BMRB Entry 17936
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17936
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Title: N/A PubMed: 22210494
Deposition date: 2011-09-13 Original release date: 2012-01-09
Authors: Barraud, Pierre; Allain, Frederic
Citation: Barraud, Pierre; Heale, Bret; Allain, Mary. "Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA." Biochimie 94, 1499-1509 (2012).
Assembly members:
dADAR-dsRBD1, polymer, 93 residues, 10262.124 Da.
Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
dADAR-dsRBD1: SDPKKKMCKERIPQPKNTVA
MLNELRHGLIYKLESQTGPV
HAPLFTISVEVDGQKYLGQG
RSKKVARIEAAATALRSFIQ
FKDGAVLSPLKPA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 263 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 559 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | dADAR-dsRBD1 | 1 |
Entities:
Entity 1, dADAR-dsRBD1 93 residues - 10262.124 Da.
| 1 | SER | ASP | PRO | LYS | LYS | LYS | MET | CYS | LYS | GLU | ||||
| 2 | ARG | ILE | PRO | GLN | PRO | LYS | ASN | THR | VAL | ALA | ||||
| 3 | MET | LEU | ASN | GLU | LEU | ARG | HIS | GLY | LEU | ILE | ||||
| 4 | TYR | LYS | LEU | GLU | SER | GLN | THR | GLY | PRO | VAL | ||||
| 5 | HIS | ALA | PRO | LEU | PHE | THR | ILE | SER | VAL | GLU | ||||
| 6 | VAL | ASP | GLY | GLN | LYS | TYR | LEU | GLY | GLN | GLY | ||||
| 7 | ARG | SER | LYS | LYS | VAL | ALA | ARG | ILE | GLU | ALA | ||||
| 8 | ALA | ALA | THR | ALA | LEU | ARG | SER | PHE | ILE | GLN | ||||
| 9 | PHE | LYS | ASP | GLY | ALA | VAL | LEU | SER | PRO | LEU | ||||
| 10 | LYS | PRO | ALA |
Samples:
sample_15N: dADAR-dsRBD1, [U-15N], 0.8 – 1.2 mM; H2O 90%; D2O 10%
sample_13C15N: dADAR-dsRBD1, [U-13C; U-15N], 0.8 – 1.2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_15N | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_13C15N | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HNCA | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_13C15N | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_13C15N | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| EMBL | CAA22774 |
| GB | AAF45665 AAF63702 AAF63703 AAK26850 AAN09057 |
| REF | NP_001033821 NP_001245469 NP_001245470 NP_001245471 NP_001245472 |
| SP | Q9NII1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts