BMRB Entry 25957
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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/BMR25957
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Title: Structure of D19S variant of the Penicillium Antifungal Protein (PAF) PubMed: 28072824
Deposition date: 2016-01-18 Original release date: 2017-01-12
Authors: Fizil, Adam; Batta, Gyula
Citation: Sonderegger, Christoph; Fizil, Adam; Burtscher, Laura; Komaromi, Istvan; Czajlik, Andras; Munoz, Alberto; Hegedus, Nikoletta; Read, Nick; Batta, Gyula; Marx, Florentine. "D19S Mutation of the Cationic, Cysteine-Rich Protein PAF: Novel Insights into Its Structural Dynamics, Thermal Unfolding and Antifungal Function" Plos One 12, e0169920-e0169920 (2017).
Assembly members:
PAFD19S, polymer, 55 residues, 6235.121 Da.
Natural source: Common Name: ascomycetes Taxonomy ID: 5076 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Penicillium chrisogenum
Experimental source: Production method: recombinant technology Host organism: Penicillium chrisogenum
Entity Sequences (FASTA):
PAFD19S: AKYTGKCTKSKNECKYKNSA
GKDTFIKCPKFDNKKCTKDN
NKCTVDTYNNAVDCD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 112 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 278 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PAFD19S | 1 |
Entities:
Entity 1, PAFD19S 55 residues - 6235.121 Da.
| 1 | ALA | LYS | TYR | THR | GLY | LYS | CYS | THR | LYS | SER | ||||
| 2 | LYS | ASN | GLU | CYS | LYS | TYR | LYS | ASN | SER | ALA | ||||
| 3 | GLY | LYS | ASP | THR | PHE | ILE | LYS | CYS | PRO | LYS | ||||
| 4 | PHE | ASP | ASN | LYS | LYS | CYS | THR | LYS | ASP | ASN | ||||
| 5 | ASN | LYS | CYS | THR | VAL | ASP | THR | TYR | ASN | ASN | ||||
| 6 | ALA | VAL | ASP | CYS | ASP |
Samples:
sample_1: PAFD19S, [U-100% 15N], 1.7 mM; D2O, [U-2H], 5 v/v; H2O 95 v/v; sodium chloride 40 mM; sodium phosphate 10 mM; potassium phosphate 0.04%
sample_conditions_1: ionic strength: 0.02 M; pH: 5.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v1.9, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Braun and Wuthrich - structure solution
ATNOS-CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution
TALOS vTalos +, Cornilescu, Delaglio and Bax - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker DRX 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts