Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1HN/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics

Journal of the American Chemical Society

Volumn 125, Issue 10, 2003, Pages 2902-2912

  Clore, G Marius ^a   Schwieters, Charles D ^b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; PROTEINS; SIMULATED ANNEALING;

CHEMICAL SHIFT;

COMPLEXATION;

NITROGEN 15; PROTEIN; PROTON; TRIPEPTIDE;

ARTICLE; CALCULATION; COMPLEX FORMATION; DIPOLE; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

BACTERIAL PROTEINS; COMPUTER SIMULATION; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE SYSTEM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTONS;

EID: 0037433504     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja028893d     Document Type: Article

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