BMRB Entry 15804
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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/BMR15804
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Title: Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8
Deposition date: 2008-06-13 Original release date: 2008-06-23
Authors: Eletsky, Alexander; Sukumaran, Dinesh; Semesi, Anthony; Guido, Valerie; Yee, Adelinda; Arrowsmith, Cheryl; Szyperski, Thomas
Citation: Eletsky, Alexander; Sukumaran, Dinesh; Semesi, Anthony; Guido, Valerie; Yee, Adelinda; Arrowsmith, Cheryl; Szyperski, Thomas. "Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8" Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
TR8_protein, polymer, 153 residues, 17284.062 Da.
Natural source: Common Name: Methanobacterium thermoautotrophicum Taxonomy ID: 145262 Superkingdom: Archaea Kingdom: not available Genus/species: Methanobacterium thermoautotrophicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TR8_protein: MGSSHHHHHHSSGLVPRGSH
MWNDLAVYIIRCSGPGTRVV
EVGAGRFLYVSDYIRKHSKV
DLVLTDIKPSHGGIVRDDIT
SPRMEIYRGAALIYSIRPPA
EIHSSLMRVADAVGARLIIK
PLTGEDIVTERKMKLVNYGR
TYFYEYIAEVRSR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 613 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 989 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TR8_protein | 1 |
Entities:
Entity 1, TR8_protein 153 residues - 17284.062 Da.
20-residue N-terminal tag MGSSHHHHHHSSGLVPRGSH
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | TRP | ASN | ASP | LEU | ALA | VAL | TYR | ILE | ILE | ||||
| 4 | ARG | CYS | SER | GLY | PRO | GLY | THR | ARG | VAL | VAL | ||||
| 5 | GLU | VAL | GLY | ALA | GLY | ARG | PHE | LEU | TYR | VAL | ||||
| 6 | SER | ASP | TYR | ILE | ARG | LYS | HIS | SER | LYS | VAL | ||||
| 7 | ASP | LEU | VAL | LEU | THR | ASP | ILE | LYS | PRO | SER | ||||
| 8 | HIS | GLY | GLY | ILE | VAL | ARG | ASP | ASP | ILE | THR | ||||
| 9 | SER | PRO | ARG | MET | GLU | ILE | TYR | ARG | GLY | ALA | ||||
| 10 | ALA | LEU | ILE | TYR | SER | ILE | ARG | PRO | PRO | ALA | ||||
| 11 | GLU | ILE | HIS | SER | SER | LEU | MET | ARG | VAL | ALA | ||||
| 12 | ASP | ALA | VAL | GLY | ALA | ARG | LEU | ILE | ILE | LYS | ||||
| 13 | PRO | LEU | THR | GLY | GLU | ASP | ILE | VAL | THR | GLU | ||||
| 14 | ARG | LYS | MET | LYS | LEU | VAL | ASN | TYR | GLY | ARG | ||||
| 15 | THR | TYR | PHE | TYR | GLU | TYR | ILE | ALA | GLU | VAL | ||||
| 16 | ARG | SER | ARG |
Samples:
NC: TR8 protein, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM
NC5: TR8 protein, [U-5% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 450 mM; benzamidine 1 mM; DTT 10 mM
sample_conditions_NC: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
sample_conditions_NC5: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_NC |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_NC |
| 3D HNCO | NC | isotropic | sample_conditions_NC |
| 3D HNCACB | NC | isotropic | sample_conditions_NC |
| 3D HNCA | NC | isotropic | sample_conditions_NC |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_NC |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_NC |
| 3D 1H-15N,13Cali,13Caro NOESY | NC | isotropic | sample_conditions_NC |
| 3D HCCH-COSY aliphatic | NC | isotropic | sample_conditions_NC |
| 3D HCCH-TOCSY aliphatic | NC | isotropic | sample_conditions_NC |
| 3D HCCH-COSY aromatic | NC | isotropic | sample_conditions_NC |
| 2D 1H-13C HSQC methyl | NC5 | isotropic | sample_conditions_NC5 |
| 2D LR 1H-15N HSQC (His) | NC5 | isotropic | sample_conditions_NC5 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
VNMR v6.1C, Varian - collection
VNMRJ v2.1B, Varian - collection
PROSA v6.0.2, Guntert - processing
XEASY v1.3.13, Bartels et al. - data analysis
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CSI v2.0, Wishart and Sykes - data analysis
TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts