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 30141

Title: NMR Solution Structure of Designed Peptide NC_EEH_D2   PubMed: 27626386

Deposition date: 2016-07-18 Original release date: 2016-09-16

Authors: Harvey, P.; Craik, D.

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:
entity_1, polymer, 27 residues, 2979.393 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: chemical synthesis

Entity Sequences (FASTA):
entity_1: TCVECXXVKVCRPDPEEARR EAEERCX

Data sets:
Data typeCount
13C chemical shifts80
15N chemical shifts22
1H chemical shifts173

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 27 residues - 2979.393 Da.

1   THRCYSVALGLUCYSDALDPRVALLYSVAL
2   CYSARGPROASPPROGLUGLUALAARGARG
3   GLUALAGLUGLUARGCYSNH2

Samples:

sample_1: design peptide NC_EEH_D2 1.0 mg/mL

sample_2: design peptide NC_EEH_D2 1.0 mg/mL

sample_conditions_1: pH: 3.0; pressure: 1 .; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D ECOSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

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