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 50265

Title: NMR backbone resonance assignment of TREM2 transmembrane helix in complex with the partner protein DAP12   PubMed: 32830336

Deposition date: 2020-05-08 Original release date: 2020-06-08

Authors: Steiner, Andrea; Hagn, Franz

Citation: Steiner, Andrea; Schlepckow, Kai; Brunner, Bettina; Steiner, Harald; Haass, Christian; Hagn, Franz. "gamma-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics"  EMBO J. 39, e104247-e104247 (2020).

Assembly members:
entity_1, polymer, 49 residues, Formula weight is not available
entity_2, polymer, 50 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
entity_1: GSGRSLLEGEIPFPPTSILL LLACIFLIKILAASALWAAA WHGQKPGTH
entity_2: GLRPVQAQAQSDSSCSTVSP GVLAGIVMGDLVLTVLIALA VYFLGRLVPR

Data sets:
Data typeCount
13C chemical shifts91
15N chemical shifts34
1H chemical shifts34

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TREM21
2DAP122

Entities:

Entity 1, TREM2 49 residues - Formula weight is not available

1   GLYSERGLYARGSERLEULEUGLUGLYGLU
2   ILEPROPHEPROPROTHRSERILELEULEU
3   LEULEUALACYSILEPHELEUILELYSILE
4   LEUALAALASERALALEUTRPALAALAALA
5   TRPHISGLYGLNLYSPROGLYTHRHIS

Entity 2, DAP12 50 residues - Formula weight is not available

1   GLYLEUARGPROVALGLNALAGLNALAGLN
2   SERASPSERSERCYSSERTHRVALSERPRO
3   GLYVALLEUALAGLYILEVALMETGLYASP
4   LEUVALLEUTHRVALLEUILEALALEUALA
5   VALTYRPHELEUGLYARGLEUVALPROARG

Samples:

sample_1: TREM2 TMH wt, [U-13C; U-15N; U-2H], 500 ± 50 uM; DAP12 1000 ± 50 uM; DPC 300 mM; NaPi 20 mM; NaCl 50 mM; EDTA 0.5 mM; DTT 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5 - collection

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP Q9NZC2
UniProt O43914

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