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 18475

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

Data sets:
Data typeCount
13C chemical shifts208
15N chemical shifts68
1H chemical shifts462

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 2LTF
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