Align

Two proteins after structure alignment

align performs a sequence alignment followed by a structural superposition, and then carries out zero or more cycles of refinement in order to reject structural outliers found during the fit. align does a good job on proteins with decent sequence similarity (identity >30%). For comparing proteins with lower sequence identity, the super and cealign commands perform better.

Usage

align mobile, target [, cutoff [, cycles
    [, gap [, extend [, max_gap [, object
    [, matrix [, mobile_state [, target_state
    [, quiet [, max_skip [, transform [, reset ]]]]]]]]]]]]]

Arguments

• mobile = string: atom selection of mobile object
• target = string: atom selection of target object
• cutoff = float: outlier rejection cutoff in RMS {default: 2.0}
• cycles = int: maximum number of outlier rejection cycles {default: 5}
• gap, extend, max_gap: sequence alignment parameters
• object = string: name of alignment object to create {default: (no alignment object)}
• matrix = string: file name of substitution matrix for sequence alignment {default: BLOSUM62}
• mobile_state = int: object state of mobile selection {default: 0 = all states}
• target_state = int: object state of target selection {default: 0 = all states}
• quiet = 0/1: suppress output {default: 0 in command mode, 1 in API}
• max_skip = ?
• transform = 0/1: do superposition {default: 1}
• reset = ?

Alignment Objects

An alignment object can be created with the object=somename argument. An alignment object provides:

• aligned sequence viewer
• graphical representation of aligned atom pairs as lines in the 3D viewer
• can be saved to a clustalw sequence alignment file

RMSD

The RMSD of the aligned atoms (after outlier rejection!) is reported in the text output. The all-atom RMSD can be obtained by setting cycles=0 and thus not doing any outlier rejection. The RMSD can also be captured with a python script, see the API paragraph below. Note that the output prints "RMS" but it is in fact "RMSD" and the units are Angstroms.

Examples

fetch 1oky 1t46, async=0

# 1) default with outlier rejection
align 1oky, 1t46

# 2) with alignment object, save to clustalw file
align 1oky, 1t46, object=alnobj
save alignment.aln, alnobj

# 3) all-atom RMSD (no outlier rejection) and without superposition
align 1oky, 1t46, cycles=0, transform=0

PyMOL API

cmd.align( string mobile, string target, float cutoff=2.0,
           int cycles=5, float gap=-10.0, float extend=-0.5,
           int max_gap=50, string object=None, string matrix='BLOSUM62',
           int mobile_state=0, int target_state=0, int quiet=1,
           int max_skip=0, int transform=1, int reset=0 )

This returns a list with 7 items:

1. RMSD after refinement
2. Number of aligned atoms after refinement
3. Number of refinement cycles
4. RMSD before refinement
5. Number of aligned atoms before refinement
6. Raw alignment score
7. Number of residues aligned

Notes

• The molecules you want to align need to be in two different objects. Else, PyMOL will answer with: ExecutiveAlign: invalid selections for alignment. You can skirt this problem by making a temporary object and aligning your original to the copy.
• By defaults, all states (like in NMR structures or trajectories) are considered, this might yield a bad or suboptimal alignment for a single state. Use the mobile_state and target_state argument to be explicit in such cases.

See Also

• super, cealign, fit, pair_fit
• rms, rms_cur,
• intra_fit, intra_rms, intra_rms_cur
• extra_fit
• align_all.py and super_all.py
• tmalign
• Color_by_conservation
• Get_raw_alignment
• mcsalign (psico)