BMRB Entry 25612
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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/BMR25612
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Title: Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358
Deposition date: 2015-05-14 Original release date: 2015-09-14
Authors: Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano
Citation: Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358" To be published ., .-..
Assembly members:
OR358, polymer, 77 residues, 8898.169 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):
OR358: MVDLKIDVSDDEEAEKIIRE
IREQWPKATVTRTNGDIKLD
AQTEKEAEKMEKAVKKVKPN
ATIRKTGGSLEHHHHHH
- assigned_chemical_shifts
- RDCs
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 306 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 508 |
| residual dipolar couplings | 47 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR358 | 1 |
Entities:
Entity 1, OR358 77 residues - 8898.169 Da.
| 1 | MET | VAL | ASP | LEU | LYS | ILE | ASP | VAL | SER | ASP | ||||
| 2 | ASP | GLU | GLU | ALA | GLU | LYS | ILE | ILE | ARG | GLU | ||||
| 3 | ILE | ARG | GLU | GLN | TRP | PRO | LYS | ALA | THR | VAL | ||||
| 4 | THR | ARG | THR | ASN | GLY | ASP | ILE | LYS | LEU | ASP | ||||
| 5 | ALA | GLN | THR | GLU | LYS | GLU | ALA | GLU | LYS | MET | ||||
| 6 | GLU | LYS | ALA | VAL | LYS | LYS | VAL | LYS | PRO | ASN | ||||
| 7 | ALA | THR | ILE | ARG | LYS | THR | GLY | GLY | SER | LEU | ||||
| 8 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_NC5: OR358, [U-13C; U-15N], 0.787 mM; H20 90%; D20 10%
sample_RDC: OR358, [U-13C; U-15N], 0.787 mM; H20 90%; D20 10%
sample_NC: OR358, [U-13C; U-15N], 0.787 mM; H20 90%; D20 10%
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_NC5 | 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 CCH-TOCSY | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_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
AutoStructure 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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts