BMRB Entry 34963
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34963
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: de Guillen, K.; Mammri, L.; Gracy, J.; Padilla, A.; Barthe, P.; Hoh, F.; Lahfa, M.; Rouffet, J.; Petit-Houdenot, Y.; Kroj, T.; Lebrun, M.. "Structural studies identify killer proteins 4 and 6 from the fungal wheat pathogen Zymoseptoria tritici toxic to fungi and related to structural effector families" .
Assembly members:
entity_1, polymer, 80 residues, 9081.172 Da.
Natural source: Common Name: Zymoseptoria tritici ST99CH_1E4 Taxonomy ID: 1276532 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Zymoseptoria tritici
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GHMAVVYAARCKFGNPLVQN
NRITRAVCDLTNEHTTKDGS
WHYVEVDNECKYLAGDNPRD
QPGWAVFVKYCTYYKGVPDA
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 540 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 80 residues - 9081.172 Da.
| 1 | GLY | HIS | MET | ALA | VAL | VAL | TYR | ALA | ALA | ARG | |
| 2 | CYS | LYS | PHE | GLY | ASN | PRO | LEU | VAL | GLN | ASN | |
| 3 | ASN | ARG | ILE | THR | ARG | ALA | VAL | CYS | ASP | LEU | |
| 4 | THR | ASN | GLU | HIS | THR | THR | LYS | ASP | GLY | SER | |
| 5 | TRP | HIS | TYR | VAL | GLU | VAL | ASP | ASN | GLU | CYS | |
| 6 | LYS | TYR | LEU | ALA | GLY | ASP | ASN | PRO | ARG | ASP | |
| 7 | GLN | PRO | GLY | TRP | ALA | VAL | PHE | VAL | LYS | TYR | |
| 8 | CYS | THR | TYR | TYR | LYS | GLY | VAL | PRO | ASP | ALA |
Samples:
sample_1: Zt-KP6-1, [U-100% 15N], 0.7 mM; ammonium citrate 20 mM; sodium chloride 150 mM; DTT 1 mM
sample_2: Zt-KP6-1, [U-100% 15N], 0.7 mM; ammonium citrate 20 mM; sodium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 150 mM; pH: 5.4; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CINDY v2.1, Padilla, A. - chemical shift assignment, peak picking
CYANA v3.98.15, Guntert, Mumenthaler and Wuthrich - structure calculation
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks