2EZC
AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 14 STRUCTURES
Summary for 2EZC
| Entry DOI | 10.2210/pdb2ezc/pdb |
| Descriptor | PHOSPHOTRANSFERASE SYSTEM, ENZYME I (1 entity in total) |
| Functional Keywords | phosphotransferase, transferase, kinase, sugar transport |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P08839 |
| Total number of polymer chains | 1 |
| Total formula weight | 28381.32 |
| Authors | Clore, G.M.,Tjandra, N.,Garrett, D.S.,Gronenborn, A.M. (deposition date: 1997-05-07, release date: 1997-08-20, Last modification date: 2024-05-22) |
| Primary citation | Tjandra, N.,Garrett, D.S.,Gronenborn, A.M.,Bax, A.,Clore, G.M. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat.Struct.Biol., 4:443-449, 1997 Cited by PubMed Abstract: 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. PubMed: 9187651DOI: 10.1038/nsb0697-443 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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