Lysine-, Arginine-, Ornithine-Binding Protein (Lao)

(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-88   ALA-89  8.9 9.1 1.4 -2.0 121.4 125.9 1.8
 ALA-89   ALA-90  5.9 6.1 -0.6 17.3 107.4 104.3 15.2
 ALA-90   ASP-91  2.4 2.4 -52.1 5.6 63.9 71.9 47.1
 ASP-91   SER-92  1.8 3.1 10.0 0.1 73.7 54.3 14.4
 SER-92   ARG-93  4.4 5.1 23.3 -10.2 60.9 64.2 16.0

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
 LYS-189   TYR-190  2.7 2.4 4.2 -15.3 120.3 126.6 17.0
 TYR-190   PHE-191  3.9 3.4 7.3 -10.6 137.0 140.9 20.4
 PHE-191   GLY-192  1.9 1.0 1.6 7.1 85.2 80.8 24.2
 GLY-192   ASP-193  2.0 2.3 -12.8 14.4 55.5 70.2 1.7
 ASP-193   GLY-194  5.0 5.8 -23.6 6.6 44.2 37.3 12.8

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