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  4.8 4.4 7.8 -15.3 60.9 53.1 -65.9
 GLY-64   PRO-65  5.2 4.8 14.6 -0.5 51.2 57.2 55.3
 PRO-65   HIS-66  3.7 3.4 -5.9 -4.5 61.5 59.5 33.4

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
 ASN-118   HIS-119  5.0 5.0 3.0 -0.8 60.0 59.7 18.5
 HIS-119   PRO-120  1.6 1.8 -2.1 3.8 55.4 53.9 -12.9
 PRO-120   LEU-121  4.3 4.7 0.2 -0.7 137.4 137.5 9.9
 LEU-121   ALA-122  3.6 4.0 -0.5 1.9 53.3 51.4 -2.6
 ALA-122   GLY-123  0.3 0.6 -0.1 4.2 20.8 20.3 -41.3
 GLY-123   LYS-124  0.7 1.0 -16.2 6.6 75.6 76.5 75.4
 LYS-124   ASP-125  4.5 4.8 1.1 -4.0 91.9 86.5 7.4
 ASP-125   LEU-126  7.5 7.8 5.9 -0.9 51.7 51.3 30.4
 LEU-126   ASP-127  10.2 10.4 -13.3 12.5 74.9 77.4 27.1

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