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 9.0 -2.2 2.3 55.7 53.7 0.5
 ALA-89   ALA-90  5.8 6.0 -2.6 15.4 108.0 104.3 10.1
 ALA-90   ASP-91  2.2 2.4 -47.9 -0.6 65.2 71.4 55.8
 ASP-91   SER-92  1.9 3.0 12.6 -2.2 70.9 54.6 13.4
 SER-92   ARG-93  4.5 5.1 22.3 -9.6 62.6 64.8 18.4

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
 LYS-189   TYR-190  2.6 2.3 4.1 -15.8 123.6 126.7 17.0
 TYR-190   PHE-191  3.9 3.4 13.9 -15.0 137.1 141.5 14.4
 PHE-191   GLY-192  1.9 1.1 -6.6 13.7 93.6 98.6 25.7
 GLY-192   ASP-193  2.2 2.3 -10.6 18.1 54.1 70.3 -6.8
 ASP-193   GLY-194  5.0 5.7 -29.2 8.0 45.9 36.7 24.5

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