BMRB Entry 18607
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18607
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Title: Solution structure of an avirulence protein AvrPzi-t from pathogen Magnaportheoryzae PubMed: 23334361
Deposition date: 2012-07-23 Original release date: 2013-02-14
Authors: Zhang, Zhi-min; Zhang, Xu; Zhou, Ziren; Hu, Hong-yu; Liu, Miali; Zhou, Bo; Zhou, Jiahai
Citation: Zhang, Zhi-Min; Zhang, Xu; Zhou, Zi-Ren; Hu, Hong-Yu; Liu, Maili; Zhou, Bo; Zhou, Jiahai. "Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t." J. Biomol. NMR 55, 219-223 (2013).
Assembly members:
Avrpiz-t, polymer, 80 residues, 8751.062 Da.
Natural source: Common Name: ascomycetes Taxonomy ID: 318829 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Magnaporthe oryzae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Avrpiz-t: SFVQCNHHLLYNGRHWGTIR
KKAGWAVRFYEEKPGQPKRL
VAICKNASPVHCNYLKCTNL
AAGFSAGTSTDVLSSGTVGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 302 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 497 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Avrpiz-t | 1 |
Entities:
Entity 1, Avrpiz-t 80 residues - 8751.062 Da.
| 1 | SER | PHE | VAL | GLN | CYS | ASN | HIS | HIS | LEU | LEU | |
| 2 | TYR | ASN | GLY | ARG | HIS | TRP | GLY | THR | ILE | ARG | |
| 3 | LYS | LYS | ALA | GLY | TRP | ALA | VAL | ARG | PHE | TYR | |
| 4 | GLU | GLU | LYS | PRO | GLY | GLN | PRO | LYS | ARG | LEU | |
| 5 | VAL | ALA | ILE | CYS | LYS | ASN | ALA | SER | PRO | VAL | |
| 6 | HIS | CYS | ASN | TYR | LEU | LYS | CYS | THR | ASN | LEU | |
| 7 | ALA | ALA | GLY | PHE | SER | ALA | GLY | THR | SER | THR | |
| 8 | ASP | VAL | LEU | SER | SER | GLY | THR | VAL | GLY | SER |
Samples:
sample_1: Avrpiz-t, [U-100% 13C; U-100% 15N], 0.3 mM; D2O 90%; H2O 10%
sample_2: Avrpiz-t, [U-100% 15N], 0.3 mM; D2O 100%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
sample_conditions_2: pH: 6.5; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Linge, O, . - chemical shift assignment, processing, structure solution
NMR spectrometers:
- Bruker INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CCC41985 CCD21890 CCD21891 CCD21894 CCD21896 |
| GB | ACF39937 AEX97148 EAQ70816 EHA46544 ELQ40553 |
| REF | XP_003721287 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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or all simulated shifts