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 26028

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26028

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 residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain   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_1-147, polymer, 167 residues, 18001.98 Da.
ZINC ION, non-polymer, 65.409 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_1-147: MGSSHHHHHHSSGLVPRGSH MAKASETERSGPGTQPADAQ TATSATVRPLSTQAVFRPDF GDEDNFPHPTLGPDTEPQDR MATTSRVRPPVRRLGGGLVE IPRAPDIDPLEALMTNPVVP ESKRFCWNCGRPVGRSDSET KGASEGWCPYCGSPYSFLPQ LNPGDIV

Data sets:
Data typeCount
13C chemical shifts394
15N chemical shifts115
1H chemical shifts124

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NORS & rubredoxin-domain (RD)1
2ZN2

Entities:

Entity 1, NORS & rubredoxin-domain (RD) 167 residues - 18001.98 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   VALARGARGLEUGLYGLYGLYLEUVALGLU
11   ILEPROARGALAPROASPILEASPPROLEU
12   GLUALALEUMETTHRASNPROVALVALPRO
13   GLUSERLYSARGPHECYSTRPASNCYSGLY
14   ARGPROVALGLYARGSERASPSERGLUTHR
15   LYSGLYALASERGLUGLYTRPCYSPROTYR
16   CYSGLYSERPROTYRSERPHELEUPROGLN
17   LEUASNPROGLYASPILEVAL

Entity 2, ZN - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: PknG 1-147, [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 C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_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