BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30240

Title: Solution structure of the de novo mini protein HHH_rd1_0142   PubMed: 28706065

Deposition date: 2017-01-31 Original release date: 2017-07-20

Authors: Houliston, S.; Rocklin, G.; Lemak, A.; Carter, L.; Chidyausiku, T.; Baker, D.; Arrowsmith, C.

Citation: Rocklin, Gabriel; Chidyausiku, Tamuka; Goreshnik, Inna; Ford, Alex; Houliston, Scott; Lemak, Alexander; Carter, Lauren; Ravichandran, Rashmi; Mulligan, Vikram; Chevalier, Aaron; Arrowsmith, Cheryl; Baker, David. "Global analysis of protein folding using massively parallel design, synthesis, and testing"  Science 357, 168-175 (2017).

Assembly members:
entity_1, polymer, 43 residues, 5190.805 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: RKWEEIAERLREEFNINPEE AREAVEKAGGNEEEARRIVK KRL

Data sets:
Data typeCount
13C chemical shifts168
15N chemical shifts40
1H chemical shifts280

Additional metadata:

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

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