BMRB Entry 34170

Title:
Solution structure of antifungal protein NFAP
Deposition date:
2017-08-14
Original release date:
2018-07-23
Authors:
Hajdu, D.; Czajlik, A.; Marx, F.; Galgoczy, L.; Batta, G.
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:
entity_1, polymer, 57 residues, 6639.575 Da.

Natural source:

Natural source:   Common Name: Neosartorya fischeri   Taxonomy ID: 331117   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Neosartorya fischeri

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Penicillium chrysogenum   Vector: pSK275nfappaf_signal

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts218
15N chemical shifts59
1H chemical shifts347

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 57 residues - 6639.575 Da.

1   LEUGLUTYRLYSGLYGLUCYSPHETHRLYS
2   ASPASNTHRCYSLYSTYRLYSILEASPGLY
3   LYSTHRTYRLEUALALYSCYSPROSERALA
4   ALAASNTHRLYSCYSGLULYSASPGLYASN
5   LYSCYSTHRTYRASPSERTYRASNARGLYS
6   VALLYSCYSASPPHEARGHIS

Samples:

sample_1: acetic acid, [U-100% 2H], 20 mM; NFAP, [U-100% 15N], 1.1 mM; H2O 95%; D2O, [U-2H], 5%

sample_2: acetic acid, [U-100% 2H], 20 mM; NFAP, [U-100% 13C; U-100% 15N], 1 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.007 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.007 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_2
3D HN(COCA)CBsample_2isotropicsample_conditions_2
3D HNHAsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2

Software:

CARA v1.9.0, Keller and Wuthrich - chemical shift assignment

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

TALOS v+, Cornilescu, Delaglio and Bax - refinement

TOPSPIN v3.0, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceII 500.13 MHz
  • Bruker AvanceII 700.13 MHz

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