BMRB Entry 16949
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16949
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NMR-STAR v3 text file.
XML gzip file.
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All files associated with the entry
Citation: Wang, Xingsheng; Tash, Brian; M. Flanagan, John; Tian, Fang. "Protein Backbone Resonance Assignment Assisted with Predicted Local Structures" .
Assembly members:
PDZ3_of_ZO-1, polymer, 113 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: recombinant technology Host organism: Escherichia coli Vector: pET
Entity Sequences (FASTA):
PDZ3_of_ZO-1: GHMPNSTHEDGILRPSMKLV
KFRKGDSVGLRLAGGNDVGI
FVAGVLEDSPAAKEGLEEGD
QILRVNNVDFTNIIREEAVL
FLLDLPKGEEVTILAQKKKD
VYRRIVESDVGDS
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 193 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 98 |
| residual dipolar couplings | 170 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ3_of_ZO-1 | 1 |
Entities:
Entity 1, PDZ3_of_ZO-1 113 residues - Formula weight is not available
| 1 | GLY | HIS | MET | PRO | ASN | SER | THR | HIS | GLU | ASP | ||||
| 2 | GLY | ILE | LEU | ARG | PRO | SER | MET | LYS | LEU | VAL | ||||
| 3 | LYS | PHE | ARG | LYS | GLY | ASP | SER | VAL | GLY | LEU | ||||
| 4 | ARG | LEU | ALA | GLY | GLY | ASN | ASP | VAL | GLY | ILE | ||||
| 5 | PHE | VAL | ALA | GLY | VAL | LEU | GLU | ASP | SER | PRO | ||||
| 6 | ALA | ALA | LYS | GLU | GLY | LEU | GLU | GLU | GLY | ASP | ||||
| 7 | GLN | ILE | LEU | ARG | VAL | ASN | ASN | VAL | ASP | PHE | ||||
| 8 | THR | ASN | ILE | ILE | ARG | GLU | GLU | ALA | VAL | LEU | ||||
| 9 | PHE | LEU | LEU | ASP | LEU | PRO | LYS | GLY | GLU | GLU | ||||
| 10 | VAL | THR | ILE | LEU | ALA | GLN | LYS | LYS | LYS | ASP | ||||
| 11 | VAL | TYR | ARG | ARG | ILE | VAL | GLU | SER | ASP | VAL | ||||
| 12 | GLY | ASP | SER |
Samples:
sample_1: PDZ3 of ZO-1, [U-100% 13C; U-100% 15N], 1 mM; PDZ3 of ZO-1, [U-100% 15N], 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA03274 |
| EMBL | CAC41969 CAC41992 CAH18091 |
| GB | ADB79761 KFO12263 KFP69448 KFP80555 KFW05584 |
| REF | XP_002825269 XP_005196258 XP_005196259 XP_005196260 XP_005196261 |
| TPG | DAA17567 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks