3PRB

structural analysis of protein folding by the methanococcus jannaschii chaperone fkbp26

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 93
  • Norm. En. per Res.: -4.9963
• 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	-148.7252	-15.2731	-300.66	-464.6584	93	26	5	11370	2	37	29

Interface residues

• A-B: ALA187A, ALA187B, ALA196A, ALA196B, ALA199A, ALA199B, ALA201A, ALA201B, ALA211A, ALA211B, ARG175A, ARG207A, ARG207B, ARG222A, ARG222B, ASN192A, ASN192B, ASN202A, ASN202B, ASP210A, ASP210B, GLN194A, GLN194B, GLU182A, GLU182B, GLU185B, GLU203A, GLU203B, GLU209A, GLU209B, GLU212A, GLU212B, GLU218A, GLU218B, GLU221A, GLU221B, GLY177A, GLY177B, ILE181A, ILE181B, ILE190A, ILE190B, ILE193A, ILE193B, ILE200A, ILE200B, ILE204A, ILE204B, LEU183A, LEU183B, LEU205A, LEU205B, LEU208A, LEU208B, LYS171A, LYS180A, LYS180B, LYS197A, LYS197B, LYS206A, LYS206B, LYS213A, LYS213B, LYS223A, LYS223B, LYS224B, MET198A, MET198B, PHE186A, PHE189A, PHE189B, PHE216A, PHE216B, PHE220A, PHE220B, PRO188A, PRO188B, PRO191A, PRO191B, SER215A, SER215B, THR178A, THR178B, THR195A, THR195B, THR219A, THR219B, VAL179A, VAL179B, VAL214A, VAL214B, VAL217A, VAL217B