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
 GLY-64   PRO-65  5.3 5.2 -15.9 0.2 96.6 96.3 -49.2
 PRO-65   HIS-66  4.5 4.2 -18.4 40.3 155.5 165.5 128.3
 HIS-66   ASP-67  4.3 4.2 10.9 -13.1 69.6 74.6 12.0

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
 PHE-117   ASN-118  2.5 2.6 5.5 0.0 27.2 26.5 38.7
 ASN-118   HIS-119  2.0 2.2 -7.6 7.9 92.1 92.5 -13.5
 HIS-119   PRO-120  2.9 3.2 -0.2 0.7 107.1 109.6 -10.1
 PRO-120   LEU-121  4.1 3.9 -5.1 9.1 168.2 172.3 17.4

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