BMRB Entry 25059
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25059
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Title: Backbone assignment for cold shock domain 1 of Drosophila Upstream of N-ras PubMed: 25209665
Deposition date: 2014-07-01 Original release date: 2014-11-07
Authors: Wang, Iren; Hennig, Janosch; Sattler, Michael
Citation: Hennig, Janosch; Militti, Cristina; Popowicz, Grzegorz; Wang, Iren; Sonntag, Miriam; Geerlof, Arie; Gabel, Frank; Gebauer, Fatima; Sattler, Michael. "Structural basis for the assembly of the Sxl-Unr translation regulatory complex" Nature 515, 287-290 (2014).
Assembly members:
dCSD1, polymer, 72 residues, Formula weight is not available
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):
dCSD1: GAMATRETGIIEKLLHSYGF
IQCCERQARLFFHFSQFSGN
IDHLKIGDPVEFEMTYDRRT
GKPIASQVSKIA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 425 |
| 13C chemical shifts | 270 |
| 15N chemical shifts | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | cold shock domain 1 of drosophila UNR | 1 |
Entities:
Entity 1, cold shock domain 1 of drosophila UNR 72 residues - Formula weight is not available
Residues 1-4 represent a residual non-native tag
| 1 | GLY | ALA | MET | ALA | THR | ARG | GLU | THR | GLY | ILE | ||||
| 2 | ILE | GLU | LYS | LEU | LEU | HIS | SER | TYR | GLY | PHE | ||||
| 3 | ILE | GLN | CYS | CYS | GLU | ARG | GLN | ALA | ARG | LEU | ||||
| 4 | PHE | PHE | HIS | PHE | SER | GLN | PHE | SER | GLY | ASN | ||||
| 5 | ILE | ASP | HIS | LEU | LYS | ILE | GLY | ASP | PRO | VAL | ||||
| 6 | GLU | PHE | GLU | MET | THR | TYR | ASP | ARG | ARG | THR | ||||
| 7 | GLY | LYS | PRO | ILE | ALA | SER | GLN | VAL | SER | LYS | ||||
| 8 | ILE | ALA |
Samples:
sample_1: CSD1, [U-99% 13C; U-99% 15N], 0.1 – 0.8 mM; potassium phosphate 10 mM; sodium chloride 50 mM; DTT 10 mM; D2O, [U-99% 2H], 10%; H2O 90%
sample_conditions_1: temperature: 298 K; pH: 6; pressure: 1 atm; ionic strength: 0.05 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis, peak picking
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts