Lysr-Type Regulatory 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
 LEU-74   ALA-75  0.2 0.3 1.5 3.2 22.8 20.2 20.3
 ALA-75   GLY-76  0.9 0.5 -8.7 10.7 93.4 91.9 -76.9
 GLY-76   ARG-77  4.7 4.3 21.0 -14.3 114.4 106.4 -20.8
 ARG-77   SER-78  5.3 5.5 -6.8 20.2 122.5 131.2 120.3
 SER-78   GLY-79  5.1 5.7 11.3 7.7 41.7 52.3 131.3
 GLY-79   ASP-80  6.5 7.7 -30.5 -4.9 67.7 63.6 85.2
 ASP-80   ARG-81  9.4 10.6 12.9 0.9 102.2 113.3 -45.7
 ARG-81   SER-82  9.9 10.3 1.7 -11.9 37.9 44.4 -122.5
 SER-82   ARG-83  10.7 11.2 6.2 -12.4 74.1 72.2 -53.7
 ARG-83   ALA-84  12.8 13.3 54.1 -62.0 128.5 134.9 60.6
 ALA-84   ALA-85  14.6 15.2 2.4 6.9 77.3 89.3 7.2
 ALA-85   ALA-86  15.5 16.1 5.3 -4.1 35.2 39.4 -18.8
 ALA-86   ARG-87  16.5 17.5 -5.9 17.2 79.2 72.1 -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