BMRB Entry 18353
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18353
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Title: 1H, 15N and 13C backbone resonance assignments of the Kelch domain of mouse Keap1 PubMed: 22688683
Deposition date: 2012-03-27 Original release date: 2012-06-11
Authors: Cino, Elio; Choy, Wing-Yiu; Fan, Jingsong; Yang, Daiwen
Citation: Cino, Elio; Fan, Jingsong; Yang, Daiwen; Choy, Wing-Yiu. "1H, 15N and 13C backbone resonance assignments of the Kelch domain of mouse Keap1." Biomol. NMR Assignments 7, 149-153 (2013).
Assembly members:
Kelch_domain_of_mouse_Keap1, polymer, 290 residues, Formula weight is not available
Natural source: Common Name: House 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):
Kelch_domain_of_mouse_Keap1: GVGRLIYTAGGYFRQSLSYL
EAYNPSNGSWLRLADLQVPR
SGLAGCVVGGLLYAVGGRNN
SPDGNTDSSALDCYNPMTNQ
WSPCASMSVPRNRIGVGVID
GHIYAVGGSHGCIHHSSVER
YEPERDEWHLVAPMLTRRIG
VGVAVLNRLLYAVGGFDGTN
RLNSAECYYPERNEWRMITP
MNTIRSGAGVCVLHNCIYAA
GGYDGQDQLNSVERYDVETE
TWTFVAPMRHHRSALGITVH
QGKIYVLGGYDGHTFLDSVE
CYDPDSDTWSEVTRMTSGRS
GVGVAVTMEP
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 490 |
15N chemical shifts | 251 |
1H chemical shifts | 251 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Kelch domain of mouse Keap1 | 1 |
Entities:
Entity 1, Kelch domain of mouse Keap1 290 residues - Formula weight is not available
The starting G was a non-native residue from the TEV recognition sequence that remained after cleavage
1 | GLY | VAL | GLY | ARG | LEU | ILE | TYR | THR | ALA | GLY | |
2 | GLY | TYR | PHE | ARG | GLN | SER | LEU | SER | TYR | LEU | |
3 | GLU | ALA | TYR | ASN | PRO | SER | ASN | GLY | SER | TRP | |
4 | LEU | ARG | LEU | ALA | ASP | LEU | GLN | VAL | PRO | ARG | |
5 | SER | GLY | LEU | ALA | GLY | CYS | VAL | VAL | GLY | GLY | |
6 | LEU | LEU | TYR | ALA | VAL | GLY | GLY | ARG | ASN | ASN | |
7 | SER | PRO | ASP | GLY | ASN | THR | ASP | SER | SER | ALA | |
8 | LEU | ASP | CYS | TYR | ASN | PRO | MET | THR | ASN | GLN | |
9 | TRP | SER | PRO | CYS | ALA | SER | MET | SER | VAL | PRO | |
10 | ARG | ASN | ARG | ILE | GLY | VAL | GLY | VAL | ILE | ASP | |
11 | GLY | HIS | ILE | TYR | ALA | VAL | GLY | GLY | SER | HIS | |
12 | GLY | CYS | ILE | HIS | HIS | SER | SER | VAL | GLU | ARG | |
13 | TYR | GLU | PRO | GLU | ARG | ASP | GLU | TRP | HIS | LEU | |
14 | VAL | ALA | PRO | MET | LEU | THR | ARG | ARG | ILE | GLY | |
15 | VAL | GLY | VAL | ALA | VAL | LEU | ASN | ARG | LEU | LEU | |
16 | TYR | ALA | VAL | GLY | GLY | PHE | ASP | GLY | THR | ASN | |
17 | ARG | LEU | ASN | SER | ALA | GLU | CYS | TYR | TYR | PRO | |
18 | GLU | ARG | ASN | GLU | TRP | ARG | MET | ILE | THR | PRO | |
19 | MET | ASN | THR | ILE | ARG | SER | GLY | ALA | GLY | VAL | |
20 | CYS | VAL | LEU | HIS | ASN | CYS | ILE | TYR | ALA | ALA | |
21 | GLY | GLY | TYR | ASP | GLY | GLN | ASP | GLN | LEU | ASN | |
22 | SER | VAL | GLU | ARG | TYR | ASP | VAL | GLU | THR | GLU | |
23 | THR | TRP | THR | PHE | VAL | ALA | PRO | MET | ARG | HIS | |
24 | HIS | ARG | SER | ALA | LEU | GLY | ILE | THR | VAL | HIS | |
25 | GLN | GLY | LYS | ILE | TYR | VAL | LEU | GLY | GLY | TYR | |
26 | ASP | GLY | HIS | THR | PHE | LEU | ASP | SER | VAL | GLU | |
27 | CYS | TYR | ASP | PRO | ASP | SER | ASP | THR | TRP | SER | |
28 | GLU | VAL | THR | ARG | MET | THR | SER | GLY | ARG | SER | |
29 | GLY | VAL | GLY | VAL | ALA | VAL | THR | MET | GLU | PRO |
Samples:
sample_1: Kelch domain, [U-13C; U-15N; U-2H], 0.2 0.3 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
SPARKY, Goddard - data analysis
NMR spectrometers:
- Varian INOVA 800 MHz
- Bruker Avance 800 MHz
Related Database Links:
PDB | |
DBJ | BAA34639 BAB23519 BAC32621 BAC36267 BAC97871 |
EMBL | CAG15151 |
GB | AAH55732 AAI51546 AAL84711 EDL25167 EDL25168 |
REF | NP_001094612 NP_001103775 NP_001103776 NP_001103777 NP_001108143 |
SP | Q684M4 Q9Z2X8 |
TPG | DAA27941 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts