Sensory Transduction Regulatory Protein, Anti-Anti-Sigma Factor Phyr

(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
 THR-219   ALA-220  3.7 5.1 25.6 1.8 103.0 109.7 -1.6
 ALA-220   PHE-221  5.6 6.0 167.1 50.6 112.7 91.4 14.3
 PHE-221   PRO-222  4.3 5.9 48.8 13.8 125.6 42.4 37.6
 PRO-222   GLU-223  2.1 7.5 156.0 -7.6 102.2 102.7 8.7
 GLU-223   ARG-224  5.3 11.2 0.3 12.4 53.5 72.3 2.3
 ARG-224   LEU-225  5.7 12.3 -5.5 18.7 78.3 46.1 -8.7
 LEU-225   LEU-226  5.0 12.2 -29.6 33.8 13.8 39.5 -2.6
 LEU-226   THR-227  6.0 13.7 120.7 -44.9 96.9 83.3 -18.1
 THR-227   GLY-228  9.8 17.4 -39.3 19.0 52.4 58.2 18.2

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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