BMRB Entry 30436
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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/BMR30436
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: Ishida, Hiroaki; Skorobogatov, Anton; Yamniuk, Aaron; Vogel, Hans. "Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels" FEBS Lett. 592, 2786-2797 (2018).
PubMed: 30058071
Assembly members:
entity_1, polymer, 61 residues, 6626.528 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):
entity_1: MVPGRSFMAVKSYQAQAEGE
ISLSKGEKIKVLSIGEGGFW
EGQVKGRVGWFPSDCLEEVA
N
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 174 |
| 15N chemical shifts | 58 |
| 1H chemical shifts | 58 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 61 residues - 6626.528 Da.
| 1 | MET | VAL | PRO | GLY | ARG | SER | PHE | MET | ALA | VAL | ||||
| 2 | LYS | SER | TYR | GLN | ALA | GLN | ALA | GLU | GLY | GLU | ||||
| 3 | ILE | SER | LEU | SER | LYS | GLY | GLU | LYS | ILE | LYS | ||||
| 4 | VAL | LEU | SER | ILE | GLY | GLU | GLY | GLY | PHE | TRP | ||||
| 5 | GLU | GLY | GLN | VAL | LYS | GLY | ARG | VAL | GLY | TRP | ||||
| 6 | PHE | PRO | SER | ASP | CYS | LEU | GLU | GLU | VAL | ALA | ||||
| 7 | ASN |
Samples:
sample_1: Shank1 SH3 domain, [U-99% 13C; U-99% 15N], 1 mM; Bis-Tirs 20 mM; KCl 100 mM
sample_2: Shank1 SH3 domain, [U-99% 15N], 1 mM; KCl 100 mM; Bis-Tris 20 mM
sample_3: Shank1 SH3 domain 1 mM; KCl 100 mM; Bis-Tris 20 mM
sample_4: Shank1 SH3 domain, [U-99% 13C; U-99% 15N], 1 mM; KCl 100 mM; Bis-Tris 20 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks