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
 TYR-86   LYS-87  7.1 7.3 -8.1 6.3 51.5 47.3 7.3
 LYS-87   SER-88  4.3 5.1 3.3 0.8 60.3 62.7 2.1
 SER-88   GLY-89  0.9 1.4 -16.2 -47.9 53.4 49.2 73.8
 GLY-89   LEU-90  2.8 2.7 1.0 23.6 56.4 52.6 15.0

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
 LEU-180   GLU-181  7.1 6.7 -11.4 -4.2 100.6 105.2 19.9
 GLU-181   ALA-182  4.7 4.1 -26.6 9.7 69.5 68.7 17.8
 ALA-182   GLN-183  1.4 2.3 18.3 2.9 77.5 73.1 34.9
 GLN-183   GLN-184  2.5 2.2 -11.4 11.4 55.7 48.2 10.9
 GLN-184   TYR-185  5.5 5.7 5.2 0.3 119.1 117.9 -5.6

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