1PPB

the refined 1.9 angstroms crystal structure of human alpha-thrombin: interaction with d-phe-pro-arg chloromethylketone and significance of the tyr-pro-pro-trp insertion segment

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: L-H
  • Int. Res.: 104
  • Norm. En. per Res.: -5.6811
• Hub Node: L(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
L-H	-105.2513	-42.1382	-443.45	-590.8396	104	34	1	16261	11	43	33

Interface residues

• L-H: ALA113H, ALA132H, ALA1L, ALA22H, ARG137H, ARG14L, ARG15L, ARG206H, ARG4L, ARG50H, ASN159H, ASN204H, ASN205H, ASP116H, ASP14L, ASP1L, ASP21H, ASP243H, ASP49H, CYS122H, CYS1L, GLN131H, GLN156H, GLN209H, GLN239H, GLN244H, GLU13L, GLU14L, GLU1L, GLU23H, GLU247H, GLU8L, GLY133H, GLY136H, GLY1L, GLY246H, GLY25H, GLY2L, HIS119H, HIS71H, ILE118H, ILE14L, ILE162H, ILE242H, ILE24H, ILE47H, LEU123H, LEU129H, LEU12L, LEU130H, LEU14L, LEU160H, LEU3L, LEU46H, LEU6L, LYS107H, LYS10L, LYS135H, LYS14L, LYS186H, LYS202H, LYS9L, MET201H, MET210H, MET26H, PHE114H, PHE199H, PHE1L, PHE204H, PHE245H, PHE7L, PRO111H, PRO120H, PRO161H, PRO204H, PRO28H, PRO5L, SER115H, SER11L, SER129H, SER14L, SER1L, SER203H, SER20H, SER27H, SER48H, THR139H, THR14L, THR1L, TRP207H, TRP29H, TRP51H, TYR117H, TYR134H, TYR14L, TYR184H, TYR208H, VAL112H, VAL121H, VAL138H, VAL157H, VAL158H, VAL200H, VAL241H