Residue　networks　are　constructed　by　defining　the　residues　as　the　vertices　and　atom　contacts　between　them　as　the　edges.　The　residue　network　of　a　protein　complex　is　divided　into　two　types　of　networks,　i.e.　the　hydrophobic　and　the　hydrophilic　residue　networks.　By　analyzing　the　network　parameters,　it　is　found　that　the　correct　binding　complex　conformations　are　of　both　higher　sum　of　the　interface　degree　values　and　lower　characteristic　path　length　than　those　incorrect　ones.　These　features　reflect　that　the　correct　binding　complex　conformations　have　better　geometric　and/or　residue　type　complementarity,　and　the　correct　binding　modes　are　very　important　for　preserving　the　characteristic　path　lengths　of　native　protein　complexes.　In　addition,　two　scoring　terms　are　proposed　based　on　the　network　parameters,　in　which　the　characteristics　of　the　entire　complex　shape　and　residue　type　complementarity　are　taken　into　account.　These　network-based　scoring　terms　have　also　been　used　in　conjunction　with　other　scoring　terms,　and　the　new　multi-term　scoring　HPNCscore　is　devised　in　this　work.　It　can　improve　the　discrimination　of　the　combined　scoring　function　of　RosettaDock　more　than　12%.　This　work　might　enhance　our　knowledge　of　the　mechanisms　of　protein-protein　interactions　and　recognition.