BMRB Entry 16087

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16087
MolProbity Validation Chart

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Title:
Solution structure of the antifungal protein PAF from Penicillium chrysogenum
Deposition date:
2008-12-23
Original release date:
2009-05-29
Authors:
Batta, Gyula; Barna, Terez; Gaspari, Zoltan; Sandor, Szabolcs; Kover, Katalin; Binder, Ulrike; Sarg, Bettina; Kaiserer, Lydia; Chhillar, Anil; Eigentler, Andrea; Leiter, Eva; Hegedus, Nikoletta; Pocsi, Istvan; Lindner, Herbert; Marx, Florentine
Citation:

Citation: Batta, Gyula; Barna, Terez; Gaspari, Zoltan; Sandor, Szabolcs; Kover, Katalin; Binder, Ulrike; Sarg, Bettina; Kaiserer, Lydia; Chhillar, Anil; Eigentler, Andrea; Leiter, Eva; Hegedus, Nikoletta; Pocsi, Istvan; Lindner, Herbert; Marx, Florentine. "Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum"  FEBS J. 276, 2875-2890 (2009).
PubMed: 19459942

Assembly members:

Assembly members:
PAF, polymer, 55 residues, Formula weight is not available

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: P. chrysogenum Q176 (ATCC 10002) was cultivated in minimal medium   Host organism: Penicillium chrysogenum

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PAF: AKYTGKCTKSKNECKYKNDA GKDTFIKCPKFDNKKCTKDN NKCTVDTYNNAVDCD

Data sets:
Data typeCount
13C chemical shifts64
15N chemical shifts53
1H chemical shifts110

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PAF1

Entities:

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

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

Samples:

sample_1: PAF, [U-100% 15N], 1.6 mM; NACL 40 mM; NAN3 0.04%

sample_conditions_1: ionic strength: 0.046 M; pH: 5.0; pressure: 1.0 atm; temperature: 304 K

Experiments:

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

Software:

CYANA v2.0, Bruker Biospin, Goddard, GROMACS, Bekker, Berendse, Dijkstra, Guntert, Mumenthaler and Wuthrich, Herrmann, Guntert and Wuthrich, Laskowski and MacArthur - automated NOE chemical shift assignment, chemical shift assignment, collection, Molecular Dynamics Calculation, NMR structure calculation, protein structure data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 700 MHz

Related Database Links:

BMRB 19657
PDB
EMBL CAP86946 CDM32600
GB AAA92718 ABE96639 ABE96640
PRF 2204241A
REF XP_002566698

Download HSQC peak lists in one of the following formats:
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