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 15127

Title: Chemical shift and constraint files for the RegB ribonuclease   PubMed: 17046813

Deposition date: 2007-02-02 Original release date: 2007-07-16

Authors: Odaert, Benoit; Saida, Fakhri; Uzan, Marc; Bontems, Francois

Citation: Odaert, Benoit; Saida, Fakhri; Aliprandi, Pascale; Durand, Sylvain; Crechet, Jean-Bernard; Guerois, Raphael; Laalami, Soumaya; Uzan, Marc; Bontems, Francois. "Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome."  J. Biol. Chem. 282, 2019-2028 (2007).

Assembly members:
RegB, polymer, 153 residues, Formula weight is not available

Natural source:   Common Name: bacteriophage T4   Taxonomy ID: 38018   Superkingdom: Viruses   Kingdom: not available   Genus/species: not available Bacteriophage

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

Entity Sequences (FASTA):
RegB: MTINTEVFIRRNKLRRHFES EFRQINNEIREASKAAGVSS FHLKYSQALLDRAIQREIDE TYVFELFHKIKDHVLEVNEF LSMPPRPDIDEDFIDGVEYR PGRLEITDGNLWLGFTVCKP NEKFKDPSLQCRMAIINSRR LPGKASKAVIKTQ

Data typeCount
13C chemical shifts488
15N chemical shifts320
1H chemical shifts1959

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RegB1

Entities:

Entity 1, RegB 153 residues - Formula weight is not available

1   METTHRILEASNTHRGLUVALPHEILEARG
2   ARGASNLYSLEUARGARGHISPHEGLUSER
3   GLUPHEARGGLNILEASNASNGLUILEARG
4   GLUALASERLYSALAALAGLYVALSERSER
5   PHEHISLEULYSTYRSERGLNALALEULEU
6   ASPARGALAILEGLNARGGLUILEASPGLU
7   THRTYRVALPHEGLULEUPHEHISLYSILE
8   LYSASPHISVALLEUGLUVALASNGLUPHE
9   LEUSERMETPROPROARGPROASPILEASP
10   GLUASPPHEILEASPGLYVALGLUTYRARG
11   PROGLYARGLEUGLUILETHRASPGLYASN
12   LEUTRPLEUGLYPHETHRVALCYSLYSPRO
13   ASNGLULYSPHELYSASPPROSERLEUGLN
14   CYSARGMETALAILEILEASNSERARGARG
15   LEUPROGLYLYSALASERLYSALAVALILE
16   LYSTHRGLN

Samples:

RegB_15N_H2O: RegB, [U-15N], 600 – 800 uM; Citrate 50 mM; NaCl 300 mM; DTT 2.0 mM; H2O 95%; D2O 5%

RegB_15N_D2O: RegB, [U-15N], 600 – 800 uM; Citrate 50 mM; NaCl 300 mM; DTT 2.0 mM; D2O 100%

RegB_13C15N_H2O: RegB, [U-100% 13C; U-100% 15N], 600 – 800 uM; Citrate 50 mM; NaCl 300 mM; DTT 2.0 mM; H2O 95%; D2O 5%

RegB_13C15N_D2O: RegB, [U-100% 13C; U-100% 15N], 600 – 800 uM; Citrate 50 mM; NaCl 300 mM; DTT 2.0 mM; D2O 100%

Citrate_pH6.0: pH: 6.0; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCRegB_15N_H2OisotropicCitrate_pH6.0
2D 1H-13C HSQCRegB_13C15N_D2OisotropicCitrate_pH6.0
3D HNCORegB_13C15N_H2OisotropicCitrate_pH6.0
3D HNCARegB_13C15N_H2OisotropicCitrate_pH6.0
3D HNCACBRegB_13C15N_H2OisotropicCitrate_pH6.0
3D HN(CO)CARegB_13C15N_H2OisotropicCitrate_pH6.0
3D CBCA(CO)NHRegB_13C15N_H2OisotropicCitrate_pH6.0
3D HBHA(CO)NHRegB_13C15N_H2OisotropicCitrate_pH6.0
3D HCCH-TOCSYRegB_13C15N_D2OisotropicCitrate_pH6.0
3D 15N-NOESY-HSQCRegB_15N_H2OisotropicCitrate_pH6.0
3D 13C-NOESY-HSQCRegB_13C15N_H2OisotropicCitrate_pH6.0
3D 13C-NOESY-HSQCRegB_13C15N_D2OisotropicCitrate_pH6.0
2D NOESYRegB_15N_D2OisotropicCitrate_pH6.0
2D TOCSYRegB_15N_D2OisotropicCitrate_pH6.0
2D 1H-15N HSQCRegB_13C15N_H2OisotropicCitrate_pH6.0
3D 13Caro-NOESY-HSQCRegB_13C15N_D2OisotropicCitrate_pH6.0

Software:

xwinnmr v3.0, Bruker Biospin - Spectra processing

SPARKY v3.113, Thomas L. Goddard - Data analysis

INCA, Bernard Gilquin - Structure Calculation

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

GB AAD42652 AAD42652 ABI94940 ACP30763 ACP31038 ADJ39833
REF NP_049726 NP_049726 YP_002854075 YP_002854455 YP_004415013 YP_006986670
PDB
DBJ BAI83127
EMBL CAA28227 CAD32702 CAD32704 CAD32706 CAD32708
SP P13312

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