BMRB Entry 26027

Name: Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG)
Published: 2016-10-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26027

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) 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:
His-PknG_1-75, polymer, 95 residues, 10241.20 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):

Entity Sequences (FASTA):
His-PknG_1-75: MGSSHHHHHHSSGLVPRGSH MAKASETERSGPGTQPADAQ TATSATVRPLSTQAVFRPDF GDEDNFPHPTLGPDTEPQDR MATTSRVRPPVRRLG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	170
15N chemical shifts	53
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

HIS

2

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

SER

ARG

VAL

ARG

PRO

10

VAL

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