Journal of Biomolecular NMR

, Volume 62, Issue 4, pp 439–451 | Cite as

Guiding automated NMR structure determination using a global optimization metric, the NMR DP score

  • Yuanpeng Janet Huang
  • Binchen Mao
  • Fei Xu
  • Gaetano T. Montelione


ASDP is an automated NMR NOE assignment program. It uses a distinct bottom-up topology-constrained network anchoring approach for NOE interpretation, with 2D, 3D and/or 4D NOESY peak lists and resonance assignments as input, and generates unambiguous NOE constraints for iterative structure calculations. ASDP is designed to function interactively with various structure determination programs that use distance restraints to generate molecular models. In the CASD–NMR project, ASDP was tested and further developed using blinded NMR data, including resonance assignments, either raw or manually-curated (refined) NOESY peak list data, and in some cases 15N–1H residual dipolar coupling data. In these blinded tests, in which the reference structure was not available until after structures were generated, the fully-automated ASDP program performed very well on all targets using both the raw and refined NOESY peak list data. Improvements of ASDP relative to its predecessor program for automated NOESY peak assignments, AutoStructure, were driven by challenges provided by these CASD–NMR data. These algorithmic improvements include (1) using a global metric of structural accuracy, the discriminating power score, for guiding model selection during the iterative NOE interpretation process, and (2) identifying incorrect NOESY cross peak assignments caused by errors in the NMR resonance assignment list. These improvements provide a more robust automated NOESY analysis program, ASDP, with the unique capability of being utilized with alternative structure generation and refinement programs including CYANA, CNS, and/or Rosetta.


AutoStructure ASDP Automated structural determination by NMR CYANA CNS Rosetta 



We thank all of the members of the Northeast Structural Genomics Consortium who generated and archived NMR data used in the CASD–NMR project, particularly scientists in the laboratories of C. Arrowsmith, M. Kennedy, G.T. Montelione, T. Szyperski, and J. Prestegard. We also thank Z. Zhang and O. Lange for providing the simulated incorrect resonance assignment tables used for testing. This work was supported by a grant from the National Institutes of Health Protein Structure Initiative Grant U54-GM094597 to GTM, and by the Jerome and Lorraine Aresty Charitable Foundation.


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Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  1. 1.Department of Molecular Biology and Biochemistry, Center for Advanced Biotechnology and Medicine, and Northeast Structural Genomics ConsortiumRutgers, The State University of New JerseyPiscatawayUSA
  2. 2.Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical SchoolRutgers, The State University of New JerseyPiscatawayUSA

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