BMRB Entry 26734
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26734
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Title: D53S/D55S variant of Penicillium Antifungal Protein, PAF PubMed: 28072824
Deposition date: 2016-01-18 Original release date: 2017-08-24
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:
Penicillium_Antifungal_Protein_D53S/D55S, polymer, 55 residues, Formula weight is not available
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 Vector: pSK275
Entity Sequences (FASTA):
Penicillium_Antifungal_Protein_D53S/D55S: AKYTGKCTKSKNECKYKNDA
GKDTFIKCPKFDNKKCTKDN
NKCTVDTYNNAVSCS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 103 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 253 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PAF D53S-D55S | 1 |
Entities:
Entity 1, PAF D53S-D55S 55 residues - Formula weight is not available
| 1 | ALA | LYS | TYR | THR | GLY | LYS | CYS | THR | LYS | SER | ||||
| 2 | LYS | ASN | GLU | CYS | LYS | TYR | LYS | ASN | ASP | 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 | SER | CYS | SER |
Samples:
sample_1: Penicillium Antifungal Protein D53S/D55S, [U-100% 15N], 0.7 mM; D2O, [U-2H], 5%; H2O 95%; potassium phosphate 0.1 mM; sodium azide 0.04%; sodium chloride 40 mM
sample_conditions_1: ionic strength: 20 mM; 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 |
| 3D 1H-15N TOCSY | 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 |
| 3D HNHA | 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
NMR spectrometers:
- Bruker Avance 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts