Bovine Mitochondrial F1-Atpase

(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  GLN-379   ASP-380  9.4 9.6 10.6 -14.2 103.5 98.6 8.2  ASP-380   TYR-381  7.0 7.0 0.2 11.3 80.3 82.8 -3.8  TYR-381   LYS-382  4.9 4.9 -6.9 4.3 166.0 166.8 3.3  LYS-382   SER-383  5.7 5.6 8.3 -19.6 68.5 66.3 24.1 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  ASP-400   LYS-401  2.8 2.6 -21.7 30.0 88.7 98.9 13.3  LYS-401   LEU-402  1.5 1.6 -22.3 14.3 125.6 123.6 34.2  LEU-402   THR-403  2.0 1.8 3.9 8.1 126.4 125.7 -52.1  THR-403   VAL-404  4.1 4.0 -22.1 15.2 50.9 64.2 98.4  VAL-404   SER-405  3.8 3.9 -3.1 -4.5 119.9 125.5 -34.1  SER-405   ARG-406  6.1 6.0 16.1 -9.4 90.9 88.3 0.0  ARG-406   ALA-407  8.0 7.8 -0.3 -1.8 29.3 32.3 4.3  ALA-407   ARG-408  8.6 8.5 9.6 -13.1 102.7 103.2 19.3 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