Table 1. Summary of interaction restraints used in protein-protein docking.

	Residues
Ambiguous interaction restraints
Hb
Active residues	αLys127, αAla130, αThr134, αLys139, αArg141, βThr12, βAla13, βGly16, βLys17, βAsn19, βGlu22, βTrp37, βAla135, βAsn139, βHis143, βLys144, βTyr145, βHis146
Passive residues	αVal1, αSer3, αHis89, αArg92, αSer138, βLys8, βSer9, βPro36, βArg40, βSer72, βThr87, βGlu90, βLys95, βLeu96, βHis97, βGlu101, βArg104
Hp
Active residues	βLys9, βPhe129, βLys130, βPhe131, βHis134, βAsp144, βAsp146, βArg150, βThr156, βVal157, βPro158, βGlu159, βLys160, βLys161, βThr162, βLeu203, βGlu204, βGlu205, βAsp206, βLys218, βVal222
Passive residues	αAsn36, αLys76, αAsn77, βLeu6, βAla8, βAsn23, βThr61, βGlu99, βLys109, βVal114, βAsn126, βAla127, βHis151, βPro163, βSer183
Hpβ *
Active residues	βLys9, βLys130, βPhe131, βAsp144, βAsp146, βArg150, βThr156, βVal157, βGlu159, βLys160, βLys161, βThr162, βLeu203, βGlu204, βGlu205, βAsp206, βVal222, βAla223
Passive residues	βHis5, βLeu6, βAla8, βVal64, βGlu99, βVal114, βPro163, βLys164, βLeu173, βSer183, βSer184, βGln186, βGlu187
Unambiguous interaction restraints
Hb	HemeFe-Nε αHis87
	HemeFe-Nε βHis92

^*Haptoglobin without α chain.