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alignment.salign() -- align two or more sequences/structures of proteins

io = <io_data>   Options for reading atom files
align3d_trf = <bool:1> False whether to transform the distances before dynamic programming
align_block = <int:1> 0 the last sequence in the first block of sequences
alignment_type = <str:1> 'PROGRESSIVE' 'PAIRWISE' 'TREE' 'PROGRESSIVE' for SALIGN
align_what = <str:1> 'BLOCK' what to align in ALIGN; 'BLOCK' | 'ALIGNMENT' | 'LAST' | 'PROFILE'
auto_overhang = <bool:1> False overhang values made dependent on sequence length difference
comparison_type = <str:1> 'MAT' 'MAT' or 'PSSM' for comparing matrices or PSSMs when profiles are compared
current_directory = <bool:1> True whether to write output .fit files to current directory
dendrogram_file = <str:1> '' File into which the SALIGN dendrogram is written out
ext_tree = <bool:1> False To read a pre computed tree for SALIGN
feature_weights = <float:6> 1 0 0 0 0 0 feature weights for SALIGN
fit_atoms = <str:1> 'CA' atom type(s) being superposed
fit_on_first = <bool:1> False whether or not all structures are to be fit on the first structure, given the final alignment
fit_pdbnam = <bool:1> True whether or not to add _fit to the PDB file name in output alifile by SALIGN
fit = <bool:1> True whether to do pairwise least-squares fitting or ALIGN2D alignment
fix_offsets = <float:5> 0 1 2 3 4 offsets of the ALIGN2D alignment score for "fixed" positions indicated by ' 123456789' in line '_fix_pos'
gap_function = <bool:1> False whether or not to switch on functional gap penalty in salign
gap_gap_score = <float:1> 0 dissimilarity score for aligning gap with gap, in SALIGN
gap_penalties_1d = <float:2> 900 50 gap creation and extension penalties for sequence/sequence alignment
gap_penalties_2d = <float:9> 0.35 1.2 0.9 1.2 0.6 8.6 1.2 0 0 gap penalties for sequence/structure alignment: helix, beta, accessibility, straightness, and CA-CA distance factor, dst min, dst power, t, structure_profile ; best U,V=-450,0
gap_penalties_3d = <float:2> 0.0 1.75 gap creation and extension penalties for structure/structure superposition
gap_residue_score = type1 0 dissimilarity score for aligning gap with residue, in SALIGN
improve_alignment = <bool:1> True whether or not to optimize alignment in SALIGN
input_weights_file = <str:1> '' Exteral weight matrix input to MODELLER (SALIGN/ALIGN)
local_alignment = <bool:1> False whether to do local as opposed to global alignment
matrix_comparison = <str:1> 'CC' 'CC', 'MAX', 'AVE', - kinds of matrix comparisons
matrix_offset = <float:1> 0.00 substitution matrix offset for local alignment
max_gap_length = <int:1> 999999 maximal length of gap in protein comparisons
normalize_pp_scores = <bool:1> False whether or not to normalize position-position scores in SALIGN
no_ter = <bool:1> False whether to not write TER into PDB
n_subopt = <int:1> 1 number of optimal and suboptimal alignments ALIGN/ALIGN2D
off_diagonal = <int:1> 100 to speed up the alignment
output_weights_file = <str:1> '' File into which the weight file is wriiten (iff WRITE_WEIGHTS = 'on')
output = <str:1> 'LONG' what and/or how to output
overhang = <int:1> 0 un-penalized overhangs in protein comparisons
overhang_auto_limit = <int:1> 60 auto_overhang effective if seq length diff greater than overhang_auto_limit
overhang_factor = <float:1> 0.4 Factor to multiply seq. length diff with when auto_overhang is on
rms_cutoffs = <float:11> 3.5 3.5 60 60 15 60 60 60 60 60 60 cutoffs for RMS, DRMS, Alpha Phi Psi Omega chi1 chi2 chi3 chi4 chi5
rr_file = <str:1> '$(LIB)/as1.sim.mat' input residue-residue scoring file
similarity_flag = <bool:1> False when turned on, the SALIGN command does not convert numbers into a distance sense.
smooth_prof_weight = <float:1> 10 for smoothing the profile aa frequency with a prior
subopt_offset = <float:1> 0.0 offset for residue-residue score in getting suboptimals in ALIGN/ALIGN2D
substitution = <bool:1> False whether to use the background in PSSM comparison
weights_type = <str:1> 'SIMILAR' or 'DISTANCE' for the kind of substitution values
write_fit = <bool:1> False whether to write out fitted coordinates to .fit files
write_weights = <bool:1> False whether to write the whole NxM weight matrix for ALIGN*
write_whole_pdb = <bool:1> True whether to write out all lines in the input PDB file

Description:
This command is a general dynamic programming based alignment procedure for aligning sequences, structures or a combination of the two. It is loosely based on the program COMPARER [Šali & Blundell, 1990]. SALIGN can be used to generate multiple protein structures/sequences alignments or to align two blocks of sequences/structures that are in memory.

Please note that the method is still in development, and has not yet been fully benchmarked. As with any other alignment method, generated alignments should be assessed for quality.

Broadly classifying, three different types of protein alignment categories are tackled by this command:

  1. Multiple structure alignments
  2. Aligning a structure block to a sequence block
  3. Multiple and pair-wise protein sequence alignment

The command incorporates the functionality of several old MODELLER commands (alignment.align(), alignment.align2d(), alignment.malign(), alignment.align3d(), and alignment.malign3d()). Some of the examples below illustrate the equivalent script files to replace the old alignment commands with alignment.salign().

In addition to these, this command has several new alignment features including profile-profile sequence alignments and a dendrogram based multiple sequence/structure alignment among others.

All pair-wise alignments make use of local or global dynamic programming. A switch from one to another can be effected by setting local_alignment to True or False. The dynamic programming can be carried out using affine gap penalties (as previously used in alignment.align()) or an environment dependent gap penalty function (as used in alignment.align2d()). The choice of gap penalty types can be regulated by switching the variable gap_function on or off. All arguments that associated to the alignment.align() and alignment.align2d() commands apply.

If at least one of the blocks in a pairwise alignment consists of structures, dynamic programming can be performed using structure dependent gap penalties.

Features of proteins used for alignment

Central to the dynamic programming algorithm is the weight matrix. In SALIGN, this matrix is constructed by weighting the contribution from six features of protein structure and sequence:

Feature 1
is the residue type. $W^1_{i,j}$ is obtained from the residue type - residue type dissimilarity matrix, specified in the file rr_file. $W^1_{i,j}$ dissimiarity score for positions $i$ and $j$ in the two compared sub-alignments is the average dissimilarity score for a comparison of all residues in one sub-alignment with all residues in the other sub-alignment (note that gaps are ignored here). Should only feature weight 1 be non-zero, the user has an option of considering residue-residue similarity scores instead of distance scores by setting similarity_flag to True.

Feature 2
is the inter-molecular distance for a pair of residues (unless align3d_trf is True: see alignment.align3d()). Only one atom per residue is of course selected, as specified by fit_atoms (e.g., ${C}_\alpha$, although we should also allow for ${C}_\beta$ in the future, which requires an intervention for Gly). This `position' feature is complicated because it depends on the relative orientation of the structures corresponding to the two compared alignments. $W^2_{i,j}$ is the Euclidean distance between the compared positions $i$ and $j$ in the two compared sub-alignments that are already optimally aligned and superposed based on their coordinates alone. This optimal alignment is obtained by an iterative procedure as follows (the same as in alignment.align3d()). The average structures for both sub-alignments are calculated for all sub-alignment positions with at least one defined selected atom. This calculation is straightforward because the structures within the two sub-alignments are already superposed with each other (see below). Then, the distance matrix for dynamic programming with affine gap penalties is calculated as the matrix of Euclidean distances between the two averages. The dynamic programming results into a new alignment, dependent also on the gap initiation and extension penalties gap_penalties_3d (a reasonable setting is (0, 3)). gap_penalties_3d[0] is a gap creation penalty (usually 0), and gap_penalties_3d[1] is a gap extension penalty, say 3. When the gap initiation penalty is 0, pairs of positions are identified as equivalent when they have their selected atoms at most 2 times gap_penalties_3d[0] angstroms apart in the current superposition, as described for the alignment.align3d() command. The new alignment is then used to generate the new superposition of the two averages, and the iteration of the distance matrix calculation, alignment and superposition is repeated until there are no changes in the number of equivalent positions and in the rotation matrix relating the two averages.

