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
 LYS-30   SER-31  1.6 2.5 -74.4 86.5 139.9 142.4 11.2
 SER-31   PRO-32  2.1 4.1 -136.0 -9.9 141.9 141.3 181.9
 PRO-32   GLU-33  0.9 2.1 -150.1 4.2 150.4 79.7 -77.2
 GLU-33   LEU-34  1.8 1.2 -113.3 -32.0 134.0 101.8 -81.9
 LEU-34   GLN-35  1.4 3.7 -63.2 -30.1 136.0 126.4 -60.4
 GLN-35   ALA-36  2.1 4.3 76.2 38.0 42.9 19.1 112.1
 ALA-36   GLU-37  3.2 2.7 -37.6 47.8 132.5 104.8 1.8
 GLU-37   ALA-38  0.4 1.7 172.1 131.4 119.5 99.6 11.6

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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