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Note that, for the case of ligands (contrary to proteins, as described above), their structures are most commonly not superimposed prior to the calculation of the RMSD. RMSD is also one of several metrics that have been proposed for quantifying evolutionary similarity between proteins, as well as the quality of sequence alignments. [7] [8]
In experimental psychology, the RMSD is used to assess how well mathematical or computational models of behavior explain the empirically observed behavior. In GIS, the RMSD is one measure used to assess the accuracy of spatial analysis and remote sensing. In hydrogeology, RMSD and NRMSD are used to evaluate the calibration of a groundwater ...
The MSE either assesses the quality of a predictor (i.e., a function mapping arbitrary inputs to a sample of values of some random variable), or of an estimator (i.e., a mathematical function mapping a sample of data to an estimate of a parameter of the population from which the data is sampled).
A free PyMol plugin easily implementing Kabsch is . (This previously linked to CEalign , but this uses the Combinatorial Extension (CE) algorithm.) VMD uses the Kabsch algorithm for its alignment. The FoldX modeling toolsuite incorporates the Kabsch algorithm to measure RMSD between Wild Type and Mutated protein structures.
The RMS value of a set of values (or a continuous-time waveform) is the square root of the arithmetic mean of the squares of the values, or the square of the function that defines the continuous waveform.
This is a list of free and open-source software (FOSS) packages, computer software licensed under free software licenses and open-source licenses.Software that fits the Free Software Definition may be more appropriately called free software; the GNU project in particular objects to their works being referred to as open-source. [1]
The data set [1, 5, 6, 8, 10, 40, 65, 88] has still more variability. Its standard deviation is 32.9 and its average is 27.9, giving a coefficient of variation of 32.9 / 27.9 = 1.18 In these examples, we will take the values given as the entire population of values .
The maximum is taken over all possible structure superpositions of the model and template (or some sample thereof). When comparing two protein structures that have the same residue order, L common {\displaystyle L_{\text{common}}} reads from the C-alpha order number of the structure files (i.e., Column 23-26 in Protein Data Bank (file format) ).