BMRB Entry 30399
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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/BMR30399
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Title: NMR-based structure of the FHA-2 domain from Mycobacterium tuberculosis ABC transporter Rv1747 PubMed: 29861345
Deposition date: 2018-01-30 Original release date: 2018-06-18
Authors: Heinkel, F.; Okon, M.; Gsponer, J.; McIntosh, L.
Citation: Heinkel, Florian; Shen, Leo; Richard-Greenblatt, Melissa; Okon, Mark; Bui, Jennifer; Gee, Christine; Gay, Laurie; Alber, Tom; Av-Gay, Yossef; Gsponer, Jorg; McIntosh, Lawrence. "Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747." Structure 26, 972-986 (2018).
Assembly members:
entity_1, polymer, 108 residues, 11602.129 Da.
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 83332 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GHMWNLATSMMKILRPGRLT
GELPPGAVRIGRANDNDIVI
PEVLASRHHATLVPTPGGTE
IRDNRSINGTFVNGARVDAA
LLHDGDVVTIGNIDLVFADG
TLARREEN
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 417 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 634 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 108 residues - 11602.129 Da.
| 1 | GLY | HIS | MET | TRP | ASN | LEU | ALA | THR | SER | MET | ||||
| 2 | MET | LYS | ILE | LEU | ARG | PRO | GLY | ARG | LEU | THR | ||||
| 3 | GLY | GLU | LEU | PRO | PRO | GLY | ALA | VAL | ARG | ILE | ||||
| 4 | GLY | ARG | ALA | ASN | ASP | ASN | ASP | ILE | VAL | ILE | ||||
| 5 | PRO | GLU | VAL | LEU | ALA | SER | ARG | HIS | HIS | ALA | ||||
| 6 | THR | LEU | VAL | PRO | THR | PRO | GLY | GLY | THR | GLU | ||||
| 7 | ILE | ARG | ASP | ASN | ARG | SER | ILE | ASN | GLY | THR | ||||
| 8 | PHE | VAL | ASN | GLY | ALA | ARG | VAL | ASP | ALA | ALA | ||||
| 9 | LEU | LEU | HIS | ASP | GLY | ASP | VAL | VAL | THR | ILE | ||||
| 10 | GLY | ASN | ILE | ASP | LEU | VAL | PHE | ALA | ASP | GLY | ||||
| 11 | THR | LEU | ALA | ARG | ARG | GLU | GLU | ASN |
Samples:
sample_1: Rv1747 FHA-2, [U-100% 13C; U-100% 15N], 300 uM; Sodium Phosphate 20 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRe, Ryu, Lim, Sung and Lee - refinement
NMR spectrometers:
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts