Generated banner for Molecular Dynamics
Generated logo for Molecular Dynamics

Molecular Dynamics

K-DenseCommunityCreated by Kuan-lin HuangDistributed by K-Dense

  • Skill
  • Tool integration
  • Science and research
  • MIT
  • Low risk

From the author

Runs and analyzes molecular dynamics simulations with OpenMM and MDAnalysis. Sets up protein/small molecule systems, defines force fields, runs energy minimization and production MD, and analyzes trajectories (RMSD, RMSF, contact maps, free energy surfaces). For structural biology, drug binding, and biophysics.
— the description by Kuan-lin Huang

AutoGineer summary

Written by AutoGineer from the skill’s own files, not by the author

This skill provides a structured workflow for conducting molecular dynamics (MD) simulations and analyzing the resulting trajectories. It leverages OpenMM for high-performance simulation, including system preparation, energy minimization, and equilibration (NVT/NPT), and MDAnalysis for post-simulation structural analysis such as RMSD, RMSF, and contact mapping. The skill emphasizes scientific rigor, requiring users to validate system construction, force field selection, and simulation parameters before execution.

What it does

  • Prepares protein and ligand systems for simulation including solvation and ionization.
  • Performs energy minimization to resolve steric clashes.
  • Executes NVT and NPT equilibration stages to stabilize the system.
  • Runs production MD simulations with checkpointing.
  • Calculates structural metrics like RMSD and RMSF to assess stability and flexibility.
  • Analyzes protein-ligand interactions through contact mapping.

When to use it

  • When investigating the stability of protein structures or the effect of mutations.
  • When characterizing the binding mode or residence time of small molecule ligands.
  • When exploring conformational sampling and protein flexibility.
  • When calculating binding free energies or analyzing protein-protein interfaces.

Advantages

  • Integrates high-performance GPU-accelerated simulation with flexible analysis tools.
  • Provides a modular, reproducible workflow for complex biophysical modeling.
  • Supports standard force fields and common trajectory formats.
  • Includes built-in validation steps to ensure simulation quality.

Usage examples

“Prepare an OpenMM system from a cleaned PDB file using the AMBER14 force field.”
The agent will initialize the system, add hydrogens, solvate with TIP3P water, and return the topology and system objects ready for minimization.
“Calculate the RMSD of the protein backbone over a simulation trajectory.”
The agent will load the trajectory, perform an alignment to the reference structure, compute the RMSD for the backbone atoms, and generate a plot.

Install

  1. Download the skill as a ZIP:

    https://mp-staging.autogineer.com/agent-skills/k-dense-ai/molecular-dynamics/download
  2. Unzip it into the cross-client skills folder of your project:

    mkdir -p .agents/skills && unzip molecular-dynamics.zip -d .agents/skills

Documentation by Kuan-lin Huang

Molecular Dynamics

Overview

Molecular dynamics (MD) simulation computationally models the time evolution of molecular systems by integrating Newton's equations of motion. This skill covers two complementary tools:

  • OpenMM (https://openmm.org/): High-performance MD simulation engine with GPU support, Python API, and flexible force field support

  • MDAnalysis (https://mdanalysis.org/): Python library for reading, writing, and analyzing MD trajectories from all major simulation packages

Reviewed versions: OpenMM 8.6.1 and MDAnalysis 2.10.0. Reference-platform smoke checks use small synthetic systems; GPU performance and scientific convergence are not established by them. OpenMM latest API pages identify a development build, so the installed 8.6.1 API is the executable reference.

Installation into a dedicated environment:

uv venv --python 3.12 .venv-md
uv pip install --python .venv-md/bin/python "openmm==8.6.1" "MDAnalysis==2.10.0" matplotlib pandas
# Windows: use .venv-md/Scripts/python.exe instead

When to Use This Skill

Use molecular dynamics when:

  • Protein stability analysis: How does a mutation affect protein dynamics?

  • Drug binding simulations: Characterize binding mode and residence time of a ligand

  • Conformational sampling: Explore protein flexibility and conformational changes

  • Protein-protein interaction: Model interface dynamics and binding energetics

  • RMSD/RMSF analysis: Quantify structural fluctuations from a reference structure

  • Free energy estimation: Compute binding free energy or conformational free energy

  • Membrane simulations: Model proteins in lipid bilayers

  • Intrinsically disordered proteins: Study IDR conformational ensembles

Core Workflow: OpenMM Simulation

Examples require system-specific preparation and validation. Review biological assembly, alternate locations, missing loops, termini, protonation, disulfides, ligands and cofactors before parameterization. An MD trajectory alone does not establish binding free energy or residence time.

The functions below form one Python module: execute their import blocks together. Use a new output prefix for every stage to avoid overwriting earlier results.

1. System Preparation
from openmm.app import *
from openmm import *
from openmm.unit import *

def prepare_system_from_pdb(pdb_file, forcefield_name="amber14-all.xml",
                              water_model="amber14/tip3pfb.xml", ph=7.0):
    """
    Prepare an OpenMM system from a PDB file.

    Args:
        pdb_file: Path to cleaned PDB file (use PDBFixer for raw PDB files)
        forcefield_name: Force field XML file
        water_model: Water model XML file

    Returns:
        modeller, system
    """
    # Load PDB
    pdb = PDBFile(pdb_file)

    # Load force field
    forcefield = ForceField(forcefield_name, water_model)

    # Add hydrogens and solvate
    modeller = Modeller(pdb.topology, pdb.positions)
    modeller.addHydrogens(forcefield, pH=ph)

    # TIP3P geometry also serves TIP3P-FB; XML supplies the parameters.
    # 10 Å padding; added salt excludes neutralizing counterions.
    modeller.addSolvent(
        forcefield,
        model='tip3p',
        padding=10*angstroms,
        ionicStrength=0.15*molar, neutralize=True
    )

    print(f"System: {modeller.topology.getNumAtoms()} atoms, "
          f"{modeller.topology.getNumResidues()} residues")

    # Create system
    system = forcefield.createSystem(
        modeller.topology,
        nonbondedMethod=PME,         # Particle Mesh Ewald for long-range electrostatics
        nonbondedCutoff=1.0*nanometer,
        constraints=HBonds,           # Constrain bonds involving H (not intermolecular H-bonds)
        rigidWater=True,
        ewaldErrorTolerance=0.0005
    )

    return modeller, system
2. Energy Minimization
from openmm.app import *
from openmm import *
from openmm.unit import *

def minimize_energy(modeller, system, output_pdb="minimized.pdb",
                     max_iterations=1000, tolerance=10.0, platform_name=None):
    """
    Energy minimize the system to remove steric clashes.

    Args:
        modeller: Modeller object with topology and positions
        system: OpenMM System
        output_pdb: Path to save minimized structure
        max_iterations: Maximum minimization steps
        tolerance: Convergence criterion in kJ/mol/nm

    Returns:
        simulation object with minimized positions
    """
    # Keep the integrator at 2 fs for the subsequent NVT/NPT examples.
    integrator = LangevinMiddleIntegrator(300*kelvin, 1/picosecond, 0.002*picoseconds)

    # Automatic platform selection, or an explicit tested platform (e.g. CPU).
    # A registered GPU plugin does not prove a working device or driver.
    platform = Platform.getPlatformByName(platform_name) if platform_name else None
    simulation = Simulation(modeller.topology, system, integrator, platform)
    simulation.context.setPositions(modeller.positions)

    # Check initial energy
    state = simulation.context.getState(getEnergy=True)
    print(f"Initial energy: {state.getPotentialEnergy()}")

    # Minimize
    simulation.minimizeEnergy(
        tolerance=tolerance*kilojoules_per_mole/nanometer,
        maxIterations=max_iterations
    )

    state = simulation.context.getState(getEnergy=True, getPositions=True)
    print(f"Minimized energy: {state.getPotentialEnergy()}")

    # Save minimized structure
    with open(output_pdb, 'w') as f:
        PDBFile.writeFile(simulation.topology, state.getPositions(), f)

    return simulation
3. NVT Equilibration
from openmm.app import *
from openmm import *
from openmm.unit import *

def run_nvt_equilibration(simulation, n_steps=50000, temperature=300,
                            report_interval=1000, output_prefix="nvt"):
    """
    NVT equilibration: constant N, V, T.
    Equilibrate velocities to target temperature.

    Args:
        simulation: OpenMM Simulation (after minimization)
        n_steps: Number of MD steps (50000 × 2fs = 100 ps)
        temperature: Temperature in Kelvin
        report_interval: Steps between data reports
        output_prefix: File prefix for trajectory and log
    """
    # This example is unrestrained; add validated restraints before Context creation.
    if any("Barostat" in type(f).__name__ and f.getFrequency() > 0
           for f in simulation.system.getForces()):
        raise ValueError("NVT requires all barostats disabled or absent")

    # Set both the thermostat target and initial velocities.
    simulation.integrator.setTemperature(temperature*kelvin)
    simulation.context.setVelocitiesToTemperature(temperature*kelvin)

    # Add reporters
    simulation.reporters = []

    # Log file
    simulation.reporters.append(
        StateDataReporter(
            f"{output_prefix}_log.txt",
            report_interval,
            step=True,
            potentialEnergy=True,
            kineticEnergy=True,
            temperature=True,
            volume=True,
            speed=True
        )
    )

    # DCD trajectory (compact binary format)
    simulation.reporters.append(
        DCDReporter(f"{output_prefix}_traj.dcd", report_interval)
    )

    duration = (n_steps * simulation.integrator.getStepSize()).value_in_unit(picoseconds)
    print(f"Running NVT equilibration: {n_steps} steps ({duration:.1f} ps)")
    simulation.step(n_steps)
    print("NVT equilibration complete")

    return simulation
4. NPT Equilibration and Production

Call this function first with a dedicated NPT equilibration prefix. Inspect density, energy, structure and replicate stability before a separate production call; the default duration is an example, not an equilibration or convergence criterion.

def run_npt_production(simulation, n_steps=500000, temperature=300, pressure=1.0,
                        report_interval=5000, output_prefix="npt"):
    """
    NPT production run: constant N, P, T.

    Args:
        n_steps: Production steps (500000 × 2fs = 1 ns)
        temperature: Temperature in Kelvin
        pressure: Pressure in bar
        report_interval: Steps between reports
    """
    # Keep the Langevin thermostat and barostat at the same temperature.
    simulation.integrator.setTemperature(temperature*kelvin)
    system = simulation.system
    barostats = [f for f in system.getForces() if "Barostat" in type(f).__name__]
    if not system.usesPeriodicBoundaryConditions():
        raise ValueError("NPT requires a periodic system")
    if not barostats:
        system.addForce(MonteCarloBarostat(pressure*bar, temperature*kelvin, 25))
        simulation.context.reinitialize(preserveState=True)
    elif len(barostats) != 1 or not isinstance(barostats[0], MonteCarloBarostat):
        raise ValueError("This example supports one isotropic MonteCarloBarostat")
    else:
        barostats[0].setDefaultPressure(pressure*bar)
        barostats[0].setDefaultTemperature(temperature*kelvin)
        barostats[0].setFrequency(25)
    # Existing Context parameters must also be updated on repeated calls.
    simulation.context.setParameter(MonteCarloBarostat.Pressure(), pressure)
    simulation.context.setParameter(MonteCarloBarostat.Temperature(), temperature)

    # Update reporters
    simulation.reporters = []
    simulation.reporters.append(
        StateDataReporter(
            f"{output_prefix}_log.txt",
            report_interval,
            step=True,
            potentialEnergy=True,
            temperature=True,
            density=True,
            speed=True
        )
    )
    simulation.reporters.append(
        DCDReporter(f"{output_prefix}_traj.dcd", report_interval)
    )

    # Save checkpoints
    simulation.reporters.append(
        CheckpointReporter(f"{output_prefix}_checkpoint.chk", 50000)
    )

    duration = (n_steps * simulation.integrator.getStepSize()).value_in_unit(nanoseconds)
    print(f"Running NPT stage: {n_steps} steps ({duration:.3f} ns)")
    simulation.step(n_steps)
    simulation.saveCheckpoint(f"{output_prefix}_checkpoint.chk")
    simulation.saveState(f"{output_prefix}_state.xml")
    print("NPT stage complete")
    return simulation

Trajectory Analysis with MDAnalysis

1. Load Trajectory

Use the solvated topology with exactly the DCD atom count and order (e.g. the minimized.pdb above), not the original unsolvated input. MDAnalysis converts lengths to Å and time to ps by default; OpenMM bare coordinates use nm. Preserve frame box vectors and actual timestamps; do not infer time from frame number.

import MDAnalysis as mda
from MDAnalysis.analysis import rms, align, contacts
import numpy as np
import matplotlib.pyplot as plt

def load_trajectory(topology_file, trajectory_file):
    """
    Load an MD trajectory with MDAnalysis.

    Args:
        topology_file: PDB, PSF, or other topology file
        trajectory_file: DCD, XTC, TRR, or other trajectory
    """
    u = mda.Universe(topology_file, trajectory_file)
    print(f"Universe: {u.atoms.n_atoms} atoms, {u.trajectory.n_frames} frames")
    first, last = u.trajectory[0].time, u.trajectory[-1].time
    print(f"Time range: {first:g} to {last:g} ps")
    u.trajectory[0]
    return u
2. RMSD Analysis
def compute_rmsd(u, selection="backbone", reference_frame=0):
    """
    Compute RMSD of selected atoms relative to reference frame.

    Args:
        u: MDAnalysis Universe
        selection: Atom selection string (MDAnalysis syntax)
        reference_frame: Frame index for reference structure

    Returns:
        numpy array with columns [frame index, time in ps, RMSD in Angstroms]
    """
    # RMSD performs its own fit; avoid rotating the stored trajectory here.
    # Make the selected molecule whole before analysis of periodic trajectories.
    R = rms.RMSD(u, select=selection, ref_frame=reference_frame)
    R.run()

    rmsd_data = R.results.rmsd  # columns: frame, time, RMSD
    return rmsd_data

def plot_rmsd(rmsd_data, title="RMSD over time", output_file="rmsd.png"):
    """Plot RMSD over simulation time."""
    fig, ax = plt.subplots(figsize=(10, 4))
    ax.plot(rmsd_data[:, 1] / 1000, rmsd_data[:, 2], 'b-', linewidth=0.5)
    ax.set_xlabel("Time (ns)")
    ax.set_ylabel("RMSD (Å)")
    ax.set_title(title)
    ax.axhline(rmsd_data[:, 2].mean(), color='r', linestyle='--',
               label=f'Mean: {rmsd_data[:, 2].mean():.2f} Å')
    ax.legend()
    plt.tight_layout()
    plt.savefig(output_file, dpi=150)
    return fig
3. RMSF Analysis (Per-Residue Flexibility)

Make molecules whole and align a separate structural-analysis copy before RMSF; RMSF does not align. Do not run periodic contacts on a rotated trajectory whose box was not rotated. See analysis reference for alignment, PCA, DSSP, hydrogen bonds and population-derived free energy.

def compute_rmsf(u, selection="protein and name CA", start_frame=0):
    """
    Compute per-residue RMSF (flexibility).

    Returns:
        residue_keys, rmsf_values; keys are (resindex, segid, resid, resname)
    """
    # Select atoms
    atoms = u.select_atoms(selection)

    if not len(atoms):
        raise ValueError("RMSF selection is empty")
    # A multi-atom selection returns mean atomic RMSF, not COM RMSF.
    R = rms.RMSF(atoms)
    R.run(start=start_frame)

    # Average by residue
    resids = []
    rmsf_per_res = []
    for res in u.select_atoms(selection).residues:
        res_atoms = res.atoms.intersection(atoms)
        if len(res_atoms) > 0:
            resids.append((res.ix, res.segid, res.resid, res.resname))
            # RMSF is indexed within the selected AtomGroup, not the Universe.
            rmsf_per_res.append(R.results.rmsf[atoms.resindices == res.ix].mean())

    return resids, np.array(rmsf_per_res)
4. Protein-Ligand Contacts
def analyze_contacts(u, protein_sel="protein", ligand_sel="resname LIG",
                      radius=4.5, start_frame=0, periodic=True):
    """
    Track protein-ligand contacts over trajectory.

    Args:
        radius: Atom-pair cutoff in Angstroms; any pair defines a residue contact.
        periodic: Require box data and use minimum-image distances.
    Returns sets of (resindex, segid, resid, resname), one per analyzed frame.
    """
    from MDAnalysis.lib.distances import distance_array

    protein = u.select_atoms(protein_sel)
    ligand = u.select_atoms(ligand_sel)

    if not len(protein) or not len(ligand):
        raise ValueError("Protein and ligand selections must both be nonempty")
    if not np.isfinite(radius) or radius <= 0:
        raise ValueError("radius must be finite and positive")
    contact_frames = []
    for ts in u.trajectory[start_frame:]:
        if periodic and (ts.dimensions is None or not np.all(np.isfinite(ts.dimensions))
                         or np.any(ts.dimensions[:3] <= 0)):
            raise ValueError("Periodic contacts require valid frame box dimensions")
        # This includes hydrogen atoms unless the caller selects heavy atoms.
        distances = contacts.contact_matrix(
            distance_array(protein.positions, ligand.positions, box=ts.dimensions if periodic else None),
            radius,
        )
        contact_residues = set()
        for i in range(distances.shape[0]):
            if distances[i].any():
                res = protein[i].residue
                contact_residues.add((res.ix, res.segid, res.resid, res.resname))
        contact_frames.append(contact_residues)

    return contact_frames

Force Fields and Preparation

Choose a validated protein/ligand/water/ion combination for the scientific system. The working example retains AMBER14/TIP3P-FB; it is not a universal recommendation. Current OpenMM also bundles amber19-all.xml (ff19SB, DNA OL21, RNA OL3, lipid21), and charmm36_2024.xml with its own charmm36_2024/water.xml. Generic TIP3P and CHARMM-modified TIP3P are not interchangeable. IDP ensembles are especially sensitive to protein-water balance. Four-site waters need extra particles and a matching Modeller geometry, unlike the three-site example above.

AMBER protein XML does not parameterize arbitrary ligands. Use a reviewed GAFF2 or OpenFF route with explicit stereochemistry, protonation, bond orders, atom mapping and charge method. A ligand-only Interchange is not a protein-ligand system. See preparation reference for conservative PDBFixer and OpenFF examples, installation requirements and current release details.

Validation and Provenance

  • Start with minimization; finite energy does not establish a valid structure.

  • Use staged NVT → NPT equilibration → production. This example has no restraints.

  • A 2 fs step with constrained H-containing bonds is a starting choice. Larger steps/HMR require integrator, stability and observable validation for that system.

  • Use per-frame boxes for periodic distances. Make molecules whole for structural observables using trusted bond topology; unwrapping cannot infer missing bonds.

  • Assess burn-in, autocorrelation, effective samples, replicas and uncertainties. Short stable temperature/density traces do not establish conformational sampling.

  • Save topology/atom order, System/Integrator XML, force-field files/versions, seeds, platform/precision, parameters and analysis selections. Checkpoints are platform/hardware/version specific; XML states are more portable but do not retain all internal random-generator state. Test restarting the actual setup.

Additional Resources

Files

references/mdanalysis_analysis.md

MDAnalysis Analysis Reference

Reviewed against MDAnalysis 2.10.0 on 2026-10-01. Examples use local topology and trajectory files and are illustrative outside the synthetic regression checks. Atom order, molecule integrity, box vectors and time units must be checked first.

MDAnalysis Universe and AtomGroup

import MDAnalysis as mda

# Load Universe
u = mda.Universe("topology.pdb", "trajectory.dcd")
# or for single structure:
u = mda.Universe("structure.pdb")

# Key attributes
print(u.atoms.n_atoms)          # Total atoms
print(u.residues.n_residues)    # Total residues
print(u.trajectory.n_frames)   # Number of frames
print(u.trajectory.dt)         # Time step in ps
print(u.trajectory.totaltime)  # Stored span, (n_frames - 1) * dt, in ps

Atom Selection Language

MDAnalysis uses a rich selection language:

# Basic selections
protein = u.select_atoms("protein")
backbone = u.select_atoms("backbone")  # CA, N, C, O
calpha = u.select_atoms("protein and name CA")
water = u.select_atoms("resname WAT or resname HOH or resname TIP3")
ligand = u.select_atoms("resname LIG")

# By residue number
region = u.select_atoms("resid 10:50")
specific = u.select_atoms("resid 45 and name CA")

# By proximity
near_ligand = u.select_atoms("protein and around 5.0 resname LIG", updating=True)

# By property
charged = u.select_atoms("resname ARG LYS ASP GLU")
hydrophobic = u.select_atoms("resname ALA VAL LEU ILE PRO PHE TRP MET")

# Boolean combinations
active_site = u.select_atoms("(resid 100 102 145 200) and protein")

# Inverse
not_water = u.select_atoms("not (resname WAT HOH)")

Geometric selections use periodic dimensions by default; updating=True re-evaluates the selection each frame. Verify residue naming (protein uses recognized residue names) and use resindex plus a saved identity map when IDs repeat across chains.

