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
 ARG-83   SER-84  1.5 2.6 -17.1 4.1 143.3 146.7 -69.2
 SER-84   MET-85  3.7 4.7 12.0 -51.1 108.2 96.0 86.1
 MET-85   LYS-86  5.6 6.2 -35.0 41.2 101.1 79.3 44.8
 LYS-86   ASP-87  5.8 5.1 153.7 -4.9 20.5 57.3 390.5
 ASP-87   ASP-88  8.0 3.7 63.9 -50.5 95.1 18.0 -163.6
 ASP-88   SER-89  8.6 4.2 -47.3 62.9 154.1 82.0 -56.7
 SER-93   GLU-94  16.3 15.9 11.1 -3.1 112.1 101.7 -7.5
 GLU-94   GLU-95  18.0 17.6 -12.3 12.3 90.6 93.2 8.9

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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