BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6762

Title: The response regulator TorI belongs to a new family of atypical excisionase   PubMed: 16079126

Deposition date: 2005-08-04 Original release date: 2007-02-06

Authors: Elantak, Latifa; Ansaldi, Mireille; Guerlesquin, Fran?oise; Mejean, Vincent; Morelli, Xavier

Citation: Elantak, Latifa; Ansaldi, Mireille; Guerlesquin, Fran?oise; Mejean, Vincent; Morelli, Xavier. "Structural and Genetic analyses reveal a key role in prophage excision for the TorI response regulator inhibitor"  J. Biol. Chem. 280, 36802-36808 (2005).

Assembly members:
prophage excisionase, polymer, 66 residues, 7677 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
prophage excisionase: MQHELQPDSLVDLKFIMADT GFGKTFIYDRIKSGDLPKAK VIHGRARWLYRDHCEFKNKL LSRANG

Data sets:
Data typeCount
1H chemical shifts890
13C chemical shifts222
15N chemical shifts124

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Tor inhibition protein1

Entities:

Entity 1, Tor inhibition protein 66 residues - 7677 Da.

1   METGLNHISGLULEUGLNPROASPSERLEU
2   VALASPLEULYSPHEILEMETALAASPTHR
3   GLYPHEGLYLYSTHRPHEILETYRASPARG
4   ILELYSSERGLYASPLEUPROLYSALALYS
5   VALILEHISGLYARGALAARGTRPLEUTYR
6   ARGASPHISCYSGLUPHELYSASNLYSLEU
7   LEUSERARGALAASNGLY

Samples:

sample_1: prophage excisionase, [U-95% 13C; U-95% 15N], 1.5 mM; phosphate buffer 50 mM; H20 90%; D20 10%

sample_2: prophage excisionase 1.5 mM; phosphate buffer 50 mM; H20 90%; D20 10%

sample_3: prophage excisionase, [U-95% 15N], 1.5 mM; phosphate buffer 50 mM; H20 90%; D20 10%

sample_4: prophage excisionase, [U-95% 13C], 1.5 mM; phosphate buffer 50 mM; H20 90%; D20 10%

Condition_1: pH: 5.9; temperature: 278 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availableCondition_1
3D-HNCOnot availablenot availableCondition_1
3D-HNCAnot availablenot availableCondition_1
CBCA(CO)NHnot availablenot availableCondition_1
HN(CO)CAnot availablenot availableCondition_1
HCCH-TOCSYnot availablenot availableCondition_1
2D NOESYnot availablenot availableCondition_1
2D TOCSYnot availablenot availableCondition_1
3D 13C-separated NOESYnot availablenot availableCondition_1
HNHAnot availablenot availableCondition_1

Software:

XWINNMR v3.1 - Processing

FELIX v2002 - data analysis

CNS vARIA 1.2 - structure solution, refinement

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAE76704 BAI26599 BAJ44158 BAL39139
EMBL CAR03832 CAS10101 CAU98520 CCK47653 CCQ29767
GB AAK28851 AAQ12208 AAY17072 ABD18695 ABE08160
REF NP_112036 NP_958194 WP_001163427 WP_001163428 WP_001163429
SP Q1R904 Q2EES9 Q716F7 Q9AZ38
AlphaFold Q9AZ38 Q1R904 Q2EES9 Q716F7

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