BMRB Entry 16559
Click here to enlarge.
PDB ID: 2kpl
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 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks