1j4v
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ezm|2EZM]], [[2ezn|2EZN]], [[3ezm|3EZM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4v OCA], [http://www.ebi.ac.uk/pdbsum/1j4v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j4v RCSB]</span> | ||
}} | }} | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:51 2008'' |
Revision as of 18:28, 30 March 2008
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| Related: | 2EZM, 2EZN, 3EZM
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYANOVIRIN-N
Overview
A simple and robust method for determining the relative orientations of covalently linked protein domains using conjoined rigid body/torsion angle dynamics simulated annealing on the basis of residual dipolar couplings is presented. In this approach each domain is treated as a rigid body and the relevant degrees of conformational freedom are restricted to the backbone torsion angles (phi, psi) of the linker between the domains. By this means translational information afforded by the presence of an intact linker is preserved. We illustrate this approach using the domain-swapped dimer of the HIV-inactivating protein cyanovirin-N as an example.
About this Structure
1J4V is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings., Clore GM, Bewley CA, J Magn Reson. 2002 Feb;154(2):329-35. PMID:11846592
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