BMRB Entry 30240

Click here to enlarge.

PDB ID: 5uoi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30240
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

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).
PubMed: 28706065

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 43 residues - 5190.805 Da.

1   ARGLYSTRPGLUGLUILEALAGLUARGLEU
2   ARGGLUGLUPHEASNILEASNPROGLUGLU
3   ALAARGGLUALAVALGLULYSALAGLYGLY
4   ASNGLUGLUGLUALAARGARGILEVALLYS
5   LYSARGLEU

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks