BMRB Entry 10124
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10124
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Title: Solution structure of the second PDZ domain of human membrane associated guanylate kinase inverted-2 (MAGI-2)
Deposition date: 2007-04-02 Original release date: 2008-09-02
Authors: Nameki, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.
Citation: Nameki, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the second PDZ domain of human membrane associated guanylate kinase inverted-2 (MAGI-2)" .
Assembly members:
PDZ domain, polymer, 96 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: cell free synthesis Vector: P021030-28
Entity Sequences (FASTA):
PDZ domain: GSSGSSGQAELMTLTIVKGA
QGFGFTIADSPTGQRVKQIL
DIQGCPGLCEGDLIVEINQQ
NVQNLSHTEVVDILKDCPIG
SETSLIIHRGSGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 366 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 614 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2) | 1 |
Entities:
Entity 1, MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2) 96 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | GLN | ALA | GLU | ||||
| 2 | LEU | MET | THR | LEU | THR | ILE | VAL | LYS | GLY | ALA | ||||
| 3 | GLN | GLY | PHE | GLY | PHE | THR | ILE | ALA | ASP | SER | ||||
| 4 | PRO | THR | GLY | GLN | ARG | VAL | LYS | GLN | ILE | LEU | ||||
| 5 | ASP | ILE | GLN | GLY | CYS | PRO | GLY | LEU | CYS | GLU | ||||
| 6 | GLY | ASP | LEU | ILE | VAL | GLU | ILE | ASN | GLN | GLN | ||||
| 7 | ASN | VAL | GLN | ASN | LEU | SER | HIS | THR | GLU | VAL | ||||
| 8 | VAL | ASP | ILE | LEU | LYS | ASP | CYS | PRO | ILE | GLY | ||||
| 9 | SER | GLU | THR | SER | LEU | ILE | ILE | HIS | ARG | GLY | ||||
| 10 | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: PDZ domain, [U-13C; U-15N], 1.3 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.811, Kobayashi, N. - data analysis
CYANA v1.0.7, Guntert, P. - structure solution
OPALp, Billeter, M., Guntert, P., Koradi, R. - refinement
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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