Search results
SAVES v6.1 is a web-based tool that allows users to upload protein structures in PDB format and run various programs to check their quality and validity. The programs include ERRAT, PROVE, PROCHECK and WHATCHECK, with references and links to original sources.
- Usage
saves @2024 - DOE-MBI Services • Usage Contact: holton at...
- Structure Validation Server
UCLA-DOE LAB — SAVES v6.1. This page displays SAVES programs...
- SAVES
Structure Analysis and Validation. SAVES has been in...
- Usage
Jul 15, 2021 · SAVES is an interactive validation server for 5 programs commonly used in protein structure validation. It runs since 2004 and can be accessed through a dashboard screen with various tools and references.
Fewer than 80% of the amino acids have scored >= 0.1 in the 3D/1D profile. We are open to suggestions for a 6th program to operate in this window. If you know of a program that we could run locally on our server that would be most useful, please let us know: email holton at mbi dot ucla dot edu with your suggestion.
3 days ago · SAVES is a web-based service that validates protein structures and provides quality assessment. See the number of jobs, program runs, and average usage for each month and year since 2020.
Feb 16, 2017 · The selection is based on the validation data calculated with SAVES server. The preferable, allowed and disallowed regions of the Ramachandran plot are 77.05%, 15.08,% and 7.87%, respectively, for the selected model versus 72.46%, 13.77%, and 13.77%, respectively, for the other model.
- Abdo A Elfiky, Samah M Mahdy, Wael M Elshemey
- 10.1002/jmv.24736
- 2017
- J Med Virol. 2017 Jun; 89(6): 1040-1047.
Learn how to refine and validate a protein structure using CCP4 programs and SAVS server. Follow the steps to model the PMSF inhibitor in the Fo-Fc electron density map of proteinase K.
Jan 1, 2016 · ProTSAV is a tool that combines multiple methods to evaluate the quality of predicted protein model structures. It provides a single score, a graphical representation and a ranking for each protein structure based on various parameters derived from experimental structures.
