BMRB Entry 30241

Title:
Solution structure of the de novo mini protein EEHEE_rd3_1049
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:

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, 64 residues, 7191.284 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):

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts42
1H chemical shifts328

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 64 residues - 7191.284 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METTHRTHRVALLYSLEUGLYASPILELYS
4   VALTHRPHEASPASNPROGLULYSALALYS
5   LYSTYRALAGLNLYSLEUALALYSILETYR
6   GLNLEUTHRVALHISVALHISGLYASPTHR
7   ILEHISVALLYS

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 HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_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 Avance III 600 MHz
  • Bruker Avance II 800 MHz

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