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
 ALA-62   TYR-63  5.6 5.7 -1.3 0.8 134.1 135.8 -5.9
 TYR-63   GLY-64  2.8 3.0 1.6 -1.2 116.0 116.6 15.5
 GLY-64   PRO-65  3.7 3.9 0.6 0.5 110.9 111.8 8.7
 PRO-65   HIS-66  4.3 4.5 -4.0 1.6 132.5 133.8 -21.0

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


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  6.1 5.9 1.9 -1.3 109.5 111.1 -8.4
 HIS-119   PRO-120  2.8 2.7 5.0 6.6 60.8 61.9 84.0
 PRO-120   LEU-121  5.6 5.4 -13.3 2.9 149.5 155.9 -113.9
 LEU-121   ALA-122  4.3 4.2 1.6 -1.4 51.1 55.5 27.9
 ALA-122   GLY-123  2.3 2.1 -25.8 31.8 158.4 153.6 92.4

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