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
 PRO-32   GLU-33  7.8 5.4 160.8 -13.8 65.7 156.8 -61.6
 GLU-33   LEU-34  5.2 6.0 123.7 -8.0 98.0 114.9 -55.9
 LEU-34   GLN-35  6.9 4.4 132.4 -26.9 162.8 140.9 172.8
 GLN-35   ALA-36  7.6 5.4 -104.0 44.5 52.2 62.1 -194.4
 ALA-36   GLU-37  4.8 5.7 -83.3 34.9 112.2 45.2 25.3
 GLU-37   ALA-38  3.0 2.7 -166.5 -87.7 118.5 113.8 20.3
 ALA-38   LYS-39  0.4 1.0 4.7 35.9 106.8 97.1 -3.7
 LYS-39   SER-40  3.9 4.0 -78.4 0.4 25.1 16.3 50.2

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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