Summary: Two web-based applications to analyze amino acids three-dimensional (3D) local environment within protein structures---SCORPION and FORMIGA---are presented. SCORPION and FORMIGA produce a graphical presentation for simple statistical data showing the frequency of residue occurrence within a given sphere (defined here as the 3D contacts). The center of that sphere is placed at the Cα and at the last heavy atom in the side chain of the selected amino acid. Further depth of detail is given in terms of a secondary structure to which the profiled amino acid belongs. Results obtained with those two applications are relevant for estimating the importance of the amino acid 3D local environment for protein folding and stability. Effectively, SCORPION and FORMIGA construct knowledge-based force fields. The difference between SCORPION and FORMIGA is in that the latter operates on protein interfaces, while the former only functions for a single protein chain. Both applications are implemented as stand-alone components of STING Millennium Suite.#R##N##R##N#Availability:http://sms.cbi.cnptia.embrapa.br/SMS, http://trantor.bioc.columbia.edu/SMS, http://mirrors.rcsb.org/SMS, http://www.es.embnet.org/SMS and http://www.ar.embnet.org/SMS. {options: Scorpion, Formiga}
['Roberto H. Higa', 'Adilton G. Oliveira', 'Luiz G. Horita', 'Ronald T. Miura', 'Marcus K. Inoue', 'Paula R. Kuser', 'Adauto L. Mancini', 'Michel Eduardo Beleza Yamagishi', 'Roberto C. Togawa', 'Goran Neshich']
Defining 3D residue environment in protein structures using SCORPION and FORMIGA