Xia, Fei Tong, Dudu Lu, Lanyuan Robust Heterogeneous Anisotropic Elastic Network Model Precisely Reproduces the Experimental B‑factors of Biomolecules A computational method called the progressive fluctuation matching (PFM) is developed for constructing robust heterogeneous anisotropic network models (HANMs) for biomolecular systems. An HANM derived through the PFM approach consists of harmonic springs with realistic positive force constants, and yields the calculated B-factors that are basically identical to the experimental ones. For the four tested protein systems including crambin, trypsin inhibitor, HIV-1 protease, and lysozyme, the root-mean-square deviations between the experimental and the computed B-factors are only 0.060, 0.095, 0.247, and 0.049 Å<sup>2</sup>, respectively, and the correlation coefficients are 0.99 for all. By comparing the HANM/ANM normal modes to their counterparts derived from both an atomistic force field and an NMR structure ensemble, it is found that HANM may provide more accurate results on protein dynamics. biomolecular systems;atomistic force field;correlation coefficients;anisotropic network models;PFM approach;HIV;NMR structure ensemble;protein systems;HANM;Robust Heterogeneous Anisotropic Elastic Network Model;protein dynamics;trypsin inhibitor;force constants 2013-08-13
    https://acs.figshare.com/articles/journal_contribution/Robust_Heterogeneous_Anisotropic_Elastic_Network_Model_Precisely_Reproduces_the_Experimental_B_factors_of_Biomolecules/2387977
10.1021/ct4002575.s001