L-3-Hydroxyacyl-Coa Dehydrogenase

(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  VAL-197   SER-198  4.4 3.7 -39.0 36.3 152.5 154.1 -17.7  SER-198   CYS-199  6.4 5.9 -27.4 40.2 137.8 133.4 87.0  CYS-199   LYS-200  6.1 5.0 6.8 2.0 35.1 28.3 69.4  LYS-200   ASP-201  7.0 6.4 -19.4 -1.4 118.5 121.3 -112.4  ASP-201   THR-202  4.6 4.3 14.7 -17.9 48.8 44.8 -5.1  THR-202   PRO-203  4.3 3.7 0.4 5.6 99.1 96.3 -15.6  PRO-203   GLY-204  3.6 3.4 -2.3 -7.0 36.4 35.5 52.8  GLY-204   PHE-205  5.0 4.8 4.4 -0.1 143.3 144.0 -22.4  PHE-205   ILE-206  3.5 3.3 1.2 2.1 119.3 115.4 -5.0  ILE-206   VAL-207  6.0 6.0 -12.1 3.0 80.2 84.3 4.2  VAL-207   ASN-208  7.1 7.5 6.4 8.0 42.8 39.8 73.4 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