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 18042

Title: Structure of EDC3:DCP2   PubMed: 22085934

Deposition date: 2011-11-07 Original release date: 2012-01-23

Authors: Truffault, Vincent

Citation: Fromm, Simon; Truffault, Vincent; Kamenz, Julia; Braun, Joerg; Hoffmann, Niklas; Izaurralde, Elisa; Sprangers, Remco. "The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex."  EMBO J. 31, 279-290 (2011).

Assembly members:
EDC3, polymer, 96 residues, Formula weight is not available
DCP2, polymer, 48 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
EDC3: MGMSVADFYGSNVEVLLNND SKARGVITNFDSSNSILQLR LANDSTKSIVTKDIKDLRIL PKNEIMPKNGTKSPSTNSTK LKSAETYSSKNKWSMD
DCP2: GATTKEKNISVDVDADASSQ LLSLLKSSTAPSDLATPQPS TFPQPPVE

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts101
1H chemical shifts678

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EDC31
2DCP22

Entities:

Entity 1, EDC3 96 residues - Formula weight is not available

1   METGLYMETSERVALALAASPPHETYRGLY
2   SERASNVALGLUVALLEULEUASNASNASP
3   SERLYSALAARGGLYVALILETHRASNPHE
4   ASPSERSERASNSERILELEUGLNLEUARG
5   LEUALAASNASPSERTHRLYSSERILEVAL
6   THRLYSASPILELYSASPLEUARGILELEU
7   PROLYSASNGLUILEMETPROLYSASNGLY
8   THRLYSSERPROSERTHRASNSERTHRLYS
9   LEULYSSERALAGLUTHRTYRSERSERLYS
10   ASNLYSTRPSERMETASP

Entity 2, DCP2 48 residues - Formula weight is not available

1   GLYALATHRTHRLYSGLULYSASNILESER
2   VALASPVALASPALAASPALASERSERGLN
3   LEULEUSERLEULEULYSSERSERTHRALA
4   PROSERASPLEUALATHRPROGLNPROSER
5   THRPHEPROGLNPROPROVALGLU

Samples:

sample_1: EDC3, [U-100% 15N], 0.7 mM; DCP2, [U-100% 15N], 0.7 mM; NaPO4 50 mM; imidazole 10 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18041
PDB
EMBL CAA22671 CAB11648
REF NP_595858 NP_593780
SP O94752 O13828
AlphaFold O94752 O13828

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