<protein id="45705C26-4ECD-43D2-AC9B-D47EC8D203E0">
	<object id="BFB0C814-B20B-4A36-9A85-E422C8043003"><sn>NS3</sn><nm>Protease/helicase NS3 </nm><sy>Hepacivirin</sy><sy>P70</sy><os id="DEDC969D-8050-4930-8D53-D1BF209326BF"><Latin>Hepatitis C virus</Latin><English>human hepatitis C virus</English></os><dbref><name>SWISS-PROT</name><ac>P26660</ac><id>POLG_HCVJ6</id></dbref><fn>active</fn><mm>monomer</mm><ref id="FE365F44-4629-45B9-8D33-B9D937C337A0"><authors>Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N., Moomaw E.W., Adachi T., Hostomska Z.</authors><journal id="journal62"><nm>Cell</nm></journal><title>The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site.</title><year>1996</year><pages><first>331</first><last>342</last></pages></ref><ref id="94EF8438-B3E-4C93-B555-A927536EFB27"><authors>Yao N., Hesson T., Cable M., Hong Z., Kwong A.D., Le H.V., Weber P.C.</authors><journal id="6BEBE366-99C7-4B65-911A-9DF7548DF853"><nm>Nat.Struct.Biol.</nm></journal><title>Structure of the hepatitis C virus RNA helicase domain.</title><year>1997</year><pages><first>463</first><last>467</last></pages></ref><ref id="BAE064B2-98C5-4DD3-9866-7770AC9679F4"><authors>Wang W., Lahser F.C., Yi .M., Wright-Minogue J., Xia E., Weber P.C., Lemon S.M., Malcolm B.A.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Conserved C-terminal threonine of hepatitis C virus NS3 regulates autoproteolysis and prevents product inhibition.</title><year>2004</year><pages><first>700</first><last>709</last></pages></ref><ref id="66C83689-3E58-437D-9AF4-316E1EF50DE6"><authors>Shoji I., Suzuki T., Sato M., Aizaki H., Chiba T., Matsuura Y., Miyamura T.</authors><journal id="journal317"><nm>Virology</nm></journal><title>Internal processing of hepatitis C virus NS3 protein.</title><year>1999</year><pages><first>315</first><last>323</last></pages></ref><ref id="94EF8438-B3E-4C93-B555-A927536EFB27"><authors>Yao N., Hesson T., Cable M., Hong Z., Kwong A.D., Le H.V., Weber P.C.</authors><journal id="6BEBE366-99C7-4B65-911A-9DF7548DF853"><nm>Nat.Struct.Biol.</nm></journal><title>Structure of the hepatitis C virus RNA helicase domain.</title><year>1997</year><pages><first>463</first><last>467</last></pages></ref><ref id="87021268-DDF9-4438-A605-63AC41EBD6FF"><authors>Locatelli G.A., Gosselin G., Spadari S., Maga G.</authors><journal id="journal199"><nm>J.Molec.Biol.</nm></journal><title>Hepatitis C virus NS3 NTPase/helicase: different stereoselectivity in nucleoside triphosphate utilisation suggests that NTPase and helicase activities are coupled by a nucleotide-dependent rate limiting step.</title><year>2001</year><pages><first>683</first><last>694</last></pages></ref><ref id="6C29AB4F-96DD-436C-ACB2-795060505C37"><authors>Muramatsu S., Ishido S., Fujita T., Itoh M., Hotta H.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Nuclear localization of the NS3 protein of hepatitis C virus and factors affecting the localization.</title><year>1997</year><pages><first>4954</first><last>4961</last></pages></ref><ref id="C67CC766-B13C-4518-8F5B-F95FBC7536E8"><authors>Kim J.L., Morgenstern K.A., Griffith J.P., Dwyer M.D., Thomson J.A., Murcko M.A., Lin C., Caron P.R.</authors><journal id="journal301"><nm>Structure</nm></journal><title>Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.</title><year>1998</year><pages><first>89</first><last>100</last></pages></ref><dt>05.10.2004;Khlebodarova T.M.;edited</dt><dt>11.10.2004;Khlebodarova T.M.;edited</dt><dt>15.10.2004;Khlebodarova T.M.;edited</dt><dt>20.10.2004;Khlebodarova T.M.;edited</dt><dt>11.11.2004;Khlebodarova T.M.;edited</dt><dt>06.10.2004;Khlebodarova T.M.;edited</dt><dt>25.11.2004;Khlebodarova T.M.;edited</dt></object>
	<x>1052.404299</x>
	<y>869.398621</y>
</protein>
