BMRB Entry 25062
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25062
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Title: Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR462
Deposition date: 2014-07-01 Original release date: 2014-07-25
Authors: Xu, Xianzhong; Nivon, Lucas; Federizon, Jasmin; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Gregory; Baker, David; Montelione, Gaetano; Szyperski, Thomas
Citation: Xu, Xianzhong; Nivon, Lucas; Federizon, Jasmin; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Gregory; Baker, David; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR462" To be published ., .-..
Assembly members:
OR462, polymer, 136 residues, 15713.062 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):
OR462: MGVVILVLTGDERIAEELRK
EVQKHDPNVKTVPTKDKEKV
KEEIEKARKQGRPIVVFVRG
GDDERAKDIAEYAQKEGLRV
IVIIVSQDEEALRKGYEDKK
KKGYDVYTSRNEDEAKKKLK
EALEKSGSLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 602 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 969 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR462 | 1 |
Entities:
Entity 1, OR462 136 residues - 15713.062 Da.
Residues 1-128 correspond to the De novo designed active lysine protein. Residues 129-136 represent a purification his-tag.
| 1 | MET | GLY | VAL | VAL | ILE | LEU | VAL | LEU | THR | GLY | ||||
| 2 | ASP | GLU | ARG | ILE | ALA | GLU | GLU | LEU | ARG | LYS | ||||
| 3 | GLU | VAL | GLN | LYS | HIS | ASP | PRO | ASN | VAL | LYS | ||||
| 4 | THR | VAL | PRO | THR | LYS | ASP | LYS | GLU | LYS | VAL | ||||
| 5 | LYS | GLU | GLU | ILE | GLU | LYS | ALA | ARG | LYS | GLN | ||||
| 6 | GLY | ARG | PRO | ILE | VAL | VAL | PHE | VAL | ARG | GLY | ||||
| 7 | GLY | ASP | ASP | GLU | ARG | ALA | LYS | ASP | ILE | ALA | ||||
| 8 | GLU | TYR | ALA | GLN | LYS | GLU | GLY | LEU | ARG | VAL | ||||
| 9 | ILE | VAL | ILE | ILE | VAL | SER | GLN | ASP | GLU | GLU | ||||
| 10 | ALA | LEU | ARG | LYS | GLY | TYR | GLU | ASP | LYS | LYS | ||||
| 11 | LYS | LYS | GLY | TYR | ASP | VAL | TYR | THR | SER | ARG | ||||
| 12 | ASN | GLU | ASP | GLU | ALA | LYS | LYS | LYS | LEU | LYS | ||||
| 13 | GLU | ALA | LEU | GLU | LYS | SER | GLY | SER | LEU | GLU | ||||
| 14 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC5: OR462, [U-13C; U-15N], 1.2 mM
NC: OR462, [U-13C; U-15N], 1.2 mM
sample_conditions_1: pH: 7.5; 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 aromatic | 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 simultaneous Cali,Caro, and N NOESY | NC | isotropic | sample_conditions_1 |
| CCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D ct-1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D ct-1H-13C HSQC aromatic | NC | isotropic | sample_conditions_1 |
| GFT(4,3d) HCCHCOSY ali | NC | isotropic | sample_conditions_1 |
| gft(4,3d) HCCHCOSY caro | NC | isotropic | sample_conditions_1 |
| 2D ct-1H-13C HSQC aliphatic 28ms | NC5 | isotropic | sample_conditions_1 |
| 2D ct-1H-13C hsqc aliphatic 28ms | NC5 | isotropic | sample_conditions_1 |
| 2D ct-1H-13C hscq aliphatic 42ms | NC5 | isotropic | sample_conditions_1 |
| 2D cr-1H-13C hsqc aliphatic 56ms | NC5 | 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 v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
TALOSN, Shen, Cornilescu, Delaglio and Bax - geometry optimization
AS-DP v1.0, (AS-DP) Huang,Tejero,Powers, and Montelione - data analysis, structure solution
Cara v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking
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