BMRB Entry 50206
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50206
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Title: Backbone chemical shift assignments of the KIX:MLLMyb complex
Deposition date: 2020-02-26 Original release date: 2020-02-26
Authors: Langelaan, David; Brown, Alex; Smith, Steven
Citation: Langelaan, David; Lochhead, Marina; Brown, Alex; Lebrun, David; Smith, Steven. "Development of a high-affinity designer peptide to probe CBP/p300 transcriptional activation in health and disease" .
Assembly members:
entity_1, polymer, 88 residues, Formula weight is not available
entity_2, polymer, 58 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 Host organism: Escherichia coli Vector: pET 21
Entity Sequences (FASTA):
entity_1: MGVRKGWHEHVTQDLRSHLV
HKLVQAIFPTPDPAALKDRR
MENLVAYAKKVEGDMYESAN
SRDEYYHLLAEKIYKIQKEL
EEKRRSRL
entity_2: GSSDDGNILPSDIMDFVLKN
TPSMQALGESPESKEKRIKE
LELLLMSTENELKGQQAL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 408 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 137 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KIX | 1 |
| 2 | MLLMyb | 2 |
Entities:
Entity 1, KIX 88 residues - Formula weight is not available
| 1 | MET | GLY | VAL | ARG | LYS | GLY | TRP | HIS | GLU | HIS | ||||
| 2 | VAL | THR | GLN | ASP | LEU | ARG | SER | HIS | LEU | VAL | ||||
| 3 | HIS | LYS | LEU | VAL | GLN | ALA | ILE | PHE | PRO | THR | ||||
| 4 | PRO | ASP | PRO | ALA | ALA | LEU | LYS | ASP | ARG | ARG | ||||
| 5 | MET | GLU | ASN | LEU | VAL | ALA | TYR | ALA | LYS | LYS | ||||
| 6 | VAL | GLU | GLY | ASP | MET | TYR | GLU | SER | ALA | ASN | ||||
| 7 | SER | ARG | ASP | GLU | TYR | TYR | HIS | LEU | LEU | ALA | ||||
| 8 | GLU | LYS | ILE | TYR | LYS | ILE | GLN | LYS | GLU | LEU | ||||
| 9 | GLU | GLU | LYS | ARG | ARG | SER | ARG | LEU |
Entity 2, MLLMyb 58 residues - Formula weight is not available
| 1 | GLY | SER | SER | ASP | ASP | GLY | ASN | ILE | LEU | PRO | ||||
| 2 | SER | ASP | ILE | MET | ASP | PHE | VAL | LEU | LYS | ASN | ||||
| 3 | THR | PRO | SER | MET | GLN | ALA | LEU | GLY | GLU | SER | ||||
| 4 | PRO | GLU | SER | LYS | GLU | LYS | ARG | ILE | LYS | GLU | ||||
| 5 | LEU | GLU | LEU | LEU | LEU | MET | SER | THR | GLU | ASN | ||||
| 6 | GLU | LEU | LYS | GLY | GLN | GLN | ALA | LEU |
Samples:
sample_1: KIX, [U-99% 13C; U-99% 15N], 0.75 mM; MLLMyb 1 mM; MES 20 mM; D2O, [U-2H], 5%; beta-mercaptoethanol 1 mM
sample_2: KIX 1.2 mM; MLLMyb, [U-99% 13C; U-99% 15N], 1 mM; MES 20 mM; D2O, [U-2H], 5%; beta-mercaptoethanol 1 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
CcpNmr Analysis - chemical shift assignment
NMRPipe - processing
VNMRj - collection
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts