Heme Activator Protein

(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
 TYR-95   MET-96  14.2 14.2 -7.2 2.0 95.5 93.9 0.9
 MET-96   GLU-97  11.2 10.8 -16.8 -34.6 84.4 85.6 -2.8
 GLU-97   GLN-98  7.7 8.2 -128.7 -55.7 29.0 69.8 -80.7
 GLN-98   THR-99  6.2 5.4 23.6 1.2 78.6 130.5 12.4
 THR-99   TRP-100  2.6 5.8 -167.2 20.2 84.6 118.8 177.6
 TRP-100   ALA-101  5.3 9.2 -44.7 46.3 132.4 118.6 -0.3
 ALA-101   GLU-102  7.4 8.6 -45.8 -25.0 151.2 141.8 -37.3
 GLU-102   GLU-103  4.9 5.7 30.8 -15.4 50.2 38.3 10.0

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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