pydangle top8000: Per-residue backbone geometry for 7,814 quality-filtered protein chains from the MolProbity reference dataset
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 1,568,561 quality-filtered protein residues from 7,814 chains in 7,607 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 Top8000 reference dataset (Williams et al., 2018, doi:10.1002/pro.3330), best-quality, 70% homology. Residue-level filtering by mainchain B-factor
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
- 16 March 2026
- Language
- EN
- Document type
- Dataset