BMRB Entry 7226
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR7226
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Title: Solution NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A
Deposition date: 2006-07-14 Original release date: 2010-03-04
Authors: Liu, G.; Lin, Y.; Parish, D.; Shen, Y.; Sukumaran, D.; Yee, A.; Semesi, A.; Arrowsmith, C.; Szyperski, T.
Citation: Liu, G.; Lin, Y.; Parish, D.; Shen, Y.; Sukumaran, D.; Yee, A.; Semesi, A.; Arrowsmith, C.; Szyperski, T.. "Solution NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A" . ., .-..
Assembly members:
Conserved protein MTH1368, polymer, 125 residues, Formula weight is not available
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):
Conserved protein MTH1368: MGSSHHHHHHSSGRENLYFQ
GHQPDGVQIDSVVPGSPASK
VLTPGLVIESINGMPTSNLT
TYSAALKTISVGEVINITTD
QGTFHLKTGRNPNNSSRAYM
GIRTSNHLRVRDSVASVLGD
TLPFA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 341 |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 737 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Conserved protein MTH1368 | 1 |
Entities:
Entity 1, Conserved protein MTH1368 125 residues - Formula weight is not available
| 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 | GLN | PRO | ASP | GLY | VAL | GLN | ILE | ASP | ||||
| 4 | SER | VAL | VAL | PRO | GLY | SER | PRO | ALA | SER | LYS | ||||
| 5 | VAL | LEU | THR | PRO | GLY | LEU | VAL | ILE | GLU | SER | ||||
| 6 | ILE | ASN | GLY | MET | PRO | THR | SER | ASN | LEU | THR | ||||
| 7 | THR | TYR | SER | ALA | ALA | LEU | LYS | THR | ILE | SER | ||||
| 8 | VAL | GLY | GLU | VAL | ILE | ASN | ILE | THR | THR | ASP | ||||
| 9 | GLN | GLY | THR | PHE | HIS | LEU | LYS | THR | GLY | ARG | ||||
| 10 | ASN | PRO | ASN | ASN | SER | SER | ARG | ALA | TYR | MET | ||||
| 11 | GLY | ILE | ARG | THR | SER | ASN | HIS | LEU | ARG | VAL | ||||
| 12 | ARG | ASP | SER | VAL | ALA | SER | VAL | LEU | GLY | ASP | ||||
| 13 | THR | LEU | PRO | PHE | ALA |
Samples:
sample_1: Conserved protein MTH1368, [U-15N; U-13C], 0.5 mM; TRIS BUFFER mM; NaCl2 200 mM; ZnSO4 10 uM; NaN3 0.01%; bezamidine 1 mM; inhibitor 1 x; H2O 93%; D2O 7%
sample_cond_1: pH: 7.0; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY | sample_1 | not available | sample_cond_1 |
| 3D HNCACB | sample_1 | not available | sample_cond_1 |
| 3D CBCACONH | sample_1 | not available | sample_cond_1 |
| GFT (4,3)D HABCAB(CO)NHN | sample_1 | not available | sample_cond_1 |
| GFT (4,3)D HCCH | sample_1 | not available | sample_cond_1 |
Software:
VNMR v6.1C - collection
NMRPipe v2.3 - processing
AutoAssign v1.15.1 - data analysis
AutoStruct v2.0 - data analysis
CYANA v2.1 - structure solution
CNS v1.1 - refinement
NMR spectrometers:
- 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