BMRB Entry 18558
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18558
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Title: Solution NMR Structure de novo designed rossmann 2x2 fold protein, Northeast Structural Genomics Consortium (NESG) Target OR16 PubMed: 23135467
Deposition date: 2012-06-29 Original release date: 2012-07-31
Authors: Liu, Gaohua; Koga, Rie; Koga, Nobuyasu; Xiao, Rong; Pederson, Kari; Hamilton, Keith; Ciccosanti, Colleen; Acton, Thomas; 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:
OR16, polymer, 110 residues, 13078.123 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):
OR16: MLLYVLIISNDKKLIEEARK
MAEKANLELRTVKTEDELKK
YLEEFRKESQNIKVLILVSN
DEELDKAKELAQKMEIDVRT
RKVTSPDEAKRWIKEFSEEG
GSLEHHHHHH
- assigned_chemical_shifts
- RDCs
- spectral_peak_list
| Data type | Count |
| residual dipolar couplings | 170 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR16 | 1 |
Entities:
Entity 1, OR16 110 residues - 13078.123 Da.
| 1 | MET | LEU | LEU | TYR | VAL | LEU | ILE | ILE | SER | ASN | |
| 2 | ASP | LYS | LYS | LEU | ILE | GLU | GLU | ALA | ARG | LYS | |
| 3 | MET | ALA | GLU | LYS | ALA | ASN | LEU | GLU | LEU | ARG | |
| 4 | THR | VAL | LYS | THR | GLU | ASP | GLU | LEU | LYS | LYS | |
| 5 | TYR | LEU | GLU | GLU | PHE | ARG | LYS | GLU | SER | GLN | |
| 6 | ASN | ILE | LYS | VAL | LEU | ILE | LEU | VAL | SER | ASN | |
| 7 | ASP | GLU | GLU | LEU | ASP | LYS | ALA | LYS | GLU | LEU | |
| 8 | ALA | GLN | LYS | MET | GLU | ILE | ASP | VAL | ARG | THR | |
| 9 | ARG | LYS | VAL | THR | SER | PRO | ASP | GLU | ALA | LYS | |
| 10 | ARG | TRP | ILE | LYS | GLU | PHE | SER | GLU | GLU | GLY | |
| 11 | GLY | SER | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_NC: OR16.004, [U-100% 13C; U-100% 15N], 1.073 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM
sample_NC5: OR16.006, [U-100% 13C; U-100% 15N], 0.867 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM
sample_NC5_RDC: OR16.013, [U-100% 13C; U-100% 15N], 0.859 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM
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 C(CO)NH | 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 |
| 2D 1H-15N HSQC | sample_NC5_RDC | 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
PALES, PALES (Zweckstetter, Bax) - geometry optimization
REDCAT, Valafar, Prestegard - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 600 MHz