BMRB Entry 16734

Name: NMR structure of the PASTA domain 3 and 4 of Mycobacterium tuberculosis of PknB
Published: 2010-05-18

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PDB ID: 2kuf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16734
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the PASTA domain 3 and 4 of Mycobacterium tuberculosis of PknB

Deposition date:

2010-02-17

Original release date:

2010-05-18

Authors:

Barthe, Philippe; Cohen-Gonsaud, Martin; Roumestand, Christian; Mukamolova, Galina

Citation:

Citation: Barthe, Philippe; Mukamolova, Galina; Roumestand, Christian; Cohen-Gonsaud, Martin. "The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation." Structure (Cambridge, MA, U. S.) 18, 606-615 (2010).
PubMed: 20462494

Assembly members:

Assembly members:
PknB_PASTA34, polymer, 139 residues, 14203.956 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PknB_PASTA34: GHMGPATKDIPDVAGQTVDV AQKNLNVYGFTKFSQASVDS PRPAGEVTGTNPPAGTTVPV DSVIELQVSKGNQFVMPDLS GMFWVDAEPRLRALGWTGML DKGADVDAGGSQHNRVVYQN PPAGTGVNRDGIITLRFGQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	378
15N chemical shifts	148
1H chemical shifts	890

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 139 residues - 14203.956 Da.

1

GLY

HIS

MET

GLY

PRO

ALA

THR

LYS

ASP

ILE

2

PRO

ASP

VAL

ALA

GLY

GLN

THR

VAL

ASP

VAL

3

ALA

GLN

LYS

ASN

LEU

ASN

VAL

TYR

GLY

PHE

4

THR

LYS

PHE

SER

GLN

ALA

SER

VAL

ASP

SER

5

PRO

ARG

PRO

ALA

GLY

GLU

VAL

THR

GLY

THR

6

ASN

PRO

ALA

GLY

THR

VAL

PRO

VAL

7

ASP

SER

VAL

ILE

GLU

LEU

GLN

VAL

SER

LYS

8

GLY

ASN

GLN

PHE

VAL

MET

PRO

ASP

LEU

SER

9

GLY

MET

PHE

TRP

VAL

ASP

ALA

GLU

PRO

ARG

10

LEU

ARG

ALA

LEU

GLY

TRP

THR

GLY

MET

LEU

11

ASP

LYS

GLY

ALA

ASP

VAL

ASP

ALA

GLY

12

SER

GLN

HIS

ASN

ARG

VAL

TYR

GLN

ASN

13

PRO

ALA

GLY

THR

GLY

VAL

ASN

ARG

ASP

14

GLY

ILE

THR

LEU

ARG

PHE

GLY

GLN

Samples:

sample_1: PknB_PASTA34, [U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 5.0 ± 0.1 %; D2O 95 ± 0.1 %

sample_2: PknB_PASTA34, [U-100% 13C; U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 95 ± 0.1 %; D2O 5 ± 0.1 %

sample_conditions_1: ionic strength: 20 mM; pH: 4.6; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance III 700 MHz
Bruker Avance III 500 MHz