BMRB Entry 17692
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17692
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Citation: Chakraborty, Swagata; Mohan, P. M Krishna; Hosur, Ramakrishna. "Residual structure and dynamics in DMSO-d6 denatured Dynein Light Chain protein." Biochimie 94, 231-241 (2012).
PubMed: 22079190
Assembly members:
DLC8, polymer, 89 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 Vector: PET14B
Entity Sequences (FASTA):
DLC8: MSDRKAVIKNADMSEEMQQD
AVDCATQALEKYNIEKDIAA
YIKKEFDKKYNPTWHCIVGR
NFGSYVTHETRHFIYFYLGQ
VAILLFKSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 260 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 180 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DLC8 | 1 |
Entities:
Entity 1, DLC8 89 residues - Formula weight is not available
| 1 | MET | SER | ASP | ARG | LYS | ALA | VAL | ILE | LYS | ASN | ||||
| 2 | ALA | ASP | MET | SER | GLU | GLU | MET | GLN | GLN | ASP | ||||
| 3 | ALA | VAL | ASP | CYS | ALA | THR | GLN | ALA | LEU | GLU | ||||
| 4 | LYS | TYR | ASN | ILE | GLU | LYS | ASP | ILE | ALA | ALA | ||||
| 5 | TYR | ILE | LYS | LYS | GLU | PHE | ASP | LYS | LYS | TYR | ||||
| 6 | ASN | PRO | THR | TRP | HIS | CYS | ILE | VAL | GLY | ARG | ||||
| 7 | ASN | PHE | GLY | SER | TYR | VAL | THR | HIS | GLU | THR | ||||
| 8 | ARG | HIS | PHE | ILE | TYR | PHE | TYR | LEU | GLY | GLN | ||||
| 9 | VAL | ALA | ILE | LEU | LEU | PHE | LYS | SER | GLY |
Samples:
sample_1: DLC8, [U-100% 13C; U-100% 15N], 1.2 – 1.5 mM; TRIS 20 mM; sodium chloride 200 mM; DTT 2 mM; DMSO 99.96%
sample_conditions_1: ionic strength: 0.2 M; pH: 2.5; pressure: 1 atm; temperature: 318 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Rochus Keller - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks