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  28.1 28.0 3.2 -6.7 41.8 42.7 -12.5
 ALA-107   ALA-108  24.9 24.8 -3.0 2.5 89.3 84.5 -4.6
 ALA-108   LEU-109  23.0 23.0 -0.2 -4.3 117.9 119.3 -30.3
 LEU-109   ARG-110  19.3 19.3 1.7 -8.1 83.9 87.1 29.7
 ARG-110   SER-111  17.9 17.8 12.7 -12.1 90.2 84.7 -49.9
 SER-111   LEU-112  14.6 14.5 -7.8 40.3 175.2 178.0 796.5
 LEU-112   PRO-113  13.1 13.1 40.9 -34.9 79.0 87.2 -884.0
 PRO-113   ALA-114  11.6 11.7 -10.2 15.2 99.1 92.8 114.1
 ALA-114   GLU-115  7.8 7.9 36.8 -55.3 48.5 52.7 -298.2
 GLU-115   ILE-116  8.7 8.4 -19.2 18.6 130.0 129.5 357.7
 ILE-116   PRO-117  10.1 10.1 -0.8 -0.3 88.6 87.3 88.1
 PRO-117   GLU-118  13.3 13.2 3.8 -1.8 26.9 27.0 61.5

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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