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
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

Structure validation

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