BMRB Entry 18081
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18081
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Title: Solution structure of Thermus thermophilus apo-CuA PubMed: 22645370
Deposition date: 2011-11-15 Original release date: 2012-06-19
Authors: Zaballa, Maria-Eugenia; Abriata, Luciano; Donaire, Antonio; Vila, Alejandro
Citation: Zaballa, Maria-Eugenia; Abriata, Luciano; Donaire, Antonio; Vila, Alejandro. "Flexibility of the metal-binding region in apo-cupredoxins." Proc. Natl. Acad. Sci. U.S.A. 109, 9254-9259 (2012).
Assembly members:
apoCuA_polypeptide, polymer, 126 residues, 13959.982 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):
apoCuA_polypeptide: MVIPAGKLERVDPTTVRQEG
PWADPAQAVVQTGPNQYTVY
VLAFAFGYQPNPIEVPQGAE
IVFKITSPDVIHGFHVEGTN
INVEVLPGEVSTVRYTFKRP
GEYRIICNQYCGLGHQNMFG
TIVVKE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 477 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 802 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | apoCuA_polypeptide | 1 |
Entities:
Entity 1, apoCuA_polypeptide 126 residues - 13959.982 Da.
| 1 | MET | VAL | ILE | PRO | ALA | GLY | LYS | LEU | GLU | ARG | ||||
| 2 | VAL | ASP | PRO | THR | THR | VAL | ARG | GLN | GLU | GLY | ||||
| 3 | PRO | TRP | ALA | ASP | PRO | ALA | GLN | ALA | VAL | VAL | ||||
| 4 | GLN | THR | GLY | PRO | ASN | GLN | TYR | THR | VAL | TYR | ||||
| 5 | VAL | LEU | ALA | PHE | ALA | PHE | GLY | TYR | GLN | PRO | ||||
| 6 | ASN | PRO | ILE | GLU | VAL | PRO | GLN | GLY | ALA | GLU | ||||
| 7 | ILE | VAL | PHE | LYS | ILE | THR | SER | PRO | ASP | VAL | ||||
| 8 | ILE | HIS | GLY | PHE | HIS | VAL | GLU | GLY | THR | ASN | ||||
| 9 | ILE | ASN | VAL | GLU | VAL | LEU | PRO | GLY | GLU | VAL | ||||
| 10 | SER | THR | VAL | ARG | TYR | THR | PHE | LYS | ARG | PRO | ||||
| 11 | GLY | GLU | TYR | ARG | ILE | ILE | CYS | ASN | GLN | TYR | ||||
| 12 | CYS | GLY | LEU | GLY | HIS | GLN | ASN | MET | PHE | GLY | ||||
| 13 | THR | ILE | VAL | VAL | LYS | GLU |
Samples:
sample_1: apoCuA_polypeptide, [U-99% 13C; U-99% 15N], 0.8 – 1.0 mM; potassium phosphate 100 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_2: apoCuA_polypeptide, [U-99% 15N], 0.8 – 1.0 mM; potassium phosphate 100 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_3: apoCuA_polypeptide0.8 – 1.0 mM; potassium phosphate 100 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K
sample_conditions_3: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_3 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
UNIO v2.0.1, Torsten Hermann - data analysis, peak picking, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS+, Cornilescu, Delaglio and Bax - constraints calculation
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAD70957 |
| GB | AAB00369 AAS81115 AFH38826 |
| REF | WP_011173203 WP_014629505 YP_144400 |
| SP | P98052 Q5SJ80 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts