BMRB Entry 16357
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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/BMR16357
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Title: Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5
Deposition date: 2009-06-17 Original release date: 2009-07-07
Authors: Swapna, G.V.T.; Gunsalus, K.; Huang, Y.; Xiao, R.; Everett, J.; Acton, T.; Montelione, G.; NESG, NESG
Citation: Swapna, S.; Gunsalus, X.; Huang, L.; Xiao, G.; Everett, K.; Acton, A.; Montelione, G.. "Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5" To be Published ., .-..
Assembly members:
TR5, polymer, 106 residues, 11927.964 Da.
Natural source: Common Name: Methanothermobacter thermoautotrophicum Taxonomy ID: 145262 Superkingdom: Archaea Kingdom: not available Genus/species: Methanothermobacter thermoautotrophicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TR5: MVGRRPGGGLKDTKPVVVRL
YPDEIEALKSRVPANTSMSA
YIRRIILNHLEDEMVGRRPG
GGLKDTKPVVVRLYPDEIEA
LKSRVPANTSMSAYIRRIIL
NHLEDE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 434 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 750 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TR5 | 1 |
Entities:
Entity 1, TR5 106 residues - 11927.964 Da.
Chain B of the dimer has been numbered from 201-253 with the first residue M at 201.
| 1 | MET | VAL | GLY | ARG | ARG | PRO | GLY | GLY | GLY | LEU | ||||
| 2 | LYS | ASP | THR | LYS | PRO | VAL | VAL | VAL | ARG | LEU | ||||
| 3 | TYR | PRO | ASP | GLU | ILE | GLU | ALA | LEU | LYS | SER | ||||
| 4 | ARG | VAL | PRO | ALA | ASN | THR | SER | MET | SER | ALA | ||||
| 5 | TYR | ILE | ARG | ARG | ILE | ILE | LEU | ASN | HIS | LEU | ||||
| 6 | GLU | ASP | GLU | MET | VAL | GLY | ARG | ARG | PRO | GLY | ||||
| 7 | GLY | GLY | LEU | LYS | ASP | THR | LYS | PRO | VAL | VAL | ||||
| 8 | VAL | ARG | LEU | TYR | PRO | ASP | GLU | ILE | GLU | ALA | ||||
| 9 | LEU | LYS | SER | ARG | VAL | PRO | ALA | ASN | THR | SER | ||||
| 10 | MET | SER | ALA | TYR | ILE | ARG | ARG | ILE | ILE | LEU | ||||
| 11 | ASN | HIS | LEU | GLU | ASP | GLU |
Samples:
sample_1: TR5-1, [U-100% 13C; U-100% 15N], 0.4 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%
sample_2: TR5-2, [U-10% 13C; U-100% 15N], 0.95 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%
sample_3: TR5-3, [U-10% 13C; U-100% 15N] + unlabeled TR5 protein, 0.4 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K
sample_conditions_2: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K
sample_conditions_3: ionic strength: 0.300 M; pH: 6.5; pressure: 1 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D- X-filtered NOESY | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_2 |
| 2D HNOE | sample_2 | isotropic | sample_conditions_2 |
Software:
AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization
CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian Unity 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts