BMRB Entry 16967
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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/BMR16967
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Title: Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN PubMed: 22894835
Deposition date: 2010-06-01 Original release date: 2012-09-20
Authors: TERRIEN, Elouan; WOLFF, Nicolas; CORDIER, Florence; SIMENEL, Catherine; LAFON, Monique; DELEPIERRE, Muriel
Citation: Terrien, Elouan; Chaffotte, Alain; Lafage, Mireille; Khan, Zakir; Prehaud, Christophe; Cordier, Florence; Simenel, Catherine; Delepierre, Muriel; Buc, Henri; Lafon, Monique; Wolff, Nicolas. "Interference with the PTEN-MAST2 Interaction by a Viral Protein Leads to Cellular Relocalization of PTEN." Sci. Signal. 5, ra58-ra58 (2012).
Assembly members:
MAST2-PDZ, polymer, 96 residues, 10452.032 Da.
PTEN-C_Terminus, polymer, 13 residues, 1559.692 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):
MAST2-PDZ: GGSMRPPIIIHRAGKKYGFT
LRAIRVYMGDSDVYTVHHMV
WHVEDGGPASEAGLRQGDLI
THVNGEPVHGLVHTEVVELI
LKSGNKVAISTTPLEN
PTEN-C_Terminus: PFDEDQHTQITKV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 406 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 664 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 96 residues - 10452.032 Da.
Residue 1 is a non residue due to TEV cleavage site
| 1 | GLY | GLY | SER | MET | ARG | PRO | PRO | ILE | ILE | ILE | ||||
| 2 | HIS | ARG | ALA | GLY | LYS | LYS | TYR | GLY | PHE | THR | ||||
| 3 | LEU | ARG | ALA | ILE | ARG | VAL | TYR | MET | GLY | ASP | ||||
| 4 | SER | ASP | VAL | TYR | THR | VAL | HIS | HIS | MET | VAL | ||||
| 5 | TRP | HIS | VAL | GLU | ASP | GLY | GLY | PRO | ALA | SER | ||||
| 6 | GLU | ALA | GLY | LEU | ARG | GLN | GLY | ASP | LEU | ILE | ||||
| 7 | THR | HIS | VAL | ASN | GLY | GLU | PRO | VAL | HIS | GLY | ||||
| 8 | LEU | VAL | HIS | THR | GLU | VAL | VAL | GLU | LEU | ILE | ||||
| 9 | LEU | LYS | SER | GLY | ASN | LYS | VAL | ALA | ILE | SER | ||||
| 10 | THR | THR | PRO | LEU | GLU | ASN |
Entity 2, entity_2 13 residues - 1559.692 Da.
| 1 | PRO | PHE | ASP | GLU | ASP | GLN | HIS | THR | GLN | ILE | ||||
| 2 | THR | LYS | VAL |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.6 mM; entity_2 1.2 mM; Tris-HCL 50 mM; NaCl 150 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-selected/12C,14N-selected NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_15N-selected/12C,14N-selected NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ARIA v2.2, Linge, O, . - structure solution
VNMRJ, Varian - collection
TALOS, Cornilescu, Delaglio and Bax - data analysis
ProcheckNMR, Laskowski and MacArthur - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 15972 |
| PDB | |
| DBJ | BAA34527 BAB40778 |
| EMBL | CAD38775 |
| GB | AAH65499 EAX06948 EAX06949 EFB27522 EHB01606 |
| REF | NP_055927 XP_001105315 XP_002810932 XP_004025774 XP_004285802 |
| SP | Q6P0Q8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts