BMRB Entry 18561
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18561
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Title: Solution NMR Structure DE NOVO DESIGNED PFK fold PROTEIN, Northeast Structural Genomics Consortium (NESG) Target OR250 PubMed: 23135467
Deposition date: 2012-06-30 Original release date: 2012-07-10
Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Kohan, Eitan; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano
Citation: Koga, Nobuyasu; Tatsumi-Koga, Rie; Liu, Gaohua; Xiao, Rong; Acton, Thomas; Montelione, Gaetano; Baker, David. "Principles for designing ideal protein structures" Nature 491, 222-227 (2012).
Assembly members:
OR250, polymer, 112 residues, 12671.271 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):
OR250: MGKVLLVISTDTNIISSVQE
RAKHNYPGREIRTATSSQDI
RDIIKSMKDNGKPLVVFVNG
ASQNDVNEFQNEAKKEGVSY
DVLKSTDPEELTQRVREFLK
TAGSLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 455 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 748 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR250 | 1 |
Entities:
Entity 1, OR250 112 residues - 12671.271 Da.
| 1 | MET | GLY | LYS | VAL | LEU | LEU | VAL | ILE | SER | THR | ||||
| 2 | ASP | THR | ASN | ILE | ILE | SER | SER | VAL | GLN | GLU | ||||
| 3 | ARG | ALA | LYS | HIS | ASN | TYR | PRO | GLY | ARG | GLU | ||||
| 4 | ILE | ARG | THR | ALA | THR | SER | SER | GLN | ASP | ILE | ||||
| 5 | ARG | ASP | ILE | ILE | LYS | SER | MET | LYS | ASP | ASN | ||||
| 6 | GLY | LYS | PRO | LEU | VAL | VAL | PHE | VAL | ASN | GLY | ||||
| 7 | ALA | SER | GLN | ASN | ASP | VAL | ASN | GLU | PHE | GLN | ||||
| 8 | ASN | GLU | ALA | LYS | LYS | GLU | GLY | VAL | SER | TYR | ||||
| 9 | ASP | VAL | LEU | LYS | SER | THR | ASP | PRO | GLU | GLU | ||||
| 10 | LEU | THR | GLN | ARG | VAL | ARG | GLU | PHE | LEU | LYS | ||||
| 11 | THR | ALA | GLY | SER | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 12 | HIS | HIS |
Samples:
sample_NC: OR250.001, [U-100% 13C; U-100% 15N], 0.784 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM
sample_NC5: OR250.003, [U-100% 13C; U-100% 15N], 0.854 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_NC | isotropic | sample_conditions_1 |
| 3D HNCO | sample_NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_NC | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_NC | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_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
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis, chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts