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  7.3 7.1 8.1 -6.3 47.3 51.5 7.3
 LYS-87   SER-88  5.1 4.3 -3.3 -0.8 62.7 60.3 2.1
 SER-88   GLY-89  1.4 0.9 16.2 47.9 49.2 53.4 73.8
 GLY-89   LEU-90  2.7 2.8 -1.0 -23.6 52.6 56.4 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  6.7 7.1 11.4 4.2 105.2 100.6 19.9
 GLU-181   ALA-182  4.1 4.7 26.6 -9.7 68.7 69.5 17.8
 ALA-182   GLN-183  2.3 1.4 -18.3 -2.9 73.1 77.5 34.9
 GLN-183   GLN-184  2.2 2.5 11.4 -11.4 48.2 55.7 10.9
 GLN-184   TYR-185  5.7 5.5 -5.2 -0.3 117.9 119.1 -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