BMRB Entry 51522
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51522
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Title: Region of Trak2 that interacts with Miro2 N-terminal GTPase
Deposition date: 2022-07-20 Original release date: 2022-08-22
Authors: Smith, Cassandra; Jones, David
Citation: Smith, Cassandra; Jones, David. "Understanding the molecular basis for the interaction of the mitochondrial associated protein Miro2 N-terminal GTPase with the trafficking protein TRAK2" .
Assembly members:
entity_1, polymer, 84 residues, 9343 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P1
Entity Sequences (FASTA):
entity_1: GPLGSGFMPEKLQIVKPLEG
SQTLYHWQQLAQPNLGTILD
PRPGVITKGFTQLPGDAIYH
ISDLEEDEEEGITFQVQQPL
EVEE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 328 |
| 15N chemical shifts | 74 |
| 1H chemical shifts | 495 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Trak2 | 1 |
Entities:
Entity 1, Trak2 84 residues - 9343 Da.
The first four residues are non-native sequence from the affinity tag used for purification.
| 1 | GLY | PRO | LEU | GLY | SER | GLY | PHE | MET | PRO | GLU | ||||
| 2 | LYS | LEU | GLN | ILE | VAL | LYS | PRO | LEU | GLU | GLY | ||||
| 3 | SER | GLN | THR | LEU | TYR | HIS | TRP | GLN | GLN | LEU | ||||
| 4 | ALA | GLN | PRO | ASN | LEU | GLY | THR | ILE | LEU | ASP | ||||
| 5 | PRO | ARG | PRO | GLY | VAL | ILE | THR | LYS | GLY | PHE | ||||
| 6 | THR | GLN | LEU | PRO | GLY | ASP | ALA | ILE | TYR | HIS | ||||
| 7 | ILE | SER | ASP | LEU | GLU | GLU | ASP | GLU | GLU | GLU | ||||
| 8 | GLY | ILE | THR | PHE | GLN | VAL | GLN | GLN | PRO | LEU | ||||
| 9 | GLU | VAL | GLU | GLU |
Samples:
sample_1: Trak2, [U-98% 13C; U-98% 15N], 700 uM; HEPES 25 mM; sodium chloride 150 mM; magnesium chloride 1 mM; sucrose 5%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS v2.5.2 - chemical shift assignment
VNMRj v4.2 - collection
NMRPipe v10.9 - processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian DD2 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts