Glutamine Binding Protein

(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
 LYS-87   SER-88  5.4 4.4 36.0 -46.7 119.0 123.6 9.9
 SER-88   GLY-89  1.7 0.7 -6.5 64.8 132.1 129.9 72.3
 GLY-89   LEU-90  2.2 2.8 -37.4 32.3 53.1 56.4 -3.2

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
 LEU-180   GLU-181  6.5 7.5 -3.6 -148.2 75.3 65.6 67.6
 GLU-181   ALA-182  4.0 4.1 127.4 -10.8 67.1 48.6 115.0
 ALA-182   GLN-183  2.1 0.9 5.1 -6.0 114.4 88.3 19.6
 GLN-183   GLN-184  2.5 2.6 -35.5 3.8 129.4 113.8 -31.0

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