BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26734

Title: D53S/D55S variant of Penicillium Antifungal Protein, PAF   PubMed: 28072824

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

Entity Sequences (FASTA):
Penicillium_Antifungal_Protein_D53S/D55S: AKYTGKCTKSKNECKYKNDA GKDTFIKCPKFDNKKCTKDN NKCTVDTYNNAVSCS

Data sets:
Data typeCount
13C chemical shifts103
15N chemical shifts54
1H chemical shifts253

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PAF D53S-D55S1

Entities:

Entity 1, PAF D53S-D55S 55 residues - Formula weight is not available

1   ALALYSTYRTHRGLYLYSCYSTHRLYSSER
2   LYSASNGLUCYSLYSTYRLYSASNASPALA
3   GLYLYSASPTHRPHEILELYSCYSPROLYS
4   PHEASPASNLYSLYSCYSTHRLYSASPASN
5   ASNLYSCYSTHRVALASPTHRTYRASNASN
6   ALAVALSERCYSSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_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

Related Database Links: