BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank

Journal of Biomolecular NMR

Volumn 26, Issue 2, 2003, Pages 139-146

  Doreleijers, Jurgen F ^a   Mading, Steve ^a   Maziuk, Dimitri ^a   Sojourner, Kassandra ^a   Yin, Lei ^b   Zhu, Jun ^a   Markley, John L ^a   Ulrich, Eldon L ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b Keithley Instruments Inc   (United States)

Author keywords

Biomolecular structure; BMRB; Constraints; Database; Dihedral angle; Nuclear magnetic resonance; Nuclear overhauser effect; Residual dipolar coupling; Structure

Indexed keywords

MOLECULAR MARKER;

ARTICLE; AUTOMATION; BIOMAGRESBANK; COMPUTER PROGRAM; IMAGE ANALYSIS; INFORMATION CENTER; INFORMATION PROCESSING; MEDICAL RESEARCH; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AUTOMATIC DATA PROCESSING; DATABASES, PROTEIN; INFORMATION STORAGE AND RETRIEVAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEINS; SOFTWARE;

EID: 0037986814     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023514106644     Document Type: Article

References (21)

1. Anger, S., Bayer, D., Cason, C., Dailey, C., Dilger, A., Demlow, S., Enzmann, A., Farmer, D., Wenger, T. and Young, C. (2002) Persistence of Vision Raytracer, http://www.povray.org
2. Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N. and Bourne, P.E. (2000) Nucl. Acids Res., 28, 235-242.
3. Bernstein, F.C., Koetzle, T.F., Williams, G.J., Meyer, E.E., Jr., Brice, M.D., Rodgers, J.R., Kennard, O., Shimanouchi, T. and Tasumi, M. (1977) J. Mol. Biol., 112, 535-542.
4. Brünger, A.T. (1992) In X-PLOR, Version 3.1: A System for X-Ray Crystallography and NMR, Yale University Press, New Haven, CT, U.S.A.
5. Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T. and Warren, G.L. (1998) Acta Cryst., D54, 905-921.
6. Chou, J.J., Li, S., Klee, C.B. and Bax, A. (2001) Nat. Struct. Biol., 8, 990-997.
7. de Alba, E., De Vries, L., Farquhar, M.G. and Tjandra, N. (1999) J. Mol. Biol., 291, 927-939.
8. Doreleijers, J.F., Raves, M.L., Rullmann, T. and Kaptein, R. (1999) J. Biomol. NMR, 14, 123-132.
9. Fogh, R.H., Ionides, J., Ulrich, E.L., Boucher, W., Vranken, W., Linge, J., Habeck, M., Rieping W., Bhat, T.N., Westbrook, J., Henrick, K., Gilliland, G., Berman, H., Thornton, J.M., Nilges, M., Markley, J.L. and Laue, E. (2002) Nat. Struct. Biol., 9, 416-418.
10. Garrett, D.S. PIPP (2002) http://spin.niddk.nih.gov/clore/Software/software.html
11. Güntert, P., Braun, W. and Wüthrich, K. (1991) J. Mol. Biol., 217, 517-530.
12. Kabsch, W. and Sander, C. (1983) Biopolymers, 22, 2577-2637.
13. Koradi, R., Billeter, M. and Wüthrich, K. (1996) J. Mol. Graph., 14, 51-55.
14. Linge, J.P., O'Donoghue, S.I. and Nilges, M. (2001) Meth. Enzymol., 339, 71-90.
15. McLoughlin, L. Mirror (1998) ftp://sunsite.org.uk/packages/mirror/
16. Nakai, T., Kidera, A. and Nakamura, H. (1993) J. Biomol. NMR, 3, 19-40.
17. Seavey, B.R., Farr, E.A., Westler, W.M. and Markley, J.L. (1991) J. Biomol. NMR, 1, 217-236.
18. Ulrich, E.L. (2002) NMR-STAR data dictionary. http://www.bmrb.wisc.edu/dictionary/htmldocs/nmr_star/dictionary.html
19. Ulrich, E.L., Ioannidis, Y.E., Livny, M., Mading, S., Slatter, N.C. and Markley, J.L. (1998) XVIIth International Conference on Magnetic Resonance in Biological Systems, Tokyo, Japan.
20. Weiner, S.J., Collman, P.A., Case, D.A., Singh, U.C., Ghio, C., Alagona, G., Profetar, J.S. and Weiner, P. (1984) J. Am. Chem. Soc., 106, 765-784.
21. Westbrook, J.D. and Bourne, P.E. (2000) Bioinformatics, 16, 159-168.