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 16188

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16188
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: NMR structure of Rv2175c   PubMed: 19457863

Deposition date: 2009-02-27 Original release date: 2009-05-29

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

Citation: Cohen-Gonsaud, Martin; Barthe, Philippe; Canova, Marc; Stagier-Simon, Charlotte; Kremer, Laurent; Roumestand, Christian; Molle, Virginie. "The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation"  J. Biol. Chem. 284, 19290-19300 (2009).

Assembly members:
Rv2175c, polymer, 146 residues, 15763.063 Da.

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
Rv2175c: MPGRAPGSTLARVGSIPAGD DVLDPDEPTYDLPRVAELLG VPVSKVAQQLREGHLVAVRR AGGVVIPQVFFTNSGQVVKS LPGLLTILHDGGYRDTEIMR WLFTPDPSLTITRDGSRDAV SNARPVDALHAHQAREVVRR AQAMAY

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts152
1H chemical shifts998

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv2175c1

Entities:

Entity 1, Rv2175c 146 residues - 15763.063 Da.

1   METPROGLYARGALAPROGLYSERTHRLEU
2   ALAARGVALGLYSERILEPROALAGLYASP
3   ASPVALLEUASPPROASPGLUPROTHRTYR
4   ASPLEUPROARGVALALAGLULEULEUGLY
5   VALPROVALSERLYSVALALAGLNGLNLEU
6   ARGGLUGLYHISLEUVALALAVALARGARG
7   ALAGLYGLYVALVALILEPROGLNVALPHE
8   PHETHRASNSERGLYGLNVALVALLYSSER
9   LEUPROGLYLEULEUTHRILELEUHISASP
10   GLYGLYTYRARGASPTHRGLUILEMETARG
11   TRPLEUPHETHRPROASPPROSERLEUTHR
12   ILETHRARGASPGLYSERARGASPALAVAL
13   SERASNALAARGPROVALASPALALEUHIS
14   ALAHISGLNALAARGGLUVALVALARGARG
15   ALAGLNALAMETALATYR

Samples:

sample_1: Rv2175c, [U-15N], 300 ± 15 mM; sodium acetate 10 ± 0.5 mM; sodium chloride 150 ± 7.5 mM; D2O 5%; H2O 95%

sample_2: Rv2175c, [U-13C; U-15N], 300 ± 15 mM; sodium acetate 10 ± 0.5 mM; sodium chloride 150 ± 7.5 mM; D2O 5%; H2O 95%

sample_3: Rv2175c 300 ± 15 mM; sodium acetate 10 ± 0.5 mM; sodium chloride 150 ± 7.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.15 M; pH: 4.6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1

Software:

GIFA v4.44, Delsuc - processing

CINDY v1.7a, Padilla - data analysis

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

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

Procheck v3.5.4, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAH26468 BAL66184 BAQ06242
EMBL CAL72178 CCC27256 CCC44529 CCC64767 CCE37647
GB AAK46516 ABQ73952 ABR06534 ACT24868 AEB03948
REF NP_216691 NP_855846 WP_003411249 WP_003900481 WP_003910516
SP O53509

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