Glycine Betaine-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
 GLY-94   SER-95  8.0 8.2 0.0 0.2 105.9 112.0 46.8
 SER-95   ALA-96  4.2 4.4 24.8 -18.7 90.1 93.2 13.1
 ALA-96   GLU-97  2.6 2.7 -6.3 18.1 65.5 62.3 2.6

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


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
 MET-248   THR-249  9.2 9.0 -0.7 2.5 36.0 42.5 -22.8
 THR-249   GLY-250  6.5 6.1 9.5 -4.8 64.7 64.1 59.3
 GLY-250   VAL-251  2.9 2.5 -0.7 6.8 131.5 131.7 41.6

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