BMRB Entry 18437
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18437
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Title: Solution structure of gpFI C-terminal domain PubMed: 22801427
Deposition date: 2012-05-02 Original release date: 2012-07-23
Authors: Popovic, Ana; Wu, Bin; Edwards, Aled; Davidson, Alan; Maxwell, Karen
Citation: Popovic, Ana; Wu, Bin; Arrowsmith, Cheryl; Edwards, Aled; Davidson, Alan; Maxwell, Karen. "Structural and biochemical characterization of phage FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity." J. Biol. Chem. 287, 32085-32095 (2012).
Assembly members:
polypeptide, polymer, 61 residues, 6495.518 Da.
Natural source: Common Name: Enterobacteria phage lambda Taxonomy ID: 10710 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage lambda
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
polypeptide: PDTVILDTSELVTVVALVKL
HTDALHATRDEPVAFVLPGT
AFRVSAGVAAEMTERGLARM
Q
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 187 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 419 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | gpFI C-terminal domain | 1 |
Entities:
Entity 1, gpFI C-terminal domain 61 residues - 6495.518 Da.
| 1 | PRO | ASP | THR | VAL | ILE | LEU | ASP | THR | SER | GLU | ||||
| 2 | LEU | VAL | THR | VAL | VAL | ALA | LEU | VAL | LYS | LEU | ||||
| 3 | HIS | THR | ASP | ALA | LEU | HIS | ALA | THR | ARG | ASP | ||||
| 4 | GLU | PRO | VAL | ALA | PHE | VAL | LEU | PRO | GLY | THR | ||||
| 5 | ALA | PHE | ARG | VAL | SER | ALA | GLY | VAL | ALA | ALA | ||||
| 6 | GLU | MET | THR | GLU | ARG | GLY | LEU | ALA | ARG | MET | ||||
| 7 | GLN |
Samples:
sample_1: gpFI, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 25 mM; sodium chloride 250 mM; H2O 90 mM; D2O 10 mM
sample_2: gpFI, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; potassium chloride 250 mM; D2O 100%
sample_conditions_1: ionic strength: 250 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
software_2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA_2.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Varian INOVA 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAB35059 BAB35596 BAI29411 |
| EMBL | CAQ31255 CBG34515 CCP95075 CDK54019 CDK83941 |
| GB | AAA96541 AAG55986 ACF32390 ACI36443 ACI39211 |
| REF | NP_040588 NP_309663 NP_310200 WP_000158905 WP_000158906 |
| SP | P03709 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts