BMRBj - BMREntryMaster

Found 1 Document (0.464 seconds)

BMRB: 50263

NMR backbone assignment of the transmembrane helix of TREM2, an Alzheimer linked disease protein

Authors

Steiner, A., Hagn, F.X.

Assembly

TREM2

Entity

1. TREM2 (polymer, Thiol state: all free), 49 monomers, 5167.076 Da Detail

GSGRSLLEGE IPFPPTSILL LLACIFLIKI LAASALWAAA WHGQKPGTH

Formula weight

5167.076 Da

Source organism

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 79.6 %, Completeness: 34.6 %, Completeness (bb): 61.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	34.6 % (196 of 566)	18.0 % (52 of 289)	48.5 % (111 of 229)	68.8 % (33 of 48)
Backbone	61.2 % (175 of 286)	36.4 % (36 of 99)	74.6 % (106 of 142)	73.3 % (33 of 45)
Sidechain	15.7 % (51 of 324)	8.4 % (16 of 190)	26.7 % (35 of 131)	0.0 % (0 of 3)
Aromatic	9.6 % (5 of 52)	19.2 % (5 of 26)	0.0 % (0 of 24)	0.0 % (0 of 2)
Methyl	14.9 % (11 of 74)	5.4 % (2 of 37)	24.3 % (9 of 37)

1. entity 1

GSGRSLLEGE IPFPPTSILL LLACIFLIKI LAASALWAAA WHGQKPGTH

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 6Z0G, Strand ID: A Detail

Release date

2020-05-07

Citation

γ-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics
Steiner, A., Schlepckow, K., Brunner, B., Steiner, H., Haass, C., Hagn, F.X.
EMBO J. (2020), 39, e104247-e104247, PubMed 32830336 , DOI 10.15252/embj.2019104247 , Abstract

Related entities 1. TREM2, : 2 : 2 entities Detail

Interaction partners 1. TREM2, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 6 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

2 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

3 3D HNCA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

5 3D HN(CO)CA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

6 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 500 uM TREM2-TMH in 200mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Type	Concentration
1	TREM2	[U-13C; U-15N; U-2H]		500 (±50.0) uM
2	DPC	natural abundance		200 mM
3	NaPi	natural abundance		20 mM
4	NaCl	natural abundance		50 mM
5	EDTA	natural abundance		0.5 mM
6	DTT	natural abundance		5 mM

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr50263_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr50263_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	167		77.6 (chain: 1, length: 49)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 49, Sequence coverage: 77.6%
- Total number of assignments
  - ¹³C chemical shifts: 103
  - ¹H chemical shifts: 32
  - ¹⁵N chemical shifts: 32
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Keywords NMR, TREM2, dynamics, intramembrane protease, structure