BMRB Entry 11141
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11141
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
Title: Solution structure of the CH domain from human Vav-3 protein
Deposition date: 2010-03-31 Original release date: 2011-04-01
Authors: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the CH domain from human Vav-3 protein" .
Assembly members:
CH domain, polymer, 143 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: cell free synthesis Host organism: E. coli - cell free Vector: P050404-11
Entity Sequences (FASTA):
CH domain: GSSGSSGMEPWKQCAQWLIH
CKVLPTNHRVTWDSAQVFDL
AQTLRDGVLLCQLLNNLRAH
SINLKEINLRPQMSQFLCLK
NIRTFLTACCETFGMRKSEL
FEAFDLFDVRDFGKVIETLS
RLSRTPIALATGIRPFPSGP
SSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 635 |
| 15N chemical shifts | 140 |
| 1H chemical shifts | 1009 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CH domain | 1 |
Entities:
Entity 1, CH domain 143 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | MET | GLU | PRO | ||||
| 2 | TRP | LYS | GLN | CYS | ALA | GLN | TRP | LEU | ILE | HIS | ||||
| 3 | CYS | LYS | VAL | LEU | PRO | THR | ASN | HIS | ARG | VAL | ||||
| 4 | THR | TRP | ASP | SER | ALA | GLN | VAL | PHE | ASP | LEU | ||||
| 5 | ALA | GLN | THR | LEU | ARG | ASP | GLY | VAL | LEU | LEU | ||||
| 6 | CYS | GLN | LEU | LEU | ASN | ASN | LEU | ARG | ALA | HIS | ||||
| 7 | SER | ILE | ASN | LEU | LYS | GLU | ILE | ASN | LEU | ARG | ||||
| 8 | PRO | GLN | MET | SER | GLN | PHE | LEU | CYS | LEU | LYS | ||||
| 9 | ASN | ILE | ARG | THR | PHE | LEU | THR | ALA | CYS | CYS | ||||
| 10 | GLU | THR | PHE | GLY | MET | ARG | LYS | SER | GLU | LEU | ||||
| 11 | PHE | GLU | ALA | PHE | ASP | LEU | PHE | ASP | VAL | ARG | ||||
| 12 | ASP | PHE | GLY | LYS | VAL | ILE | GLU | THR | LEU | SER | ||||
| 13 | ARG | LEU | SER | ARG | THR | PRO | ILE | ALA | LEU | ALA | ||||
| 14 | THR | GLY | ILE | ARG | PRO | PHE | PRO | SER | GLY | PRO | ||||
| 15 | SER | SER | GLY |
Samples:
sample_1: CH domain, [U-13C; U-15N], 1.23 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.932, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAI45437 |
| GB | AAC79695 AAD20349 AAI43970 AAI46366 AAI56727 |
| REF | NP_006104 XP_001083337 XP_002801727 XP_002801728 XP_002928351 |
| SP | Q9UKW4 |
| AlphaFold | Q9UKW4 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts