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
 GLU-33   LEU-34  3.9 7.6 -6.4 -18.4 46.8 41.1 13.4
 LEU-34   GLN-35  0.8 4.5 62.2 52.8 136.1 109.4 -30.6
 GLN-35   ALA-36  4.0 5.0 -163.9 -13.5 54.5 42.8 127.4
 ALA-36   GLU-37  6.4 3.7 -125.6 -4.2 121.0 104.9 -51.7
 GLU-37   ALA-38  7.5 6.3 26.1 -83.7 105.4 8.1 -33.9
 ALA-38   LYS-39  6.7 4.7 -18.5 -45.9 40.7 96.1 14.0
 LYS-39   SER-40  3.6 3.5 -86.4 -1.9 64.4 52.3 38.4
 SER-40   TYR-41  4.7 6.7 -22.3 13.5 36.2 17.4 6.4

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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