Fibrin Beta Chain

(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
 CYS-218   THR-219  4.1 4.1 6.9 -12.2 150.3 147.2 23.5
 THR-219   VAL-220  3.6 3.4 -9.7 11.2 51.3 48.1 9.5
 VAL-220   ASN-221  3.0 3.0 5.9 2.0 151.2 146.6 -116.1

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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