2RLN

thermodynamic and structural consequences of changing a sulphur atom to a methylene group in the m13nle mutation in ribonuclease s

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: S-E
  • Int. Res.: 55
  • Norm. En. per Res.: -3.7257
• Hub Node: S(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
S-E	-25.3676	-19.3891	-160.156	-204.9126	55	4	4	5965	1	15	23

Interface residues

• S-E: ALA109E, ALA122E, ALA4S, ALA52E, ALA5S, ALA6S, ARG10S, ARG33E, ARG39E, ASN34E, ASN44E, ASP121E, ASP14S, GLN11S, GLN55E, GLU111E, GLU2S, GLU49E, GLU9S, GLY112E, HIS119E, HIS12S, HIS48E, ILE106E, ILE107E, ILE81E, LEU35E, LEU51E, LYS1S, LYS37E, LYS41E, LYS7S, MET29E, MET30E, PHE120E, PHE46E, PHE8S, PRO114E, PRO117E, SER15S, SER32E, SER50E, SER80E, THR36E, THR3S, THR45E, THR82E, TYR25E, VAL108E, VAL116E, VAL118E, VAL43E, VAL47E, VAL54E, VAL57E