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 30242

Title: Solution structure of the de novo mini protein EHEE_rd1_0284   PubMed: 28706065

Deposition date: 2017-02-01 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, 40 residues, 4973.368 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: TQTQEFDNEEEARKAEKELR KENRRVTVTQENGRWRVTWD

Data sets:
Data typeCount
13C chemical shifts127
15N chemical shifts24
1H chemical shifts204

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 40 residues - 4973.368 Da.

1   THRGLNTHRGLNGLUPHEASPASNGLUGLU
2   GLUALAARGLYSALAGLULYSGLULEUARG
3   LYSGLUASNARGARGVALTHRVALTHRGLN
4   GLUASNGLYARGTRPARGVALTHRTRPASP

Samples:

sample_1: protein, [U-13C; U-15N], 400 uM; sodium chloride, unlabelled, 150 mM; sodium phosphate, unlabelled, 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

ABACUS, Lemak and Arrowsmith - chemical shift assignment

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker AvanceIII 600 MHz

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