BMRB Entry 25557
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25557
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Title: Backbone chemical shift assignments for reduced peroxiredoxin Q from the plant pathogen Xanthomonas campestris. PubMed: 26438558
Deposition date: 2015-03-28 Original release date: 2015-05-08
Authors: Buchko, Garry; Perkins, Arden; Karplus, P.
Citation: Buchko, Garry; Perkins, Arden; Parsonage, Derek; Poole, Leslie; Karplus, P.. "Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics" Biomol. NMR Assign. 10, 57-61 (2016).
Assembly members:
PrxQ, polymer, 160 residues, Formula weight is not available
Natural source: Common Name: Xanthomonas campestris Taxonomy ID: 339 Superkingdom: Bacteria Kingdom: not available Genus/species: Xanthomonas campestris
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PrxQ: MTDAVLELPAATFDLPLSLS
GGTQTTLRAHAGHWLVIYFY
PKDSTPGCTTEGLDFNALLP
EFDKAGAKILGVSRDSVKSH
DNFCAKQGFAFPLVSDGDEA
LCRAFDVIKEKNMYGKQVLG
IERSTFLLSPEGQVVQAWRK
VKVAGHADAVLAALKAHAKQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 504 |
15N chemical shifts | 151 |
1H chemical shifts | 151 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PrxQ | 1 |
Entities:
Entity 1, PrxQ 160 residues - Formula weight is not available
1 | MET | THR | ASP | ALA | VAL | LEU | GLU | LEU | PRO | ALA | |
2 | ALA | THR | PHE | ASP | LEU | PRO | LEU | SER | LEU | SER | |
3 | GLY | GLY | THR | GLN | THR | THR | LEU | ARG | ALA | HIS | |
4 | ALA | GLY | HIS | TRP | LEU | VAL | ILE | TYR | PHE | TYR | |
5 | PRO | LYS | ASP | SER | THR | PRO | GLY | CYS | THR | THR | |
6 | GLU | GLY | LEU | ASP | PHE | ASN | ALA | LEU | LEU | PRO | |
7 | GLU | PHE | ASP | LYS | ALA | GLY | ALA | LYS | ILE | LEU | |
8 | GLY | VAL | SER | ARG | ASP | SER | VAL | LYS | SER | HIS | |
9 | ASP | ASN | PHE | CYS | ALA | LYS | GLN | GLY | PHE | ALA | |
10 | PHE | PRO | LEU | VAL | SER | ASP | GLY | ASP | GLU | ALA | |
11 | LEU | CYS | ARG | ALA | PHE | ASP | VAL | ILE | LYS | GLU | |
12 | LYS | ASN | MET | TYR | GLY | LYS | GLN | VAL | LEU | GLY | |
13 | ILE | GLU | ARG | SER | THR | PHE | LEU | LEU | SER | PRO | |
14 | GLU | GLY | GLN | VAL | VAL | GLN | ALA | TRP | ARG | LYS | |
15 | VAL | LYS | VAL | ALA | GLY | HIS | ALA | ASP | ALA | VAL | |
16 | LEU | ALA | ALA | LEU | LYS | ALA | HIS | ALA | LYS | GLN |
Samples:
sample_1: PrxQ, [U-99% 13C; U-99% 15N], 1.0 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.2 mM; H2O 93%; D2O, [U-2H], 7%
sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.115, Goddard - data analysis
Felix v2007, Accelrys Software Inc. - processing
NMR spectrometers:
- Varian VNMRS 750 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts