2ZZ8

crystal structure of lipl32, the most abundant surface protein of pathogenic leptospira spp

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 133
  • Norm. En. per Res.: -2.1525
• 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	-9.6973	12.9701	-289.556	-286.2833	133	7	7	12783	0	27	30

Interface residues

• A-B: ARG77A, ARG77B, ASN160A, ASN160B, ASP113A, ASP113B, ASP175A, ASP175B, ASP19A, ASP19B, GLU104A, GLU104B, GLU105A, GLU105B, GLU18A, GLU18B, GLU202A, GLU202B, GLU26A, GLU26B, GLU84A, GLU84B, GLY201A, GLY201B, GLY218A, GLY218B, GLY23A, GLY23B, GLY35A, GLY35B, GLY6A, GLY6B, GLY83A, GLY83B, HIS110A, HIS110B, HIS156A, ILE219B, ILE21A, ILE21B, ILE79A, ILE79B, ILE85A, ILE85B, LEU16A, LEU16B, LEU214A, LEU214B, LEU31A, LEU31B, LEU32A, LEU32B, LEU7A, LEU7B, LYS106A, LYS106B, LYS11A, LYS11B, LYS158A, LYS158B, LYS178A, LYS178B, LYS199A, LYS199B, LYS29A, LYS29B, MET108A, MET108B, PHE112A, PHE112B, PHE174A, PHE174B, PHE207A, PHE207B, PHE98A, PHE98B, PRO103A, PRO103B, PRO109A, PRO109B, PRO200A, PRO200B, PRO217A, PRO217B, PRO220B, PRO22A, PRO22B, PRO33A, PRO33B, PRO81A, PRO81B, PRO8A, PRO8B, SER107A, SER107B, SER161A, SER161B, SER173B, SER17A, SER17B, SER206A, SER206B, SER80A, SER80B, SER9A, SER9B, THR102A, THR197A, THR197B, THR20A, THR20B, THR24A, THR24B, THR27A, THR27B, THR30A, THR30B, THR82A, THR82B, TRP111A, TRP111B, TYR159A, TYR159B, TYR198A, TYR198B, TYR34A, TYR34B, TYR41A, TYR41B, VAL208A, VAL208B, VAL28A, VAL28B