NMR Representative Structure of Intimin-190 (Int190) from Enteropathogenic E. coli
Structural Basis for Recognition of the Translocated Intimin Receptor (Tir) by Intimin from Enteropathogenic E. Coli
TLTIDDGNIEIVGTGVKGKLPTVWLQYGQVNLKASGGNGKYTWRSANPAIASVDASSGQVTLKEKGTTTISVISSDNQTA TYTIATPNSLIVPNMSKRVTYNDAVNTCKNFGGKLPSSQNELENVFKAWGAANKYEYYKSSQTIISWVQQTAQDAKSGVA STYDLVKQNPLNNIKASESNAYATCVK
HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
SHEET DETERMINATION METHOD: AUTHOR PROVIDED.
REPRESENTATIVE STRUCTURE, LEAST ENERGY. RESONANCE ASSIGNMENTS MADE USING TRIPLE RESONANCE EXPERIMENTS WERE FOLLOWED BY COLLATION OF DISTANCE RESTRAINTS USING NOESY EXPERIMENTS ON 15N,13C-LABELLED INT190 EXPERIMENTS ON 15N, 13C-LABELLED INT190. ONE BOND DIPOLAR COUPLINGS WERE MEASURED USING COUPLED HSQC AND TRIPLE RESONANCE EXPERIMENTS.
INT190 IS A TRUNCATION OF INT280 (30KDA) WHOSE GLOBAL FOLD WAS PUBLISHED IN NATURE STRUCTURAL BIOLOGY (1999) VOL.6, PP. 313-318.
HYBRID TORSION ANGLE/ CARTESIAN CO-ORDINATE DYNAMICS
INTIMIN, ESCHERICHIA COLI, CELL ADHESION, OUTER MEMBRANE PROTEIN, NMR SPECTROSCOPY