BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17586

Title: Rv0020c_FHA Structure   PubMed: 22000520

Deposition date: 2011-04-11 Original release date: 2011-10-26

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

Citation: Roumestand, Christian; Leiba, Jade; Galophe, Nathalie; Margeat, Emmanuel; Padilla, Andre; Bessin, Yannick; Barthe, Philippe; Molle, Virginie; Cohen-Gonsaud, Martin. "Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase."  Structure 19, 1525-1534 (2011).

Assembly members:
Rv0020c_FHA, polymer, 100 residues, 10888.060 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):
Rv0020c_FHA: GHGSAGTSVTLQLDDGSGRT YQLREGSNIIGRGQDAQFRL PDTGVSRRHLEIRWDGQVAL LADLNSTNGTTVNNAPVQEW QLADGDVIRLGHSEIIVRMH

Data sets:
Data typeCount
13C chemical shifts287
15N chemical shifts114
1H chemical shifts673

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv0020c_FHA1

Entities:

Entity 1, Rv0020c_FHA 100 residues - 10888.060 Da.

1   GLYHISGLYSERALAGLYTHRSERVALTHR
2   LEUGLNLEUASPASPGLYSERGLYARGTHR
3   TYRGLNLEUARGGLUGLYSERASNILEILE
4   GLYARGGLYGLNASPALAGLNPHEARGLEU
5   PROASPTHRGLYVALSERARGARGHISLEU
6   GLUILEARGTRPASPGLYGLNVALALALEU
7   LEUALAASPLEUASNSERTHRASNGLYTHR
8   THRVALASNASNALAPROVALGLNGLUTRP
9   GLNLEUALAASPGLYASPVALILEARGLEU
10   GLYHISSERGLUILEILEVALARGMETHIS

Samples:

15N: Rv0020c_FHA, [U-15N], 0.5 ± 0.01 mM

13C-15N: Rv0020c_FHA, [U-13C; U-15N], 0.5 ± 0.01 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-15N TOCSY15Nisotropicsample_conditions_1
3D HNCA13C-15Nisotropicsample_conditions_1
3D CBCA(CO)NH13C-15Nisotropicsample_conditions_1
3D HNCACB13C-15Nisotropicsample_conditions_1
3D HNCO13C-15Nisotropicsample_conditions_1
3D HCACO13C-15Nisotropicsample_conditions_1

Software:

GIFA v4.44, Delsuc - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

TALOS+ v1.2009.0721.18, Cornilescu, Delaglio and Bax - angle prediction

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAH24322 BAL63843 BAN29123 BAQ03850
EMBL CAL70034 CCC25094 CCC42360 CCC62613 CCE35563
GB AAK44245 AAS02340 ABK67403 ABQ71740 ABR04363
REF NP_214534 NP_853690 WP_003400376 WP_003872107 WP_003876793
SP P71590

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