caa a22 4500 445325291 CHVBK 20180317142718.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10858-011-9534-0 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9534-0 Biomolecular structure refinement using the GROMOS simulation software [Elektronische Daten] [Nathan Schmid, Jane Allison, Jožica Dolenc, Andreas Eichenberger, Anna-Pitschna Kunz, Wilfred van Gunsteren] For the understanding of cellular processes the molecular structure of biomolecules has to be accurately determined. Initial models can be significantly improved by structure refinement techniques. Here, we present the refinement methods and analysis techniques implemented in the GROMOS software for biomolecular simulation. The methodology and some implementation details of the computation of NMR NOE data, 3 J-couplings and residual dipolar couplings, X-ray scattering intensities from crystals and solutions and neutron scattering intensities used in GROMOS is described and refinement strategies and concepts are discussed using example applications. The GROMOS software allows structure refinement combining different types of experimental data with different types of restraining functions, while using a variety of methods to enhance conformational searching and sampling and the thermodynamically calibrated GROMOS force field for biomolecular simulation. Springer Science+Business Media B.V., 2011 GROMOS nationallicence Structure refinement nationallicence Crystallography nationallicence NMR nationallicence Schmid Nathan Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut Allison Jane Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut Dolenc Jožica Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut Eichenberger Andreas Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut Kunz Anna-Pitschna Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut van Gunsteren Wilfred Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 265-281 0925-2738 51:3<265 2011 51 10858 https://doi.org/10.1007/s10858-011-9534-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9534-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Schmid Nathan Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut NATIONALLICENCE 700 1- Allison Jane Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut NATIONALLICENCE 700 1- Dolenc Jožica Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut NATIONALLICENCE 700 1- Eichenberger Andreas Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut NATIONALLICENCE 700 1- Kunz Anna-Pitschna Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut NATIONALLICENCE 700 1- van Gunsteren Wilfred Laboratory of Physical Chemistry, Swiss Federal Institute of Technology ETH, 8093, Zürich, Switzerland aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 265-281 0925-2738 51:3<265 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer