2HF2

domain shifting confirms monomeric structure of escherichia sugar phosphatase suph

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 103
  • Norm. En. per Res.: -0.5956
• 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	-18.8548	62.4408	-104.934	-61.348	103	25	3	6515	1	22	28

Interface residues

• A-B: ALA118A, ALA121A, ALA121B, ALA124A, ALA127A, ALA18A, ALA235B, ALA236B, ARG132A, ASN103B, ASN117A, ASN152B, ASN16A, ASN209A, ASN22A, ASN234B, ASN238B, ASN250B, ASN251B, ASN45B, ASN46A, ASP11A, ASP11B, ASP155B, ASP17A, ASP17B, ASP204A, ASP215B, ASP249B, ASP99B, GLN101B, GLN157B, GLN208A, GLN23A, GLN47A, GLN50A, GLU116A, GLU120A, GLU120B, GLU156B, GLU237B, GLU57A, GLY12A, GLY12B, GLY179B, GLY181B, GLY217B, HIS129A, HIS131A, ILE158B, ILE162B, ILE239B, ILE52A, LEU102B, LEU125A, LEU133A, LEU153B, LEU15A, LEU160B, LEU1B, LEU200A, LEU205A, LEU51A, LYS100B, LYS128A, LYS137A, LYS19A, LYS19B, LYS39A, LYS4A, LYS59A, PHE122A, PHE122B, PHE180B, PHE182B, PHE54A, PHE55A, PRO119A, PRO119B, PRO135A, PRO154B, PRO159B, PRO207A, PRO24A, PRO56A, SER178B, SER206A, SER216B, SER2A, SER44A, SER53A, THR13B, THR177B, THR20A, TRP203A, TYR130A, TYR21A, TYR48A, TYR49A, VAL161B, VAL176B, VAL210A, VAL5A