BMRB Entry 17585

Title:
Rv0020c_Nter structure
Deposition date:
2011-04-11
Original release date:
2011-10-26
Authors:
Barthe, Philippe; Cohen-Gonsaud, Martin; Roumestand, Christian
Citation:

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).
PubMed: 22000520

Assembly members:

Assembly members:
Rv0020c_Nter, polymer, 132 residues, 14773.583 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: pET15b-tev

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts140
1H chemical shifts844

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv0020c_Nter1

Entities:

Entity 1, Rv0020c_Nter 132 residues - 14773.583 Da.

1   METGLYSERGLNLYSARGLEUVALGLNARG
2   VALGLUARGLYSLEUGLUGLNTHRVALGLY
3   ASPALAPHEALAARGILEPHEGLYGLYSER
4   ILEVALPROGLNGLUVALGLUALALEULEU
5   ARGARGGLUALAALAASPGLYILEGLNSER
6   LEUGLNGLYASNARGLEULEUALAPROASN
7   GLUTYRILEILETHRLEUGLYVALHISASP
8   PHEGLULYSLEUGLYALAASPPROGLULEU
9   LYSSERTHRGLYPHEALAARGASPLEUALA
10   ASPTYRILEGLNGLUGLNGLYTRPGLNTHR
11   TYRGLYASPVALVALVALARGPHEGLUGLN
12   SERSERASNLEUHISTHRGLYGLNPHEARG
13   ALAARGGLYTHRVALASNPROASPVALGLU
14   THRHIS

Samples:

15N: Rv0020c_Nter, [U-15N], 0.5 ± 0.01 mM

13C-15N: Rv0020c_Nter, [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 BAQ03850
EMBL CAL70034 CCC25094 CCC42360 CCC62613 CCE35563
GB AAK44245 ABQ71740 ABR04363 ACT23041 AEB02149
REF NP_214534 NP_853690 WP_003400376 WP_003899777 WP_003905210
SP P71590
AlphaFold P71590

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks