molforge.structure¶

structure ¶

Structural analysis: superposition, RMSD, contacts, geometry, DSSP, SASA, dihedrals, clashes.

Workhorses for analyzing the geometric properties of protein structures and comparing them.

Common entry points

:func:rmsd — RMSD between two structures (with optional superposition).
:func:superpose — Kabsch / Umeyama optimal rigid-body alignment.
:func:contact_map / :func:distance_map — residue-residue contact and distance matrices.
:func:residue_contacts — all-atom contacts as a sorted list.
:func:radius_of_gyration, :func:centroid, :func:center_of_mass — bulk geometric properties.
:func:translate, :func:rotate, :func:center_at_origin — in-place coordinate transforms.
:func:dssp / :func:dssp_3state — Kabsch-Sander secondary- structure assignment (8-state and 3-state).
:func:sasa / :func:sasa_per_residue / :func:total_sasa — solvent-accessible surface area (Shrake-Rupley).
:func:phi / :func:psi / :func:omega / :func:phi_psi_omega / :func:ramachandran / :func:dihedral — backbone dihedral angles.

BondLengthOutlier `dataclass` ¶

BondLengthOutlier(
    atom_i: int,
    atom_j: int,
    name_i: str,
    name_j: str,
    residue_i: tuple[str, int, str],
    residue_j: tuple[str, int, str],
    bond: str,
    length: float,
    ideal: float,
    sigma: float,
    deviation: float,
    z_score: float,
)

A bond whose length deviates from ideal by more than max_z.

Attributes:

Name	Type	Description
`atom_i,`	`atom_j`	Global atom indices into `protein.atom_array`.
`name_i,`	`name_j`	Atom names (e.g. `"N"`, `"CA"`).
`residue_i,`	`residue_j`	`(chain, residue_id, residue_name)` for each atom (identical for intra-residue bonds).
`bond`	`str`	Bond key from :data:`IDEAL_BOND_LENGTHS` (e.g. `"N-CA"`).
`length`	`float`	Measured length in Å.
`ideal`	`float`	Engh & Huber ideal length in Å.
`sigma`	`float`	Ideal standard deviation in Å.
`deviation`	`float`	`length - ideal` in Å (signed).
`z_score`	`float`	`deviation / sigma` (signed).

ChiralityResult `dataclass` ¶

ChiralityResult(
    residue: tuple[str, int, str],
    ca_index: int,
    configuration: ChiralityConfig,
    volume: float,
)

Cα handedness of one residue.

Attributes:

Name	Type	Description
`residue`	`tuple[str, int, str]`	`(chain_id, residue_id, residue_name)`.
`ca_index`	`int`	Global atom index of the Cα.
`configuration`	`ChiralityConfig`	`L` (natural), `D` (inverted), or `Planar` (degenerate / near-coplanar Cα).
`volume`	`float`	Signed tetrahedral volume in Å³ (`(N-CA)·((C-CA)×(CB-CA))`); positive for L.

Clash `dataclass` ¶

Clash(
    atom_i: int,
    atom_j: int,
    element_i: str,
    element_j: str,
    distance: float,
    vdw_sum: float,
    overlap: float,
    residue_i: tuple[str, int, str],
    residue_j: tuple[str, int, str],
)

A single clashing pair of atoms.

Attributes:

Name	Type	Description
`atom_i,`	`atom_j`	Global atom indices into `protein.atom_array` (`atom_i < atom_j`).
`element_i,`	`element_j`	Element symbols (upper-cased).
`distance`	`float`	Inter-atom distance in Å.
`vdw_sum`	`float`	Sum of the two van der Waals radii in Å.
`overlap`	`float`	`vdw_sum - distance` in Å (>= tolerance).
`residue_i,`	`residue_j`	`(chain_id, residue_id, residue_name)` for each atom's residue.

RamachandranResult `dataclass` ¶

RamachandranResult(
    residue: tuple[str, int, str],
    phi: float,
    psi: float,
    category: RamachandranCategory,
    classification: RamachandranClass,
)

Classification of one residue's backbone conformation.

Attributes:

Name	Type	Description
`residue`	`tuple[str, int, str]`	`(chain_id, residue_id, residue_name)`.
`phi,`	`psi`	Backbone dihedrals in degrees.
`category`	`RamachandranCategory`	Which region set was used (`General`/`Glycine`/ `Proline`).
`classification`	`RamachandranClass`	`Favored`/`Allowed`/`Outlier`.

SuperpositionResult `dataclass` ¶

SuperpositionResult(
    rotation: NDArray[float64],
    translation: NDArray[float64],
    rmsd: float,
    n_atoms: int,
    mobile_aligned: NDArray[float32],
)

Result of a structural superposition.

Attributes:

Name	Type	Description
`rotation`	`NDArray[float64]`	`(3, 3)` proper rotation matrix.
`translation`	`NDArray[float64]`	`(3,)` translation vector.
`rmsd`	`float`	Root-mean-square deviation of the superposed structures.
`n_atoms`	`int`	Number of atoms used in the superposition.
`mobile_aligned`	`NDArray[float32]`	`(n_atoms, 3)` mobile coords after superposition onto the reference.

bond_length_rmsd ¶

bond_length_rmsd(
    protein: Protein, *, include_cb: bool = True
) -> float

RMS deviation of all checked bonds from their ideal lengths (Å).

A standard-geometry quality metric: near zero for a well-refined model. Returns 0.0 when there are no checkable bonds.

check_bond_lengths ¶

check_bond_lengths(
    protein: Protein,
    *,
    max_z: float = DEFAULT_MAX_Z,
    include_cb: bool = True,
) -> list[BondLengthOutlier]

Backbone bonds whose length is more than max_z σ from ideal.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	Structure to check.	required
`max_z`	`float`	Outlier threshold in standard deviations (default 4).	`DEFAULT_MAX_Z`
`include_cb`	`bool`	Also check the `CA-CB` bond where a Cβ is present.	`True`

Returns:

Type	Description
`list[BondLengthOutlier]`	Outliers sorted by absolute z-score, worst first.

has_bond_length_outliers ¶

has_bond_length_outliers(
    protein: Protein,
    *,
    max_z: float = DEFAULT_MAX_Z,
    include_cb: bool = True,
) -> bool

Whether protein has any backbone bond-length outlier.

ca_chirality ¶

ca_chirality(
    n: NDArray[float64],
    ca: NDArray[float64],
    c: NDArray[float64],
    cb: NDArray[float64],
    *,
    planar_tolerance: float = DEFAULT_PLANAR_TOLERANCE,
) -> ChiralityConfig

Classify a Cα centre as L / D / Planar.

Parameters:

Name	Type	Description	Default
`n`	`NDArray[float64]`	Cartesian coordinates of the backbone N.	required
`ca`	`NDArray[float64]`	Cartesian coordinates of the Cα.	required
`c`	`NDArray[float64]`	Cartesian coordinates of the carbonyl C.	required
`cb`	`NDArray[float64]`	Cartesian coordinates of the Cβ.	required
`planar_tolerance`	`float`	\|signed volume\| (Å³) at or below which the centre is reported as `Planar`.	`DEFAULT_PLANAR_TOLERANCE`

Returns:

Type	Description
`ChiralityConfig`	The chirality label.

chirality_outliers ¶

chirality_outliers(
    protein: Protein,
    *,
    planar_tolerance: float = DEFAULT_PLANAR_TOLERANCE,
) -> list[ChiralityResult]

Residues whose Cα is not the natural L configuration.

Returns the D and Planar residues (everything that is not a clean L centre).

classify_chirality ¶

classify_chirality(
    protein: Protein,
    *,
    planar_tolerance: float = DEFAULT_PLANAR_TOLERANCE,
) -> list[ChiralityResult]

Classify the Cα chirality of every eligible residue.

Residues without a full N / CA / C / CB set — glycine, or any residue missing one of those atoms — are skipped (glycine is achiral). Only protein residues are considered.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	Structure to analyze.	required
`planar_tolerance`	`float`	See :func:`ca_chirality`.	`DEFAULT_PLANAR_TOLERANCE`

Returns:

Name	Type	Description
`One`	`list[ChiralityResult]`	class:`ChiralityResult` per eligible residue, in
	`list[ChiralityResult]`	chain/sequence order.

has_chirality_outliers ¶

has_chirality_outliers(
    protein: Protein,
    *,
    planar_tolerance: float = DEFAULT_PLANAR_TOLERANCE,
) -> bool

Whether protein has any non-L Cα centre.

clash_score ¶

clash_score(
    protein: Protein,
    *,
    tolerance: float = DEFAULT_TOLERANCE,
    bonded_separation: int = 3,
    include_hydrogens: bool = False,
) -> float

Clashes per 1000 atoms — a single-number quality gate.

Lower is better; a well-refined structure scores near zero. The denominator is the number of atoms actually considered (heavy atoms unless include_hydrogens is set), so the score is comparable across structures of different sizes. Returns 0.0 for an empty structure.

find_clashes ¶

find_clashes(
    protein: Protein,
    *,
    tolerance: float = DEFAULT_TOLERANCE,
    bonded_separation: int = 3,
    include_hydrogens: bool = False,
) -> list[Clash]

Find all steric clashes in protein.

A pair of atoms clashes when their van der Waals shells overlap by at least tolerance Å and they are more than bonded_separation inferred covalent bonds apart (see the module docstring).

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	The structure to check.	required
`tolerance`	`float`	Minimum overlap (Å) to count as a clash. Smaller values flag more (softer) contacts.	`DEFAULT_TOLERANCE`
`bonded_separation`	`int`	Exclude atom pairs separated by at most this many inferred bonds (default 3 → 1-2, 1-3, 1-4 neighbours). Set to 0 to disable bonded exclusion.	`3`
`include_hydrogens`	`bool`	Consider hydrogen atoms too. Off by default since folding output usually omits them.	`False`

Returns:

Type	Description
`list[Clash]`	Clashes sorted worst-first (largest overlap). Empty when the
`list[Clash]`	structure is clean or has fewer than two eligible atoms.

has_clashes ¶

has_clashes(
    protein: Protein,
    *,
    tolerance: float = DEFAULT_TOLERANCE,
    bonded_separation: int = 3,
    include_hydrogens: bool = False,
) -> bool

Whether protein has at least one steric clash.

contact_map ¶

contact_map(
    protein: Protein,
    *,
    cutoff: float = 8.0,
    atom_choice: AtomChoice = "cb",
    exclude_neighbors: int = 0,
) -> NDArray[np.bool_]

Binary contact map at cutoff Å.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	structure to analyze.	required
`cutoff`	`float`	distance below which residues are in contact (default 8.0 Å, the CASP standard for CB-CB).	`8.0`
`atom_choice`	`AtomChoice`	which atom defines the residue position — defaults to `"cb"` (the field standard); use `"ca"` for Gly-heavy structures.	`'cb'`
`exclude_neighbors`	`int`	Set the diagonal band of width `2*exclude_neighbors + 1` to False. Useful for ignoring trivial sequential contacts; pass 4 to remove the ±4 band (helix neighbors) for instance.	`0`

Returns:

Type	Description
`NDArray[bool_]`	`(n_res, n_res)` boolean array; entry `[i, j]` is True if
`NDArray[bool_]`	residue `i` and `j` are in contact.

distance_map ¶

distance_map(
    protein: Protein, *, atom_choice: AtomChoice = "ca"
) -> NDArray[np.float32]

Compute a residue-by-residue distance map.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	structure to analyze.	required
`atom_choice`	`AtomChoice`	per-residue representative point — `"ca"`, `"cb"`, or the residue centroid (`"heavy"` / `"all"`).	`'ca'`

Returns:

Type	Description
`NDArray[float32]`	`(n_res, n_res)` float32 array of pairwise Euclidean distances
`NDArray[float32]`	between the representative points.

residue_contacts ¶

residue_contacts(
    protein: Protein,
    *,
    cutoff: float = 5.0,
    chain_a: str | None = None,
    chain_b: str | None = None,
) -> list[tuple[tuple[str, int], tuple[str, int], float]]

List inter-residue contacts at the all-atom level.

