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 17658

Title: Solution structure of the estrogen receptor-binding stapled peptide SP1 (Ac-HXILHXLLQDS-NH2)   PubMed: 21612236

Deposition date: 2011-05-20 Original release date: 2011-10-26

Authors: Phillips, Chris; Bazin, Richard; Bent, Andrew; Davies, Nichola; Moore, Rob; Pannifer, Andrew; Pickford, Andrew; Prior, Stephen; Read, Christopher; Roberts, Lee; Schade, Markus; Scott, Andrew; Brown, David; Xu, Bin; Irving, Stephen

Citation: Phillips, Chris; Roberts, Lee; Schade, Markus; Bazin, Richard; Bent, Andrew; Davies, Nichola; Moore, Rob; Pannifer, Andrew; Pickford, Andrew; Prior, Stephen; Read, Christopher; Scott, Andrew; Brown, David; Xu, Bin; Irving, Stephen. "Design and structure of stapled peptides binding to estrogen receptors."  J. Am. Chem. Soc. 133, 9696-9699 (2011).

Assembly members:
stapled_peptide_SP1, polymer, 13 residues, 937.104 Da.

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

Experimental source:   Production method: chemical synthesis   Host organism: not applicable   Vector: not applicable

Entity Sequences (FASTA):
stapled_peptide_SP1: XHXILHXLLQDSX

Data sets:
Data typeCount
1H chemical shifts96

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1stapled_peptide_SP11

Entities:

Entity 1, stapled_peptide_SP1 13 residues - 937.104 Da.

1   ACEHISMK8ILELEUHISMK8LEULEUGLN
2   ASPSERNH2

Samples:

water: stapled peptide SP1 5 ± 1 mM; H2O 90 ± 1 %; D2O 10 ± 1 %; phosphate buffer 50 ± 1 mM

D2O: stapled peptide SP1 5 ± 1 mM; D2O 100 ± 1 %; phosphate buffer 50 ± 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYwaterisotropicsample_conditions_1
2D 1H-1H TOCSYwaterisotropicsample_conditions_1
2D 1H-1H NOESYwaterisotropicsample_conditions_1
2D 1H-1H COSYD2Oisotropicsample_conditions_1
2D 1H-1H TOCSYD2Oisotropicsample_conditions_1
2D 1H-1H NOESYD2Oisotropicsample_conditions_1

Software:

VNMR, Varian - collection

NMRSwarm v0.1, Andy Pickford - data analysis, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz