BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	30.2 % (168 of 556)	13.8 % (39 of 282)	41.2 % (93 of 226)	75.0 % (36 of 48)
Backbone	58.7 % (168 of 286)	39.4 % (39 of 99)	65.5 % (93 of 142)	80.0 % (36 of 45)
Sidechain	8.6 % (27 of 314)	0.0 % (0 of 183)	21.1 % (27 of 128)	0.0 % (0 of 3)
Aromatic	0.0 % (0 of 52)	0.0 % (0 of 26)	0.0 % (0 of 24)	0.0 % (0 of 2)
Methyl	9.2 % (7 of 76)	0.0 % (0 of 38)	18.4 % (7 of 38)

1. entity 1

GSGRSLLEGE IPFPPTSILL LLACIFLIAI LAASALWAAA WHGQKPGTH

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Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 310 K, pH 7, Details 500 uM TREM2-TMH K186A in 300mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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: 6Z0H, 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 TMH K186A, : 2 : 4 entities Detail

Interaction partners 1. TREM2 TMH K186A, : 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, Details 500 uM TREM2-TMH K186A in 300mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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

#	Name	Isotope labeling	Concentration
1	TREM2 TMH K186A	[U-13C; U-15N; U-2H]	500 (±50.0) uM
2	DPC	natural abundance	300 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	bmr50264_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: bmr50264_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	165		73.5 (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: 73.5%
- Total number of assignments
  - ¹H chemical shifts: 36
  - ¹³C chemical shifts: 93
  - ¹⁵N chemical shifts: 36
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	282	36	12.8
¹³C chemical shifts	226	93	41.2
¹⁵N chemical shifts	49	36	73.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	99	36	36.4
¹³C chemical shifts	98	66	67.3
¹⁵N chemical shifts	45	36	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	183	0	0.0
¹³C chemical shifts	128	27	21.1
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	0	0.0
¹³C chemical shifts	38	7	18.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	0	0.0
¹³C chemical shifts	24	0	0.0
¹⁵N chemical shifts	2	0	0.0

Keywords NMR, TREM2, dynamics, intramembrane protease, structure

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Found 1 Document (0.479 seconds)

BMRB: 50264

Sample

Related entities 1. TREM2 TMH K186A, : 2 : 4 entities Detail

Interaction partners 1. TREM2 TMH K186A, : 1 interactors Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail