BMRB Entry 34326
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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/BMR34326
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1/2 of Drosophila helicase MLE PubMed: 30805612
Deposition date: 2018-11-07 Original release date: 2019-03-14
Authors: Jagtap, P.; Buelow, S.; Masiewicz, P.; Simon, B.; Hennig, J.
Citation: Ankush Jagtap, P.; Muller, M.; Masiewicz, P.; von Bulow, S.; Hollmann, N.; Chen, P.; Simon, B.; Thomae, A.; Becker, P.; Hennig, J.. "Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless." Nucleic Acids Res. 47, 4319-4333 (2019).
Assembly members:
entity_1, polymer, 259 residues, 28589.938 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):
entity_1: GAMDIKSFLYQFCAKSQIEP
KFDIRQTGPKNRQRFLCEVR
VEPNTYIGVGNSTNKKDAEK
NACRDFVNYLVRVGKLNTND
VPADAGASGGGPRTGLEGAG
MAGGSGQQKRVFDGQSGPQD
LGEAYRPLNHDGGDGGNRYS
VIDRIQEQRDMNEAEAFDVN
AAIHGNWTIENAKERLNIYK
QTNNIRDDYKYTPVGPEHAR
SFLAELSIYVPALNRTVTAR
ESGSNKKSASKSCALSLVRQ
LFHLNVIEPFSGTLKKKKD
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 1015 |
| 15N chemical shifts | 280 |
| 1H chemical shifts | 1573 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 259 residues - 28589.938 Da.
| 1 | GLY | ALA | MET | ASP | ILE | LYS | SER | PHE | LEU | TYR | ||||
| 2 | GLN | PHE | CYS | ALA | LYS | SER | GLN | ILE | GLU | PRO | ||||
| 3 | LYS | PHE | ASP | ILE | ARG | GLN | THR | GLY | PRO | LYS | ||||
| 4 | ASN | ARG | GLN | ARG | PHE | LEU | CYS | GLU | VAL | ARG | ||||
| 5 | VAL | GLU | PRO | ASN | THR | TYR | ILE | GLY | VAL | GLY | ||||
| 6 | ASN | SER | THR | ASN | LYS | LYS | ASP | ALA | GLU | LYS | ||||
| 7 | ASN | ALA | CYS | ARG | ASP | PHE | VAL | ASN | TYR | LEU | ||||
| 8 | VAL | ARG | VAL | GLY | LYS | LEU | ASN | THR | ASN | ASP | ||||
| 9 | VAL | PRO | ALA | ASP | ALA | GLY | ALA | SER | GLY | GLY | ||||
| 10 | GLY | PRO | ARG | THR | GLY | LEU | GLU | GLY | ALA | GLY | ||||
| 11 | MET | ALA | GLY | GLY | SER | GLY | GLN | GLN | LYS | ARG | ||||
| 12 | VAL | PHE | ASP | GLY | GLN | SER | GLY | PRO | GLN | ASP | ||||
| 13 | LEU | GLY | GLU | ALA | TYR | ARG | PRO | LEU | ASN | HIS | ||||
| 14 | ASP | GLY | GLY | ASP | GLY | GLY | ASN | ARG | TYR | SER | ||||
| 15 | VAL | ILE | ASP | ARG | ILE | GLN | GLU | GLN | ARG | ASP | ||||
| 16 | MET | ASN | GLU | ALA | GLU | ALA | PHE | ASP | VAL | ASN | ||||
| 17 | ALA | ALA | ILE | HIS | GLY | ASN | TRP | THR | ILE | GLU | ||||
| 18 | ASN | ALA | LYS | GLU | ARG | LEU | ASN | ILE | TYR | LYS | ||||
| 19 | GLN | THR | ASN | ASN | ILE | ARG | ASP | ASP | TYR | LYS | ||||
| 20 | TYR | THR | PRO | VAL | GLY | PRO | GLU | HIS | ALA | ARG | ||||
| 21 | SER | PHE | LEU | ALA | GLU | LEU | SER | ILE | TYR | VAL | ||||
| 22 | PRO | ALA | LEU | ASN | ARG | THR | VAL | THR | ALA | ARG | ||||
| 23 | GLU | SER | GLY | SER | ASN | LYS | LYS | SER | ALA | SER | ||||
| 24 | LYS | SER | CYS | ALA | LEU | SER | LEU | VAL | ARG | GLN | ||||
| 25 | LEU | PHE | HIS | LEU | ASN | VAL | ILE | GLU | PRO | PHE | ||||
| 26 | SER | GLY | THR | LEU | LYS | LYS | LYS | LYS | ASP |
Samples:
sample_1: MLE dsRBD1,2, [U-13C; U-15N], 0.5 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6; pressure: 1 bar; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
Analysis, CCPN - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
ARIA, Linge, O'Donoghue and Nilges - refinement
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts