2ezb: Difference between revisions

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[[Image:2ezb.jpg|left|200px]]
[[Image:2ezb.jpg|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_2ezb", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] </span>
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{{STRUCTURE_2ezb|  PDB=2ezb |  SCENE= }}  
|RELATEDENTRY=[[2eza|2EZA]], [[2ezc|2EZC]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ezb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezb OCA], [http://www.ebi.ac.uk/pdbsum/2ezb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ezb RCSB]</span>
}}


'''AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES'''
'''AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES'''
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[[Category: Gronenborn, A M.]]
[[Category: Gronenborn, A M.]]
[[Category: Tjandra, N.]]
[[Category: Tjandra, N.]]
[[Category: kinase]]
[[Category: Kinase]]
[[Category: phosphotransferase]]
[[Category: Phosphotransferase]]
[[Category: sugar transport]]
[[Category: Sugar transport]]
[[Category: transferase]]
[[Category: Transferase]]
 
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Revision as of 03:16, 4 May 2008

File:2ezb.jpg

Template:STRUCTURE 2ezb

AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES


OverviewOverview

Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the form of short (< 5 A) interproton distances. In the case of modular or multidomain proteins and linear nucleic acids, the density of short interproton distance contacts between structural elements far apart in the sequence may be insufficient to define their relative orientations. In this paper we show how the dependence of heteronuclear longitudinal and transverse relaxation times on the rotational diffusion anisotropy of non-spherical molecules can be readily used to directly provide restraints for simulated annealing structure refinement that characterize long range order a priori. The method is demonstrated using the N-terminal domain of Enzyme I,a protein of 259 residues comprising two distinct domains with a diffusion anisotropy(Dparallel/Dperpendicular)of approximately 2.

About this StructureAbout this Structure

2EZB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy., Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM, Nat Struct Biol. 1997 Jun;4(6):443-9. PMID:9187651 Page seeded by OCA on Sun May 4 03:16:51 2008

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