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Analysis of the conformations of the HIV-1 protease from a large crystallographic data set.

Analysis of the conformations of the HIV-1 protease from a large crystallographic data set.
Author Information (click to view)

Palese LL,


Palese LL, (click to view)

Palese LL,

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Data in brief 2017 10 0615() 696-700 doi 10.1016/j.dib.2017.09.076

Abstract

The HIV-1 protease performs essential roles in viral maturation by processing specific cleavage sites in the Gag and Gag-Pol precursor polyproteins to release their mature forms. Here the analysis of a large HIV-1 protease data set (containing 552 dimer structures) are reported. These data are related to article entitled "Conformations of the HIV-1 protease: a crystal structure data set analysis" (Palese, 2017) [1].

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