1BSD

crystal structural analysis of mutations in the hydrophobic cores of barnase

• Total interactions analyzed: 3
• Total true interactions: 3
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 35
  • Norm. En. per Res.: -2.3904
• Hub Node: A(2)

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	-36.4805	0.0	-47.1819	-83.6624	35	4	0	2331	0	7	5
A-C	0.0	0.0	-0.1275	-0.1275	13	0	0	61	0	8	5
B-C	0.0	0.0	-0.0218	-0.0218	3	0	0	15	0	0	0

Interface residues

• A-B: ALA30A, ALA32A, ALA46A, ARG110B, ARG69B, ASN41A, ASP44A, ASP93B, GLN31A, GLU29A, GLY34A, GLY61B, GLY65B, ILE109B, LEU33A, LEU42A, LEU63B, LEU95B, LYS108B, LYS39A, LYS62B, LYS66B, PHE106B, PRO47A, PRO64B, SER28A, SER67B, SER91B, THR105B, THR107B, TRP35A, TRP71B, TYR97B, VAL36A, VAL45A
• A-C: ARG72A, ASP22C, GLU29C, HIS18A, LEU33C, LYS19A, LYS49C, PRO47C, SER28A, SER92A, THR26A, THR70A, TRP94A
• B-C: SER67B, THR16C, TYR17C