BMRB Entry 6837
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6837
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR Assignments of L27 Heterodimer From C. Elegans Lin-7 and H. Sapiens Lin-2 Scaffold Proteins PubMed: 16721631
Deposition date: 2005-09-26 Original release date: 2006-10-02
Authors: Petrosky, Keiko; Loehr, Frank; Doetsch, Volker
Citation: Petrosky, Keiko; Loehr, Frank; Doetsch, Volker. "NMR Assignment of the L27 Heterodimer from LIN-2 and LIN-7 Scaffold Proteins" J. Biomol. NMR 36, 15-15 (2006).
Assembly members:
construct, polymer, 164 residues, 18302.2 Da.
Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
construct: MGHHHHHHDYDIPTTENLYE
QGSLNLERDVQRILELMEHV
QKTGEVNNAKLASLQQVLQS
EFFGAVREVYETVYESIDAD
TTPEIKAAAGSGSGSGSNLP
SDAVQRAKEVLEEISCYPEN
NDAKELKRILTQPHFMALLQ
THDVVAHEVYSDEALRVTPP
PTSP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 549 |
| 15N chemical shifts | 146 |
| 1H chemical shifts | 851 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | L27 Heterodimer From Lin-7 and Lin-2 Scaffold Proteins | 1 |
Entities:
Entity 1, L27 Heterodimer From Lin-7 and Lin-2 Scaffold Proteins 164 residues - 18302.2 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | ASP | TYR | ||||
| 2 | ASP | ILE | PRO | THR | THR | GLU | ASN | LEU | TYR | GLU | ||||
| 3 | GLN | GLY | SER | LEU | ASN | LEU | GLU | ARG | ASP | VAL | ||||
| 4 | GLN | ARG | ILE | LEU | GLU | LEU | MET | GLU | HIS | VAL | ||||
| 5 | GLN | LYS | THR | GLY | GLU | VAL | ASN | ASN | ALA | LYS | ||||
| 6 | LEU | ALA | SER | LEU | GLN | GLN | VAL | LEU | GLN | SER | ||||
| 7 | GLU | PHE | PHE | GLY | ALA | VAL | ARG | GLU | VAL | TYR | ||||
| 8 | GLU | THR | VAL | TYR | GLU | SER | ILE | ASP | ALA | ASP | ||||
| 9 | THR | THR | PRO | GLU | ILE | LYS | ALA | ALA | ALA | GLY | ||||
| 10 | SER | GLY | SER | GLY | SER | GLY | SER | ASN | LEU | PRO | ||||
| 11 | SER | ASP | ALA | VAL | GLN | ARG | ALA | LYS | GLU | VAL | ||||
| 12 | LEU | GLU | GLU | ILE | SER | CYS | TYR | PRO | GLU | ASN | ||||
| 13 | ASN | ASP | ALA | LYS | GLU | LEU | LYS | ARG | ILE | LEU | ||||
| 14 | THR | GLN | PRO | HIS | PHE | MET | ALA | LEU | LEU | GLN | ||||
| 15 | THR | HIS | ASP | VAL | VAL | ALA | HIS | GLU | VAL | TYR | ||||
| 16 | SER | ASP | GLU | ALA | LEU | ARG | VAL | THR | PRO | PRO | ||||
| 17 | PRO | THR | SER | PRO |
Samples:
sample_1: construct 2 mM
sample_2: construct, [U-15N], 2 mM
sample_3: construct, [U-13C], 2 mM
sample_4: construct, [U-13C; U-15N], 2 mM; HEPES 20 mM; TCEP 0.5 mM
conditions_1: ionic strength: 20 mM; pH: 8; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H15N_HSQC | sample_1 | not available | conditions_1 |
| HNCO | sample_1 | not available | conditions_1 |
| HN(CO)CACB | sample_1 | not available | conditions_1 |
| HNCACB | sample_1 | not available | conditions_1 |
| CCCONH | sample_1 | not available | conditions_1 |
| HCCCONH | sample_1 | not available | conditions_1 |
| sample_1-NOESY-TROSY | sample_1 | not available | conditions_1 |
| 13C-NOESY-HSQC | sample_2 | not available | conditions_1 |
Software:
xwinnmr -
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts