BMRB Entry 25067
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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/BMR25067
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Title: Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459
Deposition date: 2014-07-02 Original release date: 2014-09-15
Authors: Pulavarti, Surya VSRK; Kipnis, Yakov; Sukumaran, Dinesh; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Greg; Baker, David; Montelione, Gaetano; Szyperski, Thomas
Citation: Pulavarti, Surya VSRK; Kipnis, Yakov; Sukumaran, Dinesh; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Greg; Baker, David; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459" To be published ., .-..
Assembly members:
OR459, polymer, 117 residues, 13406.451 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
OR459: MAGKELRVEIKIDCGNDDKE
TTYDLYFSKAEEAKELLKKV
AEKAADKIKKQGCKRVKIRF
EKKGLDDDARKKAKKWALEV
ANKIANELGAKQSTTTTDGD
TFEVEVILELEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 782 |
| 13C chemical shifts | 486 |
| 15N chemical shifts | 104 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR459 | 1 |
Entities:
Entity 1, OR459 117 residues - 13406.451 Da.
| 1 | MET | ALA | GLY | LYS | GLU | LEU | ARG | VAL | GLU | ILE | ||||
| 2 | LYS | ILE | ASP | CYS | GLY | ASN | ASP | ASP | LYS | GLU | ||||
| 3 | THR | THR | TYR | ASP | LEU | TYR | PHE | SER | LYS | ALA | ||||
| 4 | GLU | GLU | ALA | LYS | GLU | LEU | LEU | LYS | LYS | VAL | ||||
| 5 | ALA | GLU | LYS | ALA | ALA | ASP | LYS | ILE | LYS | LYS | ||||
| 6 | GLN | GLY | CYS | LYS | ARG | VAL | LYS | ILE | ARG | PHE | ||||
| 7 | GLU | LYS | LYS | GLY | LEU | ASP | ASP | ASP | ALA | ARG | ||||
| 8 | LYS | LYS | ALA | LYS | LYS | TRP | ALA | LEU | GLU | VAL | ||||
| 9 | ALA | ASN | LYS | ILE | ALA | ASN | GLU | LEU | GLY | ALA | ||||
| 10 | LYS | GLN | SER | THR | THR | THR | THR | ASP | GLY | ASP | ||||
| 11 | THR | PHE | GLU | VAL | GLU | VAL | ILE | LEU | GLU | LEU | ||||
| 12 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: H2O 90 ± 0.005 %; D2O 10%; OR459.005, [U-13C,15N], 1.17 mM
sample_2: H2O 90%; D2O 10%; OR459.005, [5% 13C; U-15N], 1.17 mM
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| GFT-4,3d-hcch-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
CARA, Rochus Keller - Analysis
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts