BMRB Entry 6760
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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/BMR6760
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Title: NMR assignment of the mTOR domain responsible for rapamycin binding PubMed: 16456707
Deposition date: 2005-08-04 Original release date: 2006-03-10
Authors: Veverka, Vaclav; Lennie, Gregor; Crabbe, Tom; Bird, Ian; Taylor, Richard; Carr, Mark
Citation: Veverka, Vaclav; Lennie, Gregor; Crabbe, Tom; Bird, Ian; Taylor, Richard; Carr, Mark. "NMR assignment of the mTOR domain responsible for rapamycin binding" J. Biomol. NMR 36, 3-3 (2006).
Assembly members:
FRB domain, polymer, 126 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
Entity Sequences (FASTA):
FRB domain: MSYYHHHHHHDYDIPTTENL
YFQGAMELIRVPILWHEMWH
EGLEEASRLYFGERNVKGMF
EVLEPLHAMMERGPQTLKET
SFNQAYGRDLMEAQEWCRKY
MKSGNVKDLTQAWDLYYHVF
RRISKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 347 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 803 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FRB domain | 1 |
Entities:
Entity 1, FRB domain 126 residues - Formula weight is not available
| 1 | MET | SER | TYR | TYR | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | ASP | TYR | ASP | ILE | PRO | THR | THR | GLU | ASN | LEU | ||||
| 3 | TYR | PHE | GLN | GLY | ALA | MET | GLU | LEU | ILE | ARG | ||||
| 4 | VAL | PRO | ILE | LEU | TRP | HIS | GLU | MET | TRP | HIS | ||||
| 5 | GLU | GLY | LEU | GLU | GLU | ALA | SER | ARG | LEU | TYR | ||||
| 6 | PHE | GLY | GLU | ARG | ASN | VAL | LYS | GLY | MET | PHE | ||||
| 7 | GLU | VAL | LEU | GLU | PRO | LEU | HIS | ALA | MET | MET | ||||
| 8 | GLU | ARG | GLY | PRO | GLN | THR | LEU | LYS | GLU | THR | ||||
| 9 | SER | PHE | ASN | GLN | ALA | TYR | GLY | ARG | ASP | LEU | ||||
| 10 | MET | GLU | ALA | GLN | GLU | TRP | CYS | ARG | LYS | TYR | ||||
| 11 | MET | LYS | SER | GLY | ASN | VAL | LYS | ASP | LEU | THR | ||||
| 12 | GLN | ALA | TRP | ASP | LEU | TYR | TYR | HIS | VAL | PHE | ||||
| 13 | ARG | ARG | ILE | SER | LYS | GLN |
Samples:
sample_1: FRB domain, [U-15N], 0.1 mM
sample_2: FRB domain, [U-15N; U-13C], 0.1 mM
sample_3: FRB domain 0.1 mM
conditions_1: pH: 7.0; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H15N_HSQC_NOESY | not available | not available | conditions_1 |
| HNCACB | not available | not available | conditions_1 |
| CBCACONH | not available | not available | conditions_1 |
| HCCH-TOCSY | not available | not available | conditions_1 |
| 1H13C_HSQC_NOESY | not available | not available | conditions_1 |
Software:
No software information available
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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