BMRB Entry 16917
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16917
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Pekarova, Blanka; Klumpler, Toma; Tiskova, Olga; Horak, Jakub; Jansen, Severine; Dopitova, Radka; Borkovcova, Petra; Papoukova, Veronika; Nejedla, Elika; Sklena, Vladimir; Marek, Jaromir; Zidek, Luka; Hejatko, Jan; Janda, Lubomir. "Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana." Plant J. 67, 827-839 (2011).
PubMed: 21569135
Assembly members:
CKI1RD, polymer, 207 residues, Formula weight is not available
Natural source: Common Name: thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGBKT7-DEST
- assigned_chemical_shifts
- heteronucl_NOEs
- order_parameters
| Data type | Count |
| 13C chemical shifts | 315 |
| 15N chemical shifts | 158 |
| 1H chemical shifts | 158 |
| General relaxation values | 285 |
| chemical shift anisotropy values | 95 |
| heteronuclear NOE values | 95 |
| order parameters | 95 |
| tensors | 95 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CKI1RD | 1 |
Entities:
Entity 1, CKI1RD 207 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ALA | SER | THR | ASP | SER | GLU | SER | GLU | THR | ||||
| 4 | ARG | VAL | LYS | SER | VAL | ARG | THR | GLY | ARG | LYS | ||||
| 5 | PRO | ILE | GLY | ASN | PRO | GLU | ASP | GLU | GLN | GLU | ||||
| 6 | THR | SER | LYS | PRO | SER | ASP | ASP | GLU | PHE | LEU | ||||
| 7 | ARG | GLY | LYS | ARG | VAL | LEU | VAL | VAL | ASP | ASP | ||||
| 8 | ASN | PHE | ILE | SER | ARG | LYS | VAL | ALA | THR | GLY | ||||
| 9 | LYS | LEU | LYS | LYS | MET | GLY | VAL | SER | GLU | VAL | ||||
| 10 | GLU | GLN | CYS | ASP | SER | GLY | LYS | GLU | ALA | LEU | ||||
| 11 | ARG | LEU | VAL | THR | GLU | GLY | LEU | THR | GLN | ARG | ||||
| 12 | GLU | GLU | GLN | GLY | SER | VAL | ASP | LYS | LEU | PRO | ||||
| 13 | PHE | ASP | TYR | ILE | PHE | MET | ASP | CYS | GLN | MET | ||||
| 14 | PRO | GLU | MET | ASP | GLY | TYR | GLU | ALA | THR | ARG | ||||
| 15 | GLU | ILE | ARG | LYS | VAL | GLU | LYS | SER | TYR | GLY | ||||
| 16 | VAL | ARG | THR | PRO | ILE | ILE | ALA | VAL | SER | GLY | ||||
| 17 | HIS | ASP | PRO | GLY | SER | GLU | GLU | ALA | ARG | GLU | ||||
| 18 | THR | ILE | GLN | ALA | GLY | MET | ASP | ALA | PHE | LEU | ||||
| 19 | ASP | LYS | SER | LEU | ASN | GLN | LEU | ALA | ASN | VAL | ||||
| 20 | ILE | ARG | GLU | ILE | GLU | SER | LYS | ARG | HIS | LEU | ||||
| 21 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: CKI1RD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM; EDTA 1 mM; sodium azide 0.05%; D2O, [U-2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 171 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks