Cystathionine Beta-Synthase

(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
 LYS-394   GLY-395  11.7 11.8 -2.9 -4.9 21.9 14.5 15.2
 GLY-395   PHE-396  11.7 11.4 16.7 -0.6 114.8 114.1 -9.2
 PHE-396   LEU-397  10.2 9.9 -28.3 -13.5 46.2 37.1 60.1
 LEU-397   LYS-398  6.9 6.8 156.6 146.6 152.7 119.1 89.2
 LYS-398   GLU-399  6.5 7.9 -61.7 33.6 77.5 43.4 4.5
 GLU-399   GLU-400  7.7 5.7 76.3 108.0 144.3 109.7 -307.3
 GLU-400   ASP-401  7.1 8.1 -23.2 -47.0 90.1 117.1 -5.8
 TRP-408   TRP-409  20.8 20.7 5.6 -10.9 64.3 77.1 -5.7
 TRP-409   TRP-410  22.1 22.1 5.2 0.7 72.3 66.2 5.7

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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