BMRB Entry 15836
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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/BMR15836
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Title: Solution NMR structure of protein encoded by MTH693 from Methanobacterium thermoautotrophicum: Northeast Structural Genomics Consortium target tt824a
Deposition date: 2008-06-27 Original release date: 2008-08-19
Authors: Wu, Yibing; Singarapu, Kiran Kumar; Semesi, Anthony; Sukumaran, Dinesh; Yee, Adelinda; Garcia, Maite; Arrowsmith, Cheryl; Szyperski, Thomas
Citation: Wu, Yibing; Singarapu, Kiran Kumar; Semesi, Anthony; Sukumaran, Dinesh; Yee, Adelinda; Garcia, Maite; Arrowsmith, Cheryl; Szyperski, Thomas. "Solution NMR structure of protein encoded by MTH693 from Methanobacterium thermoautotrophicum: Northeast Structural Genomics Consortium target tt824a" Not known ., .-..
Assembly members:
tt824a, polymer, 101 residues, 10932.419 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):
tt824a: MGSSHHHHHHSSGRENLYFQ
GHMAARITGEPSKKAVSDRL
IGRKGVVMEAISPQNSGLVK
VDGETWRATSGTVLDVGEEV
SVKAIEGVKLVVEKLEEQKG
S
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 374 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 617 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | tt824a | 1 |
Entities:
Entity 1, tt824a 101 residues - 10932.419 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | ARG | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 3 | GLY | HIS | MET | ALA | ALA | ARG | ILE | THR | GLY | GLU | ||||
| 4 | PRO | SER | LYS | LYS | ALA | VAL | SER | ASP | ARG | LEU | ||||
| 5 | ILE | GLY | ARG | LYS | GLY | VAL | VAL | MET | GLU | ALA | ||||
| 6 | ILE | SER | PRO | GLN | ASN | SER | GLY | LEU | VAL | LYS | ||||
| 7 | VAL | ASP | GLY | GLU | THR | TRP | ARG | ALA | THR | SER | ||||
| 8 | GLY | THR | VAL | LEU | ASP | VAL | GLY | GLU | GLU | VAL | ||||
| 9 | SER | VAL | LYS | ALA | ILE | GLU | GLY | VAL | LYS | LEU | ||||
| 10 | VAL | VAL | GLU | LYS | LEU | GLU | GLU | GLN | LYS | GLY | ||||
| 11 | SER |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.7 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 298 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 |
| 4,3D, GFT HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| 4,3D, GFT CABCACONNH | sample_1 | isotropic | sample_conditions_1 |
| 4,3D, GFT HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D, 15N-13C RESOLVEDSIMULTANIOUS NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4,3D, GFT HAHB(CABCA)CONNH | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
XEASY, Bartels et al. - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Varian INOVA 750 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