2-Succinylbenzoate--Coa Ligase

(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  LEU-380   ASP-381  9.0 9.7 -162.8 102.9 152.4 161.3 -68.0  ASP-385   LEU-386  1.7 3.2 61.0 -44.9 149.1 70.4 -24.1  LEU-386   ILE-387  1.9 2.1 10.4 -28.9 88.3 143.1 3.6  ILE-387   ILE-388  5.5 2.3 36.0 -25.3 162.6 90.3 -5.0  ILE-388   SER-389  6.8 5.1 18.4 -3.3 101.3 163.9 -12.4  SER-389   GLY-390  9.8 6.3 12.5 104.3 167.6 91.4 -11.0  GLY-390   GLY-391  11.2 8.4 -105.4 -163.9 61.8 39.6 122.7 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  GLU-411   ALA-412  21.9 18.8 -176.5 3.3 86.1 119.1 58.9  ALA-412   GLY-413  18.2 16.3 -9.0 18.3 125.8 83.0 11.5  GLY-413   VAL-414  15.7 12.8 7.9 10.8 91.4 53.0 30.0  VAL-414   SER-415  12.3 11.4 0.6 -22.5 56.8 99.9 -33.4  SER-415   GLY-416  11.4 9.5 25.1 49.4 96.2 53.3 -103.1  GLY-416   ALA-417  9.8 10.1 -18.6 -54.5 133.8 62.6 88.3  ALA-417   GLU-418  10.2 13.5 39.1 -0.9 115.9 45.5 -102.5  GLU-418   ASP-419  13.8 16.0 -20.9 -45.3 126.5 97.8 129.7 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