BMRB Entry 16534
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16534
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Title: DICER LIKE protein PubMed: 20106953
Deposition date: 2009-09-30 Original release date: 2010-02-08
Authors: Qin, Haina; Song, Jianxing; Yuan, Adam, Yu-Ren
Citation: Qin, Haina; Chen, Fading; Huan, Xuelu; Machida, Satoru; Song, Jianxing; Yuan, Y. Adam. "Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a noncanonical double-stranded RNA-binding fold for protein-protein interaction." RNA 16, 474-481 (2010).
Assembly members:
DCL4_DUF283, polymer, 102 residues, Formula weight is not available
Natural source: Common Name: thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DCL4_DUF283: ISGGSSISMMYKYCSRLPHD
EFFQPKPEFQFKPVDEFGGT
ICRITLPANAPISEIESSLL
PSTEAAKKDACLKAVHELHN
LGVLNDFLLPDSKDEIEDEL
SD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 246 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 514 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DCL4_DUF283 | 1 |
Entities:
Entity 1, DCL4_DUF283 102 residues - Formula weight is not available
| 1 | ILE | SER | GLY | GLY | SER | SER | ILE | SER | MET | MET | ||||
| 2 | TYR | LYS | TYR | CYS | SER | ARG | LEU | PRO | HIS | ASP | ||||
| 3 | GLU | PHE | PHE | GLN | PRO | LYS | PRO | GLU | PHE | GLN | ||||
| 4 | PHE | LYS | PRO | VAL | ASP | GLU | PHE | GLY | GLY | THR | ||||
| 5 | ILE | CYS | ARG | ILE | THR | LEU | PRO | ALA | ASN | ALA | ||||
| 6 | PRO | ILE | SER | GLU | ILE | GLU | SER | SER | LEU | LEU | ||||
| 7 | PRO | SER | THR | GLU | ALA | ALA | LYS | LYS | ASP | ALA | ||||
| 8 | CYS | LEU | LYS | ALA | VAL | HIS | GLU | LEU | HIS | ASN | ||||
| 9 | LEU | GLY | VAL | LEU | ASN | ASP | PHE | LEU | LEU | PRO | ||||
| 10 | ASP | SER | LYS | ASP | GLU | ILE | GLU | ASP | GLU | LEU | ||||
| 11 | SER | ASP |
Samples:
sample_1: protein, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.02 M; pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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