BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34213

Title: NMR structure of EphA2-Sam stapled peptides (S13ST)   PubMed: 30036816

Deposition date: 2017-12-11 Original release date: 2018-07-26

Authors: Mercurio, F.; Leone, M.

Citation: Mercurio, F.; Pirone, L.; Di Natale, C.; Marasco, D.; Pedone, E.; Leone, M.. "Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2"  Bioorg. Chem. 80, 602-610 (2018).

Assembly members:
entity_1, polymer, 27 residues, 2905.534 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: XKRIGVRLPGHQKRXAYSXL GLKDQVX

Data sets:
Data typeCount
1H chemical shifts200

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 - 2905.534 Da.

1   ACELYSARGILEGLYVALARGLEUPROGLY
2   HISGLNLYSARGMK8ALATYRSERMK8LEU
3   GLYLEULYSASPGLNVALNH2

Samples:

sample_1: S13ST 650 uM

sample_conditions_1: pH: 7.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - processing

XEASY, Bartels et al. - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

Chimera v1.10.1, Pettersen et al. - geometry optimization

NMR spectrometers:

  • Varian INOVA 600 MHz