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 15879

Title: Protein folding on a highly rugged landscape: Experimental observation of glassy dynamics and structural frustration   PubMed: 19240216

Deposition date: 2008-07-18 Original release date: 2009-03-12

Authors: Sadqi, Mourad; de Alba, Eva; Perez-Jimenez, Raul; Sanchez-Ruiz, Jose; Munoz, Victor

Citation: Sadqi, Mourad; de Alba, Eva; Perez-Jimenez, Raul; Sanchez-Ruiz, Jose; Munoz, Victor. "A designed protein as experimental model of primordial folding"  Proc. Natl. Acad. U.S.A. 106, 4127-4132 (2009).

Assembly members:
FSD_mod, polymer, 29 residues, 3854.456 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: chemical synthesis

Entity Sequences (FASTA):
FSD_mod: GQQYTAXIKGRTFRNEKELR DFIEKFXGR

Data sets:
Data typeCount
13C chemical shifts23
1H chemical shifts216

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FSD_mod1

Entities:

Entity 1, FSD_mod 29 residues - 3854.456 Da.

1   GLYGLNGLNTYRTHRALANALILELYSGLY
2   ARGTHRPHEARGASNGLULYSGLULEUARG
3   ASPPHEILEGLULYSPHEDNSGLYARG

Samples:

sample_1: FSD_mod 1 mM; DSS 0.05 mM; D2O, [U-99.9% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0 M; pH: 5.0; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker Avance 600 MHz

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