BMRB Entry 30691
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30691
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Title: NMR Structure of C-terminal Domain of phi29 ATPase
Deposition date: 2019-11-21 Original release date: 2020-09-28
Authors: Mahler, B.; Mao, H.; Morais, M.
Citation: Mahler, B.; Bujalowski, P.; Mao, H.; Dill, E.; Choi, K.; Jardine, P.; Morais, M.. "NMR Solution Structure and Dynamics of the C-terminal Domain of a Viral dsDNA Packaging ATPase" . ., .-..
Assembly members:
entity_1, polymer, 119 residues, 14195.173 Da.
Natural source: Common Name: Bacillus phage phi29 Taxonomy ID: 10756 Superkingdom: Viruses Kingdom: not available Genus/species: Salasvirus Bacillus phage phi29
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MFIGDSQVFIEKRSKDSKFV
FSIVYNGFTLGVWVDVNQGL
MYIDTAHDPSTKNVYTLTTD
DLNENMMLITNYKNNYHLRK
LASAFMNGYLRFDNQVIRNI
AYELFRKMRIQLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 441 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 641 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 119 residues - 14195.173 Da.
| 1 | MET | PHE | ILE | GLY | ASP | SER | GLN | VAL | PHE | ILE | ||||
| 2 | GLU | LYS | ARG | SER | LYS | ASP | SER | LYS | PHE | VAL | ||||
| 3 | PHE | SER | ILE | VAL | TYR | ASN | GLY | PHE | THR | LEU | ||||
| 4 | GLY | VAL | TRP | VAL | ASP | VAL | ASN | GLN | GLY | LEU | ||||
| 5 | MET | TYR | ILE | ASP | THR | ALA | HIS | ASP | PRO | SER | ||||
| 6 | THR | LYS | ASN | VAL | TYR | THR | LEU | THR | THR | ASP | ||||
| 7 | ASP | LEU | ASN | GLU | ASN | MET | MET | LEU | ILE | THR | ||||
| 8 | ASN | TYR | LYS | ASN | ASN | TYR | HIS | LEU | ARG | LYS | ||||
| 9 | LEU | ALA | SER | ALA | PHE | MET | ASN | GLY | TYR | LEU | ||||
| 10 | ARG | PHE | ASP | ASN | GLN | VAL | ILE | ARG | ASN | ILE | ||||
| 11 | ALA | TYR | GLU | LEU | PHE | ARG | LYS | MET | ARG | ILE | ||||
| 12 | GLN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: protein, [U-15N], 1 uM; MES 50 mM
sample_2: protein, [U-13C], 1 uM; MES, [U-2H], 50 mM
sample_3: protein, U-15N, U-13C, 1 uM; MES 50 mM
sample_conditions_1: pH: 6.0; pressure: 1013 mbar; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-edited NOESY-HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 13C-editied NOESY-HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HSQC-NOESY-HSQC | sample_2 | isotropic | sample_conditions_1 |
| HD-exchange | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.2, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v9.2.0, Johnson, One Moon Scientific - data analysis
TALOS-N, Cornilescu, Delaglio and Bax - chemical shift calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE III 750 MHz
- 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