BMRB Entry 4617
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4617
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Title: Structure of hetero complex of non structural protein (NS) of hepatitis C virus (HCV) and synthetic peptidic compound PubMed: 10716920
Deposition date: 2000-01-17 Original release date: 2001-03-08
Authors: Barbato, G.; Cicero, D.; Cordier, F.; Narjes, F.; Gerlach, B.; Sambucini, S.; Grzesiek, S.; Matassa, V.; DeFrancesco, R.; Bazzo, R.
Citation: Barbato, G.; Cicero, D.; Cordier, F.; Narjes, F.; Gerlach, B.; Sambucini, S.; Grzesiek, S.; Matassa, V.; DeFrancesco, R.; Bazzo, R.. "Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain" EMBO J. 19, 1195-1206 (2000).
Assembly members:
serine protease, polymer, 186 residues, Formula weight is not available
modified tripeptide inhibitor, polymer, 3 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: HCV Taxonomy ID: 11105 Superkingdom: Viruses Kingdom: not available Genus/species: Hepacivirus Hepatitis C virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
serine protease: APITAYSQQTRGLLGCIITS
LTGRDKNQVEGEVQVVSTAT
QSFLATCVNGVCWTVYHGAG
SKTLAGPKGPITQMYTNVDQ
DLVGWQAPPGARSLTPCTCG
SSDLYLVTRHADVIPVRRRG
DSRGSLLSPRPVSYLKGSSG
GPLLCPSGHAVGIFRAAVCT
RGVAKAVDFVPVESMETTMR
ASKKKK
modified tripeptide inhibitor: ELX
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 268 |
| coupling constants | 91 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HCV NS3 | 1 |
| 2 | Zn 2+ | 3 |
| 3 | modified tripeptide inhibitor | 2 |
Entities:
Entity 1, HCV NS3 186 residues - Formula weight is not available
| 1 | ALA | PRO | ILE | THR | ALA | TYR | SER | GLN | GLN | THR | ||||
| 2 | ARG | GLY | LEU | LEU | GLY | CYS | ILE | ILE | THR | SER | ||||
| 3 | LEU | THR | GLY | ARG | ASP | LYS | ASN | GLN | VAL | GLU | ||||
| 4 | GLY | GLU | VAL | GLN | VAL | VAL | SER | THR | ALA | THR | ||||
| 5 | GLN | SER | PHE | LEU | ALA | THR | CYS | VAL | ASN | GLY | ||||
| 6 | VAL | CYS | TRP | THR | VAL | TYR | HIS | GLY | ALA | GLY | ||||
| 7 | SER | LYS | THR | LEU | ALA | GLY | PRO | LYS | GLY | PRO | ||||
| 8 | ILE | THR | GLN | MET | TYR | THR | ASN | VAL | ASP | GLN | ||||
| 9 | ASP | LEU | VAL | GLY | TRP | GLN | ALA | PRO | PRO | GLY | ||||
| 10 | ALA | ARG | SER | LEU | THR | PRO | CYS | THR | CYS | GLY | ||||
| 11 | SER | SER | ASP | LEU | TYR | LEU | VAL | THR | ARG | HIS | ||||
| 12 | ALA | ASP | VAL | ILE | PRO | VAL | ARG | ARG | ARG | GLY | ||||
| 13 | ASP | SER | ARG | GLY | SER | LEU | LEU | SER | PRO | ARG | ||||
| 14 | PRO | VAL | SER | TYR | LEU | LYS | GLY | SER | SER | GLY | ||||
| 15 | GLY | PRO | LEU | LEU | CYS | PRO | SER | GLY | HIS | ALA | ||||
| 16 | VAL | GLY | ILE | PHE | ARG | ALA | ALA | VAL | CYS | THR | ||||
| 17 | ARG | GLY | VAL | ALA | LYS | ALA | VAL | ASP | PHE | VAL | ||||
| 18 | PRO | VAL | GLU | SER | MET | GLU | THR | THR | MET | ARG | ||||
| 19 | ALA | SER | LYS | LYS | LYS | LYS |
Entity 3, Zn 2+ - Zn - 65.409 Da.
| 1 | ZN |
Entity 2, modified tripeptide inhibitor 3 residues - Formula weight is not available
| 1 | GLU | LEU | FKI |
Samples:
sample_1: serine protease mM
sample_cond_1: pH: 6.6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| not reported | sample_1 | not available | sample_cond_1 |
Software:
No software information available
NMR spectrometers:
- Bruker DMX 500 MHz
- Bruker DMX 600 MHz