BMRB Entry 15034
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15034
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Title: 1H,13C and 15N NMR Assignments of the Yellow Fever Envelope Protein Domain III PubMed: 19636823
Deposition date: 2006-11-16 Original release date: 2007-06-27
Authors: Volk, David; Gandham, Sai; May, Fiona; Barrett, Alan; Gorenstein, David
Citation: Volk, David; Gandham, Sai; May, Fiona; Anderson, Anjenique; Barrett, Alan; Gorenstein, David. "NMR assignments of the yellow fever virus envelope protein domain III" Biomol. NMR Assignments 1, 49-50 (2007).
Assembly members:
YFED3, polymer, 112 residues, Formula weight is not available
Natural source: Common Name: Yellow fever virus Taxonomy ID: 11089 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Yellow fever virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YFED3: MSALTLKGTSYKMCTDKMSF
VKNPTDTGHGTVVMQVKVPK
GAPCKIPVIVADDLTAAINK
GILVTVNPIASTNDDEVLIE
VNPPFGDSYIIVGTGDSRLT
YQWHKEGSSIGK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 462 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 768 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YFED3 monomer | 1 |
Entities:
Entity 1, YFED3 monomer 112 residues - Formula weight is not available
All residues (1-112) represent natural amino acids in the YF-ED3
| 1 | MET | SER | ALA | LEU | THR | LEU | LYS | GLY | THR | SER | ||||
| 2 | TYR | LYS | MET | CYS | THR | ASP | LYS | MET | SER | PHE | ||||
| 3 | VAL | LYS | ASN | PRO | THR | ASP | THR | GLY | HIS | GLY | ||||
| 4 | THR | VAL | VAL | MET | GLN | VAL | LYS | VAL | PRO | LYS | ||||
| 5 | GLY | ALA | PRO | CYS | LYS | ILE | PRO | VAL | ILE | VAL | ||||
| 6 | ALA | ASP | ASP | LEU | THR | ALA | ALA | ILE | ASN | LYS | ||||
| 7 | GLY | ILE | LEU | VAL | THR | VAL | ASN | PRO | ILE | ALA | ||||
| 8 | SER | THR | ASN | ASP | ASP | GLU | VAL | LEU | ILE | GLU | ||||
| 9 | VAL | ASN | PRO | PRO | PHE | GLY | ASP | SER | TYR | ILE | ||||
| 10 | ILE | VAL | GLY | THR | GLY | ASP | SER | ARG | LEU | THR | ||||
| 11 | TYR | GLN | TRP | HIS | LYS | GLU | GLY | SER | SER | ILE | ||||
| 12 | GLY | LYS |
Samples:
sample_1: YFED3, [U-98% 13C; U-98% 15N], 0.1 – 0.3 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 5.8; 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection, data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB | |
| GB | AAA92693 AAA92694 AAA92695 AAA92698 AAA92699 |
| SP | Q074N0 Q1X880 Q1X881 Q6DV88 Q6J3P1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts