BMRB Entry 15944
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15944
MolProbity Validation Chart
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Title: Structural Basis for the Regulation of p53 Function by p300 PubMed: 19217391
Deposition date: 2008-09-08 Original release date: 2009-03-12
Authors: Bai, Yawen; Feng, Hanqiao; Jenkins, Lisa; Durell, Stewart; Wiodawer, Alex; Appella, Ettore
Citation: Feng, Hanqiao; Miller Jenkins, Lisa; Durell, Stewart; Hayashi, Ryo; Mazur, Sharlyn; Cherry, Scott; Tropea, Joseph; Miller, Maria; Wlodawer, Alexander; Appella, Ettore; Bai, Yawen. "Structural Basis for p300 Taz2-p53 TAD1 Binding and Modulation by Phosphorylation" Structure 17, 202-210 (2009).
Assembly members:
TAZ2, polymer, 90 residues, 9963.838 Da.
TAD(1-39), polymer, 39 residues, 4351.815 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):
TAZ2: ATQSPGDSRRLSIQRAIQSL
VHAAQCRNANCSLPSCQKMK
RVVQHTKGCKRKTNGGCPIC
KQLIALAAYHAKHCQENKCP
VPFCLNIKQK
TAD(1-39): MEEPQSDPSVEPPLSQETFS
DLWKLLPENNVLSPLPSQA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 506 |
15N chemical shifts | 111 |
1H chemical shifts | 751 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | TAZ2 | 1 |
2 | TAD(1-39) | 2 |
Entities:
Entity 1, TAZ2 90 residues - 9963.838 Da.
1-90 from p300(1723-1812)
1 | ALA | THR | GLN | SER | PRO | GLY | ASP | SER | ARG | ARG | |
2 | LEU | SER | ILE | GLN | ARG | ALA | ILE | GLN | SER | LEU | |
3 | VAL | HIS | ALA | ALA | GLN | CYS | ARG | ASN | ALA | ASN | |
4 | CYS | SER | LEU | PRO | SER | CYS | GLN | LYS | MET | LYS | |
5 | ARG | VAL | VAL | GLN | HIS | THR | LYS | GLY | CYS | LYS | |
6 | ARG | LYS | THR | ASN | GLY | GLY | CYS | PRO | ILE | CYS | |
7 | LYS | GLN | LEU | ILE | ALA | LEU | ALA | ALA | TYR | HIS | |
8 | ALA | LYS | HIS | CYS | GLN | GLU | ASN | LYS | CYS | PRO | |
9 | VAL | PRO | PHE | CYS | LEU | ASN | ILE | LYS | GLN | LYS |
Entity 2, TAD(1-39) 39 residues - 4351.815 Da.
1-39
1 | MET | GLU | GLU | PRO | GLN | SER | ASP | PRO | SER | VAL | ||||
2 | GLU | PRO | PRO | LEU | SER | GLN | GLU | THR | PHE | SER | ||||
3 | ASP | LEU | TRP | LYS | LEU | LEU | PRO | GLU | ASN | ASN | ||||
4 | VAL | LEU | SER | PRO | LEU | PRO | SER | GLN | ALA |
Samples:
p53cpx_3: TAZ2 1.1-1.2 mM; TAD(1-39), [U-100% 15N], 1.0-1.1 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM
TAZ2cpx_1: TAZ2, [U-100% 15N], 1.0-1.2 mM; TAD(1-39) 1.1-1.3 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM
TAZ2cpx_2: TAZ2, [U-100% 13C; U-100% 15N], 1.0-1.2 mM; TAD(1-39) 1.1-1.3 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM
TAZ2cpx_4: TAZ2 1.0-1.2 mM; TAD(1-39) 1.1-1.3 mM; MES 50 mM; NaCl 200 mM; ZnCl 0.1 mM; DTT 1 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6.3; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | TAZ2cpx_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | TAZ2cpx_4 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D HNCACB | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D HNCO | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D HNCA | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | TAZ2cpx_2 | isotropic | sample_conditions_1 |
3D HNHA | TAZ2cpx_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | TAZ2cpx_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | TAZ2cpx_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | p53cpx_3 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | p53cpx_3 | isotropic | sample_conditions_1 |
3D HNCACB | p53cpx_3 | isotropic | sample_conditions_1 |
3D HNCA | p53cpx_3 | isotropic | sample_conditions_1 |
3D HNCO | p53cpx_3 | isotropic | sample_conditions_1 |
3D HN(CA)CO | p53cpx_3 | isotropic | sample_conditions_1 |
3D H(CCO)NH | p53cpx_3 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | p53cpx_3 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | p53cpx_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | p53cpx_3 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe vupdated, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRView vupdated, Johnson, One Moon Scientific - chemical shift assignment
X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
TALOS vupdated, Cornilescu, Delaglio and Bax - structure solution
ProcheckNMR vupdated, Laskowski and MacArthur - structure validation
MolProbity v3.15, Richardson - structure validation
InsightII vupdated, Accelrys Software Inc. - figure preparation
SYBYL v8.0, Tripos - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker DRX 700 MHz
Related Database Links:
BMRB | 25484 17073 17760 18709 |
PDB | |
DBJ | BAC16799 BAG35463 BAG59884 BAG60244 BAI45431 |
EMBL | CAA26306 CAA34420 CAA38095 CAA42625 CAA42626 |
GB | AAA17994 AAA59987 AAA59988 AAA59989 AAA61211 |
PRF | 2006287A |
REF | NP_000537 NP_001040616 NP_001119584 NP_001119585 NP_001119586 |
SP | P04637 P13481 P56423 P56424 P61260 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts