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).
收藏NIAID Data Ecosystem2026-03-10 收录
数据链接：
https://figshare.com/articles/dataset/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_an/6201482数据链接链接失效反馈
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资源简介：
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.
创建时间：
2018-05-01
