BMRB Entry 16733

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:

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:

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

Natural source:

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   Vector: pET21-TEV

Experimental source:

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   Vector: pET21-TEV

Data sets:
Data typeCount
13C chemical shifts387
15N chemical shifts139
1H chemical shifts896

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 138 residues - Formula weight is not available

1   GLYHISMETGLYPROGLUGLNARGGLUILE
2   PROASPVALSERTHRLEUTHRTYRALAGLU
3   ALAVALLYSLYSLEUTHRALAALAGLYPHE
4   GLYARGPHELYSGLNALAASNSERPROSER
5   THRPROGLULEUVALGLYLYSVALILEGLY
6   THRASNPROPROALAASNGLNTHRSERALA
7   ILETHRASNVALVALILEILEILEVALGLY
8   SERGLYPROALATHRLYSASPILEPROASP
9   VALALAGLYGLNTHRVALASPVALALAGLN
10   LYSASNLEUASNVALTYRGLYPHETHRLYS
11   PHESERGLNALASERVALASPSERPROARG
12   PROALAGLYGLUVALTHRGLYTHRASNPRO
13   PROALAGLYTHRTHRVALPROVALASPSER
14   VALILEGLULEUGLNVALSERLYS

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:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_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

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts