BMRB: 15775

Backbone chemical shift assignment for the transmembrane and C-terminal domains of amyloid precursor protein (APP C99)

Authors

Sanders, C.R.

Assembly

The transmembrane C-terminal domain of the Amyloid Precursor Protein

Entity

1. The transmembrane C-terminal domain of the Amyloid Precursor Protein (polymer, Thiol state: not present), 122 monomers, 13779.58 Da Detail

MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN QGRILQISIT LAAALEHHHH HH

Formula weight

13779.58 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 87.7 %, Completeness: 34.6 %, Completeness (bb): 66.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	34.6 % (495 of 1430)	15.5 % (114 of 735)	50.1 % (282 of 563)	75.0 % (99 of 132)
Backbone	66.2 % (482 of 728)	40.6 % (102 of 251)	78.7 % (281 of 357)	82.5 % (99 of 120)
Sidechain	12.1 % (99 of 815)	2.5 % (12 of 484)	27.3 % (87 of 319)	0.0 % (0 of 12)
Aromatic	0.0 % (0 of 130)	0.0 % (0 of 65)	0.0 % (0 of 65)
Methyl	9.3 % (14 of 150)	5.3 % (4 of 75)	13.3 % (10 of 75)

1. APP C99

MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN QGRILQISIT LAAALEHHHH HH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 318 K, pH 6.5, Details 13C, 15N, 2H(70%) in 9% LMPG micelle solution, 250 mM imidazole-acetate, 1 mM EDTA, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	APP C99	[U-100% 13C; U-100% 15N; 80% 2H]		2.5 mM
2	LMPG micelle			9 %
3	imidazole-acetate			250 mM
4	EDTA			1 mM

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LACS Plot; CA

Referencing offset: 0.47 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CB

Referencing offset: 0.47 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CO

Referencing offset: 0.12 ppm, Outliers: 5 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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Protein Blocks Logo

Calculated from 30 models in PDB: 2LP1, Strand ID: A Detail

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Release date

2008-08-18

Citation

Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?
Beel, A.J., Mobley, C.K., Kim, H.J., Tian, F., Hadziselimovic, A., Jap, B., Prestegard, J.H., Sanders, C.R.
Biochemistry (2008), 47, 9428-9446, PubMed 18702528 , DOI 10.1021/bi800993c , Abstract

Related entities 1. The transmembrane C-terminal domain of the Amyloid Precursor Protein, : 7 : 17 entities Detail

Interaction partners 1. The transmembrane C-terminal domain of the Amyloid Precursor Protein, : 102 interactors Detail

Experiments performed 6 experiments Detail