Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19517
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Citation: Zazrin, Hadas; Shaked, Hadassa; Chill, Jordan. "Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR." Biochim. Biophys. Acta 1838, 784-792 (2014).
PubMed: 24192053
Assembly members:
E1TM, polymer, 54 residues, Formula weight is not available
Natural source: Common Name: Hepatitis C virus Taxonomy ID: 11103 Superkingdom: Viruses Kingdom: not available Genus/species: Hepacivirus Hepatitis C virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
E1TM: DPEREKAHWGVLAGIAYYSM
VGNWAKVLIVLLLFAGVDAE
REKDPHHHHHHHHH
Data type | Count |
13C chemical shifts | 171 |
15N chemical shifts | 61 |
1H chemical shifts | 61 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | E1TM | 1 |
Entity 1, E1TM 54 residues - Formula weight is not available
Residues 345-349 are an artificial extension for solubility Residues 350-383 are the E1 TM domain Residues 384-389 are an artificial extension for solubility Residues 390-397 are a his-tag
1 | ASP | PRO | GLU | ARG | GLU | LYS | ALA | HIS | TRP | GLY | ||||
2 | VAL | LEU | ALA | GLY | ILE | ALA | TYR | TYR | SER | MET | ||||
3 | VAL | GLY | ASN | TRP | ALA | LYS | VAL | LEU | ILE | VAL | ||||
4 | LEU | LEU | LEU | PHE | ALA | GLY | VAL | ASP | ALA | GLU | ||||
5 | ARG | GLU | LYS | ASP | PRO | HIS | HIS | HIS | HIS | HIS | ||||
6 | HIS | HIS | HIS | HIS |
sample_1: E1TM, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 0.6 mM; H2O 93 ± 1 %; D2O, [U-99% 2H], 7 ± 1 %; sodium chloride 20 ± 1 mM; sodium phosphate 20 ± 1 mM; SDS 300 ± 20 mM
sample_2: E1TM, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 0.6 mM; H2O 93 ± 1 %; D2O, [U-99% 2H], 7 ± 1 %; sodium chloride 20 ± 1 mM; sodium phosphate 20 ± 1 mM; LPPG 40 ± 4 mM
sample_conditions_1: ionic strength: 180 mM; pH: 6.7; pressure: 1 atm; temperature: 318 K
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(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
TOPSPIN v3.0, Bruker Biospin - chemical shift assignment, collection
EMBL | CAD53672 CAD53673 CAD53674 CAD53675 CAD53676 |
GB | AAK27140 AAK27141 AAK59220 AAU93985 AAU93986 |
Download HSQC peak lists in one of the following formats:
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