BMRB Entry 26027
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26027
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG) PubMed: 27632081
Deposition date: 2016-04-10 Original release date: 2016-10-14
Authors: Wittwer, Matthias; Dames, Sonja
Citation: Wittwer, Matthias; Dames, Sonja. "Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G" Biomol. NMR Assign. 10, 401-406 (2016).
Assembly members:
His-PknG_1-75, polymer, 95 residues, 10241.20 Da.
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 83332 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
His-PknG_1-75: MGSSHHHHHHSSGLVPRGSH
MAKASETERSGPGTQPADAQ
TATSATVRPLSTQAVFRPDF
GDEDNFPHPTLGPDTEPQDR
MATTSRVRPPVRRLG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 170 |
15N chemical shifts | 53 |
1H chemical shifts | 83 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NORS | 1 |
Entities:
Entity 1, NORS 95 residues - 10241.20 Da.
Residue 1-20 represents a non native poly histidine tag
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
3 | MET | ALA | LYS | ALA | SER | GLU | THR | GLU | ARG | SER | ||||
4 | GLY | PRO | GLY | THR | GLN | PRO | ALA | ASP | ALA | GLN | ||||
5 | THR | ALA | THR | SER | ALA | THR | VAL | ARG | PRO | LEU | ||||
6 | SER | THR | GLN | ALA | VAL | PHE | ARG | PRO | ASP | PHE | ||||
7 | GLY | ASP | GLU | ASP | ASN | PHE | PRO | HIS | PRO | THR | ||||
8 | LEU | GLY | PRO | ASP | THR | GLU | PRO | GLN | ASP | ARG | ||||
9 | MET | ALA | THR | THR | SER | ARG | VAL | ARG | PRO | PRO | ||||
10 | VAL | ARG | ARG | LEU | GLY |
Samples:
sample_1: PknG 1-75, [U-13C; U-15N], 0.4 0.8 mM; TRIS-HCL 20 mM; sodium chloride 150 mM; H2O 95%; D2O, [U-2H], 5%
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts