BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18437

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

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts60
1H chemical shifts419

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1gpFI C-terminal domain1

Entities:

Entity 1, gpFI C-terminal domain 61 residues - 6495.518 Da.

1   PROASPTHRVALILELEUASPTHRSERGLU
2   LEUVALTHRVALVALALALEUVALLYSLEU
3   HISTHRASPALALEUHISALATHRARGASP
4   GLUPROVALALAPHEVALLEUPROGLYTHR
5   ALAPHEARGVALSERALAGLYVALALAALA
6   GLUMETTHRGLUARGGLYLEUALAARGMET
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_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