Prolyl Oligopeptidase

(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
 ALA-77   SER-78  10.1 10.1 6.7 24.8 133.0 143.0 -61.4
 SER-78   ARG-79  8.4 8.9 -27.6 -18.6 72.1 79.7 18.9
 ARG-79   ASN-80  8.6 8.0 34.0 8.2 86.4 43.2 75.9
 ASN-80   TYR-81  5.9 6.3 -72.3 22.0 76.3 87.2 21.6
 TYR-81   ALA-82  2.8 2.8 -7.8 15.1 82.7 78.4 3.2
 ALA-82   LYS-83  4.4 4.0 -10.6 -10.0 13.9 14.3 56.8

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
 ARG-446   THR-447  10.3 10.1 -14.5 7.6 117.1 120.3 12.8
 THR-447   THR-448  7.0 7.1 -30.5 0.9 53.2 49.9 72.9
 THR-448   LYS-449  3.4 3.6 -9.1 5.9 50.9 72.6 -11.1
 LYS-449   VAL-450  3.3 3.4 7.0 34.4 99.2 104.7 11.2
 VAL-450   ASN-451  3.8 3.1 50.8 -59.5 121.6 142.0 10.5

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