BMRB Entry 16156
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16156
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Title: Solution Structure of the Coiled-coil Domain of Synphilin-1
Deposition date: 2009-02-02 Original release date: 2009-03-09
Authors: Xie, Yuanyuan; Zhou, Chenjie; Zhou, Ziren; Hu, Hongyu
Citation: Xie, Yuanyuan; Zhou, Chenjie; Zhou, Ziren; Hong, Jing; Lin, Donghai; Hu, Hongyu. "Solution Structure of the Coiled-coil Domain of Synphilin-1" Not known ., .-..
Assembly members:
Synphilin-1, polymer, 48 residues, 5371.191 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):
Synphilin-1: GSVETCMSLASQVVKLTKQL
KEQTVERVTLQNQLQQFLEA
QKSEGKSL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 174 |
| 15N chemical shifts | 46 |
| 1H chemical shifts | 271 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Synphilin-1 | 1 |
Entities:
Entity 1, Synphilin-1 48 residues - 5371.191 Da.
| 1 | GLY | SER | VAL | GLU | THR | CYS | MET | SER | LEU | ALA | ||||
| 2 | SER | GLN | VAL | VAL | LYS | LEU | THR | LYS | GLN | LEU | ||||
| 3 | LYS | GLU | GLN | THR | VAL | GLU | ARG | VAL | THR | LEU | ||||
| 4 | GLN | ASN | GLN | LEU | GLN | GLN | PHE | LEU | GLU | ALA | ||||
| 5 | GLN | LYS | SER | GLU | GLY | LYS | SER | LEU |
Samples:
sample_1: entity, [U-15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; H2O 90%
sample_2: entity, [U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; H2O 90%
sample_3: entity, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; H2O 90%
sample_conditions_1: pH: 6.0; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
ARIA, Linge, O, . - refinement, structure solution
ProcheckNMR, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA91791 BAD19017 BAD19018 BAG51060 BAH12894 |
| GB | AAD30362 AAG17478 AAH33743 AAH40552 AAH94759 |
| REF | NP_001229864 NP_001295029 NP_001295034 NP_001295035 NP_001295036 |
| SP | Q9Y6H5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts