Myosin A Tail Interacting 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
 LEU-145   ILE-146  7.6 7.3 -11.4 3.9 71.1 75.4 8.9
 ILE-146   LYS-147  5.3 5.4 -20.7 13.2 143.4 143.4 -10.1
 PHE-149   SER-150  2.7 1.4 13.5 -2.6 79.0 82.5 2.2
 SER-150   HIS-151  0.9 2.4 20.9 -8.2 39.4 32.4 17.2
 HIS-151   PHE-152  1.7 2.1 24.8 -22.3 103.2 98.7 6.0
 PHE-152   ASP-153  5.0 4.5 19.0 -1.2 134.0 133.8 -33.5
 ASP-153   ASN-154  5.2 5.8 -4.0 -19.0 122.8 111.4 -26.2
 ASN-154   ASN-155  8.1 9.4 39.9 -1.9 108.7 135.1 -45.8
 ASN-155   SER-156  10.5 10.7 30.2 19.1 123.6 100.7 -27.0
 SER-156   SER-157  7.9 11.2 -128.9 -90.1 7.8 80.2 -269.8
 SER-157   GLY-158  8.0 8.6 179.2 23.6 124.9 153.3 364.6
 GLY-158   PHE-159  4.7 6.2 -57.7 3.0 65.0 80.3 35.8
 PHE-159   LEU-160  4.9 5.0 24.1 -5.7 48.9 42.8 31.5

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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