The values of both improve_alignment and fit are used in the calculation of the position feature. That is, the initial alignment and the orientation of the coordinates can be selected not to change at all during the calculation of the inter-molecular distance matrix.

When the calculation of the inter-molecular distance matrix is finished, all the structures in the second sub-alignment are rotated and translated following the optimal rotation and translation of the second average on the first average. These superpositions prepare the individual structures for the next of the $n-1$ stages of the progressive multiple alignment, and also orient all the structures for writing out to 'alignment[i].code_fit.pdb' atom files if write_fit = True. If fit_pdbnam = False, the PDB filenames in the output alignment file will not have the '_fit.pdb' extensions. Thus, feature 2 needs to be selected by feature_weight[2] $> 0$ if you wish to write out the structures superposed according to the tree-following procedure; also, fit_on_first must be False, otherwise the structures are written out superposed on the first structure according to the final alignment (see also below).

The alignment produced within the routine that calculates $W^2$ does not generally correspond to the alignment calculated based on $W$. Therefore, the multiply superposed structures are not necessarily superposed based on the final multiple alignment produced by alignment.salign(). If you wish such a superposition, you can use alignment.malign3d() with fit = False and write_fit = True (the meaning of fit is different between alignment.salign() and alignment.malign3d()).

Unless the position feature is selected, the initial alignment does not matter. If the position feature is selected, a good starting alignment is a multiple sequence alignment, obtained either by alignment.malign() or by alignment.salign() used without the position feature (the initial alignment can also be prepared using the position feature). If the position feature is used, each pair of structures needs to have at least 3 aligned residues at all points during the alignment.

There are several possibilities as to the final orientation of the input coordinates. If fit_on_first is True, all the coordinate sets are superposed on the first structure, using the final multi-feature multiple alignment. If fit_on_first is False, and position feature was used, and fit was True, the coordinates will be superposed in the progressive manner guided by the tree, by the routine that calculates the inter-molecular distance matrices; this superposition is based only on the positions of the selected atoms (feature 2), not on other features such as residue type, secondary, structure, etc. If improve_alignment is False, it does not make much sense to have fit = True (use fit_on_first = True).

Feature 3
is the fractional sidechain accessibility. The pair-wise residue-residue dissimilarity is calculated by classifying residues into the buried ($<15$%), semi-exposed, and exposed classes ($>30$%). The dissimilarity is 0 for equal classes, 1 for neighboring classes and 2 for the buried-exposed match. The position-position dissimilarity is the average residue-residue dissimilarity for comparing all residues from one group to all residues in the other group (gaps are ignored).

Feature 4
is the secondary structure type, distinguishing between helix, strand, and other. The pair-wise residue-residue dissimilarity is 0 for equal classes, 1 for `helix' or `strand' matched to `other', and 2 for `helix' matched to 'strand'. Position-position dissimilarity is calculated in the same way as for feature 3.

Feature 5
is the local conformation. A pair-wise residue-residue score is DRMSD between the selected atoms (fit_atoms) from the segments of 5 residues centered on the two matched residues. Position-position dissimilarity is calculated in the same way as for feature 3.

Feature 6
is a user specified feature for which a external matrix (in MODELLER matrix format; see the substitution matrices in the modlib directory for examples) has to be specified using input_weights_file. The user can input either a similarity matrix (weights_type = SIMILAR) or a distance matrix (weights_type = DISTANCE).

Alignment of protein sequences

Alignment of protein structures with sequences

As stated earlier, all alignment.align and alignment.align2d related commands apply to alignment.salign too. The example below is a alignment.salign equivalent of alignment.align2d (and alignment.align). For a description of the gap_penalties_2d see the section on alignment.align2d.

