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 18412

Title: High Definition Solution Structure of PED/PEA-15 Death Effector Domain   PubMed: 22732408

Deposition date: 2012-04-20 Original release date: 2012-08-06

Authors: Twomey, Edward; Wei, Yufeng

Citation: Twomey, Edward; Wei, Yufeng. "High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions"  Biochem. Biophys. Res. Commun. 424, 141-146 (2012).

Assembly members:
pea-15, polymer, 130 residues, 10450.842 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
pea-15: MAEYGTLLQDLTNNITLEDL EQLKSACKEDIPSEKSEEIT TGSAWFSFLESHNKLDKDNL SYIEHIFEISRRPDLLTMVV DYRTRVLKISEEDELDTKLT RIPSAKKYKDIIRQPSEEEI IKLAPPPKKA

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts132
1H chemical shifts858

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1phosphoprotein enriched in astrocytes 15A1

Entities:

Entity 1, phosphoprotein enriched in astrocytes 15A 130 residues - 10450.842 Da.

1   METALAGLUTYRGLYTHRLEULEUGLNASP
2   LEUTHRASNASNILETHRLEUGLUASPLEU
3   GLUGLNLEULYSSERALACYSLYSGLUASP
4   ILEPROSERGLULYSSERGLUGLUILETHR
5   THRGLYSERALATRPPHESERPHELEUGLU
6   SERHISASNLYSLEUASPLYSASPASNLEU
7   SERTYRILEGLUHISILEPHEGLUILESER
8   ARGARGPROASPLEULEUTHRMETVALVAL
9   ASPTYRARGTHRARGVALLEULYSILESER
10   GLUGLUASPGLULEUASPTHRLYSLEUTHR
11   ARGILEPROSERALALYSLYSTYRLYSASP
12   ILEILEARGGLNPROSERGLUGLUGLUILE
13   ILELYSLEUALAPROPROPROLYSLYSALA

Samples:

sample_1: phosphoprotein enriched in astrocytes 15A, [U-100% 13C; U-100% 15N], 1 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.29, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC40734 BAE31752 BAE32041 BAE36504 BAE36662
EMBL CAA60387 CAA60499 CAA74076 CAB51573 CAG46533
GB AAC97496 AAD56775 AAH02426 AAH22554 AAH38282
REF NP_001013249 NP_001068924 NP_001127112 NP_001185596 NP_001231780
SP Q15121 Q5R529 Q5U318 Q62048 Q9Z297
TPG DAA31971

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