Troponin C

(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-87   ASP-88  8.6 8.0 -15.6 -0.9 20.7 35.0 7.7
 ASP-88   ALA-89  10.1 9.8 49.8 2.0 122.9 139.5 -29.1
 ALA-89   LYS-90  7.1 7.0 -178.7 -80.9 105.0 65.3 -3.3
 LYS-90   GLY-91  4.8 5.8 94.2 -37.0 113.1 139.9 -52.6
 GLY-91   LYS-92  7.6 3.2 -113.7 -11.9 11.4 88.2 70.1
 LYS-92   SER-93  7.2 0.6 -161.1 -15.3 76.5 152.7 56.0
 SER-93   GLU-94  3.7 3.1 -110.8 -16.9 96.8 90.2 42.5
 GLU-94   GLU-95  5.9 6.1 -12.7 11.0 52.2 45.7 -1.8

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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