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  2.5 2.8 5.2 -4.3 119.3 122.2 -20.0
 GLY-64   PRO-65  2.6 2.4 6.3 -0.8 86.4 93.2 -42.4
 PRO-65   HIS-66  4.6 4.3 -2.2 -9.8 41.3 46.8 59.7
 HIS-66   ASP-67  5.7 5.4 -5.0 10.5 47.6 42.0 -18.3
 ASP-67   PRO-68  6.7 6.4 1.3 -0.2 115.8 108.4 -22.5
 PRO-68   GLU-69  9.9 9.9 -2.0 -6.6 14.1 22.6 36.9
 GLU-69   GLY-70  8.8 9.0 1.9 5.1 101.5 94.6 34.1
 GLY-70   VAL-71  6.6 6.9 -3.3 -6.1 83.0 88.0 2.7

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
 LEU-121   ALA-122  5.4 5.5 5.5 0.0 84.6 83.3 27.2
 ALA-122   GLY-123  3.0 3.0 -1.6 -1.5 58.2 58.5 13.6
 GLY-123   LYS-124  4.8 4.7 4.4 2.2 153.6 153.6 -61.5

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