Unlike :func:contact_map, this enumerates contacts as triples of ((chain_a, resid_a), (chain_b, resid_b), distance) and uses the "any atom within cutoff" definition.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	structure to analyze.	required
`cutoff`	`float`	distance threshold in Å (default 5.0).	`5.0`
`chain_a`	`str \| None`	If both `chain_a` and `chain_b` are given, only return contacts between those two chains (useful for interface analysis).	`None`
`chain_b`	`str \| None`	see `chain_a`.	`None`

Returns:

Type	Description
`list[tuple[tuple[str, int], tuple[str, int], float]]`	Sorted list of contact tuples.

classify_ramachandran ¶

classify_ramachandran(
    protein: Protein,
) -> list[RamachandranResult]

Classify every residue with a defined (φ, ψ) pair.

Residues at chain termini or across chain breaks (where φ or ψ is undefined) are skipped, so the result holds one entry per residue that actually has a backbone conformation to judge.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	Structure to analyze.	required

Returns:

Name	Type	Description
`One`	`list[RamachandranResult]`	class:`RamachandranResult` per classifiable residue, in
	`list[RamachandranResult]`	chain/sequence order.

dihedral ¶

dihedral(
    p1: NDArray[floating],
    p2: NDArray[floating],
    p3: NDArray[floating],
    p4: NDArray[floating],
) -> float

Compute the dihedral angle (in degrees) between four 3D points.

Parameters:

Name	Type	Description	Default
`p1`	`NDArray[floating]`	`(3,)` Cartesian coordinates of the first point.	required
`p2`	`NDArray[floating]`	`(3,)` Cartesian coordinates of the second point.	required
`p3`	`NDArray[floating]`	`(3,)` Cartesian coordinates of the third point.	required
`p4`	`NDArray[floating]`	`(3,)` Cartesian coordinates of the fourth point.	required

Returns:

Name	Type	Description
	`float`	Angle in degrees in `[-180, 180]`, in the standard IUPAC sign
`convention`	matching Biopython's ``calc_dihedral``	a right-handed
	`float`	α-helix is φ ≈ −60°, ψ ≈ −45°. Uses the atan2 formula, which avoids
	`float`	the numerical issues of acos near `±1` and naturally captures the
	`float`	sign.

dihedrals_batch ¶

dihedrals_batch(
    quartets: NDArray[floating],
) -> NDArray[np.float64]

Vectorized dihedral over an array of atom quartets.

Parameters:

Name	Type	Description	Default
`quartets`	`NDArray[floating]`	`(N, 4, 3)` array of four-atom quartets.	required

Returns:

Type	Description
`NDArray[float64]`	`(N,)` float64 array of dihedral angles in degrees.

omega ¶

omega(protein: Protein) -> NDArray[np.float64]

ω (omega) angles per residue, degrees, NaN where undefined.

phi ¶

phi(protein: Protein) -> NDArray[np.float64]

φ (phi) angles per residue, degrees, NaN where undefined.

phi_psi_omega ¶

phi_psi_omega(
    protein: Protein,
) -> tuple[
    NDArray[np.float64],
    NDArray[np.float64],
    NDArray[np.float64],
]

Per-residue backbone dihedrals (φ, ψ, ω) in degrees.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	structure to analyze.	required

Returns:

Type	Description
`NDArray[float64]`	Three `(n_residues,)` float64 arrays of φ, ψ, ω values in
`NDArray[float64]`	degrees. Entries where the angle is undefined (chain termini,
`NDArray[float64]`	missing backbone atoms) are `NaN`.

psi ¶

psi(protein: Protein) -> NDArray[np.float64]

ψ (psi) angles per residue, degrees, NaN where undefined.

ramachandran ¶

ramachandran(protein: Protein) -> NDArray[np.float64]

Per-residue (φ, ψ) pairs for Ramachandran-plot construction.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	structure to analyze.	required

Returns:

Type	Description
`NDArray[float64]`	`(n_residues, 2)` float64 array. Rows where either angle is
`NDArray[float64]`	undefined contain `NaN`s.

ramachandran_favored_fraction ¶

ramachandran_favored_fraction(protein: Protein) -> float

Fraction of classifiable residues in the favored region.

A quality metric in the spirit of MolProbity's "Ramachandran favored" percentage (here from the simplified region model). Returns 1.0 for a structure with no classifiable residues (nothing to fault).

ramachandran_outliers ¶

ramachandran_outliers(
    protein: Protein,
) -> list[RamachandranResult]

Just the residues classified as Ramachandran outliers.

ramachandran_type ¶

ramachandran_type(
    phi: float,
    psi: float,
    *,
    category: RamachandranCategory = "General",
) -> RamachandranClass

Classify a single (φ, ψ) pair as Favored / Allowed / Outlier.

Parameters:

Name	Type	Description	Default
`phi`	`float`	Backbone φ dihedral in degrees, in `[-180, 180]`.	required
`psi`	`float`	Backbone ψ dihedral in degrees, in `[-180, 180]`.	required
`category`	`RamachandranCategory`	Region set to use — `General` (default), `Glycine` (symmetric map), or `Proline` (restricted φ).	`'General'`

Returns:

Type	Description
`RamachandranClass`	The region the pair falls in.

Raises:

Type	Description
`ValueError`	If `phi` or `psi` is not finite.

dssp_3state ¶

dssp_3state(protein: Protein) -> str

Return the per-residue 3-state secondary-structure string.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	structure to analyze.	required

Returns:

Type	Description
`str`	A string of `"H"` / `"E"` / `"C"` characters, one per
`str`	residue.

bounding_box ¶

bounding_box(
    protein: Protein,
) -> tuple[NDArray[np.float64], NDArray[np.float64]]

Axis-aligned bounding box of a structure.

Returns:

Type	Description
`tuple[NDArray[float64], NDArray[float64]]`	`(min_xyz, max_xyz)`, each a `(3,)` float64 array.

center_at_origin ¶

center_at_origin(
    protein: Protein, *, mass_weighted: bool = False
) -> None

Translate the structure so its centroid is at the origin (in place).

center_of_mass ¶

center_of_mass(protein: Protein) -> NDArray[np.float64]

Mass-weighted center of mass. Alias for centroid(mass_weighted=True).

centroid ¶

centroid(
    protein: Protein, *, mass_weighted: bool = False
) -> NDArray[np.float64]

Geometric (or mass-weighted) centroid of a structure.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	input structure.	required
`mass_weighted`	`bool`	If True, weight by atomic mass (i.e. compute the center of mass instead).	`False`

Returns:

Type	Description
`NDArray[float64]`	`(3,)` float64 centroid coordinate.

radius_of_gyration ¶

radius_of_gyration(
    protein: Protein, *, mass_weighted: bool = True
) -> float

Radius of gyration — RMS distance from atoms to the center of mass.

A standard compactness metric: smaller Rg means more globular.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	input structure.	required
`mass_weighted`	`bool`	If True (default), use mass-weighted Rg.	`True`

Returns:

Type	Description
`float`	Radius of gyration in angstroms.

rotate ¶

rotate(
    protein: Protein, rotation: NDArray[floating]
) -> None

Apply a 3x3 rotation in place around the origin.

For a rotation around the centroid, translate to origin first, rotate, then translate back. Use :func:center_at_origin as a helper.

translate ¶

translate(
    protein: Protein, vector: NDArray[floating]
) -> None

Translate protein in place by vector.

Mutates the underlying AtomArray.coords directly — both hierarchical and linear views reflect the change immediately.

rmsd_per_residue ¶

rmsd_per_residue(
    mobile: Protein,
    reference: Protein,
    *,
    subset: AtomSubset = "ca",
    align: bool = True,
) -> NDArray[np.float32]

Per-residue RMSD after (optionally) aligning the structures globally.

Useful for spotting which loops moved between two conformations or where a folding model disagrees with experiment.

Parameters:

Name	Type	Description	Default
`mobile`	`Protein`	First structure (the one that is moved to align with reference).	required
`reference`	`Protein`	Second structure; must have the same residue count as `mobile`.	required
`subset`	`AtomSubset`	Atom selector for both the global alignment and the per-residue comparison.	`'ca'`
`align`	`bool`	Whether to superpose first.	`True`

Returns:

Type	Description
`NDArray[float32]`	`(n_residues,)` float32 array of per-residue RMSDs.

rmsd_raw ¶

rmsd_raw(
    a: NDArray[floating], b: NDArray[floating]
) -> float

RMSD between two equal-length coordinate sets, no alignment.

Parameters:

Name	Type	Description	Default
`a`	`NDArray[floating]`	First `(n, 3)` coordinate array.	required
`b`	`NDArray[floating]`	Second `(n, 3)` coordinate array, same shape as `a`.	required

Returns:

Type	Description
`float`	Root-mean-square deviation in the input units (Å for biology).

sasa_per_residue ¶

sasa_per_residue(
    protein: Protein,
    *,
    probe_radius: float = 1.4,
    n_sphere_points: int = 100,
) -> NDArray[np.float64]

Per-residue SASA, summed across atoms in each residue.

Parameters:

Name	Type	Description	Default
`protein`	`Protein`	input structure.	required
`probe_radius`	`float`	see :func:`sasa`.	`1.4`
`n_sphere_points`	`int`	see :func:`sasa`.	`100`

Returns:

Type	Description
`NDArray[float64]`	`(n_residues,)` float64 array, one SASA value per residue
`NDArray[float64]`	in array order.

total_sasa ¶

total_sasa(
    protein: Protein,
    *,
    probe_radius: float = 1.4,
    n_sphere_points: int = 100,
) -> float

Total solvent-accessible surface area (Å²).

kabsch_rmsd ¶

kabsch_rmsd(
    mobile: NDArray[floating],
    reference: NDArray[floating],
    *,
    weights: NDArray[floating] | None = None,
) -> float

Return the minimum-RMSD over all rigid-body alignments.

Convenience wrapper around :func:superpose for when you only want the RMSD value.

superpose ¶

superpose(
    mobile: NDArray[floating],
    reference: NDArray[floating],
    *,
    weights: NDArray[floating] | None = None,
) -> SuperpositionResult

Superpose mobile onto reference by optimal rigid-body fit.

Implements the Kabsch / Umeyama algorithm via SVD of the weighted covariance matrix. The returned rotation is guaranteed to be a proper rotation (det = +1), not a reflection.

Parameters:

Name	Type	Description	Default
`mobile`	`NDArray[floating]`	`(n, 3)` coordinates to align.	required
`reference`	`NDArray[floating]`	`(n, 3)` reference coordinates.	required
`weights`	`NDArray[floating] \| None`	Optional `(n,)` per-point weights (e.g. inverse-B-factor for X-ray structures, or 1/0 for masking atoms).	`None`

Returns:

Name	Type	Description
`A`	`SuperpositionResult`	class:`SuperpositionResult` with the rotation, translation,
	`SuperpositionResult`	post-superposition RMSD, and aligned mobile coords.

Raises:

Type	Description
`ValueError`	If shapes mismatch or fewer than 3 atoms are given (degenerate; rotation under-determined).

molforge.structure¶

structure ¶

BondLengthOutlier dataclass ¶

ChiralityResult dataclass ¶

Clash dataclass ¶

RamachandranResult dataclass ¶

SuperpositionResult dataclass ¶

bond_length_rmsd ¶

check_bond_lengths ¶

has_bond_length_outliers ¶

ca_chirality ¶

chirality_outliers ¶

classify_chirality ¶

has_chirality_outliers ¶

clash_score ¶

find_clashes ¶

has_clashes ¶

contact_map ¶

distance_map ¶

residue_contacts ¶

classify_ramachandran ¶

dihedral ¶

dihedrals_batch ¶

omega ¶

phi ¶

phi_psi_omega ¶

psi ¶

ramachandran ¶

ramachandran_favored_fraction ¶

ramachandran_outliers ¶

ramachandran_type ¶

dssp_3state ¶

bounding_box ¶

center_at_origin ¶

center_of_mass ¶

centroid ¶

radius_of_gyration ¶

rotate ¶

translate ¶

rmsd_per_residue ¶

rmsd_raw ¶

sasa_per_residue ¶

total_sasa ¶

kabsch_rmsd ¶

superpose ¶

BondLengthOutlier `dataclass` ¶

ChiralityResult `dataclass` ¶

Clash `dataclass` ¶

RamachandranResult `dataclass` ¶

SuperpositionResult `dataclass` ¶