BMRB Entry 5878
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5878
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Title: 1H, 13C and 15N NMR assignment of the region 1463-1617 of mouse p53 Binding Protein 1 (53BP1) PubMed: 14752266
Deposition date: 2003-07-22 Original release date: 2004-02-11
Authors: Charier, Gaelle; Alpha-Bazin, Beatrice; Couprie, Joel; Callebaut, Isabelle; Berenguer, Frederic; Quemeneur, Eric; Gilquin, Bernard; Zinn-Justin, Sophie
Citation: Charier, Gaelle; Alpha-Bazin, Beatrice; Couprie, Joel; Callebaut, Isabelle; Berenguer, Frederic; Quemeneur, Eric; Gilquin, Bernard; Zinn-Justin, Sophie. "Letter to the Editor: 1H, 13C and 15N resonance assignments of the region 1463-1617 of the mouse p53 Binding Protein 1 (53BP1) " J. Biomol. NMR 28, 303-304 (2004).
Assembly members:
p53 Binding Protein 1, polymer, 155 residues, 17345 Da.
Natural source: Common Name: 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):
p53 Binding Protein 1: DSSSSGNSFVGLRVVAKWSS
NGYFYSGKITRDVGAGKYKL
LFDDGYECDVLGKDILLCDP
IPLDTEVTALSEDEYFSAGV
VKGHRKESGELYYSIEKEGQ
RKWYKRMAVILSLEQGNRLR
EQYGLGPYEAVTPLTKAADI
SLDNLVEGKRKRRSN
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 1023 |
| 13C chemical shifts | 676 |
| 15N chemical shifts | 162 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | 53BP1 subunit 1 | 1 |
Entities:
Entity 1, 53BP1 subunit 1 155 residues - 17345 Da.
| 1 | ASP | SER | SER | SER | SER | GLY | ASN | SER | PHE | VAL | ||||
| 2 | GLY | LEU | ARG | VAL | VAL | ALA | LYS | TRP | SER | SER | ||||
| 3 | ASN | GLY | TYR | PHE | TYR | SER | GLY | LYS | ILE | THR | ||||
| 4 | ARG | ASP | VAL | GLY | ALA | GLY | LYS | TYR | LYS | LEU | ||||
| 5 | LEU | PHE | ASP | ASP | GLY | TYR | GLU | CYS | ASP | VAL | ||||
| 6 | LEU | GLY | LYS | ASP | ILE | LEU | LEU | CYS | ASP | PRO | ||||
| 7 | ILE | PRO | LEU | ASP | THR | GLU | VAL | THR | ALA | LEU | ||||
| 8 | SER | GLU | ASP | GLU | TYR | PHE | SER | ALA | GLY | VAL | ||||
| 9 | VAL | LYS | GLY | HIS | ARG | LYS | GLU | SER | GLY | GLU | ||||
| 10 | LEU | TYR | TYR | SER | ILE | GLU | LYS | GLU | GLY | GLN | ||||
| 11 | ARG | LYS | TRP | TYR | LYS | ARG | MET | ALA | VAL | ILE | ||||
| 12 | LEU | SER | LEU | GLU | GLN | GLY | ASN | ARG | LEU | ARG | ||||
| 13 | GLU | GLN | TYR | GLY | LEU | GLY | PRO | TYR | GLU | ALA | ||||
| 14 | VAL | THR | PRO | LEU | THR | LYS | ALA | ALA | ASP | ILE | ||||
| 15 | SER | LEU | ASP | ASN | LEU | VAL | GLU | GLY | LYS | ARG | ||||
| 16 | LYS | ARG | ARG | SER | ASN |
Samples:
sample_1: p53 Binding Protein 1, [U-95% 13C; U-95% 15N], 0.8 mM; Tris-HCl 50 mM; NaCl 150 mM; D2O 100%
sample_2: p53 Binding Protein 1, [U-95% 13C; U-95% 15N], 0.8 mM; Tris-HCl 50 mM; NaCl 150 mM; H2O 90%; D2O 10%
sample_3: p53 Binding Protein 1, [U-95% 15N], 0.7 mM; Tris-HCl 50 mM; NaCl 150 mM; H2O 90%; D2O 10%
condition_1: pH: 7.1; temperature: 300 K; ionic strength: 0.2 M
condition_2: pH*: 7.0; temperature: 300 K; ionic strength: 0.2 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | not available | not available | not available |
| HNCO | not available | not available | not available |
| HNCA | not available | not available | not available |
| HN(CO)CA | not available | not available | not available |
| CBCA(CO)NH | not available | not available | not available |
| CBCANH | not available | not available | not available |
| CBCACOHA | not available | not available | not available |
| HNHA | not available | not available | not available |
| (HCA)CO(CA)NH | not available | not available | not available |
| 15N HSQC NOESY | not available | not available | not available |
| HBHA(CO)NH | not available | not available | not available |
| HCCH TOSCY | not available | not available | not available |
| HCCH COSY | not available | not available | not available |
| 13C HSQC NOESY | not available | not available | not available |
Software:
NMRPipe v2.0 - data processing
FELIX v2000 - data analysis
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 600 MHz
Related Database Links:
| BMRB | 18579 25347 25348 |
| PDB | |
| DBJ | BAC26637 BAC29383 BAE06107 BAE21103 BAG10235 |
| EMBL | CAC94013 CAD97660 |
| GB | AAA21596 AAC62018 AAH35206 AAH79906 AAI12162 |
| REF | NP_001135451 NP_001135452 NP_001162434 NP_001193326 NP_001277759 |
| SP | P70399 Q12888 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts