Cytochrome B6-F Complex Iron-Sulfur Subunit

(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  PRO-45   SER-46  23.4 23.3 -15.1 12.2 110.2 119.0 -51.1  SER-46   GLY-47  20.8 21.1 -34.5 -34.9 80.8 79.9 138.2  GLY-47   GLY-48  18.8 19.4 55.3 58.6 65.7 41.6 358.3  GLY-48   ALA-49  20.3 18.2 -99.9 68.4 148.5 112.1 -182.8  ALA-49   VAL-50  22.7 22.1 -102.7 -21.8 135.0 141.0 -481.7  THR-54   THR-55  17.7 17.4 10.5 -1.5 111.1 136.1 -173.9  THR-55   ALA-56  18.3 18.2 -42.0 48.1 50.3 44.4 -15.0  ALA-56   LYS-57  15.8 15.7 1.2 -16.1 161.9 161.9 81.9 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