BMRB Entry 15039
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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/BMR15039
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Title: solution structure of ta0956 PubMed: 17634985
Deposition date: 2006-11-20 Original release date: 2007-10-16
Authors: Koo, Bon-Kyung; Jung, Jinwon; Jung, Hyunseob; Nam, Hyung Wook; Kim, Yu Sam; Yee, Adelinda; Arrowsmith, Cheryl; Lee, Weontae
Citation: Koo, Bon-Kyung; Jung, Jinwon; Jung, Hyunseob; Nam, Hyung Wook; Kim, Yu Sam; Yee, Adelinda; Lee, Weontae. "Solution structure of the hypothetical novel-fold protein TA0956 from Thermoplasma acidophilum" Proteins 69, 444-447 (2007).
Assembly members:
ta0956, polymer, 110 residues, 12574.589 Da.
Natural source: Common Name: Thermoplasma acidophilum Taxonomy ID: 2303 Superkingdom: Archaea Kingdom: not available Genus/species: Thermoplasma acidophilum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ta0956: MTLCAMYNISMAGSHPTTIC
VVMDRFLESFSELYDIIDEN
DTDVMMDFISRFARTDEIMP
EDKTVGFVVVNADKKLMSVS
FSDIDENMKKVIKATAEKFK
NKGFKVETDM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 303 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 695 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TA0956 | 1 |
Entities:
Entity 1, TA0956 110 residues - 12574.589 Da.
| 1 | MET | THR | LEU | CYS | ALA | MET | TYR | ASN | ILE | SER | |
| 2 | MET | ALA | GLY | SER | HIS | PRO | THR | THR | ILE | CYS | |
| 3 | VAL | VAL | MET | ASP | ARG | PHE | LEU | GLU | SER | PHE | |
| 4 | SER | GLU | LEU | TYR | ASP | ILE | ILE | ASP | GLU | ASN | |
| 5 | ASP | THR | ASP | VAL | MET | MET | ASP | PHE | ILE | SER | |
| 6 | ARG | PHE | ALA | ARG | THR | ASP | GLU | ILE | MET | PRO | |
| 7 | GLU | ASP | LYS | THR | VAL | GLY | PHE | VAL | VAL | VAL | |
| 8 | ASN | ALA | ASP | LYS | LYS | LEU | MET | SER | VAL | SER | |
| 9 | PHE | SER | ASP | ILE | ASP | GLU | ASN | MET | LYS | LYS | |
| 10 | VAL | ILE | LYS | ALA | THR | ALA | GLU | LYS | PHE | LYS | |
| 11 | ASN | LYS | GLY | PHE | LYS | VAL | GLU | THR | ASP | MET |
Samples:
sample_1: ta0956, [U-98% 13C; U-98% 15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.01 w/v; DSS 0.01 w/v
sample_2: ta0956, [U-98% 13C; U-98% 15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.01 w/v; DSS 0.01 w/v
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
CYANA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
xwinnmr, Bruker Biospin - collection
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker AMX 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts