BMRB Entry 18372
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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/BMR18372
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Title: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR137
Deposition date: 2012-03-30 Original release date: 2012-05-01
Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Lee, Hsiau-Wei; Janjua, Haleema; Kohan, Eitan; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano
Citation: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Lee, Hsiau-Wei; Janjua, Haleema; Kohan, Eitan; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano. "SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR137" To be published ., .-..
Assembly members:
OR137, polymer, 134 residues, 16047.533 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):
OR137: MKELILINTNNDELIKKIKK
EVENQGYQVRDVNDSDELKK
EMKKLAEEKNFEKILIISND
KQLLKEMLELISKLGYKVFL
LLQDQDENELEEFKRKIESQ
GYEVRKVTDDEEALKIVREF
MQKAGSLEHHHHHH
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 612 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 1021 |
| residual dipolar couplings | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR137 | 1 |
Entities:
Entity 1, OR137 134 residues - 16047.533 Da.
| 1 | MET | LYS | GLU | LEU | ILE | LEU | ILE | ASN | THR | ASN | ||||
| 2 | ASN | ASP | GLU | LEU | ILE | LYS | LYS | ILE | LYS | LYS | ||||
| 3 | GLU | VAL | GLU | ASN | GLN | GLY | TYR | GLN | VAL | ARG | ||||
| 4 | ASP | VAL | ASN | ASP | SER | ASP | GLU | LEU | LYS | LYS | ||||
| 5 | GLU | MET | LYS | LYS | LEU | ALA | GLU | GLU | LYS | ASN | ||||
| 6 | PHE | GLU | LYS | ILE | LEU | ILE | ILE | SER | ASN | ASP | ||||
| 7 | LYS | GLN | LEU | LEU | LYS | GLU | MET | LEU | GLU | LEU | ||||
| 8 | ILE | SER | LYS | LEU | GLY | TYR | LYS | VAL | PHE | LEU | ||||
| 9 | LEU | LEU | GLN | ASP | GLN | ASP | GLU | ASN | GLU | LEU | ||||
| 10 | GLU | GLU | PHE | LYS | ARG | LYS | ILE | GLU | SER | GLN | ||||
| 11 | GLY | TYR | GLU | VAL | ARG | LYS | VAL | THR | ASP | ASP | ||||
| 12 | GLU | GLU | ALA | LEU | LYS | ILE | VAL | ARG | GLU | PHE | ||||
| 13 | MET | GLN | LYS | ALA | GLY | SER | LEU | GLU | HIS | HIS | ||||
| 14 | HIS | HIS | HIS | HIS |
Samples:
sample_NC: OR137.001, [U-100% 13C; U-100% 15N], 1.19418 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%
sample_NC5: OR137.006, [U-5% 13C; U-100% 15N], 1.19418 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 mM; H2O 90%; D2O 10%
sample_NC5_RDC: OR137.008, [U-5% 13C; U-100% 15N], 1.19418 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; Tris-HCl pH 7.5 10 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_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 |
| 2D 1H-13C HSQC | sample_NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_NC5_RDC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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
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