BMRB Entry 26001

Title:
Structure, Dynamics and functional Aspects of the antifungal protein sfPAFB
Deposition date:
2016-03-17
Original release date:
2017-04-17
Authors:
Batta, Gyula; Fizil, Adam; Hajdu, Dorottya
Citation:

Citation: Hajdu, Dorottya; Huber, Anna; Czajlik, Andras; Toth, Liliana; Kele, Zoltan; Kocsube, Sandor; Fizil, Adam; Marx, Florentine; Galgoczy, Laszlo; Batta, Gyula. "Solution structure and novel insights into phylogeny and mode of action of the Neosartorya (Aspergillus) fischeri antifungal protein (NFAP)"  Int. J. Biol. Macromol. 129, 511-522 (2019).
PubMed: 30738898

Assembly members:

Assembly members:
sfPAFB, polymer, 56 residues, 6316.193 Da.

Natural source:

Natural source:   Common Name: Penicillium chrysogenum   Taxonomy ID: 5076   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Penicillium chrysogenum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Penicillium chrysogenum   Vector: pSK275pafB

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts58
1H chemical shifts330

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1antifungal protein sfPAFB1

Entities:

Entity 1, antifungal protein sfPAFB 56 residues - 6316.193 Da.

1   LYSPHEGLYGLYGLUCYSSERLEULYSHIS
2   ASNTHRCYSTHRTYRLEULYSGLYGLYLYS
3   ASNHISVALVALASNCYSGLYSERALAALA
4   ASNLYSLYSCYSLYSSERASPARGHISHIS
5   CYSGLUTYRASPGLUHISHISLYSARGVAL
6   ASPCYSGLNTHRPROVAL

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.65 mM; acetic acid, [U-100% 2H], 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_2: entity 1 mM; acetic acid, [U-2H], 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 7.5 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
HBCBCGCDHDsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1; 3.0, Bruker Biospin - collection, processing

CARA v8.4, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment

TALOS+, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks