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 16187

Title: Backbone 1H Chemical Shift Assignments for FP1   PubMed: 19292861

Deposition date: 2009-02-26 Original release date: 2009-04-17

Authors: Araki, Mitsugu; Tamura, Atsuo

Citation: Araki, Mitsugu; Tamura, Atsuo. "Solubility-dependent structural formation of a 25-residue natively unfolded protein, induced by addition of a seven-residue peptide fragment"  FEBS J. 276, 2336-2347 (2009).

Assembly members:
FP1, polymer, 32 residues, 3519.278 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):
FP1: YAFACPACPKRFMRSDALSK HIKTAFIVVALG

Data sets:
Data typeCount
1H chemical shifts225

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FP11

Entities:

Entity 1, FP1 32 residues - 3519.278 Da.

1   TYRALAPHEALACYSPROALACYSPROLYS
2   ARGPHEMETARGSERASPALALEUSERLYS
3   HISILELYSTHRALAPHEILEVALVALALA
4   LEUGLY

Samples:

sample_1: FP1 3 mM; acetic acid, [U-100% 2H], 25 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 3.0; pressure: 1 atm; temperature: 293.15 K

Experiments:

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

Software:

DYANA v1.5, Guntert, Braun and Wuthrich - structure solution

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 750 MHz

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