Chemotaxis Protein Chea

(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  GLY-451   ARG-452  1.8 2.4 19.1 -10.4 81.4 69.3 -63.7  ARG-452   GLY-453  5.2 5.6 42.0 -3.1 35.1 25.4 194.5  GLY-453   ILE-454  4.1 4.3 14.5 7.9 40.4 43.7 97.8  ILE-454   ASP-455  5.4 5.0 -11.8 21.0 96.0 100.7 -37.1 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

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  VAL-505   GLY-506  13.3 13.8 30.6 -76.9 94.1 69.7 -3.9  GLY-506   MET-507  10.1 10.3 35.5 3.6 65.4 96.3 6.0  MET-507   ASP-508  7.3 6.8 -40.0 28.0 43.9 19.6 39.0  ASP-508   VAL-509  7.4 7.0 -10.0 -11.4 87.1 79.3 22.1 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