2ezc
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2ezc.jpg|left|200px]] | + | [[Image:2ezc.jpg|left|200px]] |
| - | + | ||
| - | '''AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES''' | + | {{Structure |
| + | |PDB= 2ezc |SIZE=350|CAPTION= <scene name='initialview01'>2ezc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2EZC is a [ | + | 2EZC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZC OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9187651 9187651] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoenolpyruvate--protein phosphotransferase]] | [[Category: Phosphoenolpyruvate--protein phosphotransferase]] | ||
| Line 23: | Line 32: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:20 2008'' |
Revision as of 14:46, 20 March 2008
| |||||||
| Activity: | Phosphoenolpyruvate--protein phosphotransferase, with EC number 2.7.3.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES
Overview
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 Structure
2EZC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 16:46:20 2008
