BMRB Entry 18697
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18697
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Title: 1H, 13C and 15N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase complexed with anticodon stem-loop of tRNALys,3 PubMed: 23065336
Deposition date: 2012-08-31 Original release date: 2012-10-18
Authors: Liu, Sheng; Tsang, Pearl
Citation: Liu, Sheng; Decker, Aaron; Howell, Mike; Caperelli, Carol; Tsang, Pearl. "1H, 13C and 15N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase." Biomol. NMR Assignments 7, 289-292 (2013).
Assembly members:
rmodN, polymer, 76 residues, 8311 Da.
rmodN_isoD62, polymer, 76 residues, 8312 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
Entity Sequences (FASTA):
rmodN: MAAVQAAEVKVDGSEPKLSK
NELKRRLKAEKKVAEKEAKQ
KELSEKQLSQATAAATNHTT
DNGVLPETGGHHHHHH
rmodN_isoD62: MAAVQAAEVKVDGSEPKLSK
NELKRRLKAEKKVAEKEAKQ
KELSEKQLSQATAAATNHTT
DDGVLPETGGHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 522 |
15N chemical shifts | 145 |
1H chemical shifts | 652 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | rmodN | 1 |
2 | rmodN_isoD62 | 2 |
Entities:
Entity 1, rmodN 76 residues - 8311 Da.
1 | MET | ALA | ALA | VAL | GLN | ALA | ALA | GLU | VAL | LYS | ||||
2 | VAL | ASP | GLY | SER | GLU | PRO | LYS | LEU | SER | LYS | ||||
3 | ASN | GLU | LEU | LYS | ARG | ARG | LEU | LYS | ALA | GLU | ||||
4 | LYS | LYS | VAL | ALA | GLU | LYS | GLU | ALA | LYS | GLN | ||||
5 | LYS | GLU | LEU | SER | GLU | LYS | GLN | LEU | SER | GLN | ||||
6 | ALA | THR | ALA | ALA | ALA | THR | ASN | HIS | THR | THR | ||||
7 | ASP | ASN | GLY | VAL | LEU | PRO | GLU | THR | GLY | GLY | ||||
8 | HIS | HIS | HIS | HIS | HIS | HIS |
Entity 2, rmodN_isoD62 76 residues - 8312 Da.
N62 deamidate into isoD62
1 | MET | ALA | ALA | VAL | GLN | ALA | ALA | GLU | VAL | LYS | ||||
2 | VAL | ASP | GLY | SER | GLU | PRO | LYS | LEU | SER | LYS | ||||
3 | ASN | GLU | LEU | LYS | ARG | ARG | LEU | LYS | ALA | GLU | ||||
4 | LYS | LYS | VAL | ALA | GLU | LYS | GLU | ALA | LYS | GLN | ||||
5 | LYS | GLU | LEU | SER | GLU | LYS | GLN | LEU | SER | GLN | ||||
6 | ALA | THR | ALA | ALA | ALA | THR | ASN | HIS | THR | THR | ||||
7 | ASP | ASP | GLY | VAL | LEU | PRO | GLU | THR | GLY | GLY | ||||
8 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: rmodN, [U-100% 13C; U-100% 15N], 200 ± 10 uM; ACSL 400 ± 10 uM; sodium phosphate 20 ± 10 mM; NaCl 15 ± 10 mM; KCl 35 ± 10 mM; EDTA 1 ± 10 mM; D2O 10 ± 10 %; H2O 90 ± 10 %; NaN3 0.02 ± 10 %
sample_conditions_1: ionic strength: 70 mM; pH: 6.0; pressure: 1 atm; temperature: 298.15 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 HNCO | 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 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
BMRB | 18696 18696 |
DBJ | BAA06688 BAA22084 BAC86604 BAG09591 BAA06688 BAA22084 BAC86604 BAG09591 |
GB | AAH04132 ABM83227 ABM86426 AIC54646 EAW95620 AAH04132 ABM83227 ABM86426 AIC54646 EAW95620 |
REF | NP_005539 XP_003260017 XP_003829594 XP_004058057 XP_009249230 NP_005539 XP_003260017 XP_003829594 XP_009249230 XP_511115 |
SP | Q15046 Q15046 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts