BMRB Entry 18041
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18041
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Title: Solution structure of the EDC3-LSm domain 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-LSm, polymer, 125 residues,   14016.833 Da.
Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
EDC3-LSm: GAMGMSVADFYGSNVEVLLN
NDSKARGVITNFDSSNSILQ
LRLANDSTKSIVTKDIKDLR
ILPKNEIMPKNGTKSPSTNS
TKLKSAETYSSKNKWSMDCD
EEFDFAANLEKFDKKQVFAE
FREKD
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 386 | 
| 15N chemical shifts | 93 | 
| 1H chemical shifts | 596 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | EDC3-LSm domain | 1 | 
Entities:
Entity 1, EDC3-LSm domain 125 residues - 14016.833 Da.
| 1 | GLY | ALA | MET | GLY | MET | SER | VAL | ALA | ASP | PHE | ||||
| 2 | TYR | GLY | SER | ASN | VAL | GLU | VAL | LEU | LEU | ASN | ||||
| 3 | ASN | ASP | SER | LYS | ALA | ARG | GLY | VAL | ILE | THR | ||||
| 4 | ASN | PHE | ASP | SER | SER | ASN | SER | ILE | LEU | GLN | ||||
| 5 | LEU | ARG | LEU | ALA | ASN | ASP | SER | THR | LYS | SER | ||||
| 6 | ILE | VAL | THR | LYS | ASP | ILE | LYS | ASP | LEU | ARG | ||||
| 7 | ILE | LEU | PRO | LYS | ASN | GLU | ILE | MET | PRO | LYS | ||||
| 8 | ASN | GLY | THR | LYS | SER | PRO | SER | THR | ASN | SER | ||||
| 9 | THR | LYS | LEU | LYS | SER | ALA | GLU | THR | TYR | SER | ||||
| 10 | SER | LYS | ASN | LYS | TRP | SER | MET | ASP | CYS | ASP | ||||
| 11 | GLU | GLU | PHE | ASP | PHE | ALA | ALA | ASN | LEU | GLU | ||||
| 12 | LYS | PHE | ASP | LYS | LYS | GLN | VAL | PHE | ALA | GLU | ||||
| 13 | PHE | ARG | GLU | LYS | ASP | 
Samples:
sample_1: EDC3-LSm, [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:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 | 
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts