BMRB Entry 26029

Title:
Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)
Deposition date:
2016-04-10
Original release date:
2016-10-14
Authors:
Wittwer, Matthias; Dames, Sonja
Citation:

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).
PubMed: 27632081

Assembly members:

Assembly members:
PknG_74-147, polymer, 74 residues, 7949.01 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts154
15N chemical shifts44
1H chemical shifts44

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rubredoxin domain (RD)1

Entities:

Entity 1, Rubredoxin domain (RD) 74 residues - 7949.01 Da.

1   LEUGLYGLYGLYLEUVALGLUILEPROARG
2   ALAPROASPILEASPPROLEUGLUALALEU
3   METTHRASNPROVALVALPROGLUSERLYS
4   ARGPHECYSTRPASNCYSGLYARGPROVAL
5   GLYARGSERASPSERGLUTHRLYSGLYALA
6   SERGLUGLYTRPCYSPROTYRCYSGLYSER
7   PROTYRSERPHELEUPROGLNLEUASNPRO
8   GLYASPILEVAL

Samples:

sample_1: PknG 74-147, [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 HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_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
  • Bruker Avance 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks