Backbone and side-chain 1H, 13C, and 15N chemical shift assignments for chick
cofilin

The deposited protein sequence (SWISS-PROT accession number P21566) is
incorrect. The NMR chemical shift assignments revealed that residues 53-54 are
Lys-Gln and NOT Thr-Arg as reported in the sequence database.

Backbone and side-chain 1H, 15N, and 13C assignments for chick cofilin.

Two actin-regulatory proteins of 19 and 20 kDa are involved in the regulation of
actin assembly in developing chicken skeletal muscle. They are homologous with
actin depolymerizing factor (ADF) and cofilin, a pH-dependent actin-modulating
protein, which were originally discovered in chicken and mammalian brain,
respectively. In this study, full-length cDNA clones were isolated by screening
a lambda gt11 cDNA library constructed from poly(A+) RNA of embryonic chicken
skeletal muscle with the antibodies specific for each protein, and their
complete sequences were determined. The chicken cofilin cDNA encoded a protein
of 166 amino acids, the sequence of which had over 80% identity with that of
porcine brain cofilin. The amino acid sequence of the ADF was 165 amino acids
and showed about 70% identity with either chicken or mammalian cofilin, in
spite of the fact that ADF and cofilin are functionally distinct. Like chicken
and mammalian cofilin, ADF contained a sequence similar to the nuclear
transport signal sequence of SV40 large T antigen. ADF and cofilin shared a
hexapeptide identical with the amino-terminal sequence of tropomyosin as well
as the regions homologous to other actin-regulatory proteins, including
depactin, gelsolin, and profilin. The overall nucleotide sequences and Southern
blot analysis of genomic DNA, however, indicated that the two proteins were
derived from different genes.

Abe H, Endo T, Yamamoto K, Obinata T.
Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic
chicken skeletal muscle: two functionally distinct actin-regulatory proteins
exhibit high structural homology.
Biochemistry. 1990 Aug 14;29(32):7420-5.

Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit high structural homology.

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.
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.
J Biomol NMR. 1995 Nov;6(3):277-93.

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

Bartels, C., Xia, T.-H., Billeter, M., Guntert, P., and Wuthrich, K. (1995)
J. Biomol. NMR 5, 1-10.

unnamed protein product [Macaca fascicularis]

RecName: Full=Cofilin-2; AltName: Full=Cofilin, muscle isoform [Gallus gallus]

RecName: Full=Cofilin-2; AltName: Full=Cofilin, muscle isoform [Mus musculus]

RecName: Full=Cofilin-2; AltName: Full=Cofilin, muscle isoform [Bos taurus]

RecName: Full=Cofilin-2; AltName: Full=Cofilin, muscle isoform [Sus scrofa]

RecName: Full=Cofilin-2; AltName: Full=Cofilin, muscle isoform [Homo sapiens]

The protein was expressed as a GST-fusion protein in E. coli, then purified
using glutathione affinity chromatography.

torsion angle dynamics followed by simulated annealing
The sample was equilibrated for at least 30 min prior to data acquisition.

nmrPipe was run using scripts generated on our website at
http://sbtools.uchc.edu/nmr/.