BMRB Entry 17390
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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/BMR17390
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Title: Solution NMR Structure of de novo designed protein, P-loop NTPase fold, Northeast Structural Genomics Consortium Target OR32
Deposition date: 2010-12-31 Original release date: 2011-01-24
Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Tong, Saichu; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano
Citation: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Tong, Saichu; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target OR32" To be published ., .-..
Assembly members:
OR32, polymer, 162 residues, 19701.238 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):
OR32: MSQIFVVFSSDPEILKEIVR
EIKRQGVRVVLLYSDQDEKR
RRERLEEFEKQGVDVRTVED
KEDFRENIREIWERYPQLDV
VVIVTTDDKEWIKDFIEEAK
ERGVEVFVVYNNKDDDRRKE
AQQEFRSDGVDVRTVSDKEE
LIEQVRRFVRKVGSLEHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 584 |
| 15N chemical shifts | 173 |
| 1H chemical shifts | 1181 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR32 | 1 |
Entities:
Entity 1, OR32 162 residues - 19701.238 Da.
| 1 | MET | SER | GLN | ILE | PHE | VAL | VAL | PHE | SER | SER | ||||
| 2 | ASP | PRO | GLU | ILE | LEU | LYS | GLU | ILE | VAL | ARG | ||||
| 3 | GLU | ILE | LYS | ARG | GLN | GLY | VAL | ARG | VAL | VAL | ||||
| 4 | LEU | LEU | TYR | SER | ASP | GLN | ASP | GLU | LYS | ARG | ||||
| 5 | ARG | ARG | GLU | ARG | LEU | GLU | GLU | PHE | GLU | LYS | ||||
| 6 | GLN | GLY | VAL | ASP | VAL | ARG | THR | VAL | GLU | ASP | ||||
| 7 | LYS | GLU | ASP | PHE | ARG | GLU | ASN | ILE | ARG | GLU | ||||
| 8 | ILE | TRP | GLU | ARG | TYR | PRO | GLN | LEU | ASP | VAL | ||||
| 9 | VAL | VAL | ILE | VAL | THR | THR | ASP | ASP | LYS | GLU | ||||
| 10 | TRP | ILE | LYS | ASP | PHE | ILE | GLU | GLU | ALA | LYS | ||||
| 11 | GLU | ARG | GLY | VAL | GLU | VAL | PHE | VAL | VAL | TYR | ||||
| 12 | ASN | ASN | LYS | ASP | ASP | ASP | ARG | ARG | LYS | GLU | ||||
| 13 | ALA | GLN | GLN | GLU | PHE | ARG | SER | ASP | GLY | VAL | ||||
| 14 | ASP | VAL | ARG | THR | VAL | SER | ASP | LYS | GLU | GLU | ||||
| 15 | LEU | ILE | GLU | GLN | VAL | ARG | ARG | PHE | VAL | ARG | ||||
| 16 | LYS | VAL | GLY | SER | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 17 | HIS | HIS |
Samples:
sample_NC: OR32, [U-100% 13C; U-100% 15N], 1.06 mM; H2O 90%; D2O 10%
sample_NC5: OR32, [U-5% 13C; U-100% 15N], 0.85 mM; H2O 90%; D2O 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 |
| 2D 1H-15N HSQC | sample_NC5 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_NC | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_NC | 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
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
REDCAT, Valafar, Prestegard - 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