BMRB Entry 30706
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30706
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Title: De novo designed Rossmann fold protein ROS2_49223
Deposition date: 2020-01-07 Original release date: 2020-08-14
Authors: Pan, X.; Zhang, Y.; Kelly, M.; Kortemme, T.
Citation: Pan, X.. "De novo designed Rossmann fold protein ROS2_49223" . ., .-..
Assembly members:
entity_1, polymer, 124 residues, 14153.302 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH
MTLFVLILSNDKKLIEEARK
MAEKANLILITVGDEEELKK
AIKKADDIAKKQNSSEAKIL
ILLEKPVSPEYEKKLQKYAD
AEVRVRTVTSPDEAKRWIKE
FSEE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 366 |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 737 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 124 residues - 14153.302 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | THR | LEU | PHE | VAL | LEU | ILE | LEU | SER | ASN | ||||
| 4 | ASP | LYS | LYS | LEU | ILE | GLU | GLU | ALA | ARG | LYS | ||||
| 5 | MET | ALA | GLU | LYS | ALA | ASN | LEU | ILE | LEU | ILE | ||||
| 6 | THR | VAL | GLY | ASP | GLU | GLU | GLU | LEU | LYS | LYS | ||||
| 7 | ALA | ILE | LYS | LYS | ALA | ASP | ASP | ILE | ALA | LYS | ||||
| 8 | LYS | GLN | ASN | SER | SER | GLU | ALA | LYS | ILE | LEU | ||||
| 9 | ILE | LEU | LEU | GLU | LYS | PRO | VAL | SER | PRO | GLU | ||||
| 10 | TYR | GLU | LYS | LYS | LEU | GLN | LYS | TYR | ALA | ASP | ||||
| 11 | ALA | GLU | VAL | ARG | VAL | ARG | THR | VAL | THR | SER | ||||
| 12 | PRO | ASP | GLU | ALA | LYS | ARG | TRP | ILE | LYS | GLU | ||||
| 13 | PHE | SER | GLU | GLU |
Samples:
sample_1: de novo protein RO2_25, [U-99% 13C; U-99% 15N], 0.76 mM; potassium phosphate monobasic 21.1 mM; sodium phosphate dibasic 28.9 mM
sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v4.0.6, Bruker Biospin - collection
NMRPipe v9.8, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking
ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker AVANCE 800 MHz
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts