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|title=Protein structure prediction and analysis using the Robetta server
|authors=David E. Kim, Dylan Chivian, and David Baker
|doi-access= free
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|title=SCOPmap: Automated assignment of protein structures to evolutionary superfamilies
|authors=Sara Cheek, Yuan Qi, Sri Krishna, Lisa N Kinch, and Nick V Grishin
|doi-access=free
}}</ref>
<ref name="fssa">{{cite journal
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|pages=(Suppl 1):15-19.
| doi=10.1002/prot.25005
|doi-access=free
}}</ref><ref name="Malmstrom"></ref><ref name="robetta"></ref> These decoys are notorious for getting local fragment motif structure correct, and forming some kernels of correct 3D tertiary structure but getting the full length tertiary structure wrong. In this twilight remote homology regime, Mammoth's e-values for the CASP<ref name="casp11"></ref> protein structure prediction evaluation have been show to be significantly more correlated with human ranking than SSAP or DALI.<ref name=Mammoth></ref> Mammoths ability to extract the multi-criteria partial overlaps with proteins of known structure and rank these with proper E-values, combined with its speed facilitates scanning vast numbers of decoy models against the PDB data base for identifying the most likely correct decoys based on their remote homology to known proteins.
<ref name="Malmstrom">{{cite journal
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