1PVA

comparison between the crystal and the solution structures of the ef hand parvalbumin (alpha component from pike muscle)

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 55
  • Norm. En. per Res.: -1.8523
• 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	-22.0772	14.2086	-94.0088	-101.8774	55	1	4	3725	0	44	35

Interface residues

• A-B: ALA1A, ALA1B, ALA2A, ALA2B, ALA49A, ALA49B, ALA52A, ALA52B, ALA54A, ALA54B, ALA71A, ALA71B, ALA72A, ALA72B, ASP4A, ASP4B, ASP51A, ASP51B, ASP53A, ASP53B, ASP73A, ASP73B, ASP76A, ASP76B, GLU59A, GLU59B, GLU60A, GLU61A, GLU61B, GLU62A, GLU62B, GLY56A, GLY74B, ILE11B, ILE50B, ILE58A, LEU15B, LEU63A, LEU67B, LEU6B, LYS3A, LYS3B, LYS64A, LYS68A, LYS68B, PHE57A, PHE65A, PHE65B, PHE70A, PHE70B, SER55A, SER55B, SER69A, SER69B, VAL66B