BMRB Entry 16366
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16366
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Cort, John; Yee, Adelinda; Garcia, Maite; Isern, Nancy; Arrowsmith, Cheryl; Kennedy, Michael. "solution NMR structure of Themotoga maritima protein TM1076" .
Assembly members:
TM1076, polymer, 314 residues, 17614.3 Da.
Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p15Tv lic
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 621 |
| 15N chemical shifts | 133 |
| 1H chemical shifts | 991 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TM1076 | 1 |
Entities:
Entity 1, TM1076 314 residues - 17614.3 Da.
The protein construct used in the study contains a N-terminal His tag sequence MGSSHHHHHHSSGRENLYFQG before the sequence beginning with Val1 for which coordinates have been submitted
| 1 | VAL | LYS | ARG | PHE | LEU | LEU | ILE | SER | ASP | SER | ||||
| 2 | HIS | VAL | PRO | VAL | ARG | MET | ALA | SER | LEU | PRO | ||||
| 3 | ASP | GLU | ILE | LEU | ASN | SER | LEU | LYS | GLU | TYR | ||||
| 4 | ASP | GLY | VAL | ILE | GLY | LEU | GLY | ASP | TYR | VAL | ||||
| 5 | ASP | LEU | ASP | THR | VAL | ILE | LEU | LEU | GLU | LYS | ||||
| 6 | PHE | SER | LYS | GLU | PHE | TYR | GLY | VAL | HIS | GLY | ||||
| 7 | ASN | MET | ASP | TYR | PRO | ASP | VAL | LYS | GLU | HIS | ||||
| 8 | LEU | PRO | PHE | SER | LYS | VAL | LEU | LEU | VAL | GLU | ||||
| 9 | GLY | VAL | THR | ILE | GLY | MET | CYS | HIS | GLY | TRP | ||||
| 10 | GLY | ALA | PRO | TRP | ASP | LEU | LYS | ASP | ARG | LEU | ||||
| 11 | LEU | LYS | VAL | PHE | ASN | GLU | LYS | PRO | GLN | VAL | ||||
| 12 | ILE | LEU | PHE | GLY | HIS | THR | HIS | GLU | PRO | GLU | ||||
| 13 | ASP | THR | VAL | LYS | ALA | GLY | VAL | ARG | PHE | LEU | ||||
| 14 | ASN | PRO | GLY | SER | LEU | ALA | GLU | GLY | SER | TYR | ||||
| 15 | ALA | VAL | LEU | GLU | LEU | ASP | GLY | GLY | GLU | VAL | ||||
| 16 | ARG | PHE | GLU | LEU | LYS | THR | LEU | VAL | LYS | ARG | ||||
| 17 | PHE | LEU | LEU | ILE | SER | ASP | SER | HIS | VAL | PRO | ||||
| 18 | VAL | ARG | MET | ALA | SER | LEU | PRO | ASP | GLU | ILE | ||||
| 19 | LEU | ASN | SER | LEU | LYS | GLU | TYR | ASP | GLY | VAL | ||||
| 20 | ILE | GLY | LEU | GLY | ASP | TYR | VAL | ASP | LEU | ASP | ||||
| 21 | THR | VAL | ILE | LEU | LEU | GLU | LYS | PHE | SER | LYS | ||||
| 22 | GLU | PHE | TYR | GLY | VAL | HIS | GLY | ASN | MET | ASP | ||||
| 23 | TYR | PRO | ASP | VAL | LYS | GLU | HIS | LEU | PRO | PHE | ||||
| 24 | SER | LYS | VAL | LEU | LEU | VAL | GLU | GLY | VAL | THR | ||||
| 25 | ILE | GLY | MET | CYS | HIS | GLY | TRP | GLY | ALA | PRO | ||||
| 26 | TRP | ASP | LEU | LYS | ASP | ARG | LEU | LEU | LYS | VAL | ||||
| 27 | PHE | ASN | GLU | LYS | PRO | GLN | VAL | ILE | LEU | PHE | ||||
| 28 | GLY | HIS | THR | HIS | GLU | PRO | GLU | ASP | THR | VAL | ||||
| 29 | LYS | ALA | GLY | VAL | ARG | PHE | LEU | ASN | PRO | GLY | ||||
| 30 | SER | LEU | ALA | GLU | GLY | SER | TYR | ALA | VAL | LEU | ||||
| 31 | GLU | LEU | ASP | GLY | GLY | GLU | VAL | ARG | PHE | GLU | ||||
| 32 | LEU | LYS | THR | LEU |
Samples:
sample_3: TM1076, [U-99% 15N, 7% 13C, biosynthetically directed labeling of LV methyls], 0.6 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H2O 93%; D2O 7%
sample_1: TM1076, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H2O 93%; D2O 7%
sample_2: TM1076, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; D2O 100%
sample_conditions_1: ionic strength: 300 M; pH: 7; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
PSVS, Bhattacharya and Montelione - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB | |
| GB | AAD36153 ABQ47673 ACB10074 AGL50004 AHD19016 |
| REF | NP_228882 WP_008195716 WP_010865261 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks