E3 Ubiquitin-Protein Ligase Parkin

(All numbering and residues are taken from first PDB file)

Bending Residue Dihedral Analysis

Residue
i
Residue
i+1
Distance of hinge axis to residue i in conformer 1
(A)
Distance of hinge axis to residue i in conformer 2
(A)
Change in psi (i)
(deg)
Change in phi (i+1)
(deg)
Angle of psi(i) axis to hinge axis conformer 1
(deg)
Angle of psi(i) axis to hinge axis conformer 2
(deg)
Percentage Progress
 GLN-316   GLN-317  4.0 4.3 -18.1 31.0 100.2 98.8 9.3
 GLN-317   TYR-318  1.2 0.7 -47.0 -4.1 41.0 42.6 86.7
 TYR-318   GLY-319  2.9 1.8 12.8 -6.9 80.4 91.0 0.4

Downloading Image

Graph shows rotational transition at bending residues and can be used to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees


Residue
i
Residue
i+1
Distance of hinge axis to residue i in conformer 1
(A)
Distance of hinge axis to residue i in conformer 2
(A)
Change in psi (i)
(deg)
Change in phi (i+1)
(deg)
Angle of psi(i) axis to hinge axis conformer 1
(deg)
Angle of psi(i) axis to hinge axis conformer 2
(deg)
Percentage Progress
 GLY-375   GLU-376  31.4 33.9 20.6 -44.7 59.9 51.5 -46.8
 GLU-376   CYS-377  29.1 32.0 12.8 3.4 104.4 77.8 3.9
 SER-378   ALA-379  25.4 7.3 -98.1 -23.3 142.1 78.2 -82.0
 ALA-379   VAL-380  24.4 4.6 151.9 -13.4 89.9 53.6 64.6
 TYR-391   ARG-392  2.7 5.5 -46.8 76.7 108.5 140.7 70.7
 ARG-392   VAL-393  5.9 7.1 -17.3 -50.0 92.1 84.1 23.4

Downloading Image

Graph shows rotational transition at bending residues and can be used to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees