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  8.5 8.9 1.7 9.0 85.7 84.1 -3.2
 GLY-64   PRO-65  5.2 5.8 -2.9 0.3 101.3 92.1 4.3
 PRO-65   HIS-66  1.6 2.0 1.3 7.2 9.3 15.1 25.0
 HIS-66   ASP-67  1.6 1.2 -1.0 -3.5 108.2 106.5 6.4
 ASP-67   PRO-68  1.7 2.0 5.8 5.0 43.9 46.6 43.4

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
 ASP-116   PHE-117  4.4 4.3 -4.7 -5.7 89.7 86.2 2.2
 PHE-117   ASN-118  3.9 3.6 6.2 4.9 21.0 25.5 44.8
 ASN-118   HIS-119  4.2 3.9 -3.5 2.5 96.6 97.0 15.8
 HIS-119   PRO-120  7.7 7.3 -2.5 2.5 106.7 114.9 9.9
 PRO-120   LEU-121  9.5 9.3 -10.3 9.9 170.0 179.2 1.1
 LEU-121   ALA-122  9.5 9.4 -10.7 -1.7 114.5 113.7 -28.7
 ALA-122   GLY-123  5.8 5.7 -2.1 -2.6 123.0 123.7 -4.2
 GLY-123   LYS-124  4.9 4.5 2.4 -4.8 55.6 58.5 -3.1

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