BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17897

Title: NOE-based 3D structure of the monomeric partially-folded intermediate of CylR2 at 259K (-14 Celsius degrees)   PubMed: 23396077

Deposition date: 2011-08-29 Original release date: 2013-02-15

Authors: Jaremko, Mariusz; Jaremko, Lukasz; Kim, Hai-Young; Cho, Min-Kyu; Schwieters, Charles; Giller, Karin; Becker, Stefan; Zweckstetter, Markus

Citation: Jaremko, Mariusz; Jaremko, Lukasz; Kim, Hai-Young; Cho, Min-Kyu; Schwieters, Charles; Giller, Karin; Becker, Stefan; Zweckstetter, Markus. "Cold denaturation of a protein dimer monitored at atomic resolution."  Nat. Chem. Biol. 9, 264-270 (2013).

Assembly members:
CylR2, polymer, 66 residues, 7725.070 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
CylR2: MIINNLKLIREKKKISQSEL AALLEVSRQTINGIEKNKYN PSLQLALKIAYYLNTPLEDI FQWQPE

Study: Cold denaturation of the CylR2 homodimer monitored at atomic resolution.

25 °C -3 °C -7 °C Dimer -7 °C Monomer -11 °C -14 °C -16 °C
17892178931789417895178961789717898
2lyj2lyk2lyl2lyp2lyq2lyr2lys

25°C -16°C

Adapted by permission from Macmillan Publishers Ltd: Nature Chemical Biology, copyright 2013

Molecular graphics and analyses were performed with the UCSF Chimera package. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco (supported by NIGMS P41-GM103311).
UCSF Chimera--a visualization system for exploratory research and analysis. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. J Comput Chem. 2004 Oct;25(13):1605-12.
JSmol: an open-source HTML5 viewer for chemical structures in 3D.

Data sets:
Data typeCount
13C chemical shifts168
15N chemical shifts67
1H chemical shifts381

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

BMRB 17892 17893 17894 17895 17896 17898
PDB 1UTX 2GZU 2LYJ 2LYK 2LYL 2LYP 2LYQ 2LYR 2LYS 2XI8 2XIU 2XJ3
GB AAL59476 AAL60140 AAM75247 AAO80372 AIL03173
REF NP_814301 WP_002358483 WP_002370931 WP_010773902 WP_048951311

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