BMRB Entry 18740
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18740
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Title: LMPG micelle-bound KSR1 CC-SAM PubMed: 23250398
Deposition date: 2012-09-25 Original release date: 2013-02-11
Authors: Koveal, Dorothy; Page, Rebecca; Peti, Wolfgang
Citation: Koveal, Dorothy; Schuh-Nuhfer, Natasha; Ritt, Daniel; Page, Rebecca; Morrison, Deborah; Peti, Wolfgang. "A CC-SAM, for coiled coil-sterile alpha motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane" Sci. Signal 5, ra94-ra94 (2012).
Assembly members:
KSR1_CC-SAM, polymer, 149 residues, Formula weight is not available
Natural source: Common Name: House mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
KSR1_CC-SAM: GHMDGGAGAAVSRALQQCGQ
LQKLIDISIGSLRGLRTKCS
VSNDLTQQEIRTLEAKLVKY
ICKQQQSKLSVTPSDRTAEL
NSYPRFSDWLYIFNVRPEVV
QEIPQELTLDALLEMDEAKA
KEMLRRWGASTEECSRLQQA
LTCLRKVTG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 136 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KSR1 CC-SAM | 1 |
Entities:
Entity 1, KSR1 CC-SAM 149 residues - Formula weight is not available
Residues G(22), H(23) and M(24) represent non-native residues that remain after cleavage of the N-terminal affinity tag.
| 1 | GLY | HIS | MET | ASP | GLY | GLY | ALA | GLY | ALA | ALA | ||||
| 2 | VAL | SER | ARG | ALA | LEU | GLN | GLN | CYS | GLY | GLN | ||||
| 3 | LEU | GLN | LYS | LEU | ILE | ASP | ILE | SER | ILE | GLY | ||||
| 4 | SER | LEU | ARG | GLY | LEU | ARG | THR | LYS | CYS | SER | ||||
| 5 | VAL | SER | ASN | ASP | LEU | THR | GLN | GLN | GLU | ILE | ||||
| 6 | ARG | THR | LEU | GLU | ALA | LYS | LEU | VAL | LYS | TYR | ||||
| 7 | ILE | CYS | LYS | GLN | GLN | GLN | SER | LYS | LEU | SER | ||||
| 8 | VAL | THR | PRO | SER | ASP | ARG | THR | ALA | GLU | LEU | ||||
| 9 | ASN | SER | TYR | PRO | ARG | PHE | SER | ASP | TRP | LEU | ||||
| 10 | TYR | ILE | PHE | ASN | VAL | ARG | PRO | GLU | VAL | VAL | ||||
| 11 | GLN | GLU | ILE | PRO | GLN | GLU | LEU | THR | LEU | ASP | ||||
| 12 | ALA | LEU | LEU | GLU | MET | ASP | GLU | ALA | LYS | ALA | ||||
| 13 | LYS | GLU | MET | LEU | ARG | ARG | TRP | GLY | ALA | SER | ||||
| 14 | THR | GLU | GLU | CYS | SER | ARG | LEU | GLN | GLN | ALA | ||||
| 15 | LEU | THR | CYS | LEU | ARG | LYS | VAL | THR | GLY |
Samples:
sample_1: KSR1 CC-SAM, [U-99% 13C; U-99% 15N; U-80% 2H], 0.4 mM; LMPG 300 mM; sodium chloride 100 mM; sodium phosphate 20 mM; TCEP 0.5 mM; TCEP 0.5 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 0.42 M; pH: 6.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TROSY NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.1, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 17045 17724 17725 |
| PDB | |
| EMBL | CAA57288 |
| GB | AAC52382 AAI68386 ABK42251 |
| REF | NP_038599 XP_006246986 XP_006246988 XP_006246989 XP_006532397 |
| SP | Q61097 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts