Research Topics
| C D SchwietersSummaryAffiliation: National Institutes of Health Country: USA Publications
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Detail Information
Publications
Internal coordinates for molecular dynamics and minimization in structure determination and refinementC D Schwieters
Computational Bioscience and Engineering Laboratory, Center for Information Technology, National Institutes of Health, Building 12A, Bethesda, Maryland 20892 5624, USA
J Magn Reson 152:288-302. 2001....- Reweighted atomic densities to represent ensembles of NMR structuresCharles D Schwieters
Computational Bioscience and Engineering Laboratory, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892 5624, USA
J Biomol NMR 23:221-5. 2002..The approach is illustrated using several examples... - A pseudopotential for improving the packing of ellipsoidal protein structures determined from NMR dataCharles D Schwieters
Imaging Sciences Laboratory, Center for Information Technology, National Institutes of Health, Building 12A, Bethesda, Maryland 20892 5624, USA
J Phys Chem B 112:6070-3. 2008..We demonstrate that this new gyration volume term improves structures both during the calculation of an initial unknown fold and during final refinement... - A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large-angle X-ray scattering dataCharles D Schwieters
Division of Computational Bioscience, Center for Information Technology, National Institutes of Health, Building 12A, Bethesda, Maryland 20892 5624, USA
Biochemistry 46:1152-66. 2007.... - The VMD-XPLOR visualization package for NMR structure refinementC D Schwieters
Computational Bioscience and Engineering Laboratory, Center for Information Technology, National Institutes of Health, Building 12A, Bethesda, Maryland 20892 5624, USA
J Magn Reson 149:239-44. 2001..Finally, the VMD-XPLOR interface is modular so that it is readily transferable to other refinement programs (such as CNS)... 
Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithmJohn J Kuszewski
Imaging Sciences Laboratory, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892 5624, USA
J Biomol NMR 41:221-39. 2008..We show that useful assignment information can be obtained even in the case in which a unique structure cannot be determined...- Concordance of residual dipolar couplings, backbone order parameters and crystallographic B-factors for a small alpha/beta protein: a unified picture of high probability, fast atomic motions in proteinsG Marius Clore
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0520, USA
J Mol Biol 355:879-86. 2006.... - Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurementsG Marius Clore
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0520, USA
Biochemistry 43:10678-91. 2004..In addition, direct evidence is obtained for ubiquitous crankshaft motions along the entire length of the polypeptide backbone manifested by the anticorrelation of the backbone torsion angles phi(i) and psi(i-1)... - 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?G Marius Clore
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0520, USA
J Am Chem Soc 126:2923-38. 2004..For most practical applications, however, refinement of NMR structures against dipolar couplings using a single structure representation is adequate and will not adversely impact coordinate accuracy within the limits of the NMR method... - Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamicsG Marius Clore
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0510, USA
J Am Chem Soc 125:2902-12. 2003..This methodology should be particularly useful for high throughput, NMR-based, structural proteomics... - Theoretical and computational advances in biomolecular NMR spectroscopyG Marius Clore
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0510, USA
Curr Opin Struct Biol 12:146-53. 2002.... - Completely automated, highly error-tolerant macromolecular structure determination from multidimensional nuclear overhauser enhancement spectra and chemical shift assignmentsJohn Kuszewski
Contribution from the Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624, USA
J Am Chem Soc 126:6258-73. 2004..The limits of the method are explored using simulated data on the 56-residue B1 domain of Streptococcal protein G... - Determination of multicomponent protein structures in solution using global orientation and shape restraintsJinbu Wang
Protein Nucleic Acid Interaction Section, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, USA
J Am Chem Soc 131:10507-15. 2009.... - Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexesYaroslav Ryabov
Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892 5624, USA
J Am Chem Soc 131:9522-31. 2009..In each case, the cluster containing the lowest-energy structure corresponds to the correct solution... - Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMRChun Tang
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0520, USA
Nature 449:1078-82. 2007..Using ensemble simulated annealing refinement against the PRE data we are able to determine a <r(-6)> ensemble average structure of the minor apo species and show that it is distinct from the sugar-bound state... - The structure of receptor-associated protein (RAP)Donghan Lee
Protein Nucleic Acid Interaction Section, Structural Biophysics Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, USA
Protein Sci 16:1628-40. 2007..The flexible linkers and the quasi-repetitive structural architecture may allow RAP to adopt various possible conformations when interacting with the LDL receptors, which are also made of repetitive substructure units... - Characterization of nonspecific protein-DNA interactions by 1H paramagnetic relaxation enhancementJunji Iwahara
Contribution from the Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, MD 20892-0520, USA
J Am Chem Soc 126:12800-8. 2004..Combining the (1)H-PRE data with the crystal structure of the HMGB-1 A-box/cisplatin-modified DNA complex allows one to obtain a semiquantitative estimate of the equilibrium populations at the various sites... - Direct use of 15N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexesYaroslav Ryabov
Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892 5624, USA
J Am Chem Soc 132:5987-9. 2010.... - The Xplor-NIH NMR molecular structure determination packageCharles D Schwieters
Division of Computational Bioscience, Center for Information Technology, National Institutes of Health, Building 12A, 20892-5624, Bethesda, MD, USA
J Magn Reson 160:65-73. 2003..Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis... - Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromoleculeJunji Iwahara
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, Maryland 20892-0520, USA
J Am Chem Soc 126:5879-96. 2004..This is particularly significant in the case of macromolecular complexes where intermolecular translational restraints derived from nuclear Overhauser enhancement data may be limited... - Global molecular structure and interfaces: refining an RNA:RNA complex structure using solution X-ray scattering dataXiaobing Zuo
Protein Nucleic Acid Interaction Section, Structural Biophysics Laboratory, NCI-Frederick, National Istitutes of Health, Frederick, Maryland 21702, USA
J Am Chem Soc 130:3292-3. 2008 - The structure of free L11 and functional dynamics of L11 in free, L11-rRNA(58 nt) binary and L11-rRNA(58 nt)-thiostrepton ternary complexesDonghan Lee
Protein Nucleic Acid Interaction Section, Structural Biophysics Laboratory, NCI Frederick, NIH, Frederick, MD 21702, USA
J Mol Biol 367:1007-22. 2007..Our combined analysis of both the chemical shift perturbation and dynamics data clearly indicates that thiostrepton binds to a pocket involving residues in the 3(10)-helix in L11...