3SIC

molecular recognition at the active site of subtilisin bpn': crystallographic studies using genetically engineered proteinaceous inhibitor ssi (streptomyces subtilisin inhibitor)

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: E-I
  • Int. Res.: 86
  • Norm. En. per Res.: -3.704
• Hub Node: E(1)

All Interactions

Chains	Hydro. Bond Ener. (kJ/mol)	Elec. Ener. (kJ/mol)	VDW. Ener. (kJ/mol)	Tot. Stab. Ener. (kJ/mol)	#int. res.	# Short cont.	#Hydr. int.	#VDW pairs	#salt bridges	#Pot. fav. elec. int	#Pot. unfav. elec. int
E-I	-87.4083	14.1655	-245.301	-318.5438	86	25	2	9983	0	16	11

Interface residues

• E-I: ALA105I, ALA151E, ALA152E, ALA153E, ALA179E, ALA187E, ALA223E, ALA98E, ARG65I, ASN104I, ASN155E, ASN218E, ASN62E, ASN99I, ASP32E, ASP68I, ASP76I, ASP99E, CYS101I, CYS71I, GLN103E, GLU100I, GLU102I, GLU156E, GLU67I, GLY100E, GLY102E, GLY127E, GLY128E, GLY131E, GLY154E, GLY157E, GLY166E, GLY169E, GLY202E, GLY219E, GLY65E, GLY66I, GLY97E, HIS106I, HIS64E, HIS67E, ILE107E, ILE108E, LEU126E, LEU135E, LEU96E, LYS170E, LYS73I, MET124E, MET222E, MET70I, PHE189E, PHE97I, PRO129E, PRO168E, PRO72I, PRO77I, SER101E, SER105E, SER125E, SER130E, SER132E, SER188E, SER190E, SER191E, SER204E, SER221E, SER224E, SER33E, SER63E, SER98I, THR220E, TRP106E, TYR104E, TYR167E, TYR171E, TYR217E, TYR75I, VAL165E, VAL203E, VAL68E, VAL69I, VAL74I, VAL95E, VAL96I