Spike Glycoprotein

(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-324   SER-325  5.5 9.0 -3.7 40.5 127.3 149.6 42.7  SER-325   ILE-326  8.1 8.0 -46.6 -58.7 81.4 105.6 -21.7  ILE-326   VAL-327  10.7 5.3 -30.9 -31.3 106.9 172.9 -66.8  VAL-327   ARG-328  10.6 4.4 0.4 42.5 35.7 64.9 56.6  ARG-328   PHE-329  10.7 3.1 -13.4 11.4 100.7 167.5 -18.9  PHE-329   PRO-330  9.2 3.1 35.8 6.0 34.9 77.6 30.8  PRO-330   ASN-331  9.0 5.5 -145.3 -98.9 101.7 87.5 37.8  ASN-331   ILE-332  11.4 7.3 66.8 68.1 28.0 23.8 -231.2 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  LYS-528   LYS-529  4.2 3.2 -28.0 108.3 145.7 158.5 78.5  LYS-529   SER-530  5.1 4.0 -46.3 158.9 139.4 116.2 87.3  SER-530   THR-531  4.3 1.7 39.2 -21.6 67.5 14.5 -346.3  THR-531   ASN-532  2.9 1.6 38.4 71.5 46.0 62.4 125.1  ASN-532   LEU-533  0.6 2.1 -31.9 5.4 125.0 99.1 10.4 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