HIV-1　integrase　(IN)　integrates　viral　DNA　into　host　cells　through　two　steps　metal　ions-dependent　reactions.　The　number　of　metal　ions　binding　with　HIV-1　IN　has　very　important　influence　on　interactions　between　HIV-1　IN　and　inhibitors.　At　present,　two　HIV-1　IN　dimer　core　structures　(1Mg-IN-Core　and　2Mg-IN-Core　models)　having　one　or　two　Mg2+　icons　in　each　catalytic　core　domain　were　built　in　homology　modeling　methods.　Docking　them　respectively　with　inhibitor　thiazolothiazepines　using　the　program　Auto-dock,　two　kinds　of　complex　structures　with　low　energy　were　found　and　compared.　Docking　results　indicate　that　if　the　number　of　Mg2+　binding　with　IN　is　changed,　the　interactional　modes　of　IN　and　thiazolothiazepines　will　also　change;　thiazolothiazepines　have　high　binding　specialty　and　stability　with　IN;　the　Mg2+　chelated　with　ASP64　and　GLU152　simultaneously　has　a　great　influence　on　IN　binding　with　thiazolothiazepines.　A　2000　ps　molecular　dynamics　simulation　was　carried　out　on　the　2Mg-IN-Core　and　thiazolothiazepine　complex　system.　Analyzing　the　MD　result,　it　was　found　that　the　metal　ions　Mg2+　chelated,　at　the　same　time,　with　ASP64　and　ASP116　could　form　four　stable　chelate　bonds　with　residues　of　IN,　and　the　Mg2+　chelated　with　ASP64　and　GLU152　simultaneously　could　bind　with　IN,　making　stable　coordinate　bonds　with　the　inhibitor.　The　latter　Mg2+　ion　has　a　strong　influence　on　IN　stably　binding　with　thiazolothiazepines.