3T41

1.95 angstrom resolution crystal structure of epidermin leader peptide processing serine protease (epip) s393a mutant from staphylococcus aureus

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 95
  • Norm. En. per Res.: -0.964
• Hub Node: A(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
A-B	-14.5916	19.5366	-96.5265	-91.5815	95	2	2	4457	0	46	60

Interface residues

• A-B: ALA419A, ALA419B, ARG437A, ARG437B, ASN254A, ASN254B, ASN275A, ASN275B, ASN296A, ASN296B, ASN322A, ASN322B, ASN344A, ASN344B, ASN431A, ASN431B, ASN432A, ASN432B, ASP294A, ASP294B, ASP297A, ASP321A, ASP321B, ASP347A, ASP347B, ASP417A, ASP417B, GLN257A, GLN425A, GLN425B, GLN454A, GLU312B, GLU36A, GLU36B, GLU421A, GLU421B, GLY342A, GLY342B, GLY439A, GLY439B, HIS256A, HIS256B, HIS426A, HIS426B, HIS440A, HIS440B, ILE283A, ILE420A, ILE420B, LEU422A, LEU422B, LYS253A, LYS253B, LYS264B, LYS272A, LYS272B, LYS278A, LYS278B, LYS279A, LYS279B, LYS298A, LYS298B, LYS38A, LYS38B, LYS418A, LYS418B, LYS430A, LYS430B, LYS433A, LYS433B, LYS447A, LYS447B, LYS84A, LYS84B, MET343A, MET343B, PHE341A, PHE341B, PHE435A, PHE435B, PRO416A, PRO416B, PRO434A, PRO434B, SER436A, SER436B, TYR424A, TYR424B, TYR438A, TYR438B, TYR85A, TYR85B, VAL323A, VAL323B, VAL324A