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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15775
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
Citation: Beel, Andrew; Mobley, Charles; Kim, Hak; Tian, Fang; Hadziselimovic, Arina; Jap, Bing; Prestegard, James; Sanders, Charles. "Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?" Biochemistry 47, 9428-9446 (2008).
PubMed: 18702528
Assembly members:
APP_C99, polymer, 122 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a
Entity Sequences (FASTA):
APP_C99: MDAEFRHDSGYEVHHQKLVF
FAEDVGSNKGAIIGLMVGGV
VIATVIVITLVMLKKKQYTS
IHHGVVEVDAAVTPEERHLS
KMQQNGYENPTYKFFEQMQN
QGRILQISITLAAALEHHHH
HH
Data type | Count |
13C chemical shifts | 284 |
15N chemical shifts | 99 |
1H chemical shifts | 99 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | APP C99 | 1 |
Entity 1, APP C99 122 residues - Formula weight is not available
Residues 101 to 122 represent a non-native tag; The N-terminal Met residues corresponds to site 671 in the amyloid precursor protein (APP); Asn100 represents the C-terminal residues 770 of the full length APP
1 | MET | ASP | ALA | GLU | PHE | ARG | HIS | ASP | SER | GLY | ||||
2 | TYR | GLU | VAL | HIS | HIS | GLN | LYS | LEU | VAL | PHE | ||||
3 | PHE | ALA | GLU | ASP | VAL | GLY | SER | ASN | LYS | GLY | ||||
4 | ALA | ILE | ILE | GLY | LEU | MET | VAL | GLY | GLY | VAL | ||||
5 | VAL | ILE | ALA | THR | VAL | ILE | VAL | ILE | THR | LEU | ||||
6 | VAL | MET | LEU | LYS | LYS | LYS | GLN | TYR | THR | SER | ||||
7 | ILE | HIS | HIS | GLY | VAL | VAL | GLU | VAL | ASP | ALA | ||||
8 | ALA | VAL | THR | PRO | GLU | GLU | ARG | HIS | LEU | SER | ||||
9 | LYS | MET | GLN | GLN | ASN | GLY | TYR | GLU | ASN | PRO | ||||
10 | THR | TYR | LYS | PHE | PHE | GLU | GLN | MET | GLN | ASN | ||||
11 | GLN | GLY | ARG | ILE | LEU | GLN | ILE | SER | ILE | THR | ||||
12 | LEU | ALA | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
13 | HIS | HIS |
sample_1: APP C99, [U-100% 13C; U-100% 15N; 80% 2H], 2.5 mM; LMPG micelle 9%; imidazole-acetate 250 mM; EDTA 1 mM
sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 318 K
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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
FELIX v2000, Accelrys Software Inc. - chemical shift assignment
PDB | |
DBJ | BAA22264 BAA84580 BAC34997 BAC36369 BAE01907 |
EMBL | CAA30050 CAA30488 CAA31830 CAA66230 CAA68374 |
GB | AAA35540 AAA36829 AAA37139 AAA51722 AAA51726 |
PIR | PQ0438 |
PRF | 1303338A 1403400A 1507304A 1507304B 1507304C |
REF | NP_000475 NP_001006601 NP_001013036 NP_001070264 NP_001127014 |
SP | P05067 P08592 P12023 P53601 P79307 |
TPG | DAA33655 |
AlphaFold | P05067 P79307 P53601 P12023 P08592 |
Download HSQC peak lists in one of the following formats:
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