Evidence map›Paper›PMID 27050137›Full record

ArticleActa crystallographica. Section D, Structural biology2016

XModeScore: a novel method for accurate protonation/tautomer-state determination using quantum-mechanically driven macromolecular X-ray crystallographic refinement.

Oleg Borbulevych, Roger I Martin, Ian J Tickle, Lance M Westerhoff

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

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0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

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3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
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  10. Q|R: quantum-based refinement.Acta crystallographica. Section D, Structural biology · 2017
    Article
  11. Improved ligand geometries in crystallographic refinement using AFITT in PHENIX.Acta crystallographica. Section D, Structural biology · 2016
    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

4 authors.

Oleg BorbulevychQuantumBio Inc., 2790 West College Avenue, State College, PA 16801, USA.
Roger I MartinQuantumBio Inc., 2790 West College Avenue, State College, PA 16801, USA.
Ian J TickleAstex Pharmaceuticals, 436 Science Park, Milton Road, Cambridge CB4 0QA, England.
Lance M WesterhoffQuantumBio Inc., 2790 West College Avenue, State College, PA 16801, USA.

Funding

Enhancement and Deployment of the Quantum Mechanical X-ray Refinement ModelR44GM079899 · NIGMS · QUANTUMBIO, INC. · PI WESTERHOFF, LANCE M · 2008 to 2010
$1.4M
NIGMS NIH HHS #R42GM079899NIGMS NIH HHS R44 GM079899
6 · The paper itself

Abstract

Gaining an understanding of the protein-ligand complex structure along with the proper protonation and explicit solvent effects can be important in obtaining meaningful results in structure-guided drug discovery and structure-based drug discovery. Unfortunately, protonation and tautomerism are difficult to establish with conventional methods because of difficulties in the experimental detection of H atoms owing to the well known limitations of X-ray crystallography. In the present work, it is demonstrated that semiempirical, quantum-mechanics-based macromolecular crystallographic refinement is sensitive to the choice of a protonation-state/tautomer form of ligands and residues, and can therefore be used to explore potential states. A novel scoring method, called XModeScore, is described which enumerates the possible protomeric/tautomeric modes, refines each mode against X-ray diffraction data with the semiempirical quantum-mechanics (PM6) Hamiltonian and scores each mode using a combination of energetic strain (or ligand strain) and rigorous statistical analysis of the difference electron-density distribution. It is shown that using XModeScore it is possible to consistently distinguish the correct bound protomeric/tautomeric modes based on routine X-ray data, even at lower resolutions of around 3 Å. These X-ray results are compared with the results obtained from much more expensive and laborious neutron diffraction studies for three different examples: tautomerism in the acetazolamide ligand of human carbonic anhydrase II (PDB entries 3hs4 and 4k0s), tautomerism in the 8HX ligand of urate oxidase (PDB entries 4n9s and 4n9m) and the protonation states of the catalytic aspartic acid found within the active site of an aspartic protease (PDB entry 2jjj). In each case, XModeScore applied to the X-ray diffraction data is able to determine the correct protonation state as defined by the neutron diffraction data. The impact of QM-based refinement versus conventional refinement on XModeScore is also discussed.

Indexed as

SoftwareAcetazolamideCarbonic Anhydrase IICrystallography, X-RayHumansAcetazolamideCarbonic Anhydrase IIdifference density Z scorehigh-throughput crystallographyligand strainprotonation statesquantum-mechanics X-ray refinementstructure-based drug discoverystructure-guided drug discoverytautomersXModeScoreX-ray crystallography

Identifiers

PMID27050137
PMCPMC4822566

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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.