BMRB Entry 15687
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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/BMR15687
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Title: Automated NMR Structure of the TA0895 by FAPSY
Deposition date: 2008-03-21 Original release date: 2012-08-14
Authors: Lee, Woonghee; Jung, Jin-Won; Lee, Weontae
Citation: Lee, Woonghee; Jung, Jin-Won; Lee, Weontae. "The Automated Suite for Protein Structure Determination by NMR Spectroscopy" . ., .-..
Assembly members:
TA0895, polymer, 90 residues, 10231.843 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):
TA0895: MVTVRYYATLRPITKKKEET
FNGISKISELLERLKVEYGS
EFTKQMYDGNNLFKNVIILV
NGNNITSMKGLDTEIKDDDK
IDLFPPVAGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 273 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 530 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TA0895 | 1 |
Entities:
Entity 1, TA0895 90 residues - 10231.843 Da.
| 1 | MET | VAL | THR | VAL | ARG | TYR | TYR | ALA | THR | LEU | |
| 2 | ARG | PRO | ILE | THR | LYS | LYS | LYS | GLU | GLU | THR | |
| 3 | PHE | ASN | GLY | ILE | SER | LYS | ILE | SER | GLU | LEU | |
| 4 | LEU | GLU | ARG | LEU | LYS | VAL | GLU | TYR | GLY | SER | |
| 5 | GLU | PHE | THR | LYS | GLN | MET | TYR | ASP | GLY | ASN | |
| 6 | ASN | LEU | PHE | LYS | ASN | VAL | ILE | ILE | LEU | VAL | |
| 7 | ASN | GLY | ASN | ASN | ILE | THR | SER | MET | LYS | GLY | |
| 8 | LEU | ASP | THR | GLU | ILE | LYS | ASP | ASP | ASP | LYS | |
| 9 | ILE | ASP | LEU | PHE | PRO | PRO | VAL | ALA | GLY | GLY |
Samples:
sample_1: TA0895, [U-95% 13C; U-95% 15N], 1.5 mM
sample_conditions_1: ionic strength: 0.025 M; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P. - refinement
NMR spectrometers:
- Bruker DRX 500 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