Title
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids.
Abstract
MolProbity is a general-purpose web server offering quality validation for 3D structures of proteins, nucleic acids and complexes. It provides detailed all-atom contact analysis of any steric problems within the molecules as well as updated dihedralangle diagnostics, and it can calculate and display the H-bond and van der Waals contacts in the interfaces between components. An integral step in the process is the addition and full optimization of all hydrogen atoms, both polar and nonpolar. New analysis functions have been added for RNA, for interfaces, and for NMR ensembles. Additionally, both the web site and major component programs have been rewritten to improve speed, convenience, clarity and integration with other resources. MolProbity results are reported in multiple forms: as overall numeric scores, as lists or charts of local problems, as downloadable PDB and graphics files, and most notably as informative, manipulable 3D kinemage graphics shown online in the KiNG viewer. This service is available free to all users at http://molprobity.biochem.duke.edu.
Year
DOI
Venue
2007
10.1093/nar/gkm216
NUCLEIC ACIDS RESEARCH
Keywords
Field
DocType
dihedral angle,internet,nucleic acids,nucleic acid,hydrogen bonding,computational biology,molecular structure,van der waals,protein conformation,proteins
Graphics,Structure validation,Kinemage,Biology,van der Waals force,Software,Computational science,Bioinformatics,Genetics,Protein Data Bank (RCSB PDB),Protein structure,Web server
Journal
Volume
Issue
ISSN
35
SUPnan
0305-1048
Citations 
PageRank 
References 
49
3.33
5
Authors
11
Name
Order
Citations
PageRank
Ian W. Davis1756.95
Andrew Leaver-Fay237428.70
Vincent B. Chen3513.78
Jeremy N. Block4513.78
Gary J. Kapral5493.33
Xueyi Wang613813.79
Laura Weston Murray7736.50
W. Bryan Arendall III8493.33
Jack Snoeyink92842231.68
Jane S. Richardson1013318.65
David C. Richardson1113219.80