BMRB Entry 18832
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18832
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Title: Solution structure of the SH3 domain of DOCK180 PubMed: 23239367
Deposition date: 2012-11-08 Original release date: 2012-08-12
Authors: Liu, Xiangrong; Wen, Wenyu
Citation: Liu, Xiangrong; Li, Fengjuan; Pan, Zhu; Wang, Wenning; Wen, Wenyu. "Solution structure of the SH3 domain of DOCK180." Proteins 81, 906-910 (2013).
Assembly members:
entity, polymer, 74 residues, 8659.928 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MTRWVPTKREEKYGVAFYNY
DARGADELSLQIGDTVHILE
TYEGWYRGYTLRKKSKKGIF
PASYIHLKEAIVEG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 212 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 498 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SH3 domain of DOCK180 | 1 |
Entities:
Entity 1, SH3 domain of DOCK180 74 residues - 8659.928 Da.
| 1 | MET | THR | ARG | TRP | VAL | PRO | THR | LYS | ARG | GLU | ||||
| 2 | GLU | LYS | TYR | GLY | VAL | ALA | PHE | TYR | ASN | TYR | ||||
| 3 | ASP | ALA | ARG | GLY | ALA | ASP | GLU | LEU | SER | LEU | ||||
| 4 | GLN | ILE | GLY | ASP | THR | VAL | HIS | ILE | LEU | GLU | ||||
| 5 | THR | TYR | GLU | GLY | TRP | TYR | ARG | GLY | TYR | THR | ||||
| 6 | LEU | ARG | LYS | LYS | SER | LYS | LYS | GLY | ILE | PHE | ||||
| 7 | PRO | ALA | SER | TYR | ILE | HIS | LEU | LYS | GLU | ALA | ||||
| 8 | ILE | VAL | GLU | GLY |
Samples:
SH3-1: SH3, [U-100% 15N], 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%
SH3-2: SH3, [U-100% 13C; U-100% 15N], 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%
SH3-3: SH3, [U-100% 13C; U-100% 15N], 0.4 mM; PBS 50 mM; DTT, [U-100% 2H], 1 mM; EDTA 1 mM; D2O 100%
SH3-4: SH3 0.4 mM; PBS 50 mM; DTT, [U-100% 2H], 1 mM; EDTA 1 mM; D2O 100%
sample_condition: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | SH3-1 | isotropic | sample_condition |
| 3D 1H-15N NOESY | SH3-1 | isotropic | sample_condition |
| 2D 1H-15N HSQC | SH3-2 | isotropic | sample_condition |
| 3D CBCA(CO)NH | SH3-2 | isotropic | sample_condition |
| 3D HNCACB | SH3-2 | isotropic | sample_condition |
| 3D HNCO | SH3-2 | isotropic | sample_condition |
| 2D 1H-13C HSQC | SH3-3 | isotropic | sample_condition |
| 3D 1H-13C NOESY | SH3-3 | isotropic | sample_condition |
| 2D 1H-1H NOESY | SH3-4 | anisotropic | sample_condition |
| 2D 1H-1H TOCSY | SH3-4 | anisotropic | sample_condition |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
SPARKY, Goddard - peak picking
PIPP, Garrett - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian VNMRS 600 MHz
Related Database Links:
| BMRB | 18327 |
| PDB | |
| DBJ | BAA09454 BAC38645 BAE24599 |
| GB | AAI46858 EDL17793 EDL17794 EDL17796 EDL17797 |
| REF | NP_001028592 NP_001137330 NP_001277152 NP_001371 XP_001089124 |
| SP | Q14185 Q8BUR4 |
| TPG | DAA14676 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts