Apolipoprotein A-II

(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-36   GLU-37  9.0 6.1 41.9 34.3 142.4 167.7 -110.0
 GLU-37   ALA-38  6.5 5.7 6.4 -30.5 70.2 104.1 -2.1
 ALA-38   LYS-39  3.2 2.2 130.5 -3.1 28.3 34.0 162.2
 LYS-39   SER-40  4.2 3.9 -25.5 2.3 89.1 90.1 -5.4
 SER-40   TYR-41  6.5 5.3 8.5 -6.8 99.5 96.3 -5.5

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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