Monoclonal Antibody Against Acetylcholine Receptor

(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
 LEU-104   GLU-105  5.9 5.9 -1.5 -5.4 59.4 65.4 32.3
 GLU-105   LEU-106  3.7 3.7 -24.5 42.7 25.0 23.7 -111.7
 LEU-106   LYS-106A  2.0 2.3 27.8 -40.8 137.1 124.1 211.7
 LYS-106A   ARG-107  1.8 2.5 -5.5 16.7 62.3 56.9 -96.1
 ARG-107   THR-108  3.5 2.9 -58.4 79.5 65.9 60.0 44.1
 THR-108   ALA-109  7.5 7.1 -3.2 -4.3 74.8 80.4 68.0
 ALA-109   PRO-110  11.2 11.0 -28.6 30.6 152.6 145.4 49.6

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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