BMRB Entry 16387
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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/BMR16387
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Title: Solution NMR Structure of denovo designed ferrodoxin fold like protein, Northeast Structural Genomics Consortium Target Target OR15 PubMed: 23135467
Deposition date: 2009-06-30 Original release date: 2009-08-06
Authors: Liu, G.; Koga, N.; Jiang, J.; Xiao, R.; Ciccosanti, C.; Locke, J; Everett, J.; Nair, R.; Acton, T; Rost, B; Baker, D; Montelione, G.
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:
OR15, polymer, 85 residues, 10066.570 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):
OR15: MEMDIRFRGDDLEAFEKALK
EMIRQARKFAGTVTYTLDGN
DLEIRITGVPEQVRKELAKE
AERLAKEFNITVTYTIRLEH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 349 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 597 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR15 | 1 |
Entities:
Entity 1, OR15 85 residues - 10066.570 Da.
| 1 | MET | GLU | MET | ASP | ILE | ARG | PHE | ARG | GLY | ASP | ||||
| 2 | ASP | LEU | GLU | ALA | PHE | GLU | LYS | ALA | LEU | LYS | ||||
| 3 | GLU | MET | ILE | ARG | GLN | ALA | ARG | LYS | PHE | ALA | ||||
| 4 | GLY | THR | VAL | THR | TYR | THR | LEU | ASP | GLY | ASN | ||||
| 5 | ASP | LEU | GLU | ILE | ARG | ILE | THR | GLY | VAL | PRO | ||||
| 6 | GLU | GLN | VAL | ARG | LYS | GLU | LEU | ALA | LYS | GLU | ||||
| 7 | ALA | GLU | ARG | LEU | ALA | LYS | GLU | PHE | ASN | ILE | ||||
| 8 | THR | VAL | THR | TYR | THR | ILE | ARG | LEU | GLU | HIS | ||||
| 9 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: OR15, [U-100% 13C; U-100% 15N], 0.47 mM
sample_conditions_1: pH: 6.5; pressure: 1.0 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaneous 1H, 15N, 13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, refinement, structure solution
AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
XEASY, Bartels et al. - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB |
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