BMRB Entry 27619
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27619
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone assignments of the bacterial tRNA-(N1G37) methyltransferase (TrmD) PubMed: 31175551
Deposition date: 2018-09-19 Original release date: 2019-07-10
Authors: Li, Yan; Ng, Hui Qi; Kang, CongBao
Citation: Li, Yan; Zhong, Wenhe; Koay, Ann Zhufang; Ng, Hui Qi; Nah, Qianhui; Wong, Yee Hwa; Hill, Jeffrey; Lescar, Julien; Dedon, Peter; Kang, CongBao. "Backbone resonance assignment for the full length tRNA-(N" Biomol. NMR Assign. 13, 327-332 (2019).
Assembly members:
bacterial_tRNA-(N1G37)_methyltransferase_(TrmD), polymer, 258 residues, Formula weight is not available
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: pET29b
Entity Sequences (FASTA):
bacterial_tRNA-(N1G37)_methyltransferase_(TrmD): MDKRLWVGVVSIFPEMFRAI
SDYGITSRAVKQGLLTLTCW
NPRVYTEDRHQTVDDRPFGG
GPGMVMKIKPLEGALADARQ
AAGGRKAKVIYLSPQGRQLT
QAGVRELAEEEALILIAGRY
EGIDERFIEEHVDEEWSIGD
YVLSGGELPAMVLVDAVTRL
LPGALGHADSAEEDSFTDGL
LDCPHYTRPEVYADKRVPEV
LLSGNHEHIRRWRLQQALGR
TWERRADLLDSRSLSGEEQK
LLAEYIRQRDDSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 584 |
| 15N chemical shifts | 223 |
| 1H chemical shifts | 223 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | bacterial tRNA-(N1G37) methyltransferase (TrmD) | 1 |
Entities:
Entity 1, bacterial tRNA-(N1G37) methyltransferase (TrmD) 258 residues - Formula weight is not available
| 1 | MET | ASP | LYS | ARG | LEU | TRP | VAL | GLY | VAL | VAL | ||||
| 2 | SER | ILE | PHE | PRO | GLU | MET | PHE | ARG | ALA | ILE | ||||
| 3 | SER | ASP | TYR | GLY | ILE | THR | SER | ARG | ALA | VAL | ||||
| 4 | LYS | GLN | GLY | LEU | LEU | THR | LEU | THR | CYS | TRP | ||||
| 5 | ASN | PRO | ARG | VAL | TYR | THR | GLU | ASP | ARG | HIS | ||||
| 6 | GLN | THR | VAL | ASP | ASP | ARG | PRO | PHE | GLY | GLY | ||||
| 7 | GLY | PRO | GLY | MET | VAL | MET | LYS | ILE | LYS | PRO | ||||
| 8 | LEU | GLU | GLY | ALA | LEU | ALA | ASP | ALA | ARG | GLN | ||||
| 9 | ALA | ALA | GLY | GLY | ARG | LYS | ALA | LYS | VAL | ILE | ||||
| 10 | TYR | LEU | SER | PRO | GLN | GLY | ARG | GLN | LEU | THR | ||||
| 11 | GLN | ALA | GLY | VAL | ARG | GLU | LEU | ALA | GLU | GLU | ||||
| 12 | GLU | ALA | LEU | ILE | LEU | ILE | ALA | GLY | ARG | TYR | ||||
| 13 | GLU | GLY | ILE | ASP | GLU | ARG | PHE | ILE | GLU | GLU | ||||
| 14 | HIS | VAL | ASP | GLU | GLU | TRP | SER | ILE | GLY | ASP | ||||
| 15 | TYR | VAL | LEU | SER | GLY | GLY | GLU | LEU | PRO | ALA | ||||
| 16 | MET | VAL | LEU | VAL | ASP | ALA | VAL | THR | ARG | LEU | ||||
| 17 | LEU | PRO | GLY | ALA | LEU | GLY | HIS | ALA | ASP | SER | ||||
| 18 | ALA | GLU | GLU | ASP | SER | PHE | THR | ASP | GLY | LEU | ||||
| 19 | LEU | ASP | CYS | PRO | HIS | TYR | THR | ARG | PRO | GLU | ||||
| 20 | VAL | TYR | ALA | ASP | LYS | ARG | VAL | PRO | GLU | VAL | ||||
| 21 | LEU | LEU | SER | GLY | ASN | HIS | GLU | HIS | ILE | ARG | ||||
| 22 | ARG | TRP | ARG | LEU | GLN | GLN | ALA | LEU | GLY | ARG | ||||
| 23 | THR | TRP | GLU | ARG | ARG | ALA | ASP | LEU | LEU | ASP | ||||
| 24 | SER | ARG | SER | LEU | SER | GLY | GLU | GLU | GLN | LYS | ||||
| 25 | LEU | LEU | ALA | GLU | TYR | ILE | ARG | GLN | ARG | ASP | ||||
| 26 | ASP | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: bacterial RNA-(N1G37) methyltransferase (TrmD), [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 20 mM; potassium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 170 mM; pH: 7.2; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts