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 -2.6 0.3 58.1 54.1 5.9
 ALA-89   ALA-90  5.8 6.0 -7.5 22.0 110.7 104.5 18.5
 ALA-90   ASP-91  2.3 2.4 -42.5 -2.7 65.7 71.8 43.8
 ASP-91   SER-92  1.8 3.0 8.5 4.1 74.0 54.2 16.3
 SER-92   ARG-93  4.4 5.1 21.6 -7.3 62.3 64.4 14.2

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-188   LYS-189  3.7 3.5 7.1 -7.7 56.7 59.5 5.0
 LYS-189   TYR-190  2.8 2.4 13.0 -21.2 122.3 126.7 9.6
 TYR-190   PHE-191  4.0 3.5 7.8 -12.6 136.8 141.0 23.4
 PHE-191   GLY-192  2.0 1.1 -0.3 5.5 94.9 99.1 22.6
 GLY-192   ASP-193  2.1 2.3 -9.9 14.9 57.0 70.3 -0.2
 ASP-193   GLY-194  4.9 5.7 -28.9 9.1 44.7 37.2 19.4

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