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. Author manuscript; available in PMC: 2010 May 1.
Published in final edited form as: Arch Biochem Biophys. 2009 May 1;485(1):16–23. doi: 10.1016/j.abb.2009.01.014

Table 1.

Top-scoring structures that can serve as templates for the CPAF amino acid sequence in the program MODELLER [28] as identified by the program HHPRED [26, 27]. The column labeled “Prob” is the probability that the database match is a true positive. “E-values” are defined in the same way as in PSI-BLAST [46]. The “P-value” is equal to the “E-value” divided by the number of HMMs in the protein data bank. The “Score” column gives the total score that includes the score from the secondary structure comparison, which is listed in the column labeled “SS”. “Cols” contains the total number of matched columns in the query–template alignment and the remaining columns describe the range of aligned residues in the query and template [26, 27].

No. Hit
PDB Code
Protein
Prob
E-val
P-val
Score
SS
Cols
Query HMM
Template HMM
1 1k32 [25] Tricorn Protease
Thermatoga maritima
100 0 0 335.6 32.0 363 36-601 657-1040 (1045)
2 1fc6 [45] PS II D1 Protease
Scenedesmus obliquus
100 0 0 299.5 34.8 363 34-593 2-381 (388)
3 1j7x [47] IRBP Interphotoreceptor
Xenopus laevis
100 8.9E-38 7E-42 241.1 17.4 180 321-569 104-283 (302)
4 2ejy [48] Erythrocyte membrane protein
Homo sapiens
92.7 0.096 7.5E-6 28.0 5.2 49 108-156 16-69 (97))
5 2ev8 [49] Erythrocyte membrane protein
Homo sapiens
92.1 0.093 7.3E-6 28.0 4.6 49 108-156 16-69 (97)