BMRB Entry 30068
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30068
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Title: M. Oryzae effector AVR-Pia mutant H3 PubMed: 28087830
Deposition date: 2016-04-21 Original release date: 2017-03-23
Authors: Padilla, Andre; deGuillen, Karine
Citation: Ortiz, Diana; de Guillen, Karine; Cesari, Stella; Chalvon, Veronique; Gracy, Jerome; Padilla, Andre; Kroj, Thomas. "Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5." Plant Cell 29, 156-168 (2017).
Assembly members:
Antivirulence protein AVR-Pia, polymer, 97 residues, 10830.049 Da.
Natural source: Common Name: Rice blast fungus Taxonomy ID: 318829 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Magnaporthe oryzae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
Antivirulence protein AVR-Pia: APQDNTSMGSSHHHHHHSSG
RENLYFQGHMAAPARSCVYY
DGHLPATRVLLMYVRIGNTA
TITARGHEFEVEAKDQNCKV
ILTNGKQAPDWLAAEPY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 152 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 522 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 97 residues - 10830.049 Da.
| 1 | ALA | PRO | GLN | ASP | ASN | THR | SER | MET | GLY | SER | ||||
| 2 | SER | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 3 | ARG | GLU | ASN | LEU | TYR | PHE | GLN | GLY | HIS | MET | ||||
| 4 | ALA | ALA | PRO | ALA | ARG | SER | CYS | VAL | TYR | TYR | ||||
| 5 | ASP | GLY | HIS | LEU | PRO | ALA | THR | ARG | VAL | LEU | ||||
| 6 | LEU | MET | TYR | VAL | ARG | ILE | GLY | ASN | THR | ALA | ||||
| 7 | THR | ILE | THR | ALA | ARG | GLY | HIS | GLU | PHE | GLU | ||||
| 8 | VAL | GLU | ALA | LYS | ASP | GLN | ASN | CYS | LYS | VAL | ||||
| 9 | ILE | LEU | THR | ASN | GLY | LYS | GLN | ALA | PRO | ASP | ||||
| 10 | TRP | LEU | ALA | ALA | GLU | PRO | TYR |
Samples:
sample_1: AVR-Pia-H3, [U-15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 5.4; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
TOPSPIN v3.2, Bruker Biospin - chemical shift assignment
NMR spectrometers:
- Bruker AvanceIII 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts