Bni1 Protein

(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
 ALA-1398   PHE-1399  27.0 25.9 14.3 -15.5 68.9 61.0 -4.1
 PHE-1399   ALA-1400  26.3 25.7 79.0 -97.4 130.6 137.3 8.2
 ALA-1400   ALA-1401  25.3 24.3 20.4 16.4 68.5 80.2 7.1
 ALA-1401   ARG-1402  23.3 22.4 -152.3 -9.2 58.1 77.6 73.1
 ARG-1402   GLU-1403  20.9 18.7 56.0 -84.9 105.7 134.7 23.8
 GLU-1403   ILE-1404  18.8 17.1 101.9 -25.9 168.5 78.4 -46.8
 ILE-1404   LYS-1405  20.0 14.2 14.6 -120.8 121.2 50.7 52.3
 LYS-1405   SER-1406  17.5 11.7 22.9 91.6 108.3 72.4 63.1
 SER-1406   LEU-1407  17.5 13.2 -83.9 -22.6 131.5 151.7 -85.7
 LEU-1407   ALA-1408  16.7 12.3 -60.4 116.7 106.0 95.8 16.7
 ALA-1408   SER-1409  14.2 9.2 109.9 31.4 118.3 14.0 -69.1
 SER-1409   LYS-1410  11.9 9.7 139.9 25.8 81.0 76.4 -14.2
 LYS-1410   ARG-1411  12.7 6.1 1.9 171.5 31.8 67.0 126.3
 ARG-1411   LYS-1412  11.5 6.9 20.8 -6.8 90.3 24.5 9.6
 LYS-1417   ILE-1418  7.5 7.7 -48.4 -33.7 130.2 137.1 -48.4
 ILE-1418   THR-1419  9.6 7.4 30.1 -7.7 42.3 39.1 8.7

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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