BMRB Entry 11397
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11397
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Title: Solution structure of the BACK domain of Kelch repeat and BTB domain-containing protein 4
Deposition date: 2010-09-09 Original release date: 2011-09-08
Authors: Imai, M.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.
Citation: Imai, M.; Suzuki, S.; Muto, Y.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.. "Solution structure of the BACK domain of Kelch repeat and BTB domain-containing protein 4" . ., .-..
Assembly members:
BACK domain, polymer, 105 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
Entity Sequences (FASTA):
BACK domain: GSSGSSGVQVGNCLQVMWLA
DRHSDPELYTAAKHCAKTHL
AQLQNTEEFLHLPHRLLTDI
ISDGVPCSQNPTEAIEAWIN
FNKEEREAFAESLRTSLKEI
GENVH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 435 |
15N chemical shifts | 107 |
1H chemical shifts | 695 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BACK domain | 1 |
Entities:
Entity 1, BACK domain 105 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | VAL | GLN | VAL | ||||
2 | GLY | ASN | CYS | LEU | GLN | VAL | MET | TRP | LEU | ALA | ||||
3 | ASP | ARG | HIS | SER | ASP | PRO | GLU | LEU | TYR | THR | ||||
4 | ALA | ALA | LYS | HIS | CYS | ALA | LYS | THR | HIS | LEU | ||||
5 | ALA | GLN | LEU | GLN | ASN | THR | GLU | GLU | PHE | LEU | ||||
6 | HIS | LEU | PRO | HIS | ARG | LEU | LEU | THR | ASP | ILE | ||||
7 | ILE | SER | ASP | GLY | VAL | PRO | CYS | SER | GLN | ASN | ||||
8 | PRO | THR | GLU | ALA | ILE | GLU | ALA | TRP | ILE | ASN | ||||
9 | PHE | ASN | LYS | GLU | GLU | ARG | GLU | ALA | PHE | ALA | ||||
10 | GLU | SER | LEU | ARG | THR | SER | LEU | LYS | GLU | ILE | ||||
11 | GLY | GLU | ASN | VAL | HIS |
Samples:
sample_1: BACK domain, [U-13C; U-15N], 1.15 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: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20060702, Delaglio F. - processing
NMRView v5.0.4, Johnson B.A. - data analysis
Kujira v0.9820, Kobayashi N. - data analysis
CYANA v2.1, Guntert P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
PDB | |
DBJ | BAA91616 BAA91880 BAB03555 BAB27317 BAB29305 |
EMBL | CAD28521 CAG33551 CAH90011 CAH93240 |
GB | AAH02736 AAH25103 ADZ15413 AIC51824 EAW67898 |
REF | NP_001101216 NP_001126905 NP_001247465 NP_001267133 NP_001298045 |
SP | Q5R4S6 Q8R179 Q9N010 Q9NVX7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts