Structure-Based Docking and Interaction Analysis Dataset for ELMO2 Ligand Validation

This dataset contains the docking results and interaction analyses associated with the manuscript. The archive is organized into two folders and one supplementary data table, as described below.

1. Figure6D

This folder contains the structural data used to generate Figure 6D in the manuscript.

It includes:

The complete docking complex of ligand C52 with the representative ELMO2 receptor conformation (rep_8_78)(.pse format).

a PyMOL session files (.pse) with annotated protein–ligand interactions.

The PLIP (Protein–Ligand Interaction Profiler, v2.3.0) interaction analysis report generated using default parameters.

The docking pose shown in Figure 6D represents a docking-predicted binding mode derived from structure-based virtual screening and subsequent structural inspection.

2. Ligand_Pose_Data

This folder contains docking pose files for the 63 experimentally validated ligands.

For each ligand:

The complete protein–ligand complex is provided in PDBQT format.

Ligand and receptor coordinates are contained within the same coordinate system.

Docking poses correspond to the representative molecular dynamics-derived receptor conformations used in the screening workflow.

These files allow direct visualization of docking poses in PyMOL, ChimeraX-1.8, or other compatible molecular visualization software.

3. Supplementary_Table_1.xlsx

This Excel file summarizes key information for the 63 validated ligands, including:

ID

Ligand identifier (consistent with manuscript naming)

Molecular weight

Representative conformation

Docking score

Experimental viability data

This table enables direct comparison between computational docking results and experimental validation outcomes.

Notes on Docking Workflow

Docking scores were generated using a smina scoring function and were used as part of a multi-stage enrichment strategy. The docking results represent computational predictions intended to guide compound prioritization rather than quantitative binding affinity measurements.