Penicillin Amidase Alpha Subunit

(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
 VAL-134   ALA-135  20.5 20.2 4.6 -2.5 104.6 103.7 30.1
 ALA-135   MET-136  16.7 16.5 4.4 -8.9 132.9 133.2 -36.9
 MET-136   ILE-137  17.1 16.8 -3.3 4.0 19.6 19.7 -11.3
 ILE-137   PHE-138  18.6 18.4 -6.4 5.5 63.7 65.8 56.9
 PHE-138   VAL-139  15.3 15.2 7.8 -3.8 91.0 94.2 -59.1
 VAL-139   GLY-140  13.0 12.9 -0.7 -2.0 48.3 41.7 67.0
 GLY-140   THR-141  15.1 15.2 -10.6 -5.1 12.0 18.5 198.9
 THR-141   MET-142  14.6 15.2 67.6 -62.3 98.2 108.4 -71.9
 MET-142   ALA-143  11.5 12.0 -15.7 21.6 107.6 99.9 -31.4
 ALA-143   ASN-144  9.2 9.2 27.9 -20.0 106.7 112.5 -125.4
 ASN-144   ARG-145  11.3 11.0 -4.0 21.6 16.2 4.1 -389.0
 ARG-145   PHE-146  11.9 11.5 21.6 -35.3 121.5 116.2 210.6
 PHE-146   SER-147  9.4 8.2 -8.7 5.6 105.5 116.5 108.0
 SER-147   ASP-148  6.1 5.5 -11.1 5.9 108.7 109.5 52.6
 ASP-148   SER-149  7.6 7.5 -7.4 -0.8 37.2 43.3 119.2
 SER-149   THR-150  7.5 7.4 13.7 -13.4 87.6 87.1 -19.5
 THR-150   SER-151  9.3 9.2 4.0 -3.7 122.2 121.0 -8.7
 SER-151   GLU-152  12.2 12.2 0.4 2.7 81.9 83.7 26.1
 GLU-152   ILE-153  13.7 13.7 -1.2 8.0 85.1 83.2 -55.9

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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