Skip Navigation

Nucleic Acids Research 2004 32(Web Server Issue):W590-W594; doi:10.1093/nar/gkh477
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (286K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Maiti, R.
Right arrow Articles by Wishart, D. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maiti, R.
Right arrow Articles by Wishart, D. S.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2004, the authors
Nucleic Acids Research, Vol. 32, Web Server issue © Oxford University Press 2004; all rights reserved

SuperPose: a simple server for sophisticated structural superposition

Rajarshi Maiti, Gary H. Van Domselaar, Haiyan Zhang and David S. Wishart*

Departments of Biological Sciences and Computing Science, University of Alberta, Edmonton, AB, T6G 2E8, Canada

* To whom correspondence should be addressed. Tel: +1 780 492 0383; Fax: +1 780 492 1071; Email: david.wishart{at}ualberta.ca

Received February 15, 2004; Revised April 14, 2004; Accepted May 3, 2004

The SuperPose web server rapidly and robustly calculates both pairwise and multiple protein structure superpositions using a modified quaternion eigenvalue approach. SuperPose generates sequence alignments, structure alignments, PDB (Protein Data Bank) coordinates and RMSD statistics, as well as difference distance plots and images (both static and interactive) of the superimposed molecules. SuperPose employs a simple interface that requires only PDB files or accession numbers as input. All other superposition decisions are made by the program. SuperPose is uniquely able to superimpose structures that differ substantially in sequence, size or shape. It is also capable of handling a much larger range of superposition queries and situations than many standalone programs and yields results that are intuitively more in agreement with known biological or structural data. The SuperPose web server is freely accessible at http://wishart.biology.ualberta.ca/SuperPose/.


The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. R. Myette, V. Soundararajan, J. Behr, Z. Shriver, R. Raman, and R. Sasisekharan
Heparin/Heparan Sulfate N-Sulfamidase from Flavobacterium heparinum: STRUCTURAL AND BIOCHEMICAL INVESTIGATION OF CATALYTIC NITROGEN-SULFUR BOND CLEAVAGE
J. Biol. Chem., December 11, 2009; 284(50): 35189 - 35200.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. R. Myette, V. Soundararajan, Z. Shriver, R. Raman, and R. Sasisekharan
Heparin/Heparan Sulfate 6-O-Sulfatase from Flavobacterium heparinum: INTEGRATED STRUCTURAL AND BIOCHEMICAL INVESTIGATION OF ENZYME ACTIVE SITE AND SUBSTRATE SPECIFICITY
J. Biol. Chem., December 11, 2009; 284(50): 35177 - 35188.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
T. A. Gangelhoff, P. S. Mungalachetty, J. C. Nix, and M. E. A. Churchill
Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A
Nucleic Acids Res., June 1, 2009; 37(10): 3153 - 3164.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. Siponen, G. Sciara, M. Villion, S. Spinelli, J. Lichiere, C. Cambillau, S. Moineau, and V. Campanacci
Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone
J. Bacteriol., February 1, 2009; 191(3): 728 - 734.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. B. Luther, H. Schindelin, and R. S. Haltiwanger
Structural and Mechanistic Insights into Lunatic Fringe from a Kinetic Analysis of Enzyme Mutants
J. Biol. Chem., January 30, 2009; 284(5): 3294 - 3305.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
H. Chen, H. Xu, O. Kweon, S. Chen, and C. E. Cerniglia
Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis
Microbiology, September 1, 2008; 154(9): 2659 - 2667.
[Abstract] [Full Text] [PDF]


Home page
Mol Hum ReprodHome page
I. Sanchez-Moreno, R. Coral-Vazquez, J.P. Mendez, and P. Canto
Full-length SRY protein is essential for DNA binding
Mol. Hum. Reprod., June 1, 2008; 14(6): 325 - 330.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. C. Oliver and M. Paetzel
Crystal Structure of the Major Periplasmic Domain of the Bacterial Membrane Protein Assembly Facilitator YidC
J. Biol. Chem., February 22, 2008; 283(8): 5208 - 5216.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
S. S.-W. Cot, A. K.-C. So, and G. S. Espie
A Multiprotein Bicarbonate Dehydration Complex Essential to Carboxysome Function in Cyanobacteria
J. Bacteriol., February 1, 2008; 190(3): 936 - 945.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
D. S. Wishart, D. Arndt, M. Berjanskii, A. C. Guo, Y. Shi, S. Shrivastava, J. Zhou, Y. Zhou, and G. Lin
PPT-DB: the protein property prediction and testing database
Nucleic Acids Res., January 11, 2008; 36(suppl_1): D222 - D229.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Eichinger, A. Nasreen, H. J. Kim, and A. Skerra
Structural Insight into the Dual Ligand Specificity and Mode of High Density Lipoprotein Association of Apolipoprotein D
J. Biol. Chem., October 19, 2007; 282(42): 31068 - 31075.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Lee, A. R. Feldman, B. Delmas, and M. Paetzel
Crystal Structure of the VP4 Protease from Infectious Pancreatic Necrosis Virus Reveals the Acyl-Enzyme Complex for an Intermolecular Self-cleavage Reaction
J. Biol. Chem., August 24, 2007; 282(34): 24928 - 24937.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
A. Via, D. Peluso, P. F. Gherardini, E. de Rinaldis, T. Colombo, G. Ausiello, and M. Helmer-Citterich
3dLOGO: a web server for the identification, analysis and use of conserved protein substructures
Nucleic Acids Res., July 13, 2007; 35(suppl_2): W416 - W419.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
Y. Yamaguchi, T. Matsumura, K. Ichida, K. Okamoto, and T. Nishino
Human Xanthine Oxidase Changes its Substrate Specificity to Aldehyde Oxidase Type upon Mutation of Amino Acid Residues in the Active Site: Roles of Active Site Residues in Binding and Activation of Purine Substrate
J. Biochem., April 1, 2007; 141(4): 513 - 524.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Garcia-Saez, S. DeBonis, R. Lopez, F. Trucco, B. Rousseau, P. Thuery, and F. Kozielski
Structure of Human Eg5 in Complex with a New Monastrol-based Inhibitor Bound in the R Configuration
J. Biol. Chem., March 30, 2007; 282(13): 9740 - 9747.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Cui, B. Nan, J. Hu, Y. Wang, C. Jin, and B. Xia
Identification and Solution Structures of a Single Domain Biotin/Lipoyl Attachment Protein from Bacillus subtilis
J. Biol. Chem., July 21, 2006; 281(29): 20598 - 20607.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
E. S. C. Shih, R.-c. R. Gan, and M.-J. Hwang
OPAAS: a web server for optimal, permuted, and other alternative alignments of protein structures.
Nucleic Acids Res., July 1, 2006; 34(Web Server issue): W95 - W98.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
K. Sumathi, P. Ananthalakshmi, M. N. A. Md. Roshan, and K. Sekar
3dSS: 3D structural superposition.
Nucleic Acids Res., July 1, 2006; 34(Web Server issue): W128 - W132.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
P. C. Sehnke, B. Laughner, H. Cardasis, D. Powell, and R. J. Ferl
Exposed Loop Domains of Complexed 14-3-3 Proteins Contribute to Structural Diversity and Functional Specificity
Plant Physiology, February 1, 2006; 140(2): 647 - 660.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
N. Bhardwaj, R. E. Langlois, G. Zhao, and H. Lu
Kernel-based machine learning protocol for predicting DNA-binding proteins
Nucleic Acids Res., November 10, 2005; 33(20): 6486 - 6493.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. T. Beernink, M. Hwang, M. Ramirez, M. B. Murphy, S. A. Doyle, and M. P. Thelen
Specificity of Protein Interactions Mediated by BRCT Domains of the XRCC1 DNA Repair Protein
J. Biol. Chem., August 26, 2005; 280(34): 30206 - 30213.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
H. LIANG and L. F. LANDWEBER
Molecular mimicry: Quantitative methods to study structural similarity between protein and RNA
RNA, August 1, 2005; 11(8): 1167 - 1172.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
R. Maiti, G. H. Van Domselaar, and D. S. Wishart
MovieMaker: a web server for rapid rendering of protein motions and interactions
Nucleic Acids Res., July 1, 2005; 33(suppl_2): W358 - W362.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.