Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18761
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Citation: Dietl, Andreas; Wild, Klemens; Simon, Bernd. "(1)H, (13)C, and (15)N chemical shift assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65." Biomol. NMR Assignments ., .-. (2013).
PubMed: 23315337
Assembly members:
FE65_PTB2, polymer, 140 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: pET21d
Entity Sequences (FASTA):
FE65_PTB2: APKNELVQKFQVYYLGNVPV
AKPVGVDVINGALESVLSSS
SREQWTPSHVSVAPATLTIL
HQQTEAVLGECRVRFLSFLA
VGRDVHTFAFIMAAGPASFC
CHMFWCEPNAASLSEAVQAA
CMLRYQKCLDARSQHHHHHH
Data type | Count |
13C chemical shifts | 513 |
15N chemical shifts | 131 |
1H chemical shifts | 758 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FE65 PTB2 | 1 |
Entity 1, FE65 PTB2 140 residues - Formula weight is not available
1 | ALA | PRO | LYS | ASN | GLU | LEU | VAL | GLN | LYS | PHE | |
2 | GLN | VAL | TYR | TYR | LEU | GLY | ASN | VAL | PRO | VAL | |
3 | ALA | LYS | PRO | VAL | GLY | VAL | ASP | VAL | ILE | ASN | |
4 | GLY | ALA | LEU | GLU | SER | VAL | LEU | SER | SER | SER | |
5 | SER | ARG | GLU | GLN | TRP | THR | PRO | SER | HIS | VAL | |
6 | SER | VAL | ALA | PRO | ALA | THR | LEU | THR | ILE | LEU | |
7 | HIS | GLN | GLN | THR | GLU | ALA | VAL | LEU | GLY | GLU | |
8 | CYS | ARG | VAL | ARG | PHE | LEU | SER | PHE | LEU | ALA | |
9 | VAL | GLY | ARG | ASP | VAL | HIS | THR | PHE | ALA | PHE | |
10 | ILE | MET | ALA | ALA | GLY | PRO | ALA | SER | PHE | CYS | |
11 | CYS | HIS | MET | PHE | TRP | CYS | GLU | PRO | ASN | ALA | |
12 | ALA | SER | LEU | SER | GLU | ALA | VAL | GLN | ALA | ALA | |
13 | CYS | MET | LEU | ARG | TYR | GLN | LYS | CYS | LEU | ASP | |
14 | ALA | ARG | SER | GLN | HIS | HIS | HIS | HIS | HIS | HIS |
sample_1: FE65 PTB2, [U-100% 13C; U-100% 15N], 0.2 0.7 mM
sample_2: FE65 PTB2 0.7 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 300 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
TOPSPIN, Bruker Biospin - collection
NMRView, Johnson, One Moon Scientific - chemical shift assignment
PDB | |
DBJ | BAC27116 BAC39033 BAE37645 BAE73097 BAH11511 |
EMBL | CAA42999 CAD98057 |
GB | AAB51603 AAB93631 AAC79942 AAF20141 AAH10854 |
REF | NP_001068654 NP_001155 NP_001240814 NP_001240815 NP_001240816 |
SP | O00213 P46933 Q9QXJ1 |
TPG | DAA22130 |
AlphaFold | O00213 P46933 Q9QXJ1 |
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