Type II Secretion System 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
 ARG-227   LYS-228  33.5 33.3 -6.4 24.1 94.4 93.9 -32.2
 LYS-228   PHE-229  30.4 30.7 30.7 -47.9 66.7 50.8 -49.0
 PHE-229   THR-230  27.3 27.8 111.7 -4.8 127.0 120.1 -226.7
 THR-230   ILE-231  25.2 24.3 0.9 60.6 84.0 62.5 283.3
 ILE-231   GLU-232  22.9 23.2 31.8 -170.5 118.8 75.8 28.1
 GLU-232   PRO-233  19.2 19.4 50.8 1.1 68.2 58.4 94.6
 PRO-233   LEU-234  18.5 18.1 -6.6 -9.1 69.6 70.1 21.3

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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