BMRB Entry 34498
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34498
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Title: solution structure of cold-shock domain 9 of drosophila Upstream of N-Ras (Unr) PubMed: 32697992
Deposition date: 2020-03-06 Original release date: 2020-07-14
Authors: Sweetapple, L.; Hollmann, N.; Simon, B.; Hennig, J.
Citation: Hollmann, N.; Jagtap, P.; Masiewicz, P.; Guitart, T.; Simon, B.; Provaznik, J.; Stein, F.; Haberkant, P.; Sweetapple, L.; Villacorte, L.; Mooijman, D.; Benes, V.; Savitski, M.; Gebauer, F.; Hennig, J.. "Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras" Cell Rep. 32, 107930-107930 (2020).
Assembly members:
entity_1, polymer, 94 residues, 10246.532 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: GAKGDLVSFRIDESGRAACV
NAVRQKKRATVDSIKGQFGF
LNFEVEDGKKLFFHMSEVQG
NTVALHPGDTVEFSVVTNQR
NGKSSACNVLKIND
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 360 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 562 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 94 residues - 10246.532 Da.
| 1 | GLY | ALA | LYS | GLY | ASP | LEU | VAL | SER | PHE | ARG | ||||
| 2 | ILE | ASP | GLU | SER | GLY | ARG | ALA | ALA | CYS | VAL | ||||
| 3 | ASN | ALA | VAL | ARG | GLN | LYS | LYS | ARG | ALA | THR | ||||
| 4 | VAL | ASP | SER | ILE | LYS | GLY | GLN | PHE | GLY | PHE | ||||
| 5 | LEU | ASN | PHE | GLU | VAL | GLU | ASP | GLY | LYS | LYS | ||||
| 6 | LEU | PHE | PHE | HIS | MET | SER | GLU | VAL | GLN | GLY | ||||
| 7 | ASN | THR | VAL | ALA | LEU | HIS | PRO | GLY | ASP | THR | ||||
| 8 | VAL | GLU | PHE | SER | VAL | VAL | THR | ASN | GLN | ARG | ||||
| 9 | ASN | GLY | LYS | SER | SER | ALA | CYS | ASN | VAL | LEU | ||||
| 10 | LYS | ILE | ASN | ASP |
Samples:
sample_1: protein, [U-99% 13C; U-99% 15N], 0.24 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM
sample_2: protein, [U-99% 13C; U-99% 15N], 0.24 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
TopSpin, Bruker Biospin - collection
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts