BMRB Entry 30334
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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/BMR30334
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Title: H, 13C, and 15N Chemical Shift Assignments and structure of Thioredoxin from Mycobacterium thermoresistibile ATCC 19527 and NCTC 10409
Deposition date: 2017-08-17 Original release date: 2017-10-20
Authors: Tang, C.; Yang, F.; Varani, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID
Citation: Tang, C.; Yang, F.; Varani, G.. "1H, 13C, and 15N Chemical Shift Assignments and structure of Thioredoxin from Mycobacterium thermoresistibile ATCC 19527 and NCTC 10409" . ., .-..
Assembly members:
entity_1, polymer, 115 residues, 12508.391 Da.
Natural source: Common Name: Mycobacterium thermoresistibile Taxonomy ID: 1078020 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium thermoresistibile
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MAHHHHHHMSGTVTVTDSTF
KTDVLDSDTPVLVDFWADWC
GPCKMVAPVLEEIANEKSGT
LKVAKLDVDANPEAARDFQV
VSIPTMILFKGGTPVKRIVG
AKGKAALLREIEDAL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 443 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 672 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 115 residues - 12508.391 Da.
| 1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | MET | SER | ||||
| 2 | GLY | THR | VAL | THR | VAL | THR | ASP | SER | THR | PHE | ||||
| 3 | LYS | THR | ASP | VAL | LEU | ASP | SER | ASP | THR | PRO | ||||
| 4 | VAL | LEU | VAL | ASP | PHE | TRP | ALA | ASP | TRP | CYS | ||||
| 5 | GLY | PRO | CYS | LYS | MET | VAL | ALA | PRO | VAL | LEU | ||||
| 6 | GLU | GLU | ILE | ALA | ASN | GLU | LYS | SER | GLY | THR | ||||
| 7 | LEU | LYS | VAL | ALA | LYS | LEU | ASP | VAL | ASP | ALA | ||||
| 8 | ASN | PRO | GLU | ALA | ALA | ARG | ASP | PHE | GLN | VAL | ||||
| 9 | VAL | SER | ILE | PRO | THR | MET | ILE | LEU | PHE | LYS | ||||
| 10 | GLY | GLY | THR | PRO | VAL | LYS | ARG | ILE | VAL | GLY | ||||
| 11 | ALA | LYS | GLY | LYS | ALA | ALA | LEU | LEU | ARG | GLU | ||||
| 12 | ILE | GLU | ASP | ALA | LEU |
Samples:
sample_1: D20 10 % v/v; DTT 2 mM; Thioredoxin, [U-95% 13C; U-95% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 25 mM
sample_2: D2O 100 % v/v; DTT 2 mM; Thioredoxin, [U-95% 13C; U-95% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 25 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 Pa; 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_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
Analysis, CCPN - chemical shift assignment, peak picking, refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts