Peptidyl-Prolyl Cis-Trans Isomerase

(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  GLU-35   ARG-36  3.8 4.5 8.6 0.6 105.5 99.3 0.3  ARG-36   PRO-37  3.0 2.6 0.9 9.0 74.1 75.6 5.1  PRO-37   SER-38  2.3 1.6 149.9 110.8 46.1 34.6 243.3  SER-38   GLY-39  4.7 3.8 -34.3 -173.7 122.9 79.3 -214.1  LYS-46   ASN-47  14.7 17.0 -161.7 50.1 32.0 75.0 -159.1  ASN-47   GLY-48  17.4 20.5 -144.9 173.3 78.6 44.2 -18.9  GLY-48   GLN-49  19.9 19.8 14.5 136.4 86.9 149.4 188.3  GLN-49   GLY-50  17.9 18.9 56.7 -3.7 142.6 93.1 -57.1  GLY-50   GLU-51  18.3 15.3 -165.4 -7.5 88.6 58.8 -41.6  GLU-51   PRO-52  17.4 15.0 -10.9 10.2 116.9 135.6 -3.6 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