Peptidyl-Prolyl Cis-Trans Isomerase Slyd

(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
 TYR-63   GLY-64  5.8 5.7 9.6 2.2 40.7 41.0 61.1
 GLY-64   PRO-65  3.2 3.2 7.7 -14.9 94.6 98.3 -12.8
 PRO-65   HIS-66  1.3 1.5 0.1 -5.0 88.8 93.0 -11.5

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


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
 HIS-119   PRO-120  9.4 9.4 0.9 -1.3 48.7 39.6 17.3
 PRO-120   LEU-121  9.2 9.3 7.2 -12.7 74.3 74.0 -14.8
 LEU-121   ALA-122  5.6 5.7 13.4 -10.7 141.7 144.8 -97.0

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