K. D. Berndt, P. Gü-ntert, L. P. Orbons, and K. Wü-thrich, Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures, Journal of Molecular Biology, vol.227, issue.3, pp.757-775, 1992.
DOI : 10.1016/0022-2836(92)90222-6

A. T. Brunger and M. Nilges, Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMRspectroscopy, Quarterly Reviews of Biophysics, vol.49, issue.01, pp.49-125, 1993.
DOI : 10.1107/S0108767389000437

A. T. Brunger, A. Krukowski, and J. W. Erickson, Slow-cooling protocols for crystallographic refinement by simulated annealing, Acta Crystallographica Section A Foundations of Crystallography, vol.46, issue.7, pp.585-593, 1990.
DOI : 10.1107/S0108767390002355

A. T. Brunger, G. M. Clore, A. M. Gronenborn, R. Saffrich, and M. Nilges, Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation, Science, vol.261, issue.5119, pp.328-331, 1993.
DOI : 10.1126/science.8332897

A. T. Brunger, P. D. Adams, G. M. Clore, W. L. Delano, P. Gros et al., Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, Acta Crystallographica Section D Biological Crystallography, vol.54, issue.5, pp.905-921, 1998.
DOI : 10.1107/S0907444998003254

G. M. Clore and C. D. Schwieters, 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?, Journal of the American Chemical Society, vol.126, issue.9, pp.2923-2938, 2004.
DOI : 10.1021/ja0386804

G. M. Clore, E. Appella, M. Yamada, K. Matsushima, and A. M. Gronenborn, Three-dimensional structure of interleukin 8 in solution, Biochemistry, vol.29, issue.7, pp.1689-1696, 1990.
DOI : 10.1021/bi00459a004

G. Cornilescu, J. L. Marquardt, M. Ottiger, and A. Bax, Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase, Journal of the American Chemical Society, vol.120, issue.27, pp.6836-6837, 1998.
DOI : 10.1021/ja9812610

K. L. Damm and H. A. Carlson, Gaussian-Weighted RMSD Superposition of Proteins: A Structural Comparison for Flexible Proteins and Predicted Protein Structures, Biophysical Journal, vol.90, issue.12, pp.4558-4573, 2006.
DOI : 10.1529/biophysj.105.066654

T. Gallagher, P. Alexander, P. Bryan, and G. L. Gilliland, Two Crystal Structures of the B1 Immunoglobulin-Binding Domain of Streptococcal Protein G and Comparison with NMR, Biochemistry, vol.33, issue.15, pp.4721-4729, 1994.
DOI : 10.1021/bi00181a032

J. R. Gillespie and D. Shortle, Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. paramagnetic relaxation enhancement by nitroxide spin labels, Journal of Molecular Biology, vol.268, issue.1, pp.158-169, 1997.
DOI : 10.1006/jmbi.1997.0954

A. M. Gronenborn, D. R. Filpula, N. Z. Essig, A. Achari, M. Whitlow et al., A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G, Science, vol.253, issue.5020, pp.657-661, 1991.
DOI : 10.1126/science.1871600

M. Habeck, W. Rieping, and M. Nilges, Weighting of experimental evidence in macromolecular structure determination, Proc. Natl. Acad. Sci. USA 103, pp.1756-1761, 2006.
DOI : 10.1023/A:1008360715569

R. W. Hooft, G. Vriend, C. Sander, and E. E. Abola, Errors in protein structures, Nature, vol.381, issue.6580, p.272, 1996.
DOI : 10.1038/381272a0

W. Humphrey, A. Dalke, and K. Schulten, VMD: Visual molecular dynamics, Journal of Molecular Graphics, vol.14, issue.1, pp.33-38, 1996.
DOI : 10.1016/0263-7855(96)00018-5

M. Hyvonen, M. J. Macias, M. Nilges, H. Oschkinat, M. Saraste et al., Structure of the binding site for inositol phosphates in a PH domain, EMBO J, vol.14, pp.4676-4685, 1995.

A. Jack and M. Levitt, factor, Acta Crystallographica Section A, vol.34, issue.6, pp.931-935, 1978.
DOI : 10.1107/S0567739478001904

R. Kaptein, E. R. Zuiderweg, R. Scheek, R. Boelens, and W. F. Van-gunsteren, A protein structure from nuclear magnetic resonance data, Journal of Molecular Biology, vol.182, issue.1, pp.179-182, 1985.
DOI : 10.1016/0022-2836(85)90036-1

K. Lindorff-larsen, R. B. Best, M. A. Depristo, C. M. Dobson, and M. Vendruscolo, Simultaneous determination of protein structure and dynamics, Nature, vol.25, issue.7022, pp.128-132, 2005.
DOI : 10.1006/jmbi.1999.2670

J. P. Linge, S. I. O-'donoghue, and M. Nilges, Automated Assignment of Ambiguous Nuclear Overhauser Effects with ARIA, Methods Enzymol, vol.339, pp.71-90, 2001.
DOI : 10.1016/S0076-6879(01)39310-2

J. P. Linge, M. A. Williams, C. A. Spronk, A. M. Bonvin, and M. Nilges, Refinement of protein structures in explicit solvent, Proteins: Structure, Function, and Bioinformatics, vol.8, issue.3, pp.496-506, 2003.
DOI : 10.1002/prot.10299

M. Marquart, J. Walter, J. Deisenhofer, W. Bode, and R. Huber, The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors, Acta Crystallographica Section B Structural Science, vol.39, issue.4, pp.480-485, 1983.
DOI : 10.1107/S010876818300275X

S. B. Nabuurs, C. A. Spronk, E. Krieger, H. Maassen, G. Vriend et al., Quantitative Evaluation of Experimental NMR Restraints, Journal of the American Chemical Society, vol.125, issue.39, 2003.
DOI : 10.1021/ja035440f

S. B. Nabuurs, C. A. Spronk, G. W. Vuister, and G. Vriend, Traditional Biomolecular Structure Determination by NMR Spectroscopy Allows for Major Errors, PLoS Computational Biology, vol.16, issue.2, p.9, 2006.
DOI : 1367-4803(2000)016[0404:TPPSPS]2.0.CO;2
URL : http://doi.org/10.1371/journal.pcbi.0020009.eor

M. Nilges, G. M. Clore, and A. M. Gronenborn, A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data, FEBS Letters, vol.32, issue.1, pp.11-16, 1987.
DOI : 10.1016/0022-2836(86)90146-4

M. Nilges, M. J. Macias, S. I. O-'donoghue, and H. Oschkinat, Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from ??-spectrin 1 1Edited by P. E. Wright, Journal of Molecular Biology, vol.269, issue.3, 1997.
DOI : 10.1006/jmbi.1997.1044

M. Nilges, M. Habeck, S. I. O-'donoghue, R. , and W. , Error distribution derived NOE distance restraints, Proteins: Structure, Function, and Bioinformatics, vol.309, issue.3, pp.652-664, 2006.
DOI : 10.1002/prot.20985

R. Powers, D. S. Garrett, C. J. March, E. A. Frieden, A. M. Gronenborn et al., Three-Dimensional Solution Structure of Human Interleukin-4 by Multidimensional Heteronuclear Magnetic Resonance Spectroscopy, Science, vol.256, issue.5064, pp.1673-1677, 1992.
DOI : 10.1126/science.256.5064.1673

W. Press, B. Flannery, A. Teukolsky, and W. Vetterling, Numerical Recipes: The Art of Scientific Computing, 1986.

B. Qian, S. Raman, R. Das, P. Bradley, A. J. Mccoy et al., High-resolution structure prediction and the crystallographic phase problem, Nature, vol.97, issue.7167, pp.259-264, 2007.
DOI : 10.1038/nature06249
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2504711

W. Rieping, Quality Criteria for Protein NMR Structures, 2004.

W. Rieping, M. Habeck, and M. Nilges, Inferential Structure Determination, Science, vol.309, issue.5732, pp.303-306, 2005.
DOI : 10.1126/science.1110428

W. Rieping, M. Habeck, and M. Nilges, Modeling Errors in NOE Data with a Log-normal Distribution Improves the Quality of NMR Structures, Journal of the American Chemical Society, vol.127, issue.46, pp.16026-16027, 2005.
DOI : 10.1021/ja055092c

W. Rieping, M. Habeck, B. Bardiaux, A. Bernard, T. E. Malliavin et al., ARIA2: Automated NOE assignment and data integration in NMR structure calculation, Bioinformatics, vol.23, issue.3, pp.381-382, 2007.
DOI : 10.1093/bioinformatics/btl589
URL : http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.97.90

A. Sali and T. L. Blundell, Comparative protein modeling by satisfaction of spatial restraints, Acta Crystallographica Section A Foundations of Crystallography, vol.52, issue.a1, pp.779-815, 1993.
DOI : 10.1107/S0108767396095578

L. J. Smith, C. Redfield, R. A. Smith, C. M. Dobson, G. M. Clore et al., Comparison of four independently determined structures of human recombinant interleukin???4, Nature Structural & Molecular Biology, vol.190, issue.5, pp.301-310, 1994.
DOI : 10.1107/S0021889891004399

S. Vijay-kumar, C. E. Bugg, and W. J. Cook, Structure of ubiquitin refined at 1.8 ?? resolution, Journal of Molecular Biology, vol.194, issue.3, pp.531-544, 1987.
DOI : 10.1016/0022-2836(87)90679-6

A. Wlodawer, Crystal structure of human recombinant interleukin-4 at 2.25 ?? resolution, FEBS Letters, vol.87, issue.1, pp.59-64, 1992.
DOI : 10.1073/pnas.87.18.6934