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Biological Magnetic Resonance Data Bank


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BMRB Entry 19657

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19657
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Title: Solution Structure of Penicillium Antifungal Protein PAF

Deposition date: 2013-12-05 Original release date: 2014-12-08

Authors: Fizil, Adam; Batta, Gyula

Citation: Fizil, Adam; Gaspari, Zoltan; Barna, Terezia; Marx, Florentine; Batta, Gyula. "NMR Analysis of Constrained Cold and Heat Unfolding of the Antifungal Disulfide Protein PAF: 15N-CEST Reveals Hidden Conformers"  J. Am. Chem. Soc. ., .-..

Assembly members:
entity, polymer, 55 residues, 6263.131 Da.

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

Experimental source:   Production method: purified from the natural source   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: AKYTGKCTKSKNECKYKNDA GKDTFIKCPKFDNKKCTKDN NKCTVDTYNNAVDCD

Data sets:
Data typeCount
13C chemical shifts203
15N chemical shifts59
1H chemical shifts329

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Penicillium Antifungal Protein PAF1

Entities:

Entity 1, Penicillium Antifungal Protein PAF 55 residues - 6263.131 Da.

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

Samples:

sample_1: sodium phosphate 10 ± 0.1 mM; sodium chloride 40 ± 0.1 mM; entity, [U-99% 13C; U-99% 15N], 1.7 ± 0.1 mM; sodium azide 0.6 ± 0.1 mM; H2O 10%; D2O 5%

sample_conditions_1: ionic strength: 0.025 M; pH: 6.0; 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 NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich, Herrmann, Guntert and Wuthrich, Keller and Wuthrich - chemical shift assignment, peak picking, structure solution

TALOS vTALOS+, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16087
PDB
EMBL CAP86946 CDM32600
GB AAA92718 ABE96639 ABE96640
PRF 2204241A
REF XP_002566698

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts