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  3.1 2.9 -6.2 4.7 102.8 103.1 2.5
 TYR-63   GLY-64  3.3 3.0 17.0 -2.4 34.1 37.5 38.9
 GLY-64   PRO-65  2.3 2.5 16.0 -14.2 94.6 90.6 1.4

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


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  8.7 8.8 -0.9 -0.1 116.8 121.5 16.5
 PRO-120   LEU-121  8.2 8.2 5.3 -12.7 98.5 99.1 -5.1
 LEU-121   ALA-122  4.6 4.8 9.1 -9.9 167.1 170.6 -35.1
 ALA-122   GLY-123  5.3 5.6 -162.5 175.6 85.5 65.8 9.4
 GLY-123   LYS-124  5.6 6.8 13.6 -21.3 48.1 67.9 19.3
 LYS-124   ASP-125  4.7 5.5 5.3 3.1 96.4 96.5 7.2
 ASP-125   LEU-126  5.2 5.5 6.0 6.8 20.8 19.0 58.6
 LEU-126   ASP-127  4.4 4.6 14.3 -10.3 73.7 71.2 21.4

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