BMRB Entry 50264

Name: NMR Backbone Resonance Assignment of TREM2 transmembrane helix K186A variant
Published: 2020-06-08

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PDB ID: 6z0h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50264
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Backbone Resonance Assignment of TREM2 transmembrane helix K186A variant

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

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 LLACIFLIAILAASALWAAA WHGQKPGTH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	93
15N chemical shifts	36
1H chemical shifts	36

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TREM2	1

Entities:

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

1

GLY

SER

GLY

ARG

SER

LEU

GLU

GLY

GLU

2

ILE

PRO

PHE

PRO

THR

SER

ILE

LEU

3

LEU

ALA

CYS

ILE

PHE

LEU

ILE

ALA

ILE

4

LEU

ALA

SER

ALA

LEU

TRP

ALA

5

TRP

HIS

GLY

GLN

LYS

PRO

GLY

THR

HIS

Samples:

sample_1: TREM2 TMH K186A, [U-13C; U-15N; U-2H], 500 ± 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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5 - collection

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

UNP	Q9NZC2
AlphaFold	Q8WYN6