2gat
From Proteopedia
SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF CHICKEN GATA-1 BOUND TO DNA, NMR, REGULARIZED MEAN STRUCTURE
Overview
Anisotropy of the molecular magnetic susceptibility gives rise to a small degree of alignment. The resulting residual dipolar couplings, which can now be measured with the advent of higher magnetic fields in NMR, contain information on the orientation of the internuclear vectors relative to the molecular magnetic susceptibility tensor, thereby providing information on long range order that is not accessible by any of the solution NMR parameters currently used in structure determination. Thus, the dipolar couplings constitute unique and powerful restraints in determining the structures of magnetically oriented macromolecules in solution. The method is demonstrated on a complex of the DNA-binding domain of the transcription factor GATA-1 with a 16 base pair oligodeoxyribonucleotide.
About this Structure
2GAT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution., Tjandra N, Omichinski JG, Gronenborn AM, Clore GM, Bax A, Nat Struct Biol. 1997 Sep;4(9):732-8. PMID:9303001 Page seeded by OCA on Sun May 4 04:53:54 2008
