BMRB Entry 5700
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5700
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Title: Backbone 1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein PubMed: 12815266
Deposition date: 2003-02-18 Original release date: 2003-03-21
Authors: Furrer, Julien; Enthart, Andreas; Dehner, Alexander; Klein, Christian; Hansen, Silke; Schwaiger, Manfred; Gemmecker, Gerd; Kessler, Horst
Citation: Furrer, Julien; Enthart, Andreas; Kuhlewein, Angelika; Dehner, Alexander; Klein, Christian; Hansen, Silke; Schwaiger, Manfred; Gemmecker, Gerd; Kessler, Horst. "Backbone 1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein" J. Biomol. NMR 26, 377-378 (2003).
Assembly members:
p63, polymer, 233 residues, 25832 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):
p63: GSSTFDALSPSPAIPSNTDY
PGPHSFDVSFQQSSTAKSAT
WTYSTELKKLYCQIAKTCPI
QIKVMTPPPQGAVIRAMPVY
KKAEHVTEVVKRCPNHELSR
EFNEGQIAPPSHLIRVEGNS
HAQYVEDPITGRQSVLVPYE
PPQVGTEFTTVLYNFMCNSS
CVGGMNRRPILIIVTLETRD
GQVLGRRCFEARICACPGRD
RKADEDSIRKQQVSDSTKNG
DAFRQNTHGIQMT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 608 |
| 15N chemical shifts | 200 |
| 1H chemical shifts | 370 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p63 DBD | 1 |
Entities:
Entity 1, p63 DBD 233 residues - 25832 Da.
| 1 | GLY | SER | SER | THR | PHE | ASP | ALA | LEU | SER | PRO | ||||
| 2 | SER | PRO | ALA | ILE | PRO | SER | ASN | THR | ASP | TYR | ||||
| 3 | PRO | GLY | PRO | HIS | SER | PHE | ASP | VAL | SER | PHE | ||||
| 4 | GLN | GLN | SER | SER | THR | ALA | LYS | SER | ALA | THR | ||||
| 5 | TRP | THR | TYR | SER | THR | GLU | LEU | LYS | LYS | LEU | ||||
| 6 | TYR | CYS | GLN | ILE | ALA | LYS | THR | CYS | PRO | ILE | ||||
| 7 | GLN | ILE | LYS | VAL | MET | THR | PRO | PRO | PRO | GLN | ||||
| 8 | GLY | ALA | VAL | ILE | ARG | ALA | MET | PRO | VAL | TYR | ||||
| 9 | LYS | LYS | ALA | GLU | HIS | VAL | THR | GLU | VAL | VAL | ||||
| 10 | LYS | ARG | CYS | PRO | ASN | HIS | GLU | LEU | SER | ARG | ||||
| 11 | GLU | PHE | ASN | GLU | GLY | GLN | ILE | ALA | PRO | PRO | ||||
| 12 | SER | HIS | LEU | ILE | ARG | VAL | GLU | GLY | ASN | SER | ||||
| 13 | HIS | ALA | GLN | TYR | VAL | GLU | ASP | PRO | ILE | THR | ||||
| 14 | GLY | ARG | GLN | SER | VAL | LEU | VAL | PRO | TYR | GLU | ||||
| 15 | PRO | PRO | GLN | VAL | GLY | THR | GLU | PHE | THR | THR | ||||
| 16 | VAL | LEU | TYR | ASN | PHE | MET | CYS | ASN | SER | SER | ||||
| 17 | CYS | VAL | GLY | GLY | MET | ASN | ARG | ARG | PRO | ILE | ||||
| 18 | LEU | ILE | ILE | VAL | THR | LEU | GLU | THR | ARG | ASP | ||||
| 19 | GLY | GLN | VAL | LEU | GLY | ARG | ARG | CYS | PHE | GLU | ||||
| 20 | ALA | ARG | ILE | CYS | ALA | CYS | PRO | GLY | ARG | ASP | ||||
| 21 | ARG | LYS | ALA | ASP | GLU | ASP | SER | ILE | ARG | LYS | ||||
| 22 | GLN | GLN | VAL | SER | ASP | SER | THR | LYS | ASN | GLY | ||||
| 23 | ASP | ALA | PHE | ARG | GLN | ASN | THR | HIS | GLY | ILE | ||||
| 24 | GLN | MET | THR |
Samples:
sample_1: p63, [U-75% 2H; U-98% 13C; U-98% 15N], 0.7 mM
sample_2: p63, [U-98% 15N], 0.7 mM
Ex_cond_1: pH: 6.8; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H,15N HSQC | not available | not available | Ex_cond_1 |
| HNHA | not available | not available | Ex_cond_1 |
| 1H,15N HSQC-TOCSY | not available | not available | Ex_cond_1 |
| 1H,15N HSQC-NOESY | not available | not available | Ex_cond_1 |
| 1H,15N HSQC-NOESY-1H,15N HSQC | not available | not available | Ex_cond_1 |
| HNCO | not available | not available | Ex_cond_1 |
| tr-HNCA | not available | not available | Ex_cond_1 |
| tr-HN(CA)CO | not available | not available | Ex_cond_1 |
| tr-HN(CO)CACB | not available | not available | Ex_cond_1 |
| tr-HNCACB | not available | not available | Ex_cond_1 |
Software:
xwinnmr v3.5 -
AURELIA v2.8.4 -
PASTA - automatic assignment program
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAA32432 BAA32433 BAA32592 BAA32593 BAB20631 |
| EMBL | CAA76562 CAB88216 CAC37098 CAC37099 CAC37100 |
| GB | AAC24830 AAC43038 AAC62633 AAC62634 AAC62635 |
| REF | NP_001079107 NP_001108450 NP_001108451 NP_001108452 NP_001108453 |
| SP | O88898 Q9H3D4 Q9JJP6 |
| TPG | DAA33389 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts