5P16

Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 89

Summary for 5P16

Group depositionHigh-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits. (G_1002001)
Descriptorendothiapepsin (2 entities in total)
Functional Keywordsfragment screening, method development, aspartic protease, hydrolase
Biological sourceCryphonectria parasitica
Total number of polymer chains1
Total molecular weight33813.86
Authors
Schiebel, J.,Heine, A.,Klebe, G. (deposition date: 2016-06-28, release date: 2016-08-03, Last modification date: 2018-02-21)
Primary citation
Schiebel, J.,Krimmer, S.G.,Rower, K.,Knorlein, A.,Wang, X.,Park, A.Y.,Stieler, M.,Ehrmann, F.R.,Fu, K.,Radeva, N.,Krug, M.,Huschmann, F.U.,Glockner, S.,Weiss, M.S.,Mueller, U.,Klebe, G.,Heine, A.
High-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits.
Structure, 24:1398-1409, 2016
PubMed: 27452405 (PDB entries with the same primary citation)
DOI: 10.1016/j.str.2016.06.010
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.64 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.195000.4%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution