BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34046

Title: NMR structure of the C-terminal domain of the Bacteriophage T5 decoration protein pb10   PubMed: 28165000

Deposition date: 2016-09-22 Original release date: 2017-07-26

Authors: Vernhes, E.; Gilquin, B.; Cuniasse, P.; Boulanger, P.; Zinn-justin, S.

Citation: Vernhes, Emeline; Renouard, Madalena; Gilquin, Bernard; Cuniasse, Philippe; Durand, Dominique; England, Patrick; Hoos, Sylviane; Huet, Alexis; Conway, James; Glukhov, Anatoly; Ksenzenko, Vladimir; Jacquet, Eric; Nhiri, Naima; Zinn-Justin, Sophie; Boulanger, Pascale. "High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid"  Sci. Rep. 7, 41662-41662 (2017).

Assembly members:
Decoration protein, polymer, 101 residues, 10339.291 Da.

Natural source:   Common Name: viruses   Taxonomy ID: 10726   Superkingdom: Viruses   Kingdom: not available   Genus/species: T5likevirus Enterobacteria phage T5

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Decoration protein: ALTLSKDLTASMSVEEGAAL TLSVTATGGTGPYTYAWTKD GSPIPDASGATYTKPTAAAE DAGSYKVTVTDSKQVSKDST TCAVTVNPTVPGGLEHHHHH H

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts91
1H chemical shifts581

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 101 residues - 10339.291 Da.

1   ALALEUTHRLEUSERLYSASPLEUTHRALA
2   SERMETSERVALGLUGLUGLYALAALALEU
3   THRLEUSERVALTHRALATHRGLYGLYTHR
4   GLYPROTYRTHRTYRALATRPTHRLYSASP
5   GLYSERPROILEPROASPALASERGLYALA
6   THRTYRTHRLYSPROTHRALAALAALