pydangle top2018 MC: Per-residue backbone geometry for 13,677 mainchain-filtered protein chains
Abstract
Per-residue backbone geometry (phi, psi, omega, tau), Ramachandran classifications at four granularities (6/5/4/3-class), DSSP secondary structure, peptide bond type, and chirality for 2,963,303 quality-filtered protein residues from 13,677 chains in 13,308 high-resolution, low-redundancy protein structures. Computed using pydangle-biopython v0.5.1 on "ersatz" full-structure PDB files with NQH flip corrections from Reduce 4.16. Source data from the Richardson Lab top2018 dataset (Williams et al., 2021, doi:10.1002/pro.4239), mainchain-filtered, 70% homology, 60% completeness. See README.md for full methodology.
Fields of Study & Subjects
Protein Structure and Dynamics
Enzyme Structure and Function
RNA and protein synthesis mechanisms
Publication details
- Journal / source
- Zenodo (CERN European Organization for Nuclear Research)
- Publication date
- 15 March 2026
- Language
- EN
- Document type
- Dataset