Twitching Motility Protein Pilt

(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
 ALA-106   ALA-107  7.7 7.7 2.1 -8.7 149.7 149.5 7.4
 ALA-107   ALA-108  6.8 6.7 -0.8 -0.9 60.9 62.5 -3.9
 ALA-108   LEU-109  5.7 5.8 4.5 -5.6 163.8 160.1 6.9
 LEU-109   ARG-110  6.5 6.6 0.4 -4.3 126.5 127.8 -9.4
 ARG-110   SER-111  5.6 5.6 1.4 -32.8 153.3 149.3 23.9
 SER-111   LEU-112  6.5 6.8 -71.6 43.6 67.5 37.5 23.3
 LEU-112   PRO-113  3.6 3.8 -9.7 -54.5 7.9 27.0 94.1
 PRO-113   ALA-114  3.5 4.0 23.0 -19.5 126.8 117.4 -5.5
 ALA-114   GLU-115  4.6 3.8 -176.2 173.7 27.4 26.1 -13.8
 GLU-115   ILE-116  3.3 3.1 -29.4 13.1 109.3 105.0 -20.3
 ILE-116   PRO-117  2.2 2.2 -2.3 -0.9 55.8 54.5 0.2

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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