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
 HIS-56   VAL-57  6.9 7.2 -16.5 20.2 132.7 138.0 7.1
 VAL-57   PRO-58  3.8 4.2 10.4 0.1 76.1 70.7 11.7
 PRO-58   ALA-59  2.2 2.8 -4.1 -1.8 89.3 86.5 2.0
 ALA-59   GLU-60  2.6 2.3 3.0 -1.3 46.2 48.3 16.5

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
 LYS-124   ASP-125  5.4 5.6 -3.2 2.4 77.3 81.4 9.4
 ASP-125   LEU-126  3.4 3.7 6.3 0.9 28.7 25.2 37.2
 LEU-126   ASP-127  1.8 2.1 -14.8 12.4 95.3 100.0 40.1

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