophlin PDZ domain 113 residues - 11668 Da.
| 1 | GLY | HIS | MET | GLU | LEU | PHE | PRO | VAL | GLU | LEU | ||||
| 2 | GLU | LYS | ASP | SER | GLU | GLY | LEU | GLY | ILE | SER | ||||
| 3 | ILE | ILE | GLY | MET | GLY | ALA | GLY | ALA | ASP | MET | ||||
| 4 | GLY | LEU | GLU | LYS | LEU | GLY | ILE | PHE | VAL | LYS | ||||
| 5 | THR | VAL | THR | GLU | GLY | GLY | ALA | ALA | HIS | ARG | ||||
| 6 | ASP | GLY | ARG | ILE | GLN | VAL | ASN | ASP | LEU | LEU | ||||
| 7 | VAL | GLU | VAL | ASP | GLY | THR | SER | LEU | VAL | GLY | ||||
| 8 | VAL | THR | GLN | SER | PHE | ALA | ALA | SER | VAL | LEU | ||||
| 9 | ARG | ASN | THR | LYS | GLY | ARG | VAL | ARG | PHE | MET | ||||
| 10 | ILE | GLY | ARG | GLU | ARG | PRO | GLY | GLU | GLN | SER | ||||
| 11 | GLU | VAL | ALA | GLN | LEU | ILE | GLN | GLN | THR | LEU | ||||
| 12 | GLU | GLN | GLU |
Samples:
sample_1: spinophilin 2.0 mM; Na phohphate buffer 20 mM; NaCl 50 mM; NaN3 0.02%
conditions_1: ionic strength: 50 mM; pH: 6.5; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H15N_HSQC | sample_1 | not available | conditions_1 |
| HNCA | sample_1 | not available | conditions_1 |
| HNCACB | sample_1 | not available | conditions_1 |
| CBCACONH | sample_1 | not available | conditions_1 |
| HCCH_TOCSY | sample_1 | not available | conditions_1 |
| HNCO | sample_1 | not available | conditions_1 |
Software:
CARA v1.3 - chemical shift assignment
NMR spectrometers:
- Bruker AvanceII 500 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks