NMR View: A computer program for the visualization and analysis of NMR data

SummaryNMR View is a computer program designed for the visualization and analysis of NMR data. It allows the user to interact with a practically unlimited number of 2D, 3D and 4D NMR data files. Any number of spectral windows can be displayed on the screen in any size and location. Automatic peak picking and facilitated peak analysis features are included to aid in the assignment of complex NMR spectra. NMR View provides structure analysis features and data transfer to and from structure generation programs, allowing for a tight coupling between spectral analysis and structure generation. Visual correlation between structures and spectra can be done with the Molecular Data Viewer, a molecular graphics program with bidirectional communication to NMR View. The user interface can be customized and a command language is provided to allow for the automation of various tasks.

[1]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[2]  G. Bodenhausen,et al.  Toward automated assignment of nuclear magnetic resonance spectra: pattern recognition in two-dimensional correlation spectra , 1985 .

[3]  K. Wüthrich.  NMR of proteins and nucleic acids , 1988 .

[4]  B. Oh,et al.  Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment. , 1988, Science.

[5]  Werner Braun,et al.  Automated stereospecific 1H NMR assignments and their impact on the precision of protein structure determinations in solution , 1989 .

[6]  P. J. Kraulis,et al.  ANSIG: A program for the assignment of protein 1H 2D NMR spectra by interactive computer graphics , 1989, Journal of Magnetic Resonance (1969).

[7]  S. Brown,et al.  Solution structures of human transforming growth factor alpha derived from 1H NMR data. , 1990, Biochemistry.

[8]  Gerard J. Kleywegt,et al.  A versatile approach toward the partially automatic recognition of cross peaks in 2D 1H NMR spectra , 1990 .

[9]  A M Gronenborn,et al.  1H‐Nmr stereospecific assignments by conformational data‐base searches , 1990, Biopolymers.

[10]  G. Marius Clore,et al.  1H1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins , 1990 .

[11]  John L. Markley,et al.  Drafting table and light-box software for multidimensional NMR spectral analysis (PIXI). The personal computer workstation , 1990 .

[12]  L. Kay,et al.  Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra , 1991 .

[13]  K Wüthrich,et al.  Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. , 1991, Journal of molecular biology.

[14]  K Wüthrich,et al.  Efficient analysis of protein 2D NMR spectra using the software packageEASY , 1991, Journal of biomolecular NMR.

[15]  B. A. Johnson,et al.  Determination of the three-dimensional structure of iberiotoxin in solution by 1H nuclear magnetic resonance spectroscopy. , 1992, Biochemistry.

[16]  P. Domaille,et al.  Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins , 1992 .

[17]  Axel T. Brunger,et al.  X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .

[18]  E. Laue,et al.  Sequential assignment of the backbone nuclei (1H,15N and13C) of c-H-ras p21 (1–166).GDP using a novel 4D NMR strategy , 1992, Journal of biomolecular NMR.

[19]  John K. Ousterhout,et al.  Tcl and the Tk Toolkit , 1994 .