BMRB Entry 26030

Name: Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)
Published: 2016-10-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26030

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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 reduced, metal bound 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.
ZINC ION, non-polymer, 65.409 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):
PknG_74-147: LGGGLVEIPRAPDIDPLEAL MTNPVVPESKRFCWNCGRPV GRSDSETKGASEGWCPYCGS PYSFLPQLNPGDIV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	224
15N chemical shifts	63
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rubredoxin domain (RD)	1
2	ZN	2

Entities:

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

1

LEU

GLY

LEU

VAL

GLU

ILE

PRO

ARG

2

ALA

PRO

ASP

ILE

ASP

PRO

LEU

GLU

ALA

LEU

3

MET

THR

ASN

PRO

VAL

PRO

GLU

SER

LYS

4

ARG

PHE

CYS

TRP

ASN

CYS

GLY

ARG

PRO

VAL

5

GLY

ARG

SER

ASP

SER

GLU

THR

LYS

GLY

ALA

6

SER

GLU

GLY

TRP

CYS

PRO

TYR

CYS

GLY

SER

7

PRO

TYR

SER

PHE

LEU

PRO

GLN

LEU

ASN

PRO

8

GLY

ASP

ILE

VAL

Entity 2, ZN - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: PknG 74-147, [U-13C; U-15N], 0.4 – 0.8 mM; TRIS-HCL 20 mM; sodium chloride 150 mM; TCEP0.02 – 0.06 mM; zinc chloride0.02 – 0.05 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 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
3D C(CO)NH	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