BMRB Entry 6128
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR6128
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Title: Structure of At3g01050.1, a ubiquitin-fold protein from Arabidopsis thaliana PubMed: 15782178
Deposition date: 2004-03-03 Original release date: 2004-05-15
Authors: Lytle, B.; Peterson, F.; Volkman, B.; Markley, J.
Citation: Vinarov, D.; Lytle, B.; Peterson, F.; Tyler, E.; Volkman, B.; Markley, J.. "Cell-free protein production and labeling protocol for NMR-based structural proteomics" Nat. Methods 1, 149-153 (2004).
Assembly members:
At3g01050.1, polymer, 126 residues, 12821 Da.
Natural source: Common Name: thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: cell free synthesis
Entity Sequences (FASTA):
At3g01050.1: MGHHHHHHLEAEVHNQLEIK
FRLTDGSDIGPKAFPDATTV
SALKETVISEWPREKENGPK
TVKEVKLISAGKVLENSKTV
KDYRSPVSNLAGAVTTMHVI
IQAPVTEKEKKPKGDPKMNK
CVCSVM
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 669 |
| 13C chemical shifts | 502 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | At3g01050.1 | 1 |
Entities:
Entity 1, At3g01050.1 126 residues - 12821 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | LEU | GLU | ||||
| 2 | ALA | GLU | VAL | HIS | ASN | GLN | LEU | GLU | ILE | LYS | ||||
| 3 | PHE | ARG | LEU | THR | ASP | GLY | SER | ASP | ILE | GLY | ||||
| 4 | PRO | LYS | ALA | PHE | PRO | ASP | ALA | THR | THR | VAL | ||||
| 5 | SER | ALA | LEU | LYS | GLU | THR | VAL | ILE | SER | GLU | ||||
| 6 | TRP | PRO | ARG | GLU | LYS | GLU | ASN | GLY | PRO | LYS | ||||
| 7 | THR | VAL | LYS | GLU | VAL | LYS | LEU | ILE | SER | ALA | ||||
| 8 | GLY | LYS | VAL | LEU | GLU | ASN | SER | LYS | THR | VAL | ||||
| 9 | LYS | ASP | TYR | ARG | SER | PRO | VAL | SER | ASN | LEU | ||||
| 10 | ALA | GLY | ALA | VAL | THR | THR | MET | HIS | VAL | ILE | ||||
| 11 | ILE | GLN | ALA | PRO | VAL | THR | GLU | LYS | GLU | LYS | ||||
| 12 | LYS | PRO | LYS | GLY | ASP | PRO | LYS | MET | ASN | LYS | ||||
| 13 | CYS | VAL | CYS | SER | VAL | MET |
Samples:
sample_1: At3g01050.1, [U-13C; U-15N], 0.5 mM; KCl 50 mM; phosphate buffer 10 mM; DTT 1 mM; H20 90%; D20 10%
sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 60 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | sample_1 | not available | sample_cond_1 |
| HNCA | sample_1 | not available | sample_cond_1 |
| HNCO | sample_1 | not available | sample_cond_1 |
| HN(CO)CA | sample_1 | not available | sample_cond_1 |
| HNCACB | sample_1 | not available | sample_cond_1 |
| HN(CA)CO | sample_1 | not available | sample_cond_1 |
| C(CO)NH | sample_1 | not available | sample_cond_1 |
| HCCH-TOCSY | sample_1 | not available | sample_cond_1 |
| 3D 15N-NOESY | sample_1 | not available | sample_cond_1 |
| 3D 13C-NOESY | sample_1 | not available | sample_cond_1 |
| 3D 13C-NOESY-aromatic | sample_1 | not available | sample_cond_1 |
| diffusion | sample_1 | not available | sample_cond_1 |
| N15 hetNOE | sample_1 | not available | sample_cond_1 |
Software:
XWINNMR v3.1 - collection
NMRPipe v2.1 - processing
XEASY v1.3.1 - analysis
SPSCAN v1.1.0 - peak picking
GARANT v2.1 - automated backbone assignments
TALOS - generation of torsion angle restraints
CYANA v1.0.6 - refinement (torsion angle dynamics)
XPLOR-NIH v2.0.6 - refinement (cartesian MD in explicit solvent)
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts