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 16090

Title: NMR Structure of a Monomeric Folding Intermediate Reveals the Structural Basis for Rapid Assembly of an Evolutionary Optimized Trimerization Module   PubMed: 19361528

Deposition date: 2008-12-24 Original release date: 2009-04-22

Authors: Habazettl, Judith; Reiner, Andreas; Kiefhaber, Thomas

Citation: Habazettl, Judith; Reiner, Andreas; Kiefhaber, Thomas. "NMR Structure of a Monomeric Intermediate on the Evolutionarily Optimized Assembly Pathway of a Small Trimerization Domain"  J. Mol. Biol. 389, 103-114 (2009).

Assembly members:
foldon_E5R, polymer, 29 residues, 3112.573 Da.

Natural source:   Common Name: Enterobacteria phage T4 sensu lato   Taxonomy ID: 348604   Superkingdom: Viruses   Kingdom: not available   Genus/species: T4-like viruses Enterobacteria phage T4 sensu lato

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

Entity Sequences (FASTA):
foldon_E5R: GSGYIPRAPRDGQAYVRKDG EWVLLSTFL

Data sets:
Data typeCount
15N chemical shifts26
1H chemical shifts192

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1foldon_E5R1

Entities:

Entity 1, foldon_E5R 29 residues - 3112.573 Da.

residues 1-27 represent the residues 458-484 in native fibritin

1   GLYSERGLYTYRILEPROARGALAPROARG
2   ASPGLYGLNALATYRVALARGLYSASPGLY
3   GLUTRPVALLEULEUSERTHRPHELEU

Samples:

sample_1: foldon E5R 200 uM; K_3 PO_4 10 mM

sample_2: foldon E5R, [U-99% 15N], 210 uM; K_3 PO_4 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 296.7 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker - data analysis

SPARKY, Goddard - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB

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