Evidence map›Paper›PMID 33108589›Full record

ArticleJournal of computer-aided molecular design2021

The critical role of QM/MM X-ray refinement and accurate tautomer/protomer determination in structure-based drug design.

Oleg Y Borbulevych, Roger I Martin, Lance M Westerhoff

Open access · hybridAbstract read
In one paragraph

Article in Journal of computer-aided molecular design, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 25 citations in OpenAlex.

  1. Critical evaluation of two neutron structures of Mn superoxide dismutase with quantum refinement.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. Article
  3. Review
  4. Favipiravir-Tautomeric and Complexation Properties in Solution.Pharmaceuticals (Basel, Switzerland) · 2022
    Article
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Oleg Y BorbulevychQuantumBio Inc, 2790 West College Ave, Suite 900, State College, PA, 16801, USA.
Roger I MartinQuantumBio Inc, 2790 West College Ave, Suite 900, State College, PA, 16801, USA.
Lance M WesterhoffQuantumBio Inc, 2790 West College Ave, Suite 900, State College, PA, 16801, USA. lance@quantumbioinc.com.ORCID 0000-0001-8092-6919
QuantumBio (United States) · US

Funding

Enhancement and Deployment of the Quantum Mechanical X-ray Refinement ModelR44GM079899 · NIGMS · QUANTUMBIO, INC. · PI WESTERHOFF, LANCE M · 2008 to 2010
$1.4M
Development of the Movable Type free energy method for ligand placement in X-ray crystallographyR44GM121162 · NIGMS · QUANTUMBIO, INC. · PI WESTERHOFF, LANCE M · 2017 to 2019
$1.3M
A new approach to solvent determination in QM/MM-based X-ray crystallographic refinementR43GM113555 · NIGMS · QUANTUMBIO, INC. · PI WESTERHOFF, LANCE M · 2015 to 2015
$141k
NIGMS NIH HHS R43 GM113555NIGMS NIH HHS R44 GM079899NIGMS NIH HHS R44 GM121162
6 · The paper itself

Abstract

Conventional protein:ligand crystallographic refinement uses stereochemistry restraints coupled with a rudimentary energy functional to ensure the correct geometry of the model of the macromolecule-along with any bound ligand(s)-within the context of the experimental, X-ray density. These methods generally lack explicit terms for electrostatics, polarization, dispersion, hydrogen bonds, and other key interactions, and instead they use pre-determined parameters (e.g. bond lengths, angles, and torsions) to drive structural refinement. In order to address this deficiency and obtain a more complete and ultimately more accurate structure, we have developed an automated approach for macromolecular refinement based on a two layer, QM/MM (ONIOM) scheme as implemented within our DivCon Discovery Suite and "plugged in" to two mainstream crystallographic packages: PHENIX and BUSTER. This implementation is able to use one or more region layer(s), which is(are) characterized using linear-scaling, semi-empirical quantum mechanics, followed by a system layer which includes the balance of the model and which is described using a molecular mechanics functional. In this work, we applied our Phenix/DivCon refinement method-coupled with our XModeScore method for experimental tautomer/protomer state determination-to the characterization of structure sets relevant to structure-based drug design (SBDD). We then use these newly refined structures to show the impact of QM/MM X-ray refined structure on our understanding of function by exploring the influence of these improved structures on protein:ligand binding affinity prediction (and we likewise show how we use post-refinement scoring outliers to inform subsequent X-ray crystallographic efforts). Through this endeavor, we demonstrate a computational chemistry ↔ structural biology (X-ray crystallography) "feedback loop" which has utility in industrial and academic pharmaceutical research as well as other allied fields.

Indexed as

Drug DesignBinding SitesCrystallography, X-RayDatabases, ProteinHumansIsomerismModels, MolecularPharmaceutical PreparationsPharmacologyProtein ConformationProteinsQuantum TheorySmall Molecule LibrariesPharmaceutical PreparationsProteinsSmall Molecule LibrariesCSAR setdifference density Z-scorehigh throughput crystallographyLigand strainprotonation statesQuantum mechanics X-ray refinementStructure-based drug discoveryStructure guided drug discoverytautomersX-ray crystallography

Identifiers

PMID33108589
PMCPMC8018927
OpenAlexW3095138998

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.