Acetylcholine-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
 ALA-177   THR-178  5.6 5.2 -3.3 14.7 137.0 135.9 -7.8
 THR-178   GLN-179  3.5 3.2 -12.8 36.5 157.3 156.2 57.6
 GLN-179   THR-180  3.5 3.4 19.8 -7.5 58.3 66.7 34.5

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
 ASN-197   LEU-198  3.2 3.5 4.9 1.2 46.3 39.3 32.9
 LEU-198   VAL-199  4.9 4.8 7.4 0.2 29.8 34.6 -5.5
 VAL-199   VAL-200  4.3 4.1 6.2 -6.6 43.5 39.3 43.0

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