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  8.1 6.9 0.2 1.0 77.4 70.6 -4.8
 GLY-64   PRO-65  6.3 5.1 -2.1 1.3 74.5 82.4 7.2
 PRO-65   HIS-66  3.9 2.7 2.8 -17.2 154.5 151.9 35.3
 HIS-66   ASP-67  4.5 3.6 -7.7 13.3 101.8 104.1 9.0

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
 ASP-116   PHE-117  6.9 6.5 2.7 4.5 89.4 88.2 1.4
 PHE-117   ASN-118  8.3 7.5 -0.4 -13.1 36.4 45.1 28.0
 ASN-118   HIS-119  6.4 5.2 5.4 -3.7 75.8 64.4 13.0
 HIS-119   PRO-120  6.5 4.7 7.2 -3.4 87.6 91.1 9.8
 PRO-120   LEU-121  4.1 2.3 8.2 -7.8 148.8 145.0 9.9

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