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 30355

Title: Solution structure of de novo macrocycle Design8.1   PubMed: 29242347

Authors: Shortridge, M.; Hosseinzadeh, P.; Pardo-Avila, F.; Varani, G.; Baker, D.

Citation: Hosseinzadeh, P.; Bhardwaj, G.; Mulligan, V.; Shortridge, M.; Craven, T.; Pardo-Avila, F.; Rettie, S.; Kim, D.; Silva, D.; Ibrahim, Y.; Webb, I.; Cort, J.; Adkins, J.; Varani, G.; Baker, D.. "Comprehensive computational design of ordered peptide macrocycles."  Science 358, 1461-1466 (2017).

Assembly members:
entity_1, polymer, 8 residues, 956.976 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: DDPTXXQX

Data sets:
Data typeCount
13C chemical shifts25
15N chemical shifts9
1H chemical shifts48

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, entity_1 8 residues - 956.976 Da.



sample_1: peptide 5 mg/mL; glycerol, [U-2H], 5 % v/v

sample_conditions_1: ionic strength: 0 Not defined; pH: 5.5; pressure: 1 atm; temperature: 278 K


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


SPARKY, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

gromacs, Abraham - refinement

NMR spectrometers:

  • Bruker DRX 500 MHz

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