Solution NMR structures of two alternative conformations of E. coli tryptophan repressor in dynamic equilibrium

Northeast Structural Genomics Consortium (NESG)

Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR.

Northeast Structural Genomics Consortium

The coordinates provided are for two sets of models, each representing an alternative protein conformation that differ particularly in the segment of the protein sequence corresponding to helix E.

0.5 mM [U-100% 13C; U-100% 15N] Tryptohan aporepressor, 10 mM Tris-HCl buffer pH 5.7, 100 mM NaCl, 5 mM DTT, 0.02 % sodium azide, 90% H2O/10% D2O
10 mM Tris-HCl buffer pH 5.7, 100 mM NaCl, 5 mM DTT and 0.02 % NaN3

Zimmerman, Moseley, Kulikowski and Montelione

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax

Berendsen H, van der Spoel D, van Drunen R.

The protein is a dimer and the coordinates provided are for two sets of dimers, each representing an alternative protein conformation. Each model has 4 chains A,B,C and D. Chains A and B form one dimer in WT conformation, chains C and D form a second dimer in the distorted conformation

Structural Genomics, PSI-Biology, Northeast Structural Genomics Consortium, NESG, TRANSCRIPTION