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  7.6 7.8 -22.2 25.4 91.4 99.0 -35.2
 GLY-64   PRO-65  7.0 7.1 -22.8 0.8 80.1 73.1 -23.8
 PRO-65   HIS-66  5.2 5.3 -12.9 38.4 135.6 141.1 120.6
 HIS-66   ASP-67  3.2 3.3 28.8 -25.6 64.0 63.1 29.6

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
 ASN-118   HIS-119  0.6 0.7 -9.7 13.0 97.0 97.7 3.7
 HIS-119   PRO-120  4.1 4.1 -4.8 -8.5 126.8 131.1 -75.1
 PRO-120   LEU-121  5.8 5.3 6.2 6.9 12.2 14.8 90.8
 LEU-121   ALA-122  5.4 5.4 -6.0 5.6 101.6 101.6 15.4
 ALA-122   GLY-123  2.6 2.9 22.7 -33.3 43.9 40.4 -55.6

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