BMRB Entry 16781
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16781
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Title: Backbone chemical shift assignments for the microtubule binding domain of the Dictyostelium discoideum dynein heavy chain PubMed: 20351100
Deposition date: 2010-03-21 Original release date: 2010-05-03
Authors: McNaughton, Lynn; Tikhonenko, Irina; Banavali, Nilesh; LeMaster, David; Koonce, Michael
Citation: McNaughton, Lynn; Tikhonenko, Irina; Banavali, Nilesh; LeMaster, David; Koonce, Michael. "A low affinity ground state conformation for the Dynein microtubule binding domain." J. Biol. Chem. 285, 15994-16002 (2010).
Assembly members:
dynein_microtubule_binding_domain, polymer, 134 residues, 15120 Da.
Natural source: Common Name: Dictyostelium discoideum Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
dynein_microtubule_binding_domain: GSHMLEDPPAIIEAQEAVST
IKKKHLDEIKSLPKPPTPVK
LAMEAVCLMLGGKKLEWADI
RKKIMEPNFITSIINYDTKK
MMTPKIREAITKGYLEDPGF
DYETVNRASKACGPLVKWAT
AQTYYSEILDRIKP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 364 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 116 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | dynein headpiece | 1 |
Entities:
Entity 1, dynein headpiece 134 residues - 15120 Da.
The initial 8 residues preceding the PAII... sequence are the residual sequence from a thrombin cleavage sequence
| 1 | GLY | SER | HIS | MET | LEU | GLU | ASP | PRO | PRO | ALA | ||||
| 2 | ILE | ILE | GLU | ALA | GLN | GLU | ALA | VAL | SER | THR | ||||
| 3 | ILE | LYS | LYS | LYS | HIS | LEU | ASP | GLU | ILE | LYS | ||||
| 4 | SER | LEU | PRO | LYS | PRO | PRO | THR | PRO | VAL | LYS | ||||
| 5 | LEU | ALA | MET | GLU | ALA | VAL | CYS | LEU | MET | LEU | ||||
| 6 | GLY | GLY | LYS | LYS | LEU | GLU | TRP | ALA | ASP | ILE | ||||
| 7 | ARG | LYS | LYS | ILE | MET | GLU | PRO | ASN | PHE | ILE | ||||
| 8 | THR | SER | ILE | ILE | ASN | TYR | ASP | THR | LYS | LYS | ||||
| 9 | MET | MET | THR | PRO | LYS | ILE | ARG | GLU | ALA | ILE | ||||
| 10 | THR | LYS | GLY | TYR | LEU | GLU | ASP | PRO | GLY | PHE | ||||
| 11 | ASP | TYR | GLU | THR | VAL | ASN | ARG | ALA | SER | LYS | ||||
| 12 | ALA | CYS | GLY | PRO | LEU | VAL | LYS | TRP | ALA | THR | ||||
| 13 | ALA | GLN | THR | TYR | TYR | SER | GLU | ILE | LEU | ASP | ||||
| 14 | ARG | ILE | LYS | PRO |
Samples:
sample_1: dynein microtubule binding domain, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 93%; D2O 7%; NaCl 150 mM; PIPES-d18 20 mM; EDTA 0.1 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.50; pressure: 1 atm; temperature: 293 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
FELIX v2000, Accelrys Software Inc. - data analysis
NMR spectrometers:
- 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