BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 16732

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16732
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Title: NMR structure of the PASTA domain 1 and 2 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_PASTA12, polymer, 140 residues, 14203.956 Da.

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_PASTA12: GHMGITRDVQVPDVRGQSSA DAIATLQNRGFKIRTLQKPD STIPPDHVIGTDPAANTSVS AGDEITVNVSTGPEQREIPD VSTLTYAEAVKKLTAAGFGR FKQANSPSTPELVGKVIGTN PPANQTSAITNVVIIIVGSG

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts146
1H chemical shifts908

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 140 residues - 14203.956 Da.

1   GLYHISMETGLYILETHRARGASPVALGLN
2   VALPROASPVALARGGLYGLNSERSERALA
3   ASPALAILEALATHRLEUGLNASNARGGLY
4   PHELYSILEARGTHRLEUGLNLYSPROASP
5   SERTHRILEPROPROASPHISVALILEGLY
6   THRASPPROALAALAASNTHRSERVALSER
7   ALAGLYASPGLUILETHRVALASNVALSER
8   THRGLYPROGLUGLNARGGLUILEPROASP
9   VALSERTHRLEUTHRTYRALAGLUALAVAL
10   LYSLYSLEUTHRALAALAGLYPHEGLYARG
11   PHELYSGLNALAASNSERPROSERTHRPRO
12   GLULEUVALGLYLYSVALILEGLYTHRASN
13   PROPROALAASNGLNTHRSERALAILETHR
14   ASNVALVALILEILEILEVALGLYSERGLY

Samples:

sample_1: PknB_PASTA12, [U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 95 ± 0.1 %; D2O 5.0 ± 0.1 %

sample_2: PknB_PASTA12, [U-100% 13C; U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 95 ± 0.1 %; D2O 5.0 ± 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

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