1VAI

structure of e. coli cyclophilin b k163t mutant bound to n- acetyl-ala-ala-pro-ala-7-amino-4-methylcoumarin

• Total interactions analyzed: 3
• Total true interactions: 2
• Strongest Interaction:
  • Chains: B-C
  • Int. Res.: 37
  • Norm. En. per Res.: -2.4795
• 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	0.0	5.6213	-10.3553	-4.734	24	0	0	805	0	7	5
B-C	-8.9892	0.0	-82.7518	-91.741	37	10	3	3108	0	0	0

Interface residues

• A-B: ALA13A, ALA77B, ARG118B, ARG82B, ASP114B, ASP119B, ASP78B, GLN117B, GLY116B, GLY14A, GLY80B, HIS115B, ILE138A, LYS137A, LYS155A, PHE120B, PRO142A, PRO153A, PRO156A, SER12A, SER154A, VAL141A, VAL157A, VAL158A
• B-C: ALA2C, ALA3C, ALA5C, ALA89B, ALA91B, ALA94B, ALA99B, ARG48B, ARG92B, ASN106B, ASN110B, ASN83B, GLN102B, GLN56B, GLN66B, GLY121B, GLY57B, GLY59B, HIS47B, ILE105B, ILE50B, ILE55B, LEU113B, MET54B, MET90B, PHE103B, PHE104B, PHE112B, PHE53B, PHE60B, PRO4C, SER101B, SER98B, THR100B, THR93B, TYR122B, TYR149B