BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26027

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

Data sets:
Data typeCount
13C chemical shifts170
15N chemical shifts53
1H chemical shifts83

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NORS1

Entities:

Entity 1, NORS 95 residues - 10241.20 Da.

Residue 1-20 represents a non native poly histidine tag

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALALYSALASERGLUTHRGLUARGSER
4   GLYPROGLYTHRGLNPROALAASPALAGLN
5   THRALATHRSERALATHRVALARGPROLEU
6   SERTHRGLNALAVALPHEARGPROASPPHE
7   GLYASPGLUASPASNPHEPROHISPROTHR
8   LEUGLYPROASPTHRGLUPROGLNASPARG
9   METALATHRTHRSERARGVALARGPROPRO
10   VALARGARGLEUGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_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