BMRB Entry 18588
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18588
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Title: Backbone 1H, 15N, 13C Assignments of the N-terminal Part of Tyrosine tRNA Synthase from Bacillus stearothermophilus PubMed: 22960997
Deposition date: 2012-07-10 Original release date: 2012-10-18
Authors: Krejcirikova, Anna; Tugarinov, Vitali
Citation: Krejcirikova, Anna; Tugarinov, Vitali. "3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample." J. Biomol. NMR 54, 135-143 (2012).
Assembly members:
Tyr_tRNA_Synthase, polymer, 327 residues, Formula weight is not available
Natural source: Common Name: Bacillus stearothermophilus Taxonomy ID: 1422 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus stearothermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Tyr_tRNA_Synthase: MDLLAELQWRGLVNQTTDED
GLRKLLNEERVTLYCGFDPT
ADSLHIGHLATILTMRRFQQ
AGHRPIALVGGATGLIGDPS
GKKSERTLNAKETVEAWSAR
IKEQLGRFLDFEADGNPAKI
KNNYDWIGPLDVITFLRDVG
KHFSVNYMMAKESVQSRIET
GISFTEFSYMMLQAYDFLRL
YETEGCRLQIGGSDQWGNIT
AGLELIRKTKGEARAFGLTI
PLVTKADGTKFGKTESGTIW
LDKEKTSPYEFYQFWINTDD
RDVIRYLKYFTFLSKEEIEA
LEQELREAPEKRAAQKTLAE
EVTKLVHGEEALRQAIRISL
EHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 900 |
| 15N chemical shifts | 299 |
| 1H chemical shifts | 299 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tyr_tRNA_Synthase | 1 |
Entities:
Entity 1, Tyr_tRNA_Synthase 327 residues - Formula weight is not available
| 1 | MET | ASP | LEU | LEU | ALA | GLU | LEU | GLN | TRP | ARG | ||||
| 2 | GLY | LEU | VAL | ASN | GLN | THR | THR | ASP | GLU | ASP | ||||
| 3 | GLY | LEU | ARG | LYS | LEU | LEU | ASN | GLU | GLU | ARG | ||||
| 4 | VAL | THR | LEU | TYR | CYS | GLY | PHE | ASP | PRO | THR | ||||
| 5 | ALA | ASP | SER | LEU | HIS | ILE | GLY | HIS | LEU | ALA | ||||
| 6 | THR | ILE | LEU | THR | MET | ARG | ARG | PHE | GLN | GLN | ||||
| 7 | ALA | GLY | HIS | ARG | PRO | ILE | ALA | LEU | VAL | GLY | ||||
| 8 | GLY | ALA | THR | GLY | LEU | ILE | GLY | ASP | PRO | SER | ||||
| 9 | GLY | LYS | LYS | SER | GLU | ARG | THR | LEU | ASN | ALA | ||||
| 10 | LYS | GLU | THR | VAL | GLU | ALA | TRP | SER | ALA | ARG | ||||
| 11 | ILE | LYS | GLU | GLN | LEU | GLY | ARG | PHE | LEU | ASP | ||||
| 12 | PHE | GLU | ALA | ASP | GLY | ASN | PRO | ALA | LYS | ILE | ||||
| 13 | LYS | ASN | ASN | TYR | ASP | TRP | ILE | GLY | PRO | LEU | ||||
| 14 | ASP | VAL | ILE | THR | PHE | LEU | ARG | ASP | VAL | GLY | ||||
| 15 | LYS | HIS | PHE | SER | VAL | ASN | TYR | MET | MET | ALA | ||||
| 16 | LYS | GLU | SER | VAL | GLN | SER | ARG | ILE | GLU | THR | ||||
| 17 | GLY | ILE | SER | PHE | THR | GLU | PHE | SER | TYR | MET | ||||
| 18 | MET | LEU | GLN | ALA | TYR | ASP | PHE | LEU | ARG | LEU | ||||
| 19 | TYR | GLU | THR | GLU | GLY | CYS | ARG | LEU | GLN | ILE | ||||
| 20 | GLY | GLY | SER | ASP | GLN | TRP | GLY | ASN | ILE | THR | ||||
| 21 | ALA | GLY | LEU | GLU | LEU | ILE | ARG | LYS | THR | LYS | ||||
| 22 | GLY | GLU | ALA | ARG | ALA | PHE | GLY | LEU | THR | ILE | ||||
| 23 | PRO | LEU | VAL | THR | LYS | ALA | ASP | GLY | THR | LYS | ||||
| 24 | PHE | GLY | LYS | THR | GLU | SER | GLY | THR | ILE | TRP | ||||
| 25 | LEU | ASP | LYS | GLU | LYS | THR | SER | PRO | TYR | GLU | ||||
| 26 | PHE | TYR | GLN | PHE | TRP | ILE | ASN | THR | ASP | ASP | ||||
| 27 | ARG | ASP | VAL | ILE | ARG | TYR | LEU | LYS | TYR | PHE | ||||
| 28 | THR | PHE | LEU | SER | LYS | GLU | GLU | ILE | GLU | ALA | ||||
| 29 | LEU | GLU | GLN | GLU | LEU | ARG | GLU | ALA | PRO | GLU | ||||
| 30 | LYS | ARG | ALA | ALA | GLN | LYS | THR | LEU | ALA | GLU | ||||
| 31 | GLU | VAL | THR | LYS | LEU | VAL | HIS | GLY | GLU | GLU | ||||
| 32 | ALA | LEU | ARG | GLN | ALA | ILE | ARG | ILE | SER | LEU | ||||
| 33 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Tyr tRNA Synthase, [U-13C; U-15N; U-2H], 0.8 mM; DTT 5 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAD77088 GAD11882 GAJ57796 |
| GB | AAA22877 ADI25737 AEV20456 AGE23390 AKM20083 |
| REF | WP_011232277 WP_013144460 WP_015375638 WP_020278069 WP_033014498 |
| SP | P00952 P04077 Q5KW48 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts