BMRB Entry 34555
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34555
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Title: Structural evolution of the tissue-specific U2AF2 paralog and alternative splicing factor LS2
Deposition date: 2020-09-04 Original release date: 2021-10-01
Authors: Kawale, A.; Kang, H.; Sattler, M.
Citation: Kawale, A.; Kang, H.; Sattler, M.. "Structural evolution of the tissue-specific U2AF2 paralog and alternative splicing factor LS2" .
Assembly members:
entity_1, polymer, 81 residues, 8907.245 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: AMGNKIYVGGLPTCLNQDQV
KELLQSFGELKGLNLVMDTN
TNLNKGFAFFEYCDPSVTDH
AIAGLHGMLLGDRRLVVQRS
I
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 269 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 552 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 81 residues - 8907.245 Da.
| 1 | ALA | MET | GLY | ASN | LYS | ILE | TYR | VAL | GLY | GLY | ||||
| 2 | LEU | PRO | THR | CYS | LEU | ASN | GLN | ASP | GLN | VAL | ||||
| 3 | LYS | GLU | LEU | LEU | GLN | SER | PHE | GLY | GLU | LEU | ||||
| 4 | LYS | GLY | LEU | ASN | LEU | VAL | MET | ASP | THR | ASN | ||||
| 5 | THR | ASN | LEU | ASN | LYS | GLY | PHE | ALA | PHE | PHE | ||||
| 6 | GLU | TYR | CYS | ASP | PRO | SER | VAL | THR | ASP | HIS | ||||
| 7 | ALA | ILE | ALA | GLY | LEU | HIS | GLY | MET | LEU | LEU | ||||
| 8 | GLY | ASP | ARG | ARG | LEU | VAL | VAL | GLN | ARG | SER | ||||
| 9 | ILE |
Samples:
sample_1: LS2 RRM2, [U-13C; U-15N], 0.5 mM; potassium phosphate pH 6.5 0.02 mM; sodium chloride 0.05 mM; DTT 0.002 mM
sample_conditions_1: ionic strength: 0.07 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
Sparky, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE 750 750 MHz
- Bruker AVANCE 800 800 MHz
- Bruker AVANCE 900 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts