Dear Kyle, interesting finding - worth looking into!
According to Wlodawer et al (2024) (https://journals.iucr.org/m/issues/2024/06/00/be5300/index.html) ,"An analysis of the contents of the PDB indicated that the expected ratio of the number of water molecules to the number of amino-acid residues exceeds 1.5 in atomic resolution structures, decreasing to 0.25 at around 2.5 Å resolution." So I'd expect your structure to have around 800 residues, is that about right? A lot may depend on the details of data processing ... which program; is there anisotropy? How did you determine/perform the high-resolution cutoff? Could you go to higher resolution? Do you have other datasets from the same project - do they show the same behaviour? I can imagine refinement/water-adding workflows where some atoms have surprising B-values e.g. TLS refinement mistakenly leading to anisotropic B-values, or waters being deleted and re-added with a default B-value of 16. Could you give details? As a simple test, just remove any lines from your PDB file except the ATOM, HETATM, DISU and the CRYST1 and END records. Then refine with a standard Refmac protocol and check the B-values afterwards. HTH, Kay ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
