BMRB Entry 17304
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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/BMR17304
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Title: Solution NMR Structure of de novo designed rossmann 2x3 fold protein, Northeast Structural Genomics Consortium Target OR28
Deposition date: 2010-11-17 Original release date: 2010-12-16
Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Mao, Lei; Mao, binchen; Patel, Daya; ciccosanti, colleen; Hamilton, Keith; Acton, Thomas; Baker, David; Montelione, Gaetano
Citation: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Mao, Lei; Patel, Daya; ciccosanti, colleen; Hamilton, Keith; Mao, binchen; Acton, Thomas; Baker, David; Montelione, Gaetano. "Solution NMR structure of de novo designed rossmann 2x3 fold protein, Northeast Structural Genomics Consortium Target OR28" To be published ., .-..
Assembly members:
OR28, polymer, 134 residues, 15857.373 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):
OR28: MNIVIVVFSTDEETLRKFKD
IIKKNGFKVRTVRSPQELKD
SIEELVKKYNATIVVVVVDD
KEWAEKAIRFVKSLGAQVLI
IIYDQDQNRLEEFSREVRRR
GFEVRTVTSPDDFKKSLERL
IREVGSLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 481 |
| 15N chemical shifts | 132 |
| 1H chemical shifts | 975 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR28 | 1 |
Entities:
Entity 1, OR28 134 residues - 15857.373 Da.
| 1 | MET | ASN | ILE | VAL | ILE | VAL | VAL | PHE | SER | THR | ||||
| 2 | ASP | GLU | GLU | THR | LEU | ARG | LYS | PHE | LYS | ASP | ||||
| 3 | ILE | ILE | LYS | LYS | ASN | GLY | PHE | LYS | VAL | ARG | ||||
| 4 | THR | VAL | ARG | SER | PRO | GLN | GLU | LEU | LYS | ASP | ||||
| 5 | SER | ILE | GLU | GLU | LEU | VAL | LYS | LYS | TYR | ASN | ||||
| 6 | ALA | THR | ILE | VAL | VAL | VAL | VAL | VAL | ASP | ASP | ||||
| 7 | LYS | GLU | TRP | ALA | GLU | LYS | ALA | ILE | ARG | PHE | ||||
| 8 | VAL | LYS | SER | LEU | GLY | ALA | GLN | VAL | LEU | ILE | ||||
| 9 | ILE | ILE | TYR | ASP | GLN | ASP | GLN | ASN | ARG | LEU | ||||
| 10 | GLU | GLU | PHE | SER | ARG | GLU | VAL | ARG | ARG | ARG | ||||
| 11 | GLY | PHE | GLU | VAL | ARG | THR | VAL | THR | SER | PRO | ||||
| 12 | ASP | ASP | PHE | LYS | LYS | SER | LEU | GLU | ARG | LEU | ||||
| 13 | ILE | ARG | GLU | VAL | GLY | SER | LEU | GLU | HIS | HIS | ||||
| 14 | HIS | HIS | HIS | HIS |
Samples:
sample_NC: OR28, [U-100% 13C; U-100% 15N], 0.62 mM; H2O 95%; D2O 5%
sample_NC5: OR28, [U-5% 13C; U-100% 15N], 0.47 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 313 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 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
UBNMR v1.3, Yang Shen - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 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