Hypothetical Protein Ypl007c

(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
 GLN-397   SER-398  12.2 12.1 -2.9 7.1 37.4 38.3 -55.2
 SER-398   LEU-399  13.4 13.5 -0.8 2.6 63.0 63.0 -4.2
 LEU-399   PRO-400  11.4 11.5 -3.7 7.4 28.3 28.3 -18.6
 PRO-400   LYS-401  10.0 9.9 4.5 9.6 135.5 134.0 -222.3
 LYS-401   LEU-402  11.4 10.9 3.6 -10.9 100.4 89.9 67.2
 LEU-402   PRO-403  10.1 10.4 -14.6 9.8 35.9 37.5 252.1
 PRO-403   GLU-404  11.1 11.6 -13.4 19.2 99.7 104.4 -15.1
 GLU-404   ASN-405  14.8 15.4 -29.6 15.4 93.5 104.8 -33.8
 ASN-405   PHE-406  16.4 16.9 -4.0 25.5 109.9 116.0 248.3
 PHE-406   SER-407  13.6 13.8 -17.5 22.1 154.8 151.3 249.1
 SER-407   MET-408  15.0 15.3 -9.9 12.2 116.8 108.8 -371.8
 MET-408   ASN-409  13.7 13.9 6.8 -17.8 93.9 112.3 -40.5
 ASN-409   LYS-410  16.6 16.6 -3.3 5.3 13.8 10.4 -68.7
 LYS-410   LYS-411  16.2 15.8 -3.9 -4.4 75.3 75.6 66.7
 LYS-411   LEU-412  15.9 15.7 3.4 -3.6 109.0 109.9 16.0

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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