CoNSEnsX statistics

info info

Citations per year

Number of citations per year for the bioinformatics software tool CoNSEnsX
info

Tool usage distribution map

info info

Associated diseases

info

Popular tool citations

chevron_left Protein dynamics chevron_right
Want to access the full stats & trends on this tool?

Protocols

CoNSEnsX specifications

Information


Unique identifier OMICS_19954
Name CoNSEnsX
Alternative names Compliance of NMR-derived Structural Ensembles with eXperimental data, CoNSEnsX+ (Compliance of NMR-derived Structural Ensembles with eXperimental data + selection)
Restrictions to use None
Input data PDB, NMR-Star
Programming languages Python
Computer skills Basic
Stability Stable
Maintained Yes

Download


github.png

Information


Unique identifier OMICS_19954
Name CoNSEnsX
Alternative names Compliance of NMR-derived Structural Ensembles with eXperimental data, CoNSEnsX+ (Compliance of NMR-derived Structural Ensembles with eXperimental data + selection)
Software type Application/Script
Interface Command line interface
Restrictions to use None
Operating system Unix/Linux
Programming languages Python
License MIT License
Computer skills Advanced
Stability Stable
Maintained Yes

Download


download.png
github.png

Versioning


No version available

Publications for Compliance of NMR-derived Structural Ensembles with eXperimental data

CoNSEnsX citations

 (2)
library_books

Fine tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin type peptidyl prolyl isomerases

2017
Sci Rep
PMCID: 5353683
PMID: 28300139
DOI: 10.1038/srep44504

[…] ol, unrestrained simulations were run with exactly the same setup but with S2 and distance restraint force constants set to zero. Correspondence of the ensembles to S2 parameters was checked with the CoNSEnsX server. Chemical shifts were back-calculated with shiftx2 with parameter settings corresponding to the experimental conditions for each molecule as described in the original publications (usi […]

call_split

“Invisible” Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST NMR Experiments, and Molecular Dynamics Calculations

2015
PMCID: 4464532
PMID: 25676351
DOI: 10.1002/chem.201404879
call_split See protocol

[…] ulation with 16 replicas. By discarding conformers before the first 1 ns of the run, 256 structures were selected for the final ensemble. Correspondence to experimental data was verified by using the CoNSEnsX web server.[]Approximate models for the states characteristic of the hot and cold states were obtained based on 13Cα and amide 15N chemical shifts by selecting conformers from a pre-generated […]


Want to access the full list of citations?
CoNSEnsX institution(s)
Faculty of Information technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary
CoNSEnsX funding source(s)
Supported by the National Research, Development and Innovation Office – NKFIH through grant no. NF104198.

CoNSEnsX reviews

star_border star_border star_border star_border star_border
star star star star star

Be the first to review CoNSEnsX