Common Analysis Modules

RMSD and RMSF
from MDAnalysis.analysis import rms, align

# Make molecules whole using trusted bonds before this structural analysis.
# Keep original coordinates/boxes for separate periodic contact calculations.
aligned = u.copy()
aligned.trajectory[0]
align.AlignTraj(aligned, aligned, select='backbone', in_memory=True).run()

# RMSD
R = rms.RMSD(aligned, select='backbone', groupselections=['protein and name CA'], ref_frame=0)
R.run()
# Shape (n_frames, 4): frame, time (ps), backbone RMSD, CA RMSD (Å).
# CA RMSD uses the backbone fit; groupselections are not fitted independently.

# RMSF (per-atom fluctuations)
from MDAnalysis.analysis.rms import RMSF
rmsf = RMSF(aligned.select_atoms('backbone')).run()
# rmsf.results.rmsf: per-atom RMSF values in Angstroms
Radius of Gyration
protein = aligned.select_atoms("protein")  # Must be whole; valid atomic masses required.
rg = []
for ts in aligned.trajectory:
    rg.append(protein.radius_of_gyration())
import numpy as np
print(f"Mean Rg: {np.mean(rg):.2f} Å")
Secondary Structure Analysis
from MDAnalysis.analysis.dssp import DSSP

# DSSP secondary structure assignment per frame
dssp = DSSP(u).run()
# dssp.results.dssp: per-residue per-frame secondary structure codes
# H = helix (including 3_10 and pi), E = strand, - = loop/unordered.
# Requires complete, correctly ordered backbone atoms; not eight-state DSSP.
Hydrogen Bonds
from MDAnalysis.analysis.hydrogenbonds import HydrogenBondAnalysis

# Illustrative BACKBONE-only selection; adapt names to the actual topology.
# Explicit H selection avoids charge-based guessing on PDB files without charges.
# With reliable bonds, prefer donors_sel=None to pair bonded donor and H atoms.
hbonds = HydrogenBondAnalysis(
    u,
    donors_sel="protein and name N",
    hydrogens_sel="protein and name H HN",
    acceptors_sel="protein and name O",
    d_h_cutoff=1.2,          # donor-H distance (Å)
    d_a_cutoff=3.0,          # donor-acceptor distance (Å)
    d_h_a_angle_cutoff=150   # D-H-A angle (degrees)
)
hbonds.run()

counts = hbonds.count_by_time()  # One count per analyzed frame (including zeros).
# The result table has one row per bond occurrence, not one row per frame.
import pandas as pd
df = pd.DataFrame(hbonds.results.hbonds,
                  columns=['frame', 'donor_ix', 'hydrogen_ix', 'acceptor_ix',
                           'DA_dist', 'DHA_angle'])
Principal Component Analysis (PCA)
from MDAnalysis.analysis import pca

# Requires atom types (normally inferred when reading PDB) and matched atom order.
# Fit AND project the same already aligned coordinates. transform() does not align.
pca_analysis = pca.PCA(aligned, select='backbone', align=False).run()

# PC variances
print(pca_analysis.results.variance[:5])  # Raw coordinate variance in Ų.
print(100 * pca_analysis.results.cumulated_variance[:5])  # Cumulative percent.

# Project trajectory onto PCs
projected = pca_analysis.transform(aligned.select_atoms('backbone'), n_components=3)
# Shape: (n_frames, n_components)
Free Energy Surface (FES)

This is a relative, coordinate-dependent -RT log p surface for equilibrated, unbiased sampling at one temperature. Biased/enhanced sampling requires the appropriate reweighting first. Empty bins are unsampled, not measured barriers. Bin size, coordinate Jacobians and autocorrelation affect interpretation; report replicate/block uncertainty. A projected histogram is not a binding free energy.

import numpy as np
import matplotlib.pyplot as plt

def plot_free_energy_surface(x, y, bins=50, T=300, xlabel="PC1", ylabel="PC2",
                              output="fes.png"):
    """
    Compute 2D free energy surface from two order parameters.
    FES = -kT * ln(P(x,y))
    """
    x, y = np.asarray(x, dtype=float), np.asarray(y, dtype=float)
    if x.ndim != 1 or y.shape != x.shape or len(x) < 2:
        raise ValueError("x and y must be equal-length 1D arrays with at least two samples")
    if not np.all(np.isfinite(x)) or not np.all(np.isfinite(y)) or not np.isfinite(T) or T <= 0:
        raise ValueError("Coordinates must be finite and T must be finite and positive")
    R_gas = 0.00831446261815324  # kJ/mol/K (molar gas constant)
    kT = R_gas * T

