Maltodextrin-Binding Protein (Male178 Mutant)

(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
 PRO-107   ILE-108  8.8 8.5 1.2 -5.9 25.4 25.8 -13.5
 ILE-108   ALA-109  9.0 8.8 -1.8 21.2 135.0 133.2 25.5
 ALA-109   VAL-110  5.7 5.5 -2.9 -19.8 67.5 62.8 35.7
 VAL-110   GLU-111  1.9 1.9 13.4 -25.8 59.2 64.7 -4.8
 GLU-111   ALA-112  3.1 2.1 -5.1 7.3 83.1 69.3 7.3
 ALA-112   LEU-113  5.2 5.1 18.6 10.1 47.4 49.5 44.9
 LEU-113   SER-114  8.6 8.6 2.6 0.9 44.6 43.3 -9.3

Downloading Image

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
 PHE-258   VAL-259  7.8 7.3 12.8 -17.2 118.6 123.2 -2.0
 VAL-259   GLY-260  4.2 3.9 -2.1 16.4 127.5 115.5 16.4
 GLY-260   VAL-261  2.8 1.9 -5.0 -16.2 60.0 65.7 34.1
 VAL-261   LEU-262  3.1 2.7 11.1 -9.1 76.9 80.1 20.4

Downloading Image

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
 GLU-309   GLU-310  10.6 10.1 18.6 -12.8 32.0 31.2 14.8
 GLU-310   LEU-311  9.4 9.2 -1.5 -0.8 85.6 94.1 6.3
 LEU-311   ALA-312  6.1 5.8 10.7 -11.2 81.6 76.5 -13.8
 ALA-312   LYS-313  5.9 5.1 15.5 15.0 26.1 12.6 55.1
 LYS-313   ASP-314  5.5 5.0 9.1 -18.2 78.2 83.2 27.5
 ASP-314   PRO-315  1.8 1.3 -16.4 -6.5 66.2 57.1 31.9
 PRO-315   ARG-316  2.9 4.1 25.0 -15.8 140.2 138.5 -8.6
 ARG-316   ILE-317  3.1 3.8 0.9 2.6 151.4 145.7 -11.1

Downloading Image

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-326   GLY-327  11.5 11.7 9.3 5.9 30.1 37.1 32.0
 GLY-327   GLU-328  9.9 9.7 -23.2 34.1 136.6 154.9 29.9
 GLU-328   ILE-329  8.1 8.7 -18.3 17.8 104.7 99.9 -8.4
 ILE-329   MET-330  4.6 5.2 9.2 -11.4 26.1 50.4 -2.9
 MET-330   PRO-331  4.4 4.2 -35.2 16.3 140.0 154.3 -42.1
 PRO-331   ASN-332  3.6 3.9 -30.4 2.3 100.3 103.4 8.9

Downloading Image

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