BMRB Entry 25460
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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/BMR25460
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Title: Solution structure of Fungus protein B9WZW9_MAGOR PubMed: 26506000
Deposition date: 2015-01-30 Original release date: 2015-10-12
Authors: de Guillen, Karine
Citation: de Guillen, Karine; Ortiz-Vallejo, Diana; Gracy, Jerome; Fournier, Elisabeth; Kroj, Thomas; Padilla, Andre. "Structure analysis uncovers a highly diverse but structurally conserved effector family in phytopathogenic fungi" PLOS PATHOG. 11, e1005228-e1005228 (2015).
Assembly members:
AVR-Pia, polymer, 97 residues, 8885.165 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
Entity Sequences (FASTA):
AVR-Pia: APQDNTSMGSSHHHHHHSSG
RENLYFQGHMAAPARFCVYY
DGHLPATRVLLMYVRIGTTA
TITARGHEFEVEAKDQNCKV
ILTNGKQAPDWLAAEPY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 228 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 510 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AVR-Pia | 1 |
Entities:
Entity 1, AVR-Pia 97 residues - 8885.165 Da.
the sequence "APQDNTSMGSSHHHHHHSSGRENLYFQGHM" is the His-TAG and the TEV cleavage site
| 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 | PHE | CYS | VAL | TYR | TYR | ||||
| 5 | ASP | GLY | HIS | LEU | PRO | ALA | THR | ARG | VAL | LEU | ||||
| 6 | LEU | MET | TYR | VAL | ARG | ILE | GLY | THR | 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:
13C-15N: AVR-Pia, [U-13C; U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; potassium-sodium phosphate 20 mM; NaCl 150 mM
15N: AVR-Pia, [U-15N], 1 ± 0.1 mM; D2O 10%; H2O 90%; potassium-sodium phosphate 20 mM; NaCl 150 mM
D2O: AVR-Pia 1 ± 0.1 mM; D2O 100%; potassium-sodium phosphate 20 mM; NaCl 150 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 5.4; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 15N | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCO | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCA | 13C-15N | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | 13C-15N | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C-15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 13C-15N | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 13C-15N | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | D2O | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | D2O | isotropic | sample_conditions_1 |
| 2D DQF-COSY | D2O | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CCPNMR, CCPN - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS+ v1.2, Cornilescu, Delaglio and Bax - data analysis
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts