Table 5. Qualitative and quantitative assessment of the experimentally derived protein structures of CTD of AtWRKY4, and resolved through NMR(1WJ2) and with X-Ray diffracted crystal structure of AtWRKY4 complexed(2LEX) with our predicted models SolyWRKY33 (both NTD and CTD and SolyWRKY37).

The good quality protein models the values must ranges in between 0–1.5 (RESPROX). The most favoured region in the predicted structural models was found to occuied 100% (SolyWRKY33 NTD) (PROCHECK) compared to template where number of residues in outlier and disallowed region covered significant residues.

S.No	Protein Name	Q Mean Score	Z Score	RESPROX	Most Favored (%)	Additionally allowed (%)	Outlier residues (%)
1.	N-terminal WRKY33 (NP_001306910.1) DNA binding domain (Predicted Model)	0.687	-2.61	1.91	100.0	0.0	0.0
2.	C-terminal WRKY33 (NP_001306910.1) DNA binding domain (Predicted Model)	0.537	-3.05	2.342	98.4	1.6	0.0
3.	WRKY 37 (NP_001308885.1) DNA binding Domain (Predicted Model)	0.533	-2.03	1.154	98.3	1.7	0.0
4.	C-terminal Domain of AtWRKY4 (PDB:1WJ2) (NMR determined)	0.557	-3.02	2.274	89.9	5.8	4.3
5.	C-terminal Domain of AtWRKY1 (PDB:2AYD) (X-Ray Diffraction)	0.811	-3.37	1.204	100	0.0	0.0
6.	Complex of C-terminal Domain of AtWRKY4and W- box DNA (PDB:2LEX)	0.470	-2.94	2.793	77.0	14.8	8.2