BMRB Entry 16029
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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/BMR16029
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Title: Solution NMR structure of ubiquitin-like domain of Arabidopsis thaliana protein At2g32350. Northeast Structural Genomics Consortium target AR3433A
Deposition date: 2008-11-11 Original release date: 2009-03-05
Authors: Eletsky, Alexander; Mills, Jeffrey; Sukumaran, Dinesh; Hua, Jia; Shastry, Ritu; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Everret, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Mills, Jeffrey; Sukumaran, Dinesh; Hua, Jia; Shastry, Ritu; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Everret, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of ubiquitin-like domain of Arabidopsis thaliana protein At2g32350." Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
ar3433a_protein, polymer, 94 residues, 11005.629 Da.
Natural source: Common Name: thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ar3433a_protein: MGHHHHHHSHAAVRKIHVTV
KFPSKQFTVEVDRTETVSSL
KDKIHIVENTPIKRMQLYYS
GIELADDYRNLNEYGITEFS
EIVVFLKSINRAKD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 381 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 627 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ar3433a_protein | 1 |
Entities:
Entity 1, ar3433a_protein 94 residues - 11005.629 Da.
Residues 1-10 represent a non-native affinity tag. This is a Ubiquitin-like domain (70-153) of At2g32350 protein
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | ALA | ALA | VAL | ARG | LYS | ILE | HIS | VAL | THR | VAL | ||||
| 3 | LYS | PHE | PRO | SER | LYS | GLN | PHE | THR | VAL | GLU | ||||
| 4 | VAL | ASP | ARG | THR | GLU | THR | VAL | SER | SER | LEU | ||||
| 5 | LYS | ASP | LYS | ILE | HIS | ILE | VAL | GLU | ASN | THR | ||||
| 6 | PRO | ILE | LYS | ARG | MET | GLN | LEU | TYR | TYR | SER | ||||
| 7 | GLY | ILE | GLU | LEU | ALA | ASP | ASP | TYR | ARG | ASN | ||||
| 8 | LEU | ASN | GLU | TYR | GLY | ILE | THR | GLU | PHE | SER | ||||
| 9 | GLU | ILE | VAL | VAL | PHE | LEU | LYS | SER | ILE | ASN | ||||
| 10 | ARG | ALA | LYS | ASP |
Samples:
NC: ar3433a protein, [U-100% 13C; U-100% 15N], 1.09 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; calcium cloride 5 mM; DTT 10 mM; sodium azide 0.02%; protease inhibitors 1 X; H2O 90%; D2O 10%
NC5: ar3433a protein, [U-5% 13C; U-100% 15N], 1.15 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; calcium cloride 5 mM; DTT 10 mM; sodium azide 0.02%; protease inhibitors 1 X; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 215 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (ali) | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC (ali) | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aro) | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY (ali) | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HCCH-COSY (aro) | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY (aro) | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N,13Cali,13Caro NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC (His) | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC (ali) | NC5 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
PROSA v6.0.2, Guntert - processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution, structure validation
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts