C D Schwieters

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. ncbi request reprint Internal coordinates for molecular dynamics and minimization in structure determination and refinement
    C 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
  2. ncbi request reprint Reweighted atomic densities to represent ensembles of NMR structures
    Charles 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
  3. ncbi request reprint A pseudopotential for improving the packing of ellipsoidal protein structures determined from NMR data
    Charles 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
  4. ncbi request reprint 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 data
    Charles 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
  5. ncbi request reprint The VMD-XPLOR visualization package for NMR structure refinement
    C 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
  6. pmc Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm
    John 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
  7. ncbi request reprint 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 proteins
    G 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
  8. ncbi request reprint Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurements
    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
    Biochemistry 43:10678-91. 2004
  9. ncbi request reprint 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
  10. ncbi request reprint 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 dynamics
    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 0510, USA
    J Am Chem Soc 125:2902-12. 2003

Collaborators

Detail Information

Publications22

  1. ncbi request reprint Internal coordinates for molecular dynamics and minimization in structure determination and refinement
    C 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
    ....
  2. ncbi request reprint Reweighted atomic densities to represent ensembles of NMR structures
    Charles 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...
  3. ncbi request reprint A pseudopotential for improving the packing of ellipsoidal protein structures determined from NMR data
    Charles 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...
  4. ncbi request reprint 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 data
    Charles 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
    ....
  5. ncbi request reprint The VMD-XPLOR visualization package for NMR structure refinement
    C 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)...
  6. pmc Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm
    John 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...
  7. ncbi request reprint 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 proteins
    G 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
    ....
  8. ncbi request reprint Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurements
    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
    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)...
  9. ncbi request reprint 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...
  10. ncbi request reprint 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 dynamics
    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 0510, USA
    J Am Chem Soc 125:2902-12. 2003
    ..This methodology should be particularly useful for high throughput, NMR-based, structural proteomics...
  11. ncbi request reprint Theoretical and computational advances in biomolecular NMR spectroscopy
    G 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
    ....
  12. ncbi request reprint Completely automated, highly error-tolerant macromolecular structure determination from multidimensional nuclear overhauser enhancement spectra and chemical shift assignments
    John 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...
  13. pmc Determination of multicomponent protein structures in solution using global orientation and shape restraints
    Jinbu 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
    ....
  14. pmc 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 complexes
    Yaroslav 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...
  15. ncbi request reprint Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    Chun 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...
  16. pmc 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...
  17. ncbi request reprint Characterization of nonspecific protein-DNA interactions by 1H paramagnetic relaxation enhancement
    Junji 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...
  18. pmc Direct use of 15N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexes
    Yaroslav 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
    ....
  19. ncbi request reprint The Xplor-NIH NMR molecular structure determination package
    Charles 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...
  20. ncbi request reprint Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule
    Junji 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...
  21. doi request reprint Global molecular structure and interfaces: refining an RNA:RNA complex structure using solution X-ray scattering data
    Xiaobing 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
  22. pmc The structure of free L11 and functional dynamics of L11 in free, L11-rRNA(58 nt) binary and L11-rRNA(58 nt)-thiostrepton ternary complexes
    Donghan 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...