BMRB Entry 16900
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16900
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Title: MDM4 binds ligands via an induced fit mechanism in which disordered regions become structured PubMed: 20515689
Deposition date: 2010-04-23 Original release date: 2010-06-16
Authors: Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin
Citation: Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin. "MDM4 binds ligands via a mechanism in which disordered regions become structured." FEBS Lett. 584, 3035-3041 (2010).
Assembly members:
MDM4_N-terminal_domain, polymer, 102 residues, Formula weight is not available
p53_peptide, polymer, 11 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: pET28b
Entity Sequences (FASTA):
MDM4_N-terminal_domain: GSHMDSASRISPGQINQVRP
KLPLLKILHAAGAQGEMFTV
KEVMHYLGQYIMVKQLYDQQ
EQHMVYCGGDLLGELLGRQS
FSVKDPSPLYDMLRKNLVTL
AT
p53_peptide: ETFSDLWKLLP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MDM4 | 1 |
| 2 | p53 peptide | 2 |
Entities:
Entity 1, MDM4 102 residues - Formula weight is not available
| 1 | GLY | SER | HIS | MET | ASP | SER | ALA | SER | ARG | ILE | ||||
| 2 | SER | PRO | GLY | GLN | ILE | ASN | GLN | VAL | ARG | PRO | ||||
| 3 | LYS | LEU | PRO | LEU | LEU | LYS | ILE | LEU | HIS | ALA | ||||
| 4 | ALA | GLY | ALA | GLN | GLY | GLU | MET | PHE | THR | VAL | ||||
| 5 | LYS | GLU | VAL | MET | HIS | TYR | LEU | GLY | GLN | TYR | ||||
| 6 | ILE | MET | VAL | LYS | GLN | LEU | TYR | ASP | GLN | GLN | ||||
| 7 | GLU | GLN | HIS | MET | VAL | TYR | CYS | GLY | GLY | ASP | ||||
| 8 | LEU | LEU | GLY | GLU | LEU | LEU | GLY | ARG | GLN | SER | ||||
| 9 | PHE | SER | VAL | LYS | ASP | PRO | SER | PRO | LEU | TYR | ||||
| 10 | ASP | MET | LEU | ARG | LYS | ASN | LEU | VAL | THR | LEU | ||||
| 11 | ALA | THR |
Entity 2, p53 peptide 11 residues - Formula weight is not available
| 1 | GLU | THR | PHE | SER | ASP | LEU | TRP | LYS | LEU | LEU | ||||
| 2 | PRO |
Samples:
sample_1: MDM4 N-terminal domain, [U-100% 13C; U-100% 15N], 0.1 mM; p53 peptide 0.2 ± 0.1 mM; potassium chloride 100 mM; sodium azide 0.1%; BisTris 50 mM; TCEP 2 mM; EDTA 0.1 mM; H20 99%; DMSO 1%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CC)(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v1.5.5, Keller and Wuthrich - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16893 16894 |
| PDB | |
| DBJ | BAD96948 BAG64634 BAG65468 BAK62829 |
| EMBL | CAE45961 CAH18300 |
| GB | AAH67299 AAI05107 AAO13494 AGJ70143 AGZ93683 |
| REF | NP_001191100 NP_001265445 NP_001265447 NP_001267305 NP_002384 |
| SP | O15151 |
| AlphaFold | O15151 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts