BMRB Entry 17588
Click here to enlarge.
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/BMR17588
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the RXLR effector P. capsici AVR3a4 PubMed: 21821794
Deposition date: 2011-04-12 Original release date: 2012-05-09
Authors: Li, Hua; Koshiba, Seizo; Yaeno, Takashi; Sato, Manami; Watanabe, Satoru; Harada, Takushi; Shirasu, Ken; Kigawa, Takanori
Citation: Yaeno, Takashi; Li, Hua; Chaparro-Garcia, Angela; Schornack, Sebastian; Koshiba, Seizo; Watanabe, Satoru; Kigawa, Takanori; Kamoun, Sophien; Shirasu, Ken. "Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity." Proc. Natl. Acad. Sci. U.S.A. 108, 14682-14687 (2011).
Assembly members:
AVR3a4, polymer, 108 residues, 12039.568 Da.
Natural source: Common Name: Phytophthora capsici Taxonomy ID: 4784 Superkingdom: Eukaryota Kingdom: not available Genus/species: Phytophthora capsici
Experimental source: Production method: recombinant technology Host organism: E. coli - cell free
Entity Sequences (FASTA):
AVR3a4: GSSGSSGNVDSNQNKASMLQ
ARLNDEAGGTRLLRVHHESD
TEERGFLEKAAVKKMAKAIM
ADPNKADEVYKKWADKGYTL
TQMSNFLKSKTAGKYDRVYN
GYVIHLDY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 458 |
15N chemical shifts | 110 |
1H chemical shifts | 715 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | AVR3a4 | 1 |
Entities:
Entity 1, AVR3a4 108 residues - 12039.568 Da.
1 | GLY | SER | SER | GLY | SER | SER | GLY | ASN | VAL | ASP | ||||
2 | SER | ASN | GLN | ASN | LYS | ALA | SER | MET | LEU | GLN | ||||
3 | ALA | ARG | LEU | ASN | ASP | GLU | ALA | GLY | GLY | THR | ||||
4 | ARG | LEU | LEU | ARG | VAL | HIS | HIS | GLU | SER | ASP | ||||
5 | THR | GLU | GLU | ARG | GLY | PHE | LEU | GLU | LYS | ALA | ||||
6 | ALA | VAL | LYS | LYS | MET | ALA | LYS | ALA | ILE | MET | ||||
7 | ALA | ASP | PRO | ASN | LYS | ALA | ASP | GLU | VAL | TYR | ||||
8 | LYS | LYS | TRP | ALA | ASP | LYS | GLY | TYR | THR | LEU | ||||
9 | THR | GLN | MET | SER | ASN | PHE | LEU | LYS | SER | LYS | ||||
10 | THR | ALA | GLY | LYS | TYR | ASP | ARG | VAL | TYR | ASN | ||||
11 | GLY | TYR | VAL | ILE | HIS | LEU | ASP | TYR |
Samples:
sample_1: AVR3a4, [U-100% 13C; U-100% 15N], 1.11 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 300 mM; DTT, [U-100% 2H], 1 mM; sodium azide 0.02%; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 320 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe v20090801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.0.4, Johnson, One Moon Scientific - data analysis
Kujira v0.9843, Kobayashi, N. - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts