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 30249

Title: Solution NMR structure of the de novo mini protein HEEH_rd4_0097   PubMed: 28706065

Deposition date: 2017-02-24 Original release date: 2017-07-20

Authors: Lemak, A.; Rocklin, G.; Houliston, S.; 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, 64 residues, 7469.417 Da.

Natural source:   Common Name: Escherichia   Taxonomy ID: 561   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia not available

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

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MDVEEQIRRLEEVLKKNQPV TWNGTTYTDPNEIKKVIEEL RKSM

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts46
1H chemical shifts287

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 - 7469.417 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METASPVALGLUGLUGLNILEARGARGLEU
4   GLUGLUVALLEULYSLYSASNGLNPROVAL
5   THRTRPASNGLYTHRTHRTYRTHRASPPRO
6   ASNGLUILELYSLYSVALILEGLUGLULEU
7   ARGLYSSERMET

Samples:

sample_1: protein, [U-13C; U-15N], 400 uM; sodium chloride 150 mM; sodium phosphate 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 NOESY aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

ABACUS, Lemak and Arrowsmith - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceII 800 MHz

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