BMRB Entry 6902
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6902
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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 Vector: pET28a
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 |
Samples:
sample_1: hFKBP38D 1.3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium azide 0.05 ± 0.001 %
sample_2: hFKBP38D, [U-15N], 1.3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium azide 0.05 ± 0.001 %
conditions_1: pH: 6.7; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
xwinnmr v3.5, Bruker - processing
AURELIA v2.5.9, Bruker - analysis
FELIX v2000, Accelrys - analysis
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker Avance 700 MHz
Related Database Links:
| BMRB | 6923 |
| PDB | |
| DBJ | BAD96558 BAG36163 BAG72557 BAH13306 |
| EMBL | CAD98028 CAL37783 |
| GB | AAB00102 AAC28753 AAH09966 AAI22595 AAO39020 |
| REF | NP_001247999 NP_001272500 NP_036313 XP_002761955 XP_002828980 |
| SP | Q14318 |
| AlphaFold | Q14318 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts