Chaperone Protein Htpg

(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
 ASN-228   LYS-229  8.7 7.0 11.8 -26.9 82.7 75.1 2.7
 LYS-229   ALA-230  5.1 4.0 10.6 -1.4 151.2 120.1 -5.4
 ALA-230   GLN-231  5.0 1.1 5.7 94.6 111.7 57.3 15.3
 GLN-231   ALA-232  3.4 2.6 -22.2 -97.2 43.9 56.1 58.4
 ALA-232   LEU-233  4.8 4.3 -24.8 -16.2 108.6 112.9 -11.1

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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