BMRB Entry 18266
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18266
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Title: Backbone assignment of Dengue Virus NS2B/NS3 in complex with Aprotinin PubMed: 22623057
Deposition date: 2012-02-15 Original release date: 2012-06-05
Authors: Bi, Yunchen; Zhu, Lei; Wang, Junfeng
Citation: Bi, Yunchen; Zhu, Lei; Li, Hua; Wu, Bo; Liu, Jinsong; Wang, Junfeng. "Backbone 1H, 13C and 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin." Biomol. NMR Assignments 7, 137-139 (2013).
Assembly members:
entity, polymer, 247 residues, Formula weight is not available
Aprotinin, polymer, 58 residues, Formula weight is not available
Natural source: Common Name: Dengue virus Taxonomy ID: 12637 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Dengue virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSHMLEADLELERAADVRWE
EQAEISGSSPILSITISEDG
SMSIKNEEEEQTLGGGGSGG
GGAGVLWDVPSPPPVGKAEL
EDGAYRIKQKGILGYSQIGA
GVYKEGTFHTMWHVTRGAVL
MHKGKRIEPSWADVKKDLIS
YGGGWKLEGEWKEGEEVQVL
ALEPGKNPRAVQTKPGLFKT
NTGTIGAVSLDFSPGTSGSP
IVDKKGKVVGLYGNGVVTRS
GAYVSAIAQTEKSIEDNPEI
EDDIFRK
Aprotinin: RPDFCLEPPYTGPCKARIIR
YFYNAKAGLCQTFVYGGCRA
KRNNFKSAEDCMRTCGGA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 530 |
| 15N chemical shifts | 172 |
| 1H chemical shifts | 172 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Dengue Virus NS2B/NS3 | 1 |
| 2 | Aprotinin | 2 |
Entities:
Entity 1, Dengue Virus NS2B/NS3 247 residues - Formula weight is not available
| 1 | GLY | SER | HIS | MET | LEU | GLU | ALA | ASP | LEU | GLU | ||||
| 2 | LEU | GLU | ARG | ALA | ALA | ASP | VAL | ARG | TRP | GLU | ||||
| 3 | GLU | GLN | ALA | GLU | ILE | SER | GLY | SER | SER | PRO | ||||
| 4 | ILE | LEU | SER | ILE | THR | ILE | SER | GLU | ASP | GLY | ||||
| 5 | SER | MET | SER | ILE | LYS | ASN | GLU | GLU | GLU | GLU | ||||
| 6 | GLN | THR | LEU | GLY | GLY | GLY | GLY | SER | GLY | GLY | ||||
| 7 | GLY | GLY | ALA | GLY | VAL | LEU | TRP | ASP | VAL | PRO | ||||
| 8 | SER | PRO | PRO | PRO | VAL | GLY | LYS | ALA | GLU | LEU | ||||
| 9 | GLU | ASP | GLY | ALA | TYR | ARG | ILE | LYS | GLN | LYS | ||||
| 10 | GLY | ILE | LEU | GLY | TYR | SER | GLN | ILE | GLY | ALA | ||||
| 11 | GLY | VAL | TYR | LYS | GLU | GLY | THR | PHE | HIS | THR | ||||
| 12 | MET | TRP | HIS | VAL | THR | ARG | GLY | ALA | VAL | LEU | ||||
| 13 | MET | HIS | LYS | GLY | LYS | ARG | ILE | GLU | PRO | SER | ||||
| 14 | TRP | ALA | ASP | VAL | LYS | LYS | ASP | LEU | ILE | SER | ||||
| 15 | TYR | GLY | GLY | GLY | TRP | LYS | LEU | GLU | GLY | GLU | ||||
| 16 | TRP | LYS | GLU | GLY | GLU | GLU | VAL | GLN | VAL | LEU | ||||
| 17 | ALA | LEU | GLU | PRO | GLY | LYS | ASN | PRO | ARG | ALA | ||||
| 18 | VAL | GLN | THR | LYS | PRO | GLY | LEU | PHE | LYS | THR | ||||
| 19 | ASN | THR | GLY | THR | ILE | GLY | ALA | VAL | SER | LEU | ||||
| 20 | ASP | PHE | SER | PRO | GLY | THR | SER | GLY | SER | PRO | ||||
| 21 | ILE | VAL | ASP | LYS | LYS | GLY | LYS | VAL | VAL | GLY | ||||
| 22 | LEU | TYR | GLY | ASN | GLY | VAL | VAL | THR | ARG | SER | ||||
| 23 | GLY | ALA | TYR | VAL | SER | ALA | ILE | ALA | GLN | THR | ||||
| 24 | GLU | LYS | SER | ILE | GLU | ASP | ASN | PRO | GLU | ILE | ||||
| 25 | GLU | ASP | ASP | ILE | PHE | ARG | LYS |
Entity 2, Aprotinin 58 residues - Formula weight is not available
| 1 | ARG | PRO | ASP | PHE | CYS | LEU | GLU | PRO | PRO | TYR | ||||
| 2 | THR | GLY | PRO | CYS | LYS | ALA | ARG | ILE | ILE | ARG | ||||
| 3 | TYR | PHE | TYR | ASN | ALA | LYS | ALA | GLY | LEU | CYS | ||||
| 4 | GLN | THR | PHE | VAL | TYR | GLY | GLY | CYS | ARG | ALA | ||||
| 5 | LYS | ARG | ASN | ASN | PHE | LYS | SER | ALA | GLU | ASP | ||||
| 6 | CYS | MET | ARG | THR | CYS | GLY | GLY | ALA |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; NS2B-NS3, [U-100% 13C; U-100% 15N; U-80% 2H], 0.6 mM; Aprotinin 1.2 mM
sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 850 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts