BMRB Entry 18475
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18475
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Title: The solution structure of Phage P2 gpX PubMed: 24097944
Deposition date: 2012-05-22 Original release date: 2013-05-20
Authors: Maxwell, Karen; Bona, Diane; Chang, Tom; Edwards, Aled; Davidson, Alan
Citation: Maxwell, Karen; Fatehi Hassanabad, Mostafa; Chang, Tom; Pirani, Nawaz; Bona, Diane; Edwards, Aled; Davidson, Alan. "Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages." J. Bacteriol. 195, 5461-5468 (2013).
Assembly members:
P2_gpX, polymer, 71 residues, 7591.617 Da.
Natural source: Common Name: Bacteriophage P2 Taxonomy ID: 10679 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage P2
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
P2_gpX: MKTFALQGDTLDAICVRYYG
RTEGVVETVLAANPGLAELG
AVLPHGTAVELPDVQTAPVA
ETVNLWEVEHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 208 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 462 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | P2_gpX | 1 |
Entities:
Entity 1, P2_gpX 71 residues - 7591.617 Da.
| 1 | MET | LYS | THR | PHE | ALA | LEU | GLN | GLY | ASP | THR | ||||
| 2 | LEU | ASP | ALA | ILE | CYS | VAL | ARG | TYR | TYR | GLY | ||||
| 3 | ARG | THR | GLU | GLY | VAL | VAL | GLU | THR | VAL | LEU | ||||
| 4 | ALA | ALA | ASN | PRO | GLY | LEU | ALA | GLU | LEU | GLY | ||||
| 5 | ALA | VAL | LEU | PRO | HIS | GLY | THR | ALA | VAL | GLU | ||||
| 6 | LEU | PRO | ASP | VAL | GLN | THR | ALA | PRO | VAL | ALA | ||||
| 7 | GLU | THR | VAL | ASN | LEU | TRP | GLU | VAL | GLU | HIS | ||||
| 8 | HIS |
Samples:
sample_1: P2_gpX, [U-100% 13C; U-100% 15N], 1.1 mM; sodium phosphate 25 mM; sodium chloride 200 mM; DTT 2 mM; H2O 90%; D2O 10%
sample_2: P2 gpX, [U-100% 13C; U-100% 15N], 1.1 mM; sodium phosphate 25 mM; sodium chloride 200 mM; DTT 2 mM; D2O 100%
sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 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 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P. - refinement
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAP10043 BAT37380 BAT38781 GAL53203 |
| EMBL | CAC43076 CAC43081 CAC43090 CAC43095 CAC43100 |
| GB | AAD03274 AAN28225 AAO64727 AAP04444 ACB19449 |
| REF | NP_046763 NP_839856 WP_000846398 WP_000846399 WP_000846400 |
| SP | P51772 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts