Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27566
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Citation: Li, Yan; Zhong, Wenhe; Koay, Ann Zhufang; Ng, Hui Qi; Koh-Stenta, Xiaoying; Nah, Qianhui; Lim, Siau Hoi; Larsson, Andreas; Lescar, Julien; Hill, Jeffrey; Dedon, Peter; Kang, CongBao. "Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N'1G37) methyltransferase" Biomol. NMR Assign. 13, 49-53 (2019).
PubMed: 30298375
Assembly members:
N_domain_of_bacterial_tRNA-(N1G37)_methyltransferase_(TrmD), polymer, 172 residues, Formula weight is not available
Nilotinib, non-polymer, 529.516 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: pET29b
Entity Sequences (FASTA):
N_domain_of_bacterial_tRNA-(N1G37)_methyltransferase_(TrmD): MDKRLWVGVVSIFPEMFRAI
SDYGITSRAVKQGLLTLTCW
NPRVYTEDRHQTVDDRPFGG
GPGMVMKIKPLEGALADARQ
AAGGRKAKVIYLSPQGRQLT
QAGVRELAEEEALILIAGRY
EGIDERFIEEHVDEEWSIGD
YVLSGGELPAMVLVDAVTRL
LPGALGHHHHHH
Data type | Count |
13C chemical shifts | 446 |
15N chemical shifts | 144 |
1H chemical shifts | 144 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | N domain of bacterial tRNA-(N1G37) methyltransferase (TrmD) | 1 |
Entity 1, N domain of bacterial tRNA-(N1G37) methyltransferase (TrmD) 172 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 | HIS | HIS | HIS | ||||
18 | HIS | HIS |
sample_1: N domain of bacterial tRNA-(N1G37) methyltransferase (TrmD), [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
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 |
NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks