BMRB Entry 10214
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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/BMR10214
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Solution structure of the second WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1. MAGI-1 PubMed: 18562638
Deposition date: 2008-04-22 Original release date: 2009-04-04
Authors: Ohnishi, S.; Tochio, N.; Tomizawa, T.; Akasaka, R.; Harada, T.; Seki, E.; Sato, M.; Watanabe, S.; Fujikura, Y.; Koshiba, S.; Terada, T.; Shirouzu, M.; Tanaka, A.; Kigawa, T.; Yokoyama, S.
Citation: Ohnishi, S.; Tochio, N.; Tomizawa, T.; Akasaka, R.; Harada, T.; Seki, E.; Sato, M.; Watanabe, S.; Fujikura, Y.; Koshiba, S.; Terada, T.; Shirouzu, M.; Tanaka, A.; Kigawa, T.; Yokoyama, S.. "Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily." Protein Sci. 17, 1531-1541 (2008).
Assembly members:
WW domain, polymer, 60 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: P061024-05
Entity Sequences (FASTA):
WW domain: GSSGSSGLDSELELPAGWEK
IEDPVYGIYYVDHINRKTQY
ENPVLEAKRKKQLESGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 253 |
| 15N chemical shifts | 57 |
| 1H chemical shifts | 369 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | WW domain | 1 |
Entities:
Entity 1, WW domain 60 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | LEU | ASP | SER | |
| 2 | GLU | LEU | GLU | LEU | PRO | ALA | GLY | TRP | GLU | LYS | |
| 3 | ILE | GLU | ASP | PRO | VAL | TYR | GLY | ILE | TYR | TYR | |
| 4 | VAL | ASP | HIS | ILE | ASN | ARG | LYS | THR | GLN | TYR | |
| 5 | GLU | ASN | PRO | VAL | LEU | GLU | ALA | LYS | ARG | LYS | |
| 6 | LYS | GLN | LEU | GLU | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: WW domain, [U-13C; U-15N], 1.0 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02 mM; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 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 v3.5, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.9820, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA32002 BAD90296 BAE07184 BAE07185 BAE37498 |
| EMBL | CAH91366 |
| GB | AAB91995 AAC04844 AAH95943 AAI50821 AAI67863 |
| REF | NP_001025021 NP_001028229 NP_001076789 NP_001076790 NP_001125806 |
| SP | Q6RHR9 Q96QZ7 |
| TPG | DAA17112 |
| AlphaFold | Q96QZ7 Q6RHR9 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts