Prediction Performance in CASP4

In the recent Fourth Community Wide Experiment on the Critical Assessment of Techniques for Protein Structure Prediction (CASP4), PROSPECT finished the 6th in the total scores in the fold recognition category out of 123 groups in the world. This is a benchmark experiment conducted every two years by groups from all over the world to test their methods and algorithms for protein structure predictions. None of the five groups that outperformed PROSPECT used threading methods, and this makes PROSPECT the best threading program in the contest. The following table summarizes the prediction performance in CASP4 based on the 32 experimental structures released so far among the 43 prediction targets.


target  model   length  segment  SARF   identity quality

T0087   1       309     1-116    63     -        good alignment (domain)
T0089   1       378              200    8%       good alignment
T0092   1       227              148    12%      good alignment
T0094   1       177     18-40    28     -        motif
T0096   1       222     10-73    55     15%      good alignment (domain)
T0097   1       105              35     -        unrecognized
T0098   2       119              60     -        good alignment
T0099   1       56               43     48%      perfect alignment
T0100   1       342              177    -        good alignment
T0101   1       400              195    -        fold recognized
T0102   1       70               31     -        fold recognized
T0103   1       368              209    17%      good alignment
T0105   1       94               25     -        unrecognized
T0106   1       125     27-57    31     -        motif
T0107   5       188              74     -        fold recognized
T0108   1       179              69     -        fold recognized
T0109   1       182              90     -        fold recognized
T0110   1       95               48     -        fold recognized
T0111   1       429              414    50%      perfect alignment
T0112   1       348              294    21%      perfect alignment
T0114   4       87               42     -        fold recognized
T0115   1       296              46     -        unrecognized
T0116   1       759     572-713  73     -        fold recognized (domain)
T0120   1       203              26     -        unrecognized
T0121   1       372              173    27%      perfect alignment
T0122   1       241              216    33%      perfect alignment
T0123   1       160              120    61%      perfect alignment
T0124   1       242     999-1143 96     -        fold recognized (domain)
T0125   1       137              107    17%      perfect alignment
T0126   1       162              27     -        unrecognized
T0127   1       332              105    -        good alignment
T0128   1       211              198    50%      perfect alignment

Target represents CASP4 target identification number. Model gives the model number among our five submitted structures. Length is the number of amino acids in the experimental structure. Segment gives the range in the sequence when only a domain or motif is recognized by our prediction. SARF provides the number of equivalent residues for the structurally alignable portion between the experimental structure and the predicted one in a sequence independent superposition using SARF. Identity represents the sequence identity between the target and its closest homologue in PDB if it has one defined by CAFASP2 organizers (see http://www.cs.bgu.ac.il/~dfischer/CAFASP2/targets.html); otherwise a "-" is given. We have divided our prediction results into five categories: (a) perfect alignment: the predicted model and the experimental structure have a perfect alignment in the sequence-dependent superposition; (b) good alignment: the model has small errors in the alignment to the correct fold; (c) fold recognized: the correct fold is identified, but the alignment is not good; (d) motif: only a motif or a super-secondary structure is predicted correctly with a small RMSD to the corresponding portion of the experimental structure in the sequence-dependent superposition; (e) unrecognized: the model has a significantly different fold from the experimental structure.

 


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