Backbone and Sidechain 1H, 13C, and 15N Chemical Shift Assigments for Complex
between p67SH3(C) and p47 Tail Peptide

Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.

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. et al.
J. Biomol. NMR 6, 277-293 (1995).

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

The recommendations presented here are designed to support easier communication
of NMR data and NMR structures of proteins and nucleic acids through unified
nomenclature and reporting standards. Much of this document pertains to the
reporting of data in journal articles; however, in the interest of the future
development of structural biology, it is desirable that the bulk of the
reported information be stored in computer-accessible form and be freely
accessible to the scientific community in standardized formats for data
exchange. These recommendations stem from an IUPAC-IUBMB-IUPAB inter-union
venture with the direct involvement of ICSU and CODATA. The Task Group has
reviewed previous formal recommendations and has extended them in the light of
more recent developments in the field of biomolecular NMR spectroscopy. Drafts
of the recommendations presented here have been examined critically by more
than 50 specialists in the field and have gone through two rounds of extensive
modification to incorporate suggestions and criticisms.

Recommendations for the presentation of NMR structures of proteins and nucleic acids.

p47phox C-terminal region, p47 tail peptide

Solution Structure Of The C-Terminal Sh3 Domain Of P67phox Complexed With The C-Terminal Tail Region Of P47phox

neutrophil cytosolic factor 1 variant [Homo sapiens]

neutrophil cytosolic factor 1 [synthetic construct]

neutrophil cytosol factor 1 [Homo sapiens]

autosomal chronic granulomatous disease protein [Homo sapiens]

Neutrophil cytosolic factor 1 [Homo sapiens]

PREDICTED: neutrophil cytosol factor 1 [Macaca mulatta]

PREDICTED: neutrophil cytosol factor 1 [Pan troglodytes]

PREDICTED: neutrophil cytosol factor 1 [Pongo abelii]

PREDICTED: neutrophil cytosol factor 1 [Nomascus leucogenys]

RecName: Full=Putative neutrophil cytosol factor 1B; Short=NCF-1B; AltName: Full=Putative SH3 and PX domain-containing protein

RecName: Full=Putative neutrophil cytosol factor 1C; Short=NCF-1C; AltName: Full=Putative SH3 and PX domain-containing protein

RecName: Full=Neutrophil cytosol factor 1; Short=NCF-1; AltName: Full=47 kDa autosomal chronic granulomatous disease protein; A

3D F1 13C-filtered F3 13C-resolved NOESY

3D F1 15N-filtered F3 15N-resolved NOESY