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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
MolProbity Validation Chart
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NMR-STAR v3 text file.
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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).
PubMed: 22210494
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 Vector: pET28a
Entity Sequences (FASTA):
dADAR-dsRBD1: SDPKKKMCKERIPQPKNTVA
MLNELRHGLIYKLESQTGPV
HAPLFTISVEVDGQKYLGQG
RSKKVARIEAAATALRSFIQ
FKDGAVLSPLKPA
Data type | Count |
13C chemical shifts | 263 |
15N chemical shifts | 75 |
1H chemical shifts | 559 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | dADAR-dsRBD1 | 1 |
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 |
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
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 |
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
PDB | |
EMBL | CAA22774 |
GB | AAF45665 AAF63702 AAF63703 AAK26850 AAN09057 |
REF | NP_001033821 NP_001245469 NP_001245470 NP_001245471 NP_001245472 |
SP | Q9NII1 |
AlphaFold | Q9NII1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks