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errat score

by Bo Lebsack Published 3 years ago Updated 2 years ago

ERRAT is a so-called “overall quality factor” for non-bonded atomic interactions, with higher scores indicating higher quality. The generally accepted range is >50 for a high quality model. For the current 3D model, the overall quality factor predicted by the ERRAT server was 80.524 (Figure 3).02-Apr-2013

What is the errat program?

02/04/2013 · ERRAT is a so-called “overall quality factor” for non-bonded atomic interactions, with higher scores indicating higher quality. The generally accepted range is >50 for a high quality model. For the current 3D model, the overall quality factor predicted by the ERRAT server was 80.524 (Figure 3). The Verify 3D server predicted that 88.77% of the residues in VEB-1 β …

What is errat and who wrote it?

In the ERRAT plot the overall quality factor of the model was 96.0784. But the plot showed there were some residues (within the refined region) which attained zero (0) value (Fig attached). Can ...

What is the errat score of the histamine H4 receptor?

22/05/2015 · This compatibility score of an atomic model (3D) with its sequence (1D) ranges from -1 (bad) to +1 (good), so, score 0.77 in verify 3D determines good environmental profile of the structure . ERRAT, the structure verification algorithm interpreted the overall quality of the model with the resulting score 78.313; this score denotes the percentage of the protein that …

What is the quality factor of the errat plot?

02/02/2021 · Again in ERRAT, the structure verification algorithm interpreted the overall quality of the model with the resulting score 93.33; this score denoted the percentage of the protein that fell below the rejection limit of 95% [ 73 ]. So ERRAT program also verified the protein 3D structure as acceptable.

What is Errat in bioinformatics?

ERRAT is a program for verifying protein structures determined by crystallography. ... The error function is based on the statistics of non-bonded atom-atom interactions in the reported structure (compared to a database of reliable high-resolution structures). The figure shows a plot of an initial model and a final model.

What is Q mean score?

QMEAN, which stands for Qualitative Model Energy ANalysis, is a composite scoring function describing the major geometrical aspects of protein structures. Five different structural descriptors are used. The local geometry is analyzed by a new kind of torsion angle potential over three consecutive amino acids.

How to interpret VERIFY 3D results?

On verify3D, a score of more than 80% means that your model has good quality - however you must check with other evaluation tolls such as voromqa, Proq3 etc to make sure you have a high quality model.

What is verify3D?

 Determines the compatibility of an atomic model (3D) with its own amino acid sequence (1D) by assigning a structural class based on its location and environment (alpha, beta, loop, polar, nonpolar etc) and comparing the results to good structures.

What is a good GMQE?

In general a higher QSQE is "better", while a value above 0.7 can be considered reliable to follow the predicted quaternary structure in the modelling process. This complements the GMQE score which estimates the accuracy of the tertiary structure of the resulting model.

What is Z score in SWISS-MODEL?

In SWISS-MODEL the QMEAN z-score represents an estimate of how comparable the model is to experimentally derived structures of similar size. QMEAN z-scores around zero indicate good agreement between the model structure and experimental structures of similar size.

How do you use Modrefiner?

Cut and paste the structure you want to refine (C-alpha trace, main-chain model or full-atomic model) in PDB format here: Or upload the target structure file from your local computer: Upload a reference structure (only C-alpha trace required) to which the refined model will be driven (Optional):

How do you cite Pdbsum?

PDBsum is a database that provides an overview of the contents of each 3D macromolecular structure deposited in the Protein Data Bank....PDBsum.ContentAuthorsRoman Laskowski & al. (1997)Primary citationPMID 9433130AccessWebsitewww.ebi.ac.uk/pdbsum/8 more rows

How do you cite MolProbity?

Cite MolProbity: Chen et al. (2010) MolProbity: all-atom structure validation for macromolecular crystallography.

When was tazobactam developed?

Sulbactam and tazobactam are penicillinate sulfones developed as synthetic compounds in 1978 and 1980 , respectively [17,18]. Class A β-lactamase is inhibited to comparable levels by moxalactam, imipenem and cefoxitin. The crystal structure of VEB-1 β-lactamase has not been described.

Does clavulanate lower MICs?

Clavulanate (the salt form of the acid in solution) presented with little antimicrobial activity in isolation, but when combined with amoxicillin, it significantly lowered amoxicillin MICs against Staphylococcus aureus, Klebsiella pneumoniae, Proteus mirabilisand E. coli[16].

Most recent answer

On verify3D, a score of more than 80% means that your model has good quality - however you must check with other evaluation tolls such as voromqa, Proq3 etc to make sure you have a high quality model.

All Answers (9)

You can check Ramachandran Plot from procheck and look for residues in favored regions and outliers. This will give you estimation about your model quality.

Abstract

The M4 family of metalloproteases is comprised of a large number of zinc-containing metalloproteases. A large number of these enzymes are important virulence factors of pathogenic bacteria and therefore potential drug targets.

Background

Proteases are enzymes that can hydrolyze proteins and are composed of a diverse group of exoproteases and endoproteases depending on their activity. Based on their catalytic mechanism, endoproteases are divided into aspartic proteases, cysteine proteases, metalloproteases, serine proteases, and threonine proteases [ 1 ].

Methods

A total of 31 different M4 metalloprotease sequences of bacterial origin have been retrieved from UniProt ( https://www.uniprot.org/ ). Corresponding gene sequences of 31 bacterial M4 metalloprotease proteins were retrieved from NCBI ( https://www.ncbi.nlm.nih.gov/ ).

Results

The protein sequences of M4 metalloprotease enzymes belonging to different bacterial strains were retrieved from UniProt and FASTA format of these sequences have been selected based on the overall quality parameters in UniProt tool (Supplementary table 1 ).

Conclusion

Metalloproteases of M4 family are widely dispersed across the nature. The importance of these proteases has been perceived since their roles in bacterial pathogenicity along with in industrial sectors.

Availability of data and materials

All the protein sequences are available in Uniprot. Uniprot ID was provided into the manuscript.

Acknowledgements

Authors are thankful to Basic and Applied Research on Jute Project, Bangladesh Jute Research Institute, for pursuing research activities.

1. Introduction

Estimating the quality of protein structure models is a vital step in protein structure prediction. Often one ends up in having a set of alternative models ( e.g. from different modeling servers or based on alternative template structures and alignments) from which the best candidate shall be selected.

3. Input Format Requirements

Either a model in PDB format or tar.gz -archives with multiple models in PDB format sharing the same reference sequence (SEQRES) can be uploaded.

4. Input Data Processing

Local qualities are visible as color gradients in the model viewer. They additionally get mapped onto the structures available in the downloadable archives as bfactors. The server provides you with two alternative structures in the archives that undergo certain processing steps.

5. Programmatic Access

One can access QMEAN-SERVER programatically with provided API. In order to use QMEAN submission API you have to make a POST request to the https://swissmodel.expasy.org/qmean/submit/ with following parameters. (Parameters "structure" and "email" are required)

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 1 2 3 4 5 6 7 8 9
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