BMRB Entry 15782
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15782
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Title: 1H, 13C and 15N chemical shifts of the sylvatic Dengue 1 Envelope Protein Domain III, strain P72-1244 PubMed: 19636893
Deposition date: 2008-05-27 Original release date: 2008-09-12
Authors: Volk, David; Anderson, Kurtis; Gandham, Sai; May, Fiona; Beasley, David; Barrett, Alan; Gorenstein, David
Citation: Volk, David; Anderson, Kurtis; Gandham, Sai; May, Fiona; Li, Li; Beasley, David; Barrett, Alan; Gorenstein, David. "NMR assignments of the sylvatic dengue 1 virus envelope protein domain III" Biomol. NMR Assignments 2, 155-157 (2008).
Assembly members:
DEN1ED3, polymer, 112 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):
DEN1ED3: MDKLTLKGMSYVMCTGSFKL
EKEVAETQHGTVLVQVKYEG
TDAPCKIPFSTQDEKGITQN
GRLITANPIVTDKEKPVSIE
AKPPFGESYIVVGAGEKALK
LSWFKKGSSIGK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 442 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 746 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit1 | 1 |
Entities:
Entity 1, subunit1 112 residues - Formula weight is not available
M289-K400 of the sylvatic Dengue 1 ED3, with mutations N366S,E370K
| 1 | MET | ASP | LYS | LEU | THR | LEU | LYS | GLY | MET | SER | ||||
| 2 | TYR | VAL | MET | CYS | THR | GLY | SER | PHE | LYS | LEU | ||||
| 3 | GLU | LYS | GLU | VAL | ALA | GLU | THR | GLN | HIS | GLY | ||||
| 4 | THR | VAL | LEU | VAL | GLN | VAL | LYS | TYR | GLU | GLY | ||||
| 5 | THR | ASP | ALA | PRO | CYS | LYS | ILE | PRO | PHE | SER | ||||
| 6 | THR | GLN | ASP | GLU | LYS | GLY | ILE | THR | GLN | ASN | ||||
| 7 | GLY | ARG | LEU | ILE | THR | ALA | ASN | PRO | ILE | VAL | ||||
| 8 | THR | ASP | LYS | GLU | LYS | PRO | VAL | SER | ILE | GLU | ||||
| 9 | ALA | LYS | PRO | PRO | PHE | GLY | GLU | SER | TYR | ILE | ||||
| 10 | VAL | VAL | GLY | ALA | GLY | GLU | LYS | ALA | LEU | LYS | ||||
| 11 | LEU | SER | TRP | PHE | LYS | LYS | GLY | SER | SER | ILE | ||||
| 12 | GLY | LYS |
Samples:
sample_1: DEN1ED3, [U-99% 13C; U-99% 15N], 0.25 ± 0.05 mM; sodium chloride 25 ± 1 mM; TRIS, [U-2H], 25 ± 1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
FELIX v2000, Accelrys Software Inc. - chemical shift assignment, processing
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts