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 17896

Title: NOE-based 3D structure of the monomeric intermediate of CylR2 at 262K (-11 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

Data sets:
Data typeCount
13C chemical shifts186
15N chemical shifts69
1H chemical shifts419

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CylR21

Entities:

Entity 1, CylR2 66 residues - 7725.070 Da.

1   METILEILEASNASNLEULYSLEUILEARG
2   GLULYSLYSLYSILESERGLNSERGLULEU
3   ALAALALEULEUGLUVALSERARGGLNTHR
4   ILEASNGLYILEGLULYSASNLYSTYRASN
5   PROSERLEUGLNLEUALALEULYSILEALA
6   TYRTYRLEUASNTHRPROLEUGLUASPILE
7   PHEGLNTRPGLNPROGLU

Samples:

sample_1: CylR2, [U-100% 13C; U-100% 15N], 0.52 mM; sodium chloride 600 mM; HEPES 50 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.6 M; pH: 7.0; pressure: 1 atm; temperature: 262 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance III 700 MHz

Related Database Links:

BMRB 17892 17893 17894 17895 17897 17898
PDB
GB AAL59476 AAL60140 AAM75247 AAO80372 AIL03173
REF NP_814301 WP_002358483 WP_002370931 WP_010773902 WP_048951311

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts