Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Jaudzems, K.
  • Pedrini, B.
  • Geralt, M.
  • Serrano-Navarro, Pedro
  • Wuthrich, Kurt

publication date

  • January 2015

journal

  • Journal of Biomolecular NMR  Journal

abstract

  • The NMR structure of the 206-residue protein NP_346487.1 was determined with the J-UNIO protocol, which includes extensive automation of the structure determination. With input from three APSY-NMR experiments, UNIO-MATCH automatically yielded 77 % of the backbone assignments, which were interactively validated and extended to 97 %. With an input of the near-complete backbone assignments and three 3D heteronuclear-resolved [(1)H,(1)H]-NOESY spectra, automated side chain assignment with UNIO-ATNOS/ASCAN resulted in 77 % of the expected assignments, which was extended interactively to about 90 %. Automated NOE assignment and structure calculation with UNIO-ATNOS/CANDID in combination with CYANA was used for the structure determination of this two-domain protein. The individual domains in the NMR structure coincide closely with the crystal structure, and the NMR studies further imply that the two domains undergo restricted hinge motions relative to each other in solution. NP_346487.1 is so far the largest polypeptide chain to which the J-UNIO structure determination protocol has successfully been applied.

subject areas

  • Bacterial Proteins
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphoric Monoester Hydrolases
  • Protein Structure, Tertiary
  • Streptococcus pneumoniae
scroll to property group menus

Research

keywords

  • APSY-NMR spectroscopy
  • Automatic data analysis
  • NOESY
  • Protein structure
  • Putative phosphoglycolate phosphatase
scroll to property group menus

Identity

PubMed Central ID

  • PMC4304919

International Standard Serial Number (ISSN)

  • 0925-2738

Digital Object Identifier (DOI)

  • 10.1007/s10858-014-9886-3

PubMed ID

  • 25428766
scroll to property group menus

Additional Document Info

start page

  • 65

end page

  • 72

volume

  • 61

issue

  • 1

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support