BMRB Entry 16733

Name: NMR structure of the PASTA domain 2 and 3 of Mycobacterium tuberculosis of PknB
Published: 2010-05-18

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PDB ID: 2kue
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16733
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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 2 and 3 of Mycobacterium tuberculosis of PknB PubMed: 20462494

Deposition date: 2010-02-17 Original release date: 2010-05-18

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

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).

Assembly members:
PknB_PASTA23, polymer, 138 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
PknB_PASTA23: GHMGPEQREIPDVSTLTYAE AVKKLTAAGFGRFKQANSPS TPELVGKVIGTNPPANQTSA ITNVVIIIVGSGPATKDIPD VAGQTVDVAQKNLNVYGFTK FSQASVDSPRPAGEVTGTNP PAGTTVPVDSVIELQVSK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	387
15N chemical shifts	139
1H chemical shifts	896

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 138 residues - Formula weight is not available

1

GLY

HIS

MET

GLY

PRO

GLU

GLN

ARG

GLU

ILE

2

PRO

ASP

VAL

SER

THR

LEU

THR

TYR

ALA

GLU

3

ALA

VAL

LYS

LEU

THR

ALA

GLY

PHE

4

GLY

ARG

PHE

LYS

GLN

ALA

ASN

SER

PRO

SER

5

THR

PRO

GLU

LEU

VAL

GLY

LYS

VAL

ILE

GLY

6

THR

ASN

PRO

ALA

ASN

GLN

THR

SER

ALA

7

ILE

THR

ASN

VAL

ILE

VAL

GLY

8

SER

GLY

PRO

ALA

THR

LYS

ASP

ILE

PRO

ASP

9

VAL

ALA

GLY

GLN

THR

VAL

ASP

VAL

ALA

GLN

10

LYS

ASN

LEU

ASN

VAL

TYR

GLY

PHE

THR

LYS

11

PHE

SER

GLN

ALA

SER

VAL

ASP

SER

PRO

ARG

12

PRO

ALA

GLY

GLU

VAL

THR

GLY

THR

ASN

PRO

13

PRO

ALA

GLY

THR

VAL

PRO

VAL

ASP

SER

14

VAL

ILE

GLU

LEU

GLN

VAL

SER

LYS

Samples:

sample_1: PknB_PASTA23, [U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 95 ± 0.1 %; D2O 5 ± 0.1 %

sample_2: PknB_PASTA23, [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

Biological Magnetic Resonance Data Bank