3.4.21.98	KKGSVVIVGRIVLSCK	-	690462	
3.4.21.98	KKGSVVIVGRIVLSGK	-	693388	
3.4.21.98	KKGSVVIVGRIVLSGK	cofactor peptide KK4A	692999	
3.4.21.98	KKGSVVIVGRIVLSGK	NS4A cofactor	691207	
3.4.21.98	KKGSVVIVGRIVLSGKPAIIPKK	NS-4A cofactor	692999	
3.4.21.98	additional information	cofactor NS2B strongly influences the preference of flavivirus proteases for lysine or arginine at P2 in substrates	692982	
3.4.21.98	additional information	efficient NS3-4A proteolytic activity requires the protease domain and its NS4A cofactor but does not require the NS3 helicase domain	692986	
3.4.21.98	additional information	enhancement of NS3 catalytic efficiency by the NS4A cofactor depends on a few specific amino acid residues	695259	
3.4.21.98	additional information	full NS3 protease activity requires association with NS4A	693438	
3.4.21.98	additional information	NS-4A cofactor	684506, 691969	
3.4.21.98	additional information	NS2B domain important in substrate-based inhibitor binding	693529	
3.4.21.98	additional information	NS2B required	681172	
3.4.21.98	additional information	NS4 required	652756	
3.4.21.98	additional information	NS4A cofactor peptide	690462, 691208	
3.4.21.98	additional information	NS4A cofactor, KKGSVVIVGRIVLSGK	691209	
3.4.21.98	additional information	requires the noncovalently-associated viral protein NS4A for optimal catalytic activity. NS4A increases the enzymatic activity of NS3 by stabilizing the N-terminal domain of the protease, by optimizing the orientation of the residues of the catalytic triad and by contributing to the formation of the substrate recognition site	690304	
3.4.21.98	additional information	solution structure and dynamics of the single-chain hepatitis C virus NS3 protease NS4A cofactor complex. The NS4A-bound NS3 protease is in slow conformation exchange with the NS4A-free conformation	652839