 |
PDBsum entry 2a06
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
2a06
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
443 a.a.
|
 |
|
|
|
|
|
|
|
424 a.a.
|
 |
|
|
|
|
|
|
|
365 a.a.
|
 |
|
|
|
|
|
|
|
241 a.a.
|
 |
|
|
|
|
|
|
|
196 a.a.
|
 |
|
|
|
|
|
|
|
99 a.a.
|
 |
|
|
|
|
|
|
|
75 a.a.
|
 |
|
|
|
|
|
|
|
66 a.a.
|
 |
|
|
|
|
|
|
|
42 a.a.
|
 |
|
|
|
|
|
|
|
30 a.a.
|
 |
|
|
|
|
|
|
|
62 a.a.
|
 |
|
|
|
|
|
|
|
|
×6
|
 |
|
|
|
|
|
|
|
×11
|
 |
|
|
|
|
|
|
|
×4
|
 |
|
|
|
|
|
|
|
×74
|
 |
|
|
|
|
|
|
|
×5
|
 |
|
|
|
|
|
|
|
×4
|
 |
|
|
|
|
|
|
|
×2
|
 |
|
|
|
|
|
|
|
×2
|
 |
|
|
|
|
|
|
|
×4
|
 |
|
|
|
|
|
|
|
×7
|
 |
|
|
|
|
|
|
|
×2
|
 |
|
|
|
|
|
|
|
×2
|
 |
|
|
|
|
|
|
|
|
|
Generate full PROCHECK analyses
|
PROCHECK summary for 2a06
Ramachandran plot
PROCHECK statistics
1. Ramachandran Plot statistics
No. of
residues %-tage
------ ------
Most favoured regions [A,B,L] 3223 92.6%
Additional allowed regions [a,b,l,p] 239 6.9%
Generously allowed regions [~a,~b,~l,~p] 13 0.4%
Disallowed regions [XX] 7 0.2%*
---- ------
Non-glycine and non-proline residues 3482 100.0%
End-residues (excl. Gly and Pro) 46
Glycine residues 265
Proline residues 207
----
Total number of residues 4000
Based on an analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20.0 a good
quality model would be expected to have over 90% in the most favoured regions [A,B,L].
2. G-Factors
Average
Parameter Score Score
--------- ----- -----
Dihedral angles:-
Phi-psi distribution 0.04
Chi1-chi2 distribution 0.05
Chi1 only 0.18
Chi3 & chi4 0.50
Omega 0.53
0.26
=====
Main-chain covalent forces:-
Main-chain bond lengths 0.63
Main-chain bond angles 0.38
0.48
=====
OVERALL AVERAGE 0.35
=====
G-factors provide a measure of how unusual, or out-of-the-ordinary, a property is.
Values below -0.5* - unusual
Values below -1.0** - highly unusual
Important note: The main-chain
bond-lengths and bond angles are compared with
the Engh & Huber (1991) ideal values derived
from small-molecule data. Therefore, structures
refined using different restraints may show
apparently large deviations from normality.
|
|
 |