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Dataset associated with “An in-frame deletion mutation in the degron tail of auxin co-receptor IAA2 confers resistance to the herbicide 2,4-D in Sisymbrium orientale”

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DataCite Commons2023-06-30 更新2024-07-13 收录
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https://mountainscholar.org/handle/10217/234027
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Output files from protein docking analysis of the wild-type IAA2 protein and the mutant IAA2 version containing a nine amino acid deletion. These residues were used as docking parameters in HADDOCK 2.4 (https://wenmr.science.uu.nl/haddock2.4/). Docking calculations were performed under expert level, deactivating the DNA/RNA functions and activating the Surface Contact Restrains to enforce contact between the molecules. Degron residues KNNN of SoIAA2 were assigned semiflexible properties during docking whereas the shorter connection in SoIAA2Δ9 was not allowed to be flexible to preserve the structural integrity of PB1. The binding affinities of the SoIAA2/TIR1 and SoIAA2Δ9/TIR1 biological complexes were calculated using PRODIGY (https://bianca.science.uu.nl/prodigy/) for all top 4 poses from the best HADDOCK clusters. Plots are in .html format and protein models are in .pdb format. Files are in TGZ after gzip compression.
提供机构:
Mountain Scholar
创建时间:
2021-10-29
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