Example: examples/salign/salign_align2d.py


# align2d/align using salign

# parameters to be input by the user 
# 1.  gap_penalties_1d
# 2.  gap_penalties_2d = (4.35, 1.2, 0.9, 1.2, 0.6, 8.6, 1.2, 0., 0.) (default)
# 3.  input alignment file 

log.verbose()
env = environ()
env.io.atom_files_directory='./'

aln = alignment(env, file='align2d_in.ali', align_codes='all')
aln.salign(rr_file='$(LIB)/as1.sim.mat',  # Substitution matrix used
           output='',
           max_gap_length=20,
           gap_function=True,              # If False then align2d not done 
           feature_weights=(1., 0., 0., 0., 0., 0.),
           gap_penalties_1d=(-1000, 0),
           gap_penalties_2d=(4.35, 1.2, 0.9, 1.2, 0.6, 8.6, 1.2, 0.0, 0.0),
           # d.p. score matrix 
           #write_weights=True, output_weights_file='salign.mtx'
           similarity_flag=True)   # Ensuring that the dynamic programming 
                                   # matrix is not scaled to a difference matrix
aln.write(file='align2d.ali', alignment_format='PIR')
aln.write(file='align2d.pap', alignment_format='PAP')

Alignment of protein structures

Structure alignments can make use of all the 5 structure/sequence features as well as the 6th user provided feature matrix. Pairwise alignments of structures can make use of the constant gap penalties or the environment dependent gap penalties. Multiple structure alignments are constructed from pairwise structure alignments.

The alignment of proteins within a sub-alignment does not change when the sub-alignment is aligned with another protein or sub-alignment. The pairwise alignment of sub-alignments is guided by the dendrogram. First, the most similar pair of proteins are aligned. Second, the next most similar pair of proteins are aligned, or the third protein is aligned with the sub-alignment of the first two, as indicated by the dendrogram. This greedy, progressive procedure requires $n-1$ steps to align all $n$ proteins, and each step requires a pairwise alignment of two sub-alignments.

If in a multiple alignment, overhangs are to be penalized differently for the pairs of alignments that create the multiple, auto_overhang can be set to True. This will ensure that the value of overhang changes as overhang_factor times the numerical difference in the residues of the pair. Further, this is only effected if the difference is greater than overhang_auto_limit.

The dendrogram can be written out in a separate file by specifying the file name to dendrogram_file.

Example: examples/salign/salign_multiple.py


# Illustrates the SALIGN multiple structure/sequence alignment

log.verbose()
env = environ()
env.io.atom_files_directory = './:../atom_files/'

aln = alignment(env)
for (code, chain) in (('1is4', 'A'), ('1uld', 'D'), ('1ulf', 'B'),
                      ('1ulg', 'B'), ('1is5', 'A')):
    mdl = model(env, file=code, model_segment=('FIRST:'+chain, 'LAST:'+chain))
    aln.append_model(mdl, atom_files=code, align_codes=code+chain)

for (weights, write_fit, whole) in (((1., 0., 0., 0., 1., 0.), False, True),
                                    ((1., 0.5, 1., 1., 1., 0.), False, True),
                                    ((1., 1., 1., 1., 1., 0.), True, False)):
    aln.salign(rms_cutoffs=(3.5, 6., 60, 60, 15, 60, 60, 60, 60, 60, 60),
               normalize_pp_scores=False,
               rr_file='$(LIB)/as1.sim.mat', overhang=30,
               gap_penalties_1d=(-450, -50),
               gap_penalties_3d=(0, 3), gap_gap_score=0, gap_residue_score=0,
               dendrogram_file='1is3A.tree',
               alignment_type='tree', # If 'progresive', the tree is not
                                      # computed and all structues will be
                                      # aligned sequentially to the first
               #ext_tree=True,        # Tree building can be avoided if the tree
                                      # is input
               #input_weights_file='1is3A_exmat.mtx',
               feature_weights=weights, # For a multiple sequence alignment only
                                        # the first feature needs to be non-zero
               improve_alignment=True, fit=True, write_fit=write_fit,
               write_whole_pdb=whole, output='ALIGNMENT QUALITY')

aln.write(file='1is3A.pap', alignment_format='PAP')
aln.write(file='1is3A.ali', alignment_format='PIR')

# The number of equivalent positions at different RMS_CUTOFF values can be
# computed by changing the RMS value and keeping all feature weights = 0
aln.salign(rms_cutoffs=(1.0, 6., 60, 60, 15, 60, 60, 60, 60, 60, 60),
           normalize_pp_scores=False, rr_file='$(LIB)/as1.sim.mat', overhang=30,
           gap_penalties_1d=(-450, -50), gap_penalties_3d=(0, 3),
           gap_gap_score=0, gap_residue_score=0, dendrogram_file='1is3A.tree',
           alignment_type='progressive', feature_weights=[0]*6,
           improve_alignment=False, fit=False, write_fit=True,
           write_whole_pdb=False, output='QUALITY')

Sub-optimal alignments

The weight matrix can be offset at random, many times over, to generate several `sub-optimal' alignments. The number of sub-optimal alignments to be output can be specified with n_subopt. Though the matrix positions at which these offsets are applied cannot be controlled, the user can choose by how much the matrix will be offset (subopt_offset). The output suboptimal alignments are written into the file 'suboptimal_alignments.out' and is of the format that specifies the serial residue numbers of the two sequences.

Example: examples/salign/salign_subopt.py


log.verbose()
env = environ()
aln = alignment(env, file='fm07254_test.ali', alignment_format='PIR')
aln.salign(feature_weights=(1., 0, 0, 0, 0, 0), gap_penalties_1d=(-450, -50),
           n_subopt = 5, subopt_offset = 15)

Alignments using external restraints

Fix positions: The user can choose to have certain alignment positions "fixed" by offsetting the appropriate matrix entries. This is achieved by setting fix_offset to True. Below the given pair of sequence blocks in the input alignment file, a new pseudo sequence is introduced with the align code ._fix_pos. The residues of this pseudo sequence are integer values from 0 through 4 (alternatively, a blank is equivalent to 0). The placement of the non-zero integers is done so that they are below the positions that are to be offset, in an effort to ensure that the alignment implied by that position is restrained. The extent to which this alignment position is restrained depends on the offset that the numerical value (0-4) corresponds to. This can also be specified by the user by setting the matrix offset values with fix_offsets.

Example: examples/salign/salign_fix_positions.py


# Demonstrating the use of alignment restraints, only available in
# align2d and salign:

log.verbose()
env = environ()

# The special alignment entry '_fix_pos' has to be the last entry in the 
# alignment array. Its sequence contains characters blank, 1, 2, 3, and 4 
# at the restrained alignment positions. The residue-residue score from
# the substitution matrix for these positions will be offset by the scalar
# value FIX_OFFSETS[1..5].
aln = alignment(env, file='fix_positions.ali', align_codes=('1leh', '3btoA',
                                                            '_fix_pos'))

# fix_offsets specifies the offset corresponding to character ' 1234' in the
# _fix_pos entry in the alignment
# (this offsets unlabeled positions for 0, the ones indicated by 1 by
#  1000, those indicated by 2 by 2000, etc.)
aln.salign(fix_offsets=(0, 1000, 2000, 3000, 4000),
           gap_penalties_2d=(0, 0, 0, 0, 0, 0, 0, 0, 0), # Any values are
                                                         # possible here
           local_alignment=False, # Local alignment works, too
           gap_penalties_1d=(-600, -400)) # This is best with the default value
                                          # of gap_penalties_2d

# Write it out, the _fix_pos is erased automatically in salign:
aln.write(file='fix_positions_salign.pap', alignment_format='PAP')

External weight matrix: An example of using feature 6.

Example: examples/salign/salign_external_matrix.py


# Reads an external matrix

log.verbose()
env = environ()

aln = alignment(env, file='1dubA-1nzyA.ali', align_codes='all')

aln.salign(alignment_type='pairwise', output='',
           rr_file='$(LIB)/blosum62.sim.mat',
           #rr_file='$(LIB)/as1.sim.mat',
           #max_gap_length=20,
           gap_function=False,
           input_weights_file='external.mtx',   # External weight matrix
           #weights_type='DISTANCE',            # type of ext. wgt. mtx
           # ensure appropriate gap penalites for the ext. matrix
           #feature_weights=(1., 0., 0., 0., 0., 0.), gap_penalties_1d=(30, 26),
           #write_weights=True, output_weights_file='score.mtx',
           feature_weights=(1., 0., 0., 0., 0., 1.),
           gap_penalties_1d=(-500, -300))
aln.write(file='output.ali', alignment_format='PIR')
aln.write(file='output.pap', alignment_format='PAP')

Multiple structure alignment according to a user specified dendrogram The user has the option of inputting an $n$ X $n$ matrix from which a dendrogram can be inferred. The multiple tree alignment is then confined to follow this externally input dendrogram. To effect this, ext_tree is set to True and the external matrix file is specified in input_weights_file. A word of caution: it is not advisible to have feature 6 as non zero when an external dendrogram matrix is read.

Gap penalties and correcting for gaps

SALIGN makes use of three sets of gap penalties. gap_penalty_1d is for dynamic programming making use of constant gap penalties. gap_penalty_2d is when a variable function for gap penalty is used. gap_penalty_3d is used along with feature 2 only, when structures are aligned by a least squares fit of their atomic positions. All SALIGN features produce some measure of residue equivalence (similarity or distance scores). The scales of these scores differ depending on the feature used. For optimal usage, gap_penalties_1d should be set appropriately considering the features used. For example, if feature 1 is non zero, and the residue substitution matrix used is the BLOSUM62 similarity matrix, gap_penalties_1d is set to (-450, -50) and when feature 1 is zero gap_penalties_1d is set to (2, 3). A word of caution: gap penalties have not yet been optimized for aligning sequences by their profiles and for structure alignments.

The gap correction function is $g_{i,j} = \frac{n_{rg}}{(n_1 n_2)} r + \frac{n_{gg}}{(n_1 n_2)} g$, where $n_1$ and $n_2$ are the number of proteins in the two sub-alignments, $n_{rg}$ is the number of gap-residue pairs, and $n_{gg}$ is the number of gap-gap pairs when comparing protein positions from one sub-alignment with protein position from the other sub-alignment, $r$ is gap_residue_score and $g$ is gap_gap_score. The smaller (even negative) is gap_gap_score, and the larger is gap_residue_score, the more will the gaps be aligned with gaps.

Useful SALIGN information and commands

The alignment.salign() command uses position-position dissimilarity scores (except when similarity_flag is switched on), as opposed to similarity scores. This convention applies to all the features, including the residue-residue similarities read from the rr_file; however, if a residue type - residue type similarity matrix is read in, it is automatically converted into the distance matrix by $D = \max_{i,j} S_{i,j} - S$. In addition, it is also scaled linearly such that the residue-residue dissimilarity scores range from 0 to 1 (to facilitate weighting this feature with other features).

For each pairwise alignment, the weight matrix $W$ has dimensions $N$ and $M$ that correspond to the lengths of the sub-alignments to be aligned based on the weight matrix $W$. The dissimilarity score for aligning position $i$ with position $j$ is calculated as $W_{i,j} = \sum_f [ \frac{\omega_f}{\sum_f \omega_f} W^f_{i,j} ] + g_{i,j}$, where the sum runs over all selected features $f$, and $g$ is a function that may be used to correct the $W_{i,j}$ score for the presence of gaps within the sub-alignments (see below). A feature $f$ is selected when its weight $\omega_f$ (specified in feature_weights) is non-zero. The matrices $W^f$ are normalized to have the mean of 0 and standard deviation of 1 when normalize_pp_scores is True, but it is recommended not to use this option for now (i.e., use feature_weights to scale the contributions of the different features to the final $W$). The weights of 1 will weigh the different features approximately evenly (the residue-residue dissimilarities of feature 1 are scaled to a range from 0 to 1, the position differences of feature 2 are in angstroms, the fractional solvent accessibility scores of feature 3 and the secondary structure scores of feature 4 range from 0 to 2, and the DRMS difference of feature 5 is expressed in angstroms).

If you enable verbose logging with log.verbose(), there will be more output in the 'log' file, such as the dendrogram. The dendrogram can also be written out in a separate file by specifying the file name to dendrogram_file.

Argument output can contain the following values:

If write_fit is True, the fitted atom files are written out in their fitted orientations. For this and other options below, also read the text above.

If write_weights is True, the dynamic programming weight matrix is written out into the file specified by output_weights_file.

If current_directory is True, the output _pdb.fit files will be written to the current directory. Otherwise, the output will be in the directory with the original files.

If write_whole_pdb is True, the whole PDB files are written out; otherwise only the parts corresponding to the aligned sequences are output.

If fit is False, the initial superposition is not changed. This is useful when all the structures have to be compared with a given alignment as is, without changing their relative orientation.

If fit_on_first is True, the structures are fit to the first structure according to the final alignment before they are written out.

If improve_alignment is False, the initial alignment is not changed, though the structures may still be superimposed if fit = True. This is useful when all the structures have to be superimposed with the initial alignment.


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Next: alignment.to_profile() convert Up: The alignment class: comparison Previous: alignment.malign3d() align   Contents   Index
Ben Webb 2005-06-20