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
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Title: Solution structure of the antifungal protein PAF from Penicillium chrysogenum PubMed: 19459942
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: 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).
Assembly members:
PAF, polymer, 55 residues, Formula weight is not available
Natural source: Common Name: Penicillium chrysogenum Taxonomy ID: 5076 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Penicillium chrysogenum
Experimental source: Production method: P. chrysogenum Q176 (ATCC 10002) was cultivated in minimal medium Host organism: Penicillium chrysogenum
Entity Sequences (FASTA):
PAF: AKYTGKCTKSKNECKYKNDA
GKDTFIKCPKFDNKKCTKDN
NKCTVDTYNNAVDCD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 64 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 110 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PAF | 1 |
Entities:
Entity 1, PAF 55 residues - Formula weight is not available
| 1 | ALA | LYS | TYR | THR | GLY | LYS | CYS | THR | LYS | SER | ||||
| 2 | LYS | ASN | GLU | CYS | LYS | TYR | LYS | ASN | ASP | ALA | ||||
| 3 | GLY | LYS | ASP | THR | PHE | ILE | LYS | CYS | PRO | LYS | ||||
| 4 | PHE | ASP | ASN | LYS | LYS | CYS | THR | LYS | ASP | ASN | ||||
| 5 | ASN | LYS | CYS | THR | VAL | ASP | THR | TYR | ASN | ASN | ||||
| 6 | ALA | VAL | ASP | CYS | ASP |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts