BMRB Entry 50265

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50265
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR backbone resonance assignment of TREM2 transmembrane helix in complex with the partner protein DAP12
Deposition date:
2020-05-08
Original release date:
2020-06-08
Authors:
Steiner, Andrea; Hagn, Franz
Citation:

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).
PubMed: 32830336

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

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
AlphaFold Q8WYN6 Q9UMT3

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks