BMRB Entry 5925
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5925
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Title: Solution structure of the N-terminal SH3 domain of Drk (drkN SH3 domain) PubMed: 16300404
Deposition date: 2003-08-28 Original release date: 2006-01-12
Authors: Bezsonova, I.; Singer, A.; Choy, W.-Y.; Tollinger, M.; Forman-Kay, J.
Citation: Bezsonova, Irina; Singer, Alex; Choy, Wing-Yiu; Tollinger, Martin; Forman-Kay, Julie. "Structural comparison of the unstable drkN SH3 domain and a stable mutant" Biochemistry 44, 15550-15560 (2005).
Assembly members:
The Drosophila N-terminal SH3 domain of Downstream of Receptor Kinases protein, polymer, 59 residues, Formula weight is not available
Natural source: Common Name: Fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
The Drosophila N-terminal SH3 domain of Downstream of Receptor Kinases protein: MEAIAKHDFSATADDELSFR
KTGILKILNMGDDSNWYRAE
LDGKEGLIPSNYIEMKNHD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 56 |
15N chemical shifts | 56 |
1H chemical shifts | 56 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SH2-SH3 adapter protein drk | 1 |
Entities:
Entity 1, SH2-SH3 adapter protein drk 59 residues - Formula weight is not available
1 | MET | GLU | ALA | ILE | ALA | LYS | HIS | ASP | PHE | SER | ||||
2 | ALA | THR | ALA | ASP | ASP | GLU | LEU | SER | PHE | ARG | ||||
3 | LYS | THR | GLY | ILE | LEU | LYS | ILE | LEU | ASN | MET | ||||
4 | GLY | ASP | ASP | SER | ASN | TRP | TYR | ARG | ALA | GLU | ||||
5 | LEU | ASP | GLY | LYS | GLU | GLY | LEU | ILE | PRO | SER | ||||
6 | ASN | TYR | ILE | GLU | MET | LYS | ASN | HIS | ASP |
Samples:
sample_1: The Drosophila N-terminal SH3 domain of Downstream of Receptor Kinases protein, [U-13C; U-15N], 1.0 mM; Na2SO4 500 mM; phosphate buffer 50 mM; D2O 10%; H2O 90%
sample_cond_1: ionic strength: 1.664 M; pH: 6.0; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|
Software:
NMRPipe - processing
CNS v1.0 - refinement
PIPP - data analysis
NMR spectrometers:
- Varian INOVA 500 MHz
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