    # 2D histogram
    H, xedges, yedges = np.histogram2d(x, y, bins=bins, density=True)
    H = H.T

    # Free energy
    H_safe = np.where(H > 0, H, np.nan)
    fes = -kT * np.log(H_safe)
    fes -= np.nanmin(fes)  # Shift minimum to 0

    # Plot
    fig, ax = plt.subplots(figsize=(8, 6))
    im = ax.pcolormesh(xedges, yedges, np.ma.masked_invalid(fes),
                       shading='flat', cmap='RdYlBu_r')
    plt.colorbar(im, ax=ax, label='Free Energy (kJ/mol)')
    ax.set_xlabel(xlabel)
    ax.set_ylabel(ylabel)
    plt.savefig(output, dpi=150, bbox_inches='tight')
    return fig

Trajectory Formats Supported

FormatExtensionNotes
DCD.dcdCHARMM/NAMD binary; widely used
XTC.xtcGROMACS compressed
TRR.trrGROMACS full precision
NetCDF.ncAMBER format
LAMMPS.lammpstrjLAMMPS dump
HDF5.h5mdH5MD standard
PDB.pdbMulti-model PDB

MDAnalysis Interoperability

# Convert to numpy
positions = u.atoms.positions.copy()  # Snapshot in Å: shape (N, 3)

# Write to PDB
with mda.Writer("frame_10.pdb", u.atoms.n_atoms) as W:
    u.trajectory[10]  # Move to frame 10
    W.write(u.atoms)

# Write a topology with exactly the subset atom order before its trajectory.
protein = u.select_atoms("protein")
protein.write("protein_topology.pdb")
# Write a uniformly sampled trajectory subset, preserving the frame interval.
# DCD cannot represent arbitrary timestamps; separately record the time origin.
with mda.Writer("protein_traj.dcd", protein.n_atoms, dt=u.trajectory.dt) as W:
    for ts in u.trajectory:
        W.write(u.select_atoms("protein"))

# Convert to MDTraj (for compatibility)
# import mdtraj as md
# traj = md.load("trajectory.dcd", top="topology.pdb")

Performance Tips

  • Use in_memory=True for AlignTraj when RAM allows (much faster iteration)

  • Select minimal atoms before analysis to reduce memory/compute

  • Parallel execution: inspect get_supported_backends() for that class; do not assume every analysis or coordinate transformation supports multiprocessing

  • Choose a frame slice with start/stop/step; slicing is not a general streaming guarantee (PCA still builds a coordinate covariance matrix):

# Analyze every 10th frame from frame 100 to 1000
R.run(start=100, stop=1000, step=10)

Official API references

Requirements and compatibility

Works with: Claude Code, Claude apps, OpenAI Codex, GitHub Copilot, Cursor, Gemini CLI, Kiro, OpenCode, Goose, Amp, Roo Code, JetBrains Junie, Factory Droid, Devin (ex-Windsurf), Mistral Vibe, OpenHands, Letta

“Works with” means the tool reads the open Agent Skills format; a skill written for one tool may use features others lack.

Needs: Needs Python

The author says: Requires Python 3.11+ with OpenMM and MDAnalysis; matplotlib for plots. Optional PDBFixer and OpenFF need separate installation. Network access for installation; local simulation and analysis run offline.

Security

What our scanner noticed· Low risk

  • Instructions that use the network

A static scan is not a guarantee. Skills are third-party content: review a skill before you let an agent use it.

Attribution and licence

Created by
Kuan-lin Huang
Publisher
K-Dense (Community)
Distributed by
K-Dense
Source
K-Dense-AI/scientific-agent-skills · skills/molecular-dynamics · commit a25cf9e
Licence
MIT License (redistribution allowed)
  • LICENSE (added by AutoGineer from LICENSE.md)
  • ATTRIBUTION.md (written by AutoGineer)
Synced

AutoGineer is not affiliated with or endorsed by Kuan-lin Huang or K-Dense.

Download ZIP

The ZIP holds the skill’s files, its licence files and an ATTRIBUTION.md. Download molecular-dynamics.zip