BMRB Entry 34452
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34452
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Reconstructing the Origins of the HemD-like fold PubMed: 31724394
Deposition date: 2019-11-19 Original release date: 2019-11-22
Authors: Coles, M.; Toledo-Patino, S.; Chaubey, M.; Hocker, B.
Citation: Toledo-Patino, S.; Chaubey, M.; Coles, M.; Hoecker, B.. "Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor" Biochemistry ., .-. (2019).
Assembly members:
entity_1, polymer, 125 residues, 13651.649 Da.
Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MDPKVLIMRGEGGREFLAER
LRGQGVQVDYLPLDYPAGEL
LARVRAERLNGLVVSSGQGL
QNLYQLAAADWPEIGRLPLF
VPSPRVAEMARELGAQRVID
CRGASAPALLAALTSAALEH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 477 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 817 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 125 residues - 13651.649 Da.
| 1 | MET | ASP | PRO | LYS | VAL | LEU | ILE | MET | ARG | GLY | ||||
| 2 | GLU | GLY | GLY | ARG | GLU | PHE | LEU | ALA | GLU | ARG | ||||
| 3 | LEU | ARG | GLY | GLN | GLY | VAL | GLN | VAL | ASP | TYR | ||||
| 4 | LEU | PRO | LEU | ASP | TYR | PRO | ALA | GLY | GLU | LEU | ||||
| 5 | LEU | ALA | ARG | VAL | ARG | ALA | GLU | ARG | LEU | ASN | ||||
| 6 | GLY | LEU | VAL | VAL | SER | SER | GLY | GLN | GLY | LEU | ||||
| 7 | GLN | ASN | LEU | TYR | GLN | LEU | ALA | ALA | ALA | ASP | ||||
| 8 | TRP | PRO | GLU | ILE | GLY | ARG | LEU | PRO | LEU | PHE | ||||
| 9 | VAL | PRO | SER | PRO | ARG | VAL | ALA | GLU | MET | ALA | ||||
| 10 | ARG | GLU | LEU | GLY | ALA | GLN | ARG | VAL | ILE | ASP | ||||
| 11 | CYS | ARG | GLY | ALA | SER | ALA | PRO | ALA | LEU | LEU | ||||
| 12 | ALA | ALA | LEU | THR | SER | ALA | ALA | LEU | GLU | HIS | ||||
| 13 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: cU3Sd, [U-13C; U-15N], 29 mM
sample_conditions_1: ionic strength: 1 Not defined; pH: 8; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 |
Software:
TopSpin, Bruker Biospin - collection
Sparky, Goddard - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts