Riboflavin Biosynthesis Protein Ribd

(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-135   LYS-136  1.7 2.1 7.3 -9.9 97.7 108.9 -48.9
 LYS-136   PHE-137  3.6 3.5 -19.4 27.7 136.7 132.2 47.9
 PHE-137   LEU-138  4.4 4.5 -2.2 10.3 99.1 95.9 1.6
 LEU-138   HIS-139  2.8 2.6 -17.0 6.3 43.2 46.7 53.0

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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