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 11524

Title: NMR Structure of designed protein, AF.2A1, (Ensembles)   PubMed: 24356963

Deposition date: 2013-04-18 Original release date: 2014-01-02

Authors: Watanabe, Hideki; Yamasaki, Kazuhiko; Honda, Shinya

Citation: Watanabe, Hideki; Yamasaki, Kazuhiko; Honda, Shinya. "Structurally guided stepwise segment elongation for the design of a small sized protein: implications for primordial protein evolution"  J. Biol. Chem. ., .-. (2013).

Assembly members:
entity, polymer, 25 residues, 2716.968 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):
entity: GVVRQWSGYDPRTGTWRSSI AYGGG

Data sets:
Data typeCount
1H chemical shifts155

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 25 residues - 2716.968 Da.

1   GLYVALVALARGGLNTRPSERGLYTYRASP
2   PROARGTHRGLYTHRTRPARGSERSERILE
3   ALATYRGLYGLYGLY

Samples:

sample_1: entity 1.8 mM; sodium acetate-d4, [U-100% 2H], 10 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 10 mM; pH: 4.5; pressure: 1 atm; temperature: 283 K

Experiments:

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

Software:

No software information available

NMR spectrometers:

  • Bruker AMX 500 MHz

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