1VLZ

uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 angstrom structure of a threonine to isoleucine mutant at position 87 of chey

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 58
  • Norm. En. per Res.: -1.8344
• 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	-18.5564	0.9744	-88.8137	-106.3957	58	2	3	4139	0	9	10

Interface residues

• A-B: ALA101A, ALA101B, ALA103A, ALA103B, ALA74A, ALA74B, ALA77A, ALA80A, ALA80B, ALA97A, ALA97B, ALA98A, ALA98B, ALA99A, ALA99B, ARG73A, ARG73B, ASP75A, ASP75B, GLN100A, GLN100B, GLU125A, GLU93B, GLY102A, GLY102B, GLY105A, GLY105B, GLY128A, GLY76A, GLY76B, ILE123A, ILE123B, ILE72A, ILE72B, ILE95B, ILE96B, LEU127A, LEU69A, LEU69B, LEU81A, LYS122B, LYS126A, LYS126B, LYS70A, LYS70B, LYS92B, MET129A, MET78A, MET78B, PHE124A, PRO82A, SER104A, SER104B, SER79A, SER79B, THR71B, TYR106B, VAL83A