BMRB Entry 50839
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50839
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR backbone resonance assignment of Japanese encephalitis virus capsid protein PubMed: 34170495
Deposition date: 2021-03-21 Original release date: 2021-04-05
Authors: Guo, Yuting; Cheng, Kai; Wu, Qiong; Xu, Guohua; Jiang, Ling; Li, Conggang
Citation: Guo, Yuting; Yao, Chendie; Cheng, Kai; Wu, Qiong; Xu, Guohua; Jiang, Ling; Li, Conggang. "NMR backbone resonance assignment of Japanese encephalitis virus capsid protein" Biomol. NMR Assign. 15, 403-407 (2021).
Assembly members:
entity_1, polymer, 119 residues, Formula weight is not available
Natural source: Common Name: Flavivirus Taxonomy ID: 11072 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Japanese encephalitis virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a
Entity Sequences (FASTA):
entity_1: HHHHHHMTKKPGGPGKNRAI
NMLKRGLPRVFPLVGVKRVV
MSLLDGRGPVRFVLALITFF
KFTALAPTKALLGRWKAVEK
SVAMKHLTSFKRELGTLIDA
VNKRGRKQNKRGGNEGSIM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 305 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 104 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Japanese encephalitis virus capsid protein | 1 |
Entities:
Entity 1, Japanese encephalitis virus capsid protein 119 residues - Formula weight is not available
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | MET | THR | LYS | LYS | ||||
| 2 | PRO | GLY | GLY | PRO | GLY | LYS | ASN | ARG | ALA | ILE | ||||
| 3 | ASN | MET | LEU | LYS | ARG | GLY | LEU | PRO | ARG | VAL | ||||
| 4 | PHE | PRO | LEU | VAL | GLY | VAL | LYS | ARG | VAL | VAL | ||||
| 5 | MET | SER | LEU | LEU | ASP | GLY | ARG | GLY | PRO | VAL | ||||
| 6 | ARG | PHE | VAL | LEU | ALA | LEU | ILE | THR | PHE | PHE | ||||
| 7 | LYS | PHE | THR | ALA | LEU | ALA | PRO | THR | LYS | ALA | ||||
| 8 | LEU | LEU | GLY | ARG | TRP | LYS | ALA | VAL | GLU | LYS | ||||
| 9 | SER | VAL | ALA | MET | LYS | HIS | LEU | THR | SER | PHE | ||||
| 10 | LYS | ARG | GLU | LEU | GLY | THR | LEU | ILE | ASP | ALA | ||||
| 11 | VAL | ASN | LYS | ARG | GLY | ARG | LYS | GLN | ASN | LYS | ||||
| 12 | ARG | GLY | GLY | ASN | GLU | GLY | SER | ILE | MET |
Samples:
sample_1: entity_1, [U-2H; U-13C; U-15N], 0.42 mM; sodium phosphate 20 mM; sodium chloride 200 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - data analysis
SPARKY - chemical shift assignment
TOPSPIN - collection
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts