pydangle top2018 MC: Per-residue backbone geometry for 13,677 mainchain-filtered protein chains

Read full text
Authors: Michael G. Prisant
Cited by: 0

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