BMRB Entry 16520
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16520
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Title: Solution structure of humar Par-3b PDZ2 (residues 451-549) PubMed: 20073081
Deposition date: 2009-09-24 Original release date: 2010-01-28
Authors: Volkman, B.; Tyler, R.; Peterson, F.
Citation: Jensen, Davin; Woytovich, Christopher; Li, Margie; Duvnjak, Petar; Cassidy, Michael; Frederick, Ronnie; Bergeman, Lai; Peterson, Francis; Volkman, Brian. "Rapid, robotic, small-scale protein production for NMR screening and structure determination." Protein Sci. 19, 570-578 (2010).
Assembly members:
hPar-3_PDZ2, polymer, 121 residues, 13394.356 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):
hPar-3_PDZ2: MRGSHHHHHHHHGSENLYFQ
GSYNTKKIGKRLNIQLKKGT
EGLGFSITSRDVTIGGSAPI
YVKNILPRGAAIQDGRLKAG
DRLIEVNGVDLVGKSQEEVV
SLLRSTKMEGTVSLLVFRQE
D
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 393 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 616 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hPar3 PDZ2 | 1 |
Entities:
Entity 1, hPar3 PDZ2 121 residues - 13394.356 Da.
Residues 429-450 (MRGSHHHHHHHHGSENLYFQGS) are a octa-His tag that was not removed from the protein prior to structure determination.
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | HIS | HIS | GLY | SER | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 3 | GLY | SER | TYR | ASN | THR | LYS | LYS | ILE | GLY | LYS | ||||
| 4 | ARG | LEU | ASN | ILE | GLN | LEU | LYS | LYS | GLY | THR | ||||
| 5 | GLU | GLY | LEU | GLY | PHE | SER | ILE | THR | SER | ARG | ||||
| 6 | ASP | VAL | THR | ILE | GLY | GLY | SER | ALA | PRO | ILE | ||||
| 7 | TYR | VAL | LYS | ASN | ILE | LEU | PRO | ARG | GLY | ALA | ||||
| 8 | ALA | ILE | GLN | ASP | GLY | ARG | LEU | LYS | ALA | GLY | ||||
| 9 | ASP | ARG | LEU | ILE | GLU | VAL | ASN | GLY | VAL | ASP | ||||
| 10 | LEU | VAL | GLY | LYS | SER | GLN | GLU | GLU | VAL | VAL | ||||
| 11 | SER | LEU | LEU | ARG | SER | THR | LYS | MET | GLU | GLY | ||||
| 12 | THR | VAL | SER | LEU | LEU | VAL | PHE | ARG | GLN | GLU | ||||
| 13 | ASP |
Samples:
sample_1: hPar-3 PDZ2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%; sodium azide 0.02%
sample_conditions_1: ionic strength: 53 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY (AROMATIC) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
TOPSPIN v2.1, Bruker - collection
NMRPipe v2007, Delagio,F. et al. - processing
XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis
GARANT v2.1, C. Bartels - data analysis
CYANA v2.1, Guntert, P. - structural calculation
NMR spectrometers:
- Bruker Avance III 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts