15N-TOCSY-HSQC acquired at 500MHz, mix=100ms

15N-NOESY-HSQC acquired at 800MHz, mix=100ms

MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like repeats.

A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were
cloned, expressed and purified for structural studies. Of these, approximately
20% were found to be suitable candidates for X-ray crystallographic or NMR
spectroscopic analysis without further optimization of conditions, providing an
estimate of the number of the most accessible structural targets in the
proteome. A retrospective analysis of the experimental behavior of these
proteins suggested some simple relations between sequence and solubility,
implying that data bases of protein properties will be useful in optimizing
high throughput strategies. Of the first 10 structures determined, several
provided clues to biochemical functions that were not detectable from sequence
analysis, and in many cases these putative functions could be readily confirmed
by biochemical methods. This demonstrates that structural proteomics is
feasible and can play a central role in functional genomics.

Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V,
Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP,
Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM,
Arrowsmith CH.
Structural proteomics of an archaeon.
Nat Struct Biol. 2000 Oct;7(10):903-9.

Solution Structure Of Mth187. Ontario Centre For Structural Proteomics Target Mth0187_1_111; Northeast Structural Genomics Targ

conserved protein [Methanothermobacter thermautotrophicus str. Delta H]

hypothetical protein MTH187, partial [Methanothermobacter thermautotrophicus str. Delta H]

hypothetical protein, partial [Methanothermobacter thermautotrophicus]

1H, 13C, and 15N resonance assignments and topology of MTH187, a conserved
protein from Methanobacterium thermoautotrophicum

The sample was equilibrated for 30 minutes under these conditions before the
spectra were collected.

NMRView: A computer program for the visualization and analysis of NMR data
(1994) B. A. Johnson and R. A. Blevins, J. Biomolecular NMR 4:603-614.