BMRB Entry 6902
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6902
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Title: Complete 1H and 15N assignment of the FK506-binding domain of human FKBP38 PubMed: 16604427
Deposition date: 2005-11-16 Original release date: 2006-04-24
Authors: Maestre-Martinez, Mitcheell; Edlich, Frank; Jarczowski, Franziska; Weiwad, Matthias; Fischer, Gunter; Luecke, Christian
Citation: Maestre-Martinez, Mitcheell; Edlich, Frank; Jarczowski, Franziska; Weiwad, Matthias; Fischer, Gunter; Luecke, Christian. "NMR Structure Note: Solution structure of the FK506-binding domain of human FKBP38" J. Biomol. NMR 34, 197-202 (2006).
Assembly members:
hFKBP38D, polymer, 121 residues, 13056 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
hFKBP38D: MREWLDILGNGLLRKKTLVP
GPPGSSRPVKGQVVTVHLQT
SLENGTRVQEEPELVFTLGD
CDVIQALDLSVPLMDVGETA
MVTADSKYCYGPQGRSPYIP
PHAALCLEVTLKTAVDGPDL
E
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 119 |
1H chemical shifts | 868 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | hFKBP38D | 1 |
Entities:
Entity 1, hFKBP38D 121 residues - 13056 Da.
According to Swiss-Prot entry Q14318, the residue numbers have to be increased by 32 relative to the BMRB numbering
1 | MET | ARG | GLU | TRP | LEU | ASP | ILE | LEU | GLY | ASN | ||||
2 | GLY | LEU | LEU | ARG | LYS | LYS | THR | LEU | VAL | PRO | ||||
3 | GLY | PRO | PRO | GLY | SER | SER | ARG | PRO | VAL | LYS | ||||
4 | GLY | GLN | VAL | VAL | THR | VAL | HIS | LEU | GLN | THR | ||||
5 | SER | LEU | GLU | ASN | GLY | THR | ARG | VAL | GLN | GLU | ||||
6 | GLU | PRO | GLU | LEU | VAL | PHE | THR | LEU | GLY | ASP | ||||
7 | CYS | ASP | VAL | ILE | GLN | ALA | LEU | ASP | LEU | SER | ||||
8 | VAL | PRO | LEU | MET | ASP | VAL | GLY | GLU | THR | ALA | ||||
9 | MET | VAL | THR | ALA | ASP | SER | LYS | TYR | CYS | TYR | ||||
10 | GLY | PRO | GLN | GLY | ARG | SER | PRO | TYR | ILE | PRO | ||||
11 | PRO | HIS | ALA | ALA | LEU | CYS | LEU | GLU | VAL | THR | ||||
12 | LEU | LYS | THR | ALA | VAL | ASP | GLY | PRO | ASP | LEU | ||||
13 | GLU |