BMRB Entry 15076
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15076
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Citation: Benison, Gregory; Karplus, P.; Barbar, Elisar. "Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site" J. Mol. Biol. 371, 457-468 (2007).
PubMed: 17570393
Assembly members:
LC8, 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: PET-15da
Entity Sequences (FASTA):
LC8: MSDRKAVIKNADMSEEMQQD
AVDCATQALEKYNIEKDIAA
YIKKEFDKKYNPTWHCIVGR
NFGSYVTHETRHFIYFYLGQ
VAILLFKSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 87 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 87 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LC8, chain 1 | 1 |
| 2 | LC8, chain 2 | 1 |
Entities:
Entity 1, LC8, chain 1 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: LC8, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium citrate 50 mM; glycerol 3%; DSS 1 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.3 M; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker DRX 600 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