BRCT is mostly found in cell cycle regulation and DNA repair proteins

BRCT is probably a protein-protein interaction domain

Solution NMR structure of the BRCT domain from Thermus thermophilus DNA ligase

The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks.

Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A.
J. Biomol. NMR 6, 277-293, (1995).

NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed.

Zimmerman, D. E., Kulikowski, C. A., Huang, Y., Feng, W., Tashiro, M.,
Shimotakahara, S., Chien, C. Y., Powers, R., and Montelione, G. T.
J. Mol. Biol. 269, 592-610, (1997).

Automated analysis of protein NMR assignments using methods from artificial intelligence.

Moseley, H.N., Monleon, D., Montelione, G.T. Methods Enzymol, 339, 91-108, (2001).
Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.

Methionine starting sequence
Residues 588-676 including BRCT domain (588-676)
Rinally a Glycine and Serine.

Solution Nmr Structure Of Brct Domain Of T. Thermophilus: Northeast Structural Genomics Consortium Target Wr64tt

DNA ligase [NAD+] [Thermus thermophilus HB8]

NAD-dependent DNA ligase [Thermus thermophilus HB27]

DNA ligase [Thermus thermophilus SG0.5JP17-16]

DNA ligase, NAD-dependent [Thermus thermophilus JL-18]

DNA ligase (NAD) (EC 6.5.1.2) - Thermus aquaticus

NAD-dependent DNA ligase LigA [Thermus sp. RL]

NAD-dependent DNA ligase LigA [Thermus thermophilus]

RecName: Full=DNA ligase; AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)]; AltName: Full=Tth DNA ligase [Thermus thermo

RecName: Full=DNA ligase; AltName: Full=Polydeoxyribonucleotide synthase [Thermus thermophilus HB27]

NorthEast Structural Genomics Consortium (NESG) target WR64Tt.

Please see references in $ref-2 and $ref-3.

automated backbone 1H, 13C and 15N assignments

Zimmerman, Moseley, Kulikowski and Montelione

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax