Glutamine Phosphoribosylpyrophosphate Amidotransferase
(All numbering and residues are taken from first PDB file)
Bending Residue Dihedral Analysis
Residue
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
VAL-325
LYS-326
7.5
7.9
10.3
2.1
89.8
83.5
0.4
LYS-326
ASN-327
5.3
5.4
-8.7
10.1
54.0
52.2
3.2
ASN-327
ARG-328
1.8
1.9
-16.9
21.7
49.3
48.4
-3.7
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
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
ARG-343
LYS-344
8.5
7.5
179.7
17.8
67.8
113.3
-117.5
LYS-344
SER-345
6.8
4.2
165.1
10.4
30.1
51.2
164.0
SER-345
VAL-346
6.6
4.1
-8.0
-7.1
82.7
115.2
-2.3
VAL-346
ARG-347
5.0
1.6
2.3
7.9
90.8
40.4
6.3
ARG-347
ARG-348
1.5
1.6
-0.5
26.5
151.8
149.3
32.2
ARG-348
LYS-349
2.3
2.4
-22.2
9.3
133.4
122.6
-9.9
LYS-349
LEU-350
2.8
2.7
-15.5
-3.5
85.5
106.0
-4.7
LEU-350
ASN-351
3.8
3.6
25.4
9.2
115.2
101.1
-18.8
ASN-351
ALA-352
5.3
5.8
9.6
-27.7
87.8
102.7
8.9
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