BMRB Entry 34095
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34095
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Title: Structure Of P63 SAM Domain L514F Mutant Causative Of AEC Syndrome
Deposition date: 2017-02-08 Original release date: 2018-02-02
Authors: Rinnenthal, J.; Wuerz, J.; Osterburg, C.; Guentert, P.; Doetsch, V.
Citation: Rinnenthal, J.; Wuerz, J.; Osterburg, C.; Guentert, P.; Doetsch, V.. "Structure Of P63 SAM Domain L514F Mutant Causative For AEC Syndrome" . ., .-..
Assembly members:
entity_1, polymer, 70 residues, 7957.985 Da.
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):
entity_1: GPLGSTDCSIVSFFARLGCS
SCLDYFTTQGLTTIYQIEHY
SMDDLASLKIPEQFRHAIWK
GILDHRQLHD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 113 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 413 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 70 residues - 7957.985 Da.
| 1 | GLY | PRO | LEU | GLY | SER | THR | ASP | CYS | SER | ILE | |
| 2 | VAL | SER | PHE | PHE | ALA | ARG | LEU | GLY | CYS | SER | |
| 3 | SER | CYS | LEU | ASP | TYR | PHE | THR | THR | GLN | GLY | |
| 4 | LEU | THR | THR | ILE | TYR | GLN | ILE | GLU | HIS | TYR | |
| 5 | SER | MET | ASP | ASP | LEU | ALA | SER | LEU | LYS | ILE | |
| 6 | PRO | GLU | GLN | PHE | ARG | HIS | ALA | ILE | TRP | LYS | |
| 7 | GLY | ILE | LEU | ASP | HIS | ARG | GLN | LEU | HIS | ASP |
Samples:
sample_1: Tumor protein 63, [U-13C; U-15N], 350 uM; NaCl 100 mM; HEPES 20 mM
sample_2: Tumor protein 63 350 uM; NaCl 100 mM; HEPES 20 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA 3.97, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
CYANA 3.97 v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation
OPALp 1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
SPARKY, Goddard - chemical shift assignment, peak picking
TALOS+, Cornilescu, Delaglio and Bax - data analysis
xwinnmr, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts