BMRB Entry 16559
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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/BMR16559
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Charbonier, Sebastian; Nomine, Yves; Ramirez, Juan; Luck, Katja; Chapelle, Anne; Stote, Roland; Trave, Gilles; Kieffer, Bruno; Atkinson, Robert. "The Structural and Dynamic Response of MAGI-1 PDZ1 with Noncanonical Domain Boundaries to the Binding of Human Papillomavirus E6" J. Mol. Biol. 406, 745-763 (2011).
PubMed: 21238461
Assembly members:
MAGI-1_PDZ1, polymer, 129 residues, 13871.942 Da.
E6CT, polymer, 11 residues, 1375.31 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 Vector: pETM-41
Entity Sequences (FASTA):
MAGI-1_PDZ1: GAMGKPFFTRNPSELKGKFI
HTKLRKSSRGFGFTVVGGDE
PDEFLQIKSLVLDGPAALDG
KMETGDVIVSVNDTCVLGHT
HAQVVKIFQSIPIGASVDLE
LCRGYPLPFDPDDPNTSLVT
SVAILDKEP
E6CT: RSSRTRRETQV
- assigned_chemical_shifts
- spectral_density_values
| Data type | Count |
| 13C chemical shifts | 481 |
| 15N chemical shifts | 105 |
| 1H chemical shifts | 835 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MAGI-1 PDZ1 | 1 |
| 2 | E6CT | 2 |
Entities:
Entity 1, MAGI-1 PDZ1 129 residues - 13871.942 Da.
| 1 | GLY | ALA | MET | GLY | LYS | PRO | PHE | PHE | THR | ARG | ||||
| 2 | ASN | PRO | SER | GLU | LEU | LYS | GLY | LYS | PHE | ILE | ||||
| 3 | HIS | THR | LYS | LEU | ARG | LYS | SER | SER | ARG | GLY | ||||
| 4 | PHE | GLY | PHE | THR | VAL | VAL | GLY | GLY | ASP | GLU | ||||
| 5 | PRO | ASP | GLU | PHE | LEU | GLN | ILE | LYS | SER | LEU | ||||
| 6 | VAL | LEU | ASP | GLY | PRO | ALA | ALA | LEU | ASP | GLY | ||||
| 7 | LYS | MET | GLU | THR | GLY | ASP | VAL | ILE | VAL | SER | ||||
| 8 | VAL | ASN | ASP | THR | CYS | VAL | LEU | GLY | HIS | THR | ||||
| 9 | HIS | ALA | GLN | VAL | VAL | LYS | ILE | PHE | GLN | SER | ||||
| 10 | ILE | PRO | ILE | GLY | ALA | SER | VAL | ASP | LEU | GLU | ||||
| 11 | LEU | CYS | ARG | GLY | TYR | PRO | LEU | PRO | PHE | ASP | ||||
| 12 | PRO | ASP | ASP | PRO | ASN | THR | SER | LEU | VAL | THR | ||||
| 13 | SER | VAL | ALA | ILE | LEU | ASP | LYS | GLU | PRO |
Entity 2, E6CT 11 residues - 1375.31 Da.
| 1 | ARG | SER | SER | ARG | THR | ARG | ARG | GLU | THR | GLN | ||||
| 2 | VAL |
Samples:
Unlabelled: MAGI-1 PDZ10.2 – 0.6 mM; sodium phosphate0.02 – 0.10 mM; sodium chloride 50 mM; DTT 2 mM; E6CT0.6 – 1.8 mM
15N: MAGI-1 PDZ1, [U-15N], 0.2 – 0.6 mM; sodium phosphate0.02 – 0.10 mM; sodium chloride 50 mM; DTT 2 mM; E6CT0.6 – 1.8 mM
13C-15N: MAGI-1 PDZ1, [U-100% 13C; U-100% 15N], 0.2 – 0.6 mM; sodium phosphate0.02 – 0.10 mM; sodium chloride 50 mM; DTT 2 mM; E6CT0.6 – 1.8 mM
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HN(CO)CA | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCA | 13C-15N | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCO | 13C-15N | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 13C-15N | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | 13C-15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 15N | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 15N | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | Unlabelled | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | Unlabelled | isotropic | sample_conditions_1 |
| 2D 15N T1 | 15N | isotropic | sample_conditions_1 |
| 2D 15N T2 | 15N | isotropic | sample_conditions_1 |
| 2D 1H-15N NOE | 15N | isotropic | sample_conditions_1 |
| 3D 12C-filtered 13C-edited NOESY | 13C-15N | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY vCARA, Bartels et al. - chemical shift assignment
ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks