CS23D - generating protein structure from NMR chemical shifts and sequence homology
CS23D website
CS23D is a web server for rapidly generating accurate 3D protein structures using only assigned NMR chemical shifts as input. CS23D uses a combination of maximal subfragment assembly, chemical shift threading, shift-based torsion angle prediction and chemical shift refinement to generate and refine the protein coordinates. CS23D accepts chemical shift files in either SHIFTY or BMRB formats and produces a set of PDB coordinates for the protein normally within 10-15 minutes (3 hours max). CS23D performance is dependent on the completeness of the chemical shift assignments and...
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
J Med Chem. 2011 Jan 27;
Authors: Orcajo-Rinco?n AL, Ortega-Gutie?rrez S, Serrano P, Torrecillas IR, Wu?thrich K, Campillo M, Pardo L, Viso A, Benhamu? B, Lo?pez-Rodri?guez ML
We report a novel series of non-peptide ligands that inhibit the growth...
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01-29-2011 12:35 PM
[NMR paper] NMR solution structure, backbone mobility, and homology modeling of c-type cytochrome
NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Related Articles NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Chembiochem. 2002 Apr 2;3(4):299-310
Authors: Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR
The solution structure of oxidized cytochrome c(553) (71 amino acid residues) from the Gram-positive bacterium Bacillus pasteurii is here reported and compared with the...
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11-24-2010 08:49 PM
[NMR paper] Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Related Articles Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Biochem Biophys Res Commun. 2001 Oct 26;288(2):462-7
Authors: Randazzo A, Acklin C, Schäfer BW, Heizmann CW, Chazin WJ
The S100 subfamily of EF-hand proteins is distinguished by the binding of Zn(2+) in addition to Ca(2+). In an effort to understand the role of Zn(2+) in modulating the activity of S100 proteins, we have carried out heteronuclear NMR studies of...
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11-19-2010 08:44 PM
[NMR paper] A computational method for NMR-constrained protein threading.
A computational method for NMR-constrained protein threading.
Related Articles A computational method for NMR-constrained protein threading.
J Comput Biol. 2000;7(3-4):449-67
Authors: Xu Y, Xu D, Crawford OH, Einstein JR
Protein threading provides an effective method for fold recognition and backbone structure prediction. But its application is currently limited due to its level of prediction accuracy and scope of applicability. One way to significantly improve its usefulness is through the incorporation of underconstrained (or partial) NMR...
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11-18-2010 09:15 PM
[NMR paper] The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general
The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
Related Articles The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
EMBO J. 1998 Nov 2;17(21):6377-84
Authors: Stoldt M, Wöhnert J, Görlach M, Brown LR
The structure of the Escherichia coli ribosomal protein L25 has been determined to an r.m.s. displacement of backbone heavy atoms of 0.62 +/- 0.14 A by multi-dimensional...
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11-17-2010 11:15 PM
[NMR paper] A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of s
A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
Biochemistry. 1996 Apr 9;35(14):4540-50
Authors: Modi S, Paine MJ, Sutcliffe MJ, Lian LY, Primrose WU, Wolf CR, Roberts GC
The cytochrome P450 responsible for the debrisoquine/sparteine polymorphism (P450 2D6) has been produced in large...
Protein Structure Prediction: Threading & Homology Modeling - Thomas Steinke
Linear Mode
