Evidence map›Paper›PMID 34076588›Full record

ArticleActa crystallographica. Section D, Structural biology2021

The missing link: covalent linkages in structural models.

Robert A Nicholls, Marcin Wojdyr, Robbie P Joosten, Lucrezia Catapano, Fei Long, Marcus Fischer, Paul Emsley, Garib N Murshudov

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. A database overview of metal-coordination distances in metalloproteins.Acta crystallographica. Section D, Structural biology · 2024
    Article
  5. Neutron crystallographic refinement with REFMAC5 from the CCP4 suite.Acta crystallographica. Section D, Structural biology · 2023
    Article
  6. The CCP4 suite: integrative software for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2023
    Article
  7. GEMMI and Servalcat restrain REFMAC5.Acta crystallographica. Section D, Structural biology · 2023
    Article
  8. Updated restraint dictionaries for carbohydrates in the pyranose form.Acta crystallographica. Section D, Structural biology · 2022
    Article
  9. Ten things I `hate' about refinement.Acta crystallographica. Section D, Structural biology · 2021
    Article
  10. Cryo-EM single-particle structure refinement and map calculation using Servalcat.Acta crystallographica. Section D, Structural biology · 2021
    Article
  11. New restraints and validation approaches for nucleic acid structures in PDB-REDO.Acta crystallographica. Section D, Structural biology · 2021
    Article
  12. Modelling covalent linkages in CCP4.Acta crystallographica. Section D, Structural biology · 2021
    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

8 authors.

Robert A NichollsStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-8577-8617
Marcin WojdyrGlobal Phasing Limited, Sheraton House, Castle Park, Cambridge CB3 0AX, United Kingdom.ORCID 0000-0003-3980-4092
Robbie P JoostenNetherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.ORCID 0000-0002-2323-2686
Lucrezia CatapanoStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-5641-0098
Fei LongStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-2553-9841
Marcus FischerChemical Biology and Therapeutics and Structural Biology, St Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105-3678, USA.ORCID 0000-0002-7179-2581
Paul EmsleyStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.
Garib N MurshudovStructural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0001-6483-3587

Funding

Biotechnology and Biological Sciences Research Council BB/S007083/1Horizon 2020 Framework Programme, iNEXT-Discovery 871037Medical Research Council MC_UP_A025_1012
6 · The paper itself

Abstract

Covalent linkages between constituent blocks of macromolecules and ligands have been subject to inconsistent treatment during the model-building, refinement and deposition process. This may stem from a number of sources, including difficulties with initially detecting the covalent linkage, identifying the correct chemistry, obtaining an appropriate restraint dictionary and ensuring its correct application. The analysis presented herein assesses the extent of problems involving covalent linkages in the Protein Data Bank (PDB). Not only will this facilitate the remediation of existing models, but also, more importantly, it will inform and thus improve the quality of future linkages. By considering linkages of known type in the CCP4 Monomer Library (CCP4-ML), failure to model a covalent linkage is identified to result in inaccurate (systematically longer) interatomic distances. Scanning the PDB for proximal atom pairs that do not have a corresponding type in the CCP4-ML reveals a large number of commonly occurring types of unannotated potential linkages; in general, these may or may not be covalently linked. Manual consideration of the most commonly occurring cases identifies a number of genuine classes of covalent linkages. The recent expansion of the CCP4-ML is discussed, which has involved the addition of over 16 000 and the replacement of over 11 000 component dictionaries using AceDRG. As part of this effort, the CCP4-ML has also been extended using AceDRG link dictionaries for the aforementioned linkage types identified in this analysis. This will facilitate the identification of such linkage types in future modelling efforts, whilst concurrently easing the process involved in their application. The need for a universal standard for maintaining link records corresponding to covalent linkages, and references to the associated dictionaries used during modelling and refinement, following deposition to the PDB is emphasized. The importance of correctly modelling covalent linkages is demonstrated using a case study, which involves the covalent linkage of an inhibitor to the main protease in various viral species, including SARS-CoV-2. This example demonstrates the importance of properly modelling covalent linkages using a comprehensive restraint dictionary, as opposed to just using a single interatomic distance restraint or failing to model the covalent linkage at all.

Indexed as

Models, StructuralCrystallography, X-RayDatabases, ProteinLigandsSARS-CoV-2Viral ProteinsLigandsViral ProteinsAceDRGCCP4 Monomer Librarycovalent linkagerestraint dictionarySARS-CoV-2

Identifiers

PMID34076588
PMCPMC8171067

What OpenQuestion holds

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Registered trials

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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.