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  9.2 9.1 -47.4 55.0 114.1 124.5 4.3
 SER-31   PRO-32  6.7 6.4 -135.0 -8.8 157.8 168.3 264.4
 PRO-32   GLU-33  7.5 8.1 -7.3 -62.7 115.2 107.9 -37.3
 GLU-33   LEU-34  7.1 8.5 -142.7 -36.1 147.0 175.2 -215.5
 LEU-34   GLN-35  4.0 6.9 -0.8 6.8 101.9 99.8 1.6

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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