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Calculation of The Protein Structure Quality Score (PSQS)

PSQS is calculated in two steps:

  • Geometrical parameters of a given structure are obtained including: local backbone geometry class, burial status of all residues (based on the number of interatomic contacts with other residues), and contact distances between different residues

  • Calculation of local, burial and contact energy is accomplished by application of statistical potentials of mean force to these parameters

We have found that in many cases PSQS makes it possible to differentiate between correct and incorrect protein structures. It should be noted, however, that essentially PSQS reflects the similarity between a given protein structure and a "typical protein structure", so it is expected to yield best results for monomeric globular proteins without large ligands or significant biases in amino-acid composition.

PSQS may be used in homology modelling to evaluate alternative protein models based on different alignments. It may also be useful during structure refinement to locate the places that are significantly different from typical geometries.

The graph on Fig. 1 shows the joint empirical distribution density of psqs and rmsd. The distribution was calculated on the data base of 41,000 Levitt Decoys. As expected PSQS values increase with increasing distance from the native structure. This relationship holds within about 5 A RMSD from the native structure.

Fig. 2 shows the distribution of PSQS on a representative set of structures covering all folds taken from the SCOP data base. The average PSQS for this set is -0.27 and most have structures have PSQS less than -0.1. These statisics were used to calibrate the coloring scheme used for analysis of 3D distribution of PSQS along the protein chain.




Figure 1 (the graph was made with gnuplot)




   

Figure 2




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  Last Modified Wed Oct 3 10:22:39 2001