BMRB Entry 26021
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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/BMR26021
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Title: Sr33 Coiled-coil domain PubMed: 27791121
Deposition date: 2016-03-30 Original release date: 2016-10-13
Authors: Lavrencic, Peter; Mobli, Mehdi
Citation: Casey, Lachlan; Lavrencic, Peter; Bentham, Adam; Cesari, Stella; Ericsson, Daniel; Croll, Tristan; Turk, Dusan; Anderson, Peter; Mark, Alan; Dodds, Peter; Mobli, Mehdi; Kobe, Bostjan; Williams, Simon. "The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins" Proc. Natl. Acad. Sci. U.S.A. ., .-. (2016).
Assembly members:
entity, polymer, 118 residues, 13138.456 Da.
Natural source: Common Name: bread wheat Taxonomy ID: 4565 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum aestivum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: SNAGAIAKLIPKLGELLVGE
YKLHKGVKKNIEDLLKELKT
MNAALIKIGEVPPDQLDSQD
KLWADEVRELSYVIEDAVDK
FLVRVHGVEPDDNTNGFKGL
MKRTTKLLKKVVDKHGIA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 506 |
| 15N chemical shifts | 120 |
| 1H chemical shifts | 865 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 118 residues - 13138.456 Da.
| 1 | SER | ASN | ALA | GLY | ALA | ILE | ALA | LYS | LEU | ILE | ||||
| 2 | PRO | LYS | LEU | GLY | GLU | LEU | LEU | VAL | GLY | GLU | ||||
| 3 | TYR | LYS | LEU | HIS | LYS | GLY | VAL | LYS | LYS | ASN | ||||
| 4 | ILE | GLU | ASP | LEU | LEU | LYS | GLU | LEU | LYS | THR | ||||
| 5 | MET | ASN | ALA | ALA | LEU | ILE | LYS | ILE | GLY | GLU | ||||
| 6 | VAL | PRO | PRO | ASP | GLN | LEU | ASP | SER | GLN | ASP | ||||
| 7 | LYS | LEU | TRP | ALA | ASP | GLU | VAL | ARG | GLU | LEU | ||||
| 8 | SER | TYR | VAL | ILE | GLU | ASP | ALA | VAL | ASP | LYS | ||||
| 9 | PHE | LEU | VAL | ARG | VAL | HIS | GLY | VAL | GLU | PRO | ||||
| 10 | ASP | ASP | ASN | THR | ASN | GLY | PHE | LYS | GLY | LEU | ||||
| 11 | MET | LYS | ARG | THR | THR | LYS | LEU | LEU | LYS | LYS | ||||
| 12 | VAL | VAL | ASP | LYS | HIS | GLY | ILE | ALA |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 450 uM; HEPES 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, refinement, structure solution
TALOS vTALOS+, Cornilescu, Delaglio and Bax - geometry optimization
CCPNMR v2.4.1, Vranken WF et al. - data analysis, peak picking
Rowland_NMR_toolkit v3, JC Hoch et al. - processing
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts