BMRB Entry 11057
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11057
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Citation: Kato, Y.; Yagi, T.; Ohki, S.; Harris, S.; Yura, K.; Shimizu, Y.; Honda, S.; Kamiya, R.; Burgess, S.; Tanokura, M.. "Structure of the Microtubule-Binding Domain of Flagellar Dynein" .
Assembly members:
the microtubule-binding domain of dynein heavy chain 9, polymer, 155 residues, 17391.582 Da.
Natural source: Common Name: Chlamydomonas reinhardtii Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Chlamydomonas reinhardtii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-TEV
Entity Sequences (FASTA):
the microtubule-binding domain of dynein heavy chain 9: GSQADLAEALPLLEAALKAL
DTLKPADITEVKGMKSPPAG
VRRVLEAICIMKGVKPARVK
DTASGRMVDDYWEASKKMLM
EFDFLDSLRKFDKDHIPPEV
IVKIRPFAQDPEFQPKVIEK
QSVACAGLCSWVIALEKYDK
VIKEVEPKRQKLREA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 500 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 1115 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | the microtubule-binding domain of dynein heavy chain 9 | 1 |
Entities:
Entity 1, the microtubule-binding domain of dynein heavy chain 9 155 residues - 17391.582 Da.
| 1 | GLY | SER | GLN | ALA | ASP | LEU | ALA | GLU | ALA | LEU | ||||
| 2 | PRO | LEU | LEU | GLU | ALA | ALA | LEU | LYS | ALA | LEU | ||||
| 3 | ASP | THR | LEU | LYS | PRO | ALA | ASP | ILE | THR | GLU | ||||
| 4 | VAL | LYS | GLY | MET | LYS | SER | PRO | PRO | ALA | GLY | ||||
| 5 | VAL | ARG | ARG | VAL | LEU | GLU | ALA | ILE | CYS | ILE | ||||
| 6 | MET | LYS | GLY | VAL | LYS | PRO | ALA | ARG | VAL | LYS | ||||
| 7 | ASP | THR | ALA | SER | GLY | ARG | MET | VAL | ASP | ASP | ||||
| 8 | TYR | TRP | GLU | ALA | SER | LYS | LYS | MET | LEU | MET | ||||
| 9 | GLU | PHE | ASP | PHE | LEU | ASP | SER | LEU | ARG | LYS | ||||
| 10 | PHE | ASP | LYS | ASP | HIS | ILE | PRO | PRO | GLU | VAL | ||||
| 11 | ILE | VAL | LYS | ILE | ARG | PRO | PHE | ALA | GLN | ASP | ||||
| 12 | PRO | GLU | PHE | GLN | PRO | LYS | VAL | ILE | GLU | LYS | ||||
| 13 | GLN | SER | VAL | ALA | CYS | ALA | GLY | LEU | CYS | SER | ||||
| 14 | TRP | VAL | ILE | ALA | LEU | GLU | LYS | TYR | ASP | LYS | ||||
| 15 | VAL | ILE | LYS | GLU | VAL | GLU | PRO | LYS | ARG | GLN | ||||
| 16 | LYS | LEU | ARG | GLU | ALA |
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