메뉴 건너뛰기




Volumn 16, Issue 9, 2008, Pages 1305-1312

Accurate NMR Structures Through Minimization of an Extended Hybrid Energy

Author keywords

PROTEINS

Indexed keywords

ARTICLE; BAYES THEOREM; NORMAL DISTRIBUTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

EID: 50849144050     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.07.008     Document Type: Article
Times cited : (52)

References (40)
  • 2
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt K.D., Güntert P., Orbons L.P., and Wüthrich K. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol. Biol. 227 (1992) 757-775
    • (1992) J. Mol. Biol. , vol.227 , pp. 757-775
    • Berndt, K.D.1    Güntert, P.2    Orbons, L.P.3    Wüthrich, K.4
  • 3
    • 0027293559 scopus 로고
    • Computational challenges for macromolecular structure determination by x-ray crystallography and solution NMR-spectroscopy
    • Brunger A.T., and Nilges M. Computational challenges for macromolecular structure determination by x-ray crystallography and solution NMR-spectroscopy. Q. Rev. Biophys. 26 (1993) 49-125
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 49-125
    • Brunger, A.T.1    Nilges, M.2
  • 4
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brunger A.T., Krukowski A., and Erickson J.W. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A. 46 (1990) 585-593
    • (1990) Acta Crystallogr. A. , vol.46 , pp. 585-593
    • Brunger, A.T.1    Krukowski, A.2    Erickson, J.W.3
  • 5
    • 0027918891 scopus 로고
    • Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation
    • Brunger A.T., Clore G.M., Gronenborn A.M., Saffrich R., and Nilges M. Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science 261 (1993) 328-331
    • (1993) Science , vol.261 , pp. 328-331
    • Brunger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Saffrich, R.4    Nilges, M.5
  • 7
    • 1542317796 scopus 로고    scopus 로고
    • How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
    • Clore G.M., and Schwieters C.D. How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?. J. Am. Chem. Soc. 126 (2004) 2923-2938
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2923-2938
    • Clore, G.M.1    Schwieters, C.D.2
  • 9
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carabonyl chemical shifts in a dilute liquid crystalline phase
    • Cornilescu G., Marquardt J.L., Ottiger M., and Bax A. Validation of protein structure from anisotropic carabonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120 (1998) 6836-6837
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 10
    • 33744807436 scopus 로고    scopus 로고
    • Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures
    • Damm K.L., and Carlson H.A. Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures. Biophys. J. 90 (2006) 4558-4573
    • (2006) Biophys. J. , vol.90 , pp. 4558-4573
    • Damm, K.L.1    Carlson, H.A.2
  • 11
    • 0028354429 scopus 로고
    • Two crystal structures of the b1 immunoglobulin-binding domain of streptococcal protein g and comparison with nmr
    • Gallagher T., Alexander P., Bryan P., and Gilliland G.L. Two crystal structures of the b1 immunoglobulin-binding domain of streptococcal protein g and comparison with nmr. Biochemistry 33 (1994) 4721-4729
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 12
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie J.R., and Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268 (1997) 158-169
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 14
    • 32444439415 scopus 로고    scopus 로고
    • Weighting of experimental evidence in macromolecular structure determination
    • Habeck M., Rieping W., and Nilges M. Weighting of experimental evidence in macromolecular structure determination. Proc. Natl. Acad. Sci. USA 103 (2006) 1756-1761
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1756-1761
    • Habeck, M.1    Rieping, W.2    Nilges, M.3
  • 18
    • 84918314491 scopus 로고
    • Refinement of large structures by simultaneous minimization of energy and R factor
    • Jack A., and Levitt M. Refinement of large structures by simultaneous minimization of energy and R factor. Acta Crystallogr. A 34 (1978) 931-935
    • (1978) Acta Crystallogr. A , vol.34 , pp. 931-935
    • Jack, A.1    Levitt, M.2
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0034919240 scopus 로고    scopus 로고
    • Automated assignment of ambiguous nuclear overhauser effects with aria
    • Linge J.P., O'Donoghue S.I., and Nilges M. Automated assignment of ambiguous nuclear overhauser effects with aria. Methods Enzymol. 339 (2001) 71-90
    • (2001) Methods Enzymol. , vol.339 , pp. 71-90
    • Linge, J.P.1    O'Donoghue, S.I.2    Nilges, M.3
  • 24
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
    • Marquart M., Walter J., Deisenhofer J., Bode W., and Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallogr. B 39 (1983) 480-485
    • (1983) Acta Crystallogr. B , vol.39 , pp. 480-485
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 26
    • 33645790319 scopus 로고    scopus 로고
    • Traditional biomolecular structure determination by nmr spectroscopy allows for major errors
    • Nabuurs S.B., Spronk C.A., Vuister G.W., and Vriend G. Traditional biomolecular structure determination by nmr spectroscopy allows for major errors. PLoS Comput. Biol. 2 (2006) e9
    • (2006) PLoS Comput. Biol. , vol.2
    • Nabuurs, S.B.1    Spronk, C.A.2    Vuister, G.W.3    Vriend, G.4
  • 27
    • 45949117843 scopus 로고
    • A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data
    • Nilges M., Clore G.M., and Gronenborn A.M. A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data. FEBS Lett. 219 (1987) 11-16
    • (1987) FEBS Lett. , vol.219 , pp. 11-16
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 28
    • 0031566434 scopus 로고    scopus 로고
    • Automated noesy interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
    • Nilges M., Macias M.J., O'Donoghue S.I., and Oschkinat H. Automated noesy interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. J. Mol. Biol. 269 (1997) 408-422
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 29
  • 30
    • 0026764439 scopus 로고
    • Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy
    • Powers R., Garrett D.S., March C.J., Frieden E.A., Gronenborn A.M., and Clore G.M. Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science 256 (1992) 1673-1677
    • (1992) Science , vol.256 , pp. 1673-1677
    • Powers, R.1    Garrett, D.S.2    March, C.J.3    Frieden, E.A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 32
    • 36049029967 scopus 로고    scopus 로고
    • High-resolution structure prediction and the crystallographic phase problem
    • Qian B., Raman S., Das R., Bradley P., McCoy A.J., Read R.J., and Baker D. High-resolution structure prediction and the crystallographic phase problem. Nature 450 (2007) 259-264
    • (2007) Nature , vol.450 , pp. 259-264
    • Qian, B.1    Raman, S.2    Das, R.3    Bradley, P.4    McCoy, A.J.5    Read, R.J.6    Baker, D.7
  • 34
    • 22144489530 scopus 로고    scopus 로고
    • Inferential structure determination
    • Rieping W., Habeck M., and Nilges M. Inferential structure determination. Science 309 (2005) 303-306
    • (2005) Science , vol.309 , pp. 303-306
    • Rieping, W.1    Habeck, M.2    Nilges, M.3
  • 35
    • 28044443150 scopus 로고    scopus 로고
    • Modeling errors in noe data with a lognormal distribution improves the quality of nmr structures
    • Rieping W., Habeck M., and Nilges M. Modeling errors in noe data with a lognormal distribution improves the quality of nmr structures. J. Am. Chem. Soc. 127 (2005) 16026-16027
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16026-16027
    • Rieping, W.1    Habeck, M.2    Nilges, M.3
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 39
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 å resolution
    • Vijay-Kumar S., Bugg C.E., and Cook W.J. Structure of ubiquitin refined at 1.8 å resolution. J. Mol. Biol. 194 (1987) 531-544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 40
    • 0026661731 scopus 로고
    • Crystal structure of human recombinant interleukin-4 at 2.25 å resolution
    • Wlodawer A. Crystal structure of human recombinant interleukin-4 at 2.25 å resolution. FEBS Lett. 309 (1992) 59-64
    • (1992) FEBS Lett. , vol.309 , pp. 59-64
    • Wlodawer, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.