BMRB Entry 16206

Title:
THE RRM DOMAIN IN GW182 PROTEINS CONTRIBUTES TO MIRNA-MEDIATED GENE SILENCING
Deposition date:
2009-03-09
Original release date:
2009-03-30
Authors:
Eulalio, A.; Tritschler, F.; Buettner, R.; Weichenrieder, O.; Izaurralde, E.; Truffault, V.
Citation:

Citation: Eulalio, Ana; Tritschler, Felix; Buettner, Regina; Weichenrieder, Oliver; Izaurralde, Elisa; Truffault, Vincent. "The RRM Domain in GW182 Proteins Contributes to miRNA-mediated gene silencing"  Nucleic Acids Res. 37, 2974-2983 (2009).
PubMed: 19295135

Assembly members:

Assembly members:
RRM_DOMAIN_OF_GW182, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PETM60

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts336
15N chemical shifts94
1H chemical shifts600

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM DOMAIN OF GW1821

Entities:

Entity 1, RRM DOMAIN OF GW182 89 residues - Formula weight is not available

1   GLYALAMETALATRPGLYSERSERTRPLEU
2   LEULEULYSASNLEUTHRALAGLNILEASP
3   GLYPROTHRLEUARGTHRLEUCYSMETGLN
4   HISGLYPROLEUVALSERPHEHISPROTYR
5   LEUASNGLNGLYILEALALEUCYSLYSTYR
6   THRTHRARGGLUGLUALAASNLYSALAGLN
7   METALALEUASNASNCYSVALLEUALAASN
8   THRTHRILEPHEALAGLUSERPROSERGLU
9   ASNGLUVALGLNSERILEMETGLNHIS

Samples:

sample_1: RRM DOMAIN OF GW182, [U-100% 13C; U-100% 15N], 1 mM

sample_2: RRM DOMAIN OF GW182, [U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1.0 ATM; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
CBCACONHsample_1isotropicsample_conditions_1
CCCONHsample_1isotropicsample_conditions_1
CCHCOSYsample_1isotropicsample_conditions_1
CCHNOESYsample_1isotropicsample_conditions_1
CCHTOCSYsample_1isotropicsample_conditions_1
CHSQCsample_1isotropicsample_conditions_1
CNHNOESYsample_1isotropicsample_conditions_1
HBHACONHsample_1isotropicsample_conditions_1
HCHNOESYsample_1isotropicsample_conditions_1
HNCAsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
HNCOsample_1isotropicsample_conditions_1
HNHAsample_1isotropicsample_conditions_1
HNHBsample_1isotropicsample_conditions_1
HNHNOESYsample_1isotropicsample_conditions_1
NHSQCsample_1isotropicsample_conditions_1
NNHNOESYsample_1isotropicsample_conditions_1
NOESYNONsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.4A, BRUNGER - refinement

SPARKY, Goddard - structure solution

NMR spectrometers:

  • BRUKER AVANCE III 800 MHz

Related Database Links:

PDB

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