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 25957

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

Data sets:
Data typeCount
13C chemical shifts112
15N chemical shifts60
1H chemical shifts278

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PAFD19S1

Entities:

Entity 1, PAFD19S 55 residues - 6235.121 Da.

1   ALALYSTYRTHRGLYLYSCYSTHRLYSSER
2   LYSASNGLUCYSLYSTYRLYSASNSERALA
3   GLYLYSASPTHRPHEILELYSCYSPROLYS
4   PHEASPASNLYSLYSCYSTHRLYSASPASN
5   ASNLYSCYSTHRVALASPTHRTYRASNASN
6   ALAVALASPCYSASP

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_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