BMRB Entry 17475
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17475
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Title: Structural basis of p63a SAM domain mutants involved in AEC syndrome PubMed: 21615690
Deposition date: 2011-02-18 Original release date: 2011-06-01
Authors: Sathyamurthy, A.; Freund, S.; Johnson, C.; Allen, Mark
Citation: Sathyamurthy, Aruna; Freund, Stefan; Johnson, Christopher; Allen, Mark; Bycroft, Mark. "Structural basis of p63 SAM domain mutants involved in AEC syndrome." FEBS J. 278, 2680-2688 (2011).
Assembly members:
TUMOR_PROTEIN_63, polymer, 82 residues, 9321.517 Da.
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
Entity Sequences (FASTA):
TUMOR_PROTEIN_63: GSYPTDCSIVSFLARLGCSS
CLDYFTTQGLTTIYQIEHYS
MDDLASLKIPEQFRHAIWKG
ILDHRQLHEFSSPSHLLRTP
SS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 157 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 340 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TUMOR PROTEIN 63 | 1 |
Entities:
Entity 1, TUMOR PROTEIN 63 82 residues - 9321.517 Da.
| 1 | GLY | SER | TYR | PRO | THR | ASP | CYS | SER | ILE | VAL | ||||
| 2 | SER | PHE | LEU | ALA | ARG | LEU | GLY | CYS | SER | SER | ||||
| 3 | CYS | LEU | ASP | TYR | PHE | THR | THR | GLN | GLY | LEU | ||||
| 4 | THR | THR | ILE | TYR | GLN | ILE | GLU | HIS | TYR | SER | ||||
| 5 | MET | ASP | ASP | LEU | ALA | SER | LEU | LYS | ILE | PRO | ||||
| 6 | GLU | GLN | PHE | ARG | HIS | ALA | ILE | TRP | LYS | GLY | ||||
| 7 | ILE | LEU | ASP | HIS | ARG | GLN | LEU | HIS | GLU | PHE | ||||
| 8 | SER | SER | PRO | SER | HIS | LEU | LEU | ARG | THR | PRO | ||||
| 9 | SER | SER |
Samples:
sample_1: TUMOR PROTEIN 63, [U-13C; U-15N], 1.5 mM; NaCl 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150.000 mM; pH: 6.500; pressure: 1 atm; temperature: 298.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H NOESY | sample_1 | solution | sample_conditions_1 |
| 2D TOCSY | sample_1 | solution | sample_conditions_1 |
| DQF COSY | sample_1 | solution | sample_conditions_1 |
| HSQC (13C and 15N) | sample_1 | solution | sample_conditions_1 |
| 3D HNCACB | sample_1 | solution | sample_conditions_1 |
| CBCACONH | sample_1 | solution | sample_conditions_1 |
| CCCONH | sample_1 | solution | sample_conditions_1 |
| HNCACO | sample_1 | solution | sample_conditions_1 |
| HNCO | sample_1 | solution | sample_conditions_1 |
| HNHB | sample_1 | solution | sample_conditions_1 |
Software:
Ansig3.3 vany, Kraulis -
AutoDep v4.3, PDBe -
CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read -
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
| UNP | P63_HUMAN |
| PDB | |
| DBJ | BAA32432 BAA32433 BAA32593 BAB20591 BAE23286 |
| EMBL | CAA76562 CAB88216 CAC37098 CAC37099 |
| GB | AAC43038 AAC62635 AAC62636 AAC62641 AAC62644 |
| REF | NP_001108452 NP_001120731 NP_001120736 NP_001120814 NP_003713 |
| SP | O88898 Q9H3D4 Q9JJP6 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts