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 30069

Title: Solution structure of the de novo miniprotein EEHE_02   PubMed: 27626386

Deposition date: 2016-04-21 Original release date: 2016-09-22

Authors: Buchko, G.; Bahl, C.

Citation: Bhardwaj, G.; Mulligan, V.; Bahl, C.; Gilmore, J.; Harvey, P.; Cheneval, O.; Buchko, G.; Pulavarti, S.; Kaas, Q.; Eletsky, A.; Huang, P.; Johnsen, W.; Greisen, P.; Rocklin, G.; Song, Y.; Linsky, T.; Watkins, A.; Rettie, S.; Xu, X.; Carter, L.; Bonneau, R.; Olson, J.; Coutsias, E.; Correnti, C.; Szyperski, T.; Craik, D.; Baker, D.. "Accurate de novo design of hyperstable constrained peptides."  Nature 538, 329-335 (2016).

Assembly members:
W37, polymer, 37 residues, 4054.548 Da.

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
W37: APCECDVNGETYTVSSSEEC ERLCRKLGVTNCRVHCG

Data sets:
Data typeCount
13C chemical shifts84
15N chemical shifts39
1H chemical shifts220

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 37 residues - 4054.548 Da.

1   ALAPROCYSGLUCYSASPVALASNGLYGLU
2   THRTYRTHRVALSERSERSERGLUGLUCYS
3   GLUARGLEUCYSARGLYSLEUGLYVALTHR
4   ASNCYSARGVALHISCYSGLY

Samples:

sample_1: W37, [U-99% 15N], 1 ± 0.2 mM; sodium acetate 25 ± 1 mM; sodium chloride 50 ± 1 mM; H2O 93%; D2O 7%

sample_2: W37, [U-99% 15N], 1 mM; sodium acetate 25 ± 1 mM; sodium chloride 50 ± 1 mM; D2O 100%

sample_conditions_1: ionic strength: 75 mM; pH: 4.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
Deuterium Exchangesample_2isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

SPARKY v3.115, Goddard - data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

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