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. 2021 Mar 19;22(5):580–601. doi: 10.1111/mpp.13045

TABLE 1.

Main quality scores of the 3D protein models obtained for PHEC27213 using different servers

Server Model quality score a Structural analogues b TM‐score c Coverage d
I‐TASSER −0.70 AA11 LPMO from A. oryzae (4MAH) 0.715 0.764
IntFOLD 0.463 LPMO‐like from L. arvalis (6IBH) 0.721 0.733
Phyre2 LPMO‐like from L. arvalis (6IBH) 97.5% 0.670
a

In I‐TASSER, this value is the C‐score. C‐score is in the range of −5 and 2, where a C‐score of higher value signifies a model with a high confidence. In IntFOLD, the global model quality scores range between 0 and 1, where scores less than 0.2 indicate there may be incorrectly modelled domains and scores greater than 0.4 generally indicate more complete and confident models. This value is not available in Phyre2.

b

Protein structurally closest to the corresponding PHEC27213 model according to protein fold recognition analysis. The corresponding PDB (Protein Data Bank) code is shown in parentheses.

c

TM‐score values are known standards for measuring the structural similarity between two structures, which are usually used to measure the accuracy of structure modelling when the native structure is known. In I‐Tasser and IntFOLD, TM‐scores are in the range of 0 to 1, being 1 a perfect match between models. In Phyre2, TM‐scores range between 0% and 100%.

d

Coverage represents the coverage of the alignment by TM‐align and is equal to the number of structurally aligned residues divided by length of the query protein.