BMRB Entry 25025
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25025
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Title: Conformational Plasticity Surrounding the Active Site of NADH Oxidase from Thermus thermophilus PubMed: 25970557
Deposition date: 2014-06-17 Original release date: 2019-07-11
Authors: Mittermaier, Anthony; Miletti, Teresa; Levros, Louis-Charles; Di Trani, Justin
Citation: Miletti, Teresa; Di Trani, Justin; Levros, Louis-Charles; Mittermaier, Anthony. "Conformational plasticity surrounding the active site of NADH oxidase from Thermus thermophilus" Protein Sci. 24, 1114-1128 (2015).
Assembly members:
NOX, polymer, 205 residues, Formula weight is not available
Natural source: Common Name: Bacteria Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTNADOX
Entity Sequences (FASTA):
NOX: MEATLPVLDAKTAALKRRSI
RRYRKDPVPEGLLREILEAA
LRAPSAWNLQPWRIVVVRDP
ATKRALREAAFGQAHVEEAP
VVLVLYADLEDALAHLDEVI
HPGVQGERREAQKQAIQRAF
AAMGQEARKAWASGQSYILL
GYLLLLLEAYGLGSVPMLGF
DPERVRAILGLPSRAAIPAL
VALGYPAEEGYPSHRLPLER
VVLWR
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
| Data type | Count |
| 13C chemical shifts | 464 |
| 15N chemical shifts | 165 |
| 1H chemical shifts | 165 |
| T1 relaxation values | 426 |
| T2 relaxation values | 426 |
| heteronuclear NOE values | 328 |
| order parameters | 216 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NOX, 1 | 1 |
| 2 | NOX, 2 | 1 |
Entities:
Entity 1, NOX, 1 205 residues - Formula weight is not available
| 1 | MET | GLU | ALA | THR | LEU | PRO | VAL | LEU | ASP | ALA | ||||
| 2 | LYS | THR | ALA | ALA | LEU | LYS | ARG | ARG | SER | ILE | ||||
| 3 | ARG | ARG | TYR | ARG | LYS | ASP | PRO | VAL | PRO | GLU | ||||
| 4 | GLY | LEU | LEU | ARG | GLU | ILE | LEU | GLU | ALA | ALA | ||||
| 5 | LEU | ARG | ALA | PRO | SER | ALA | TRP | ASN | LEU | GLN | ||||
| 6 | PRO | TRP | ARG | ILE | VAL | VAL | VAL | ARG | ASP | PRO | ||||
| 7 | ALA | THR | LYS | ARG | ALA | LEU | ARG | GLU | ALA | ALA | ||||
| 8 | PHE | GLY | GLN | ALA | HIS | VAL | GLU | GLU | ALA | PRO | ||||
| 9 | VAL | VAL | LEU | VAL | LEU | TYR | ALA | ASP | LEU | GLU | ||||
| 10 | ASP | ALA | LEU | ALA | HIS | LEU | ASP | GLU | VAL | ILE | ||||
| 11 | HIS | PRO | GLY | VAL | GLN | GLY | GLU | ARG | ARG | GLU | ||||
| 12 | ALA | GLN | LYS | GLN | ALA | ILE | GLN | ARG | ALA | PHE | ||||
| 13 | ALA | ALA | MET | GLY | GLN | GLU | ALA | ARG | LYS | ALA | ||||
| 14 | TRP | ALA | SER | GLY | GLN | SER | TYR | ILE | LEU | LEU | ||||
| 15 | GLY | TYR | LEU | LEU | LEU | LEU | LEU | GLU | ALA | TYR | ||||
| 16 | GLY | LEU | GLY | SER | VAL | PRO | MET | LEU | GLY | PHE | ||||
| 17 | ASP | PRO | GLU | ARG | VAL | ARG | ALA | ILE | LEU | GLY | ||||
| 18 | LEU | PRO | SER | ARG | ALA | ALA | ILE | PRO | ALA | LEU | ||||
| 19 | VAL | ALA | LEU | GLY | TYR | PRO | ALA | GLU | GLU | GLY | ||||
| 20 | TYR | PRO | SER | HIS | ARG | LEU | PRO | LEU | GLU | ARG | ||||
| 21 | VAL | VAL | LEU | TRP | ARG |
Samples:
15N_no_urea: NOX, [U-100% 15N], 1 mM; H2O 90%; D2O 10%
15N13C_no_urea: NOX, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
15N_urea: NOX, [U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | 15N13C_no_urea | isotropic | sample_conditions_1 |
| 3D HNCO | 15N13C_no_urea | isotropic | sample_conditions_1 |
| 3D HNCA | 15N13C_no_urea | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 15N13C_no_urea | isotropic | sample_conditions_1 |
| 3D HCACO | 15N13C_no_urea | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 15N13C_no_urea | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 15N13C_no_urea | isotropic | sample_conditions_1 |
| {1H}NOE | 15N_no_urea | isotropic | sample_conditions_1 |
| R1rho | 15N_no_urea | isotropic | sample_conditions_1 |
| R1 | 15N_no_urea | isotropic | sample_conditions_1 |
| {1H}NOE | 15N_no_urea | isotropic | sample_conditions_1 |
| R1rho | 15N_no_urea | isotropic | sample_conditions_1 |
| R1 | 15N_no_urea | isotropic | sample_conditions_1 |
| R1rho | 15N_urea | isotropic | sample_conditions_1 |
| R1 | 15N_urea | isotropic | sample_conditions_1 |
| {1H}NOE | 15N_urea | isotropic | sample_conditions_1 |
| R1rho | 15N_urea | isotropic | sample_conditions_1 |
| R1 | 15N_urea | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts