Fibrinogen 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  LYS-111   PHE-112  5.9 6.2 57.1 -52.9 17.3 35.3 41.7  PHE-112   SER-113  3.9 4.1 -1.0 7.9 131.3 142.0 25.5  SER-113   ASP-114  7.3 6.9 3.6 -11.0 87.8 75.1 -2.1  ASP-114   THR-115  9.2 9.1 12.6 1.6 57.0 64.8 57.6  THR-115   SER-116  7.6 7.2 -9.7 3.6 167.4 166.2 -49.3  SER-116   THR-117  6.3 5.5 35.3 -34.6 60.5 57.7 57.6  THR-117   THR-118  9.9 9.2 -3.5 -4.5 101.7 94.8 4.0  THR-118   MET-119  11.6 10.9 38.2 -36.6 38.5 52.0 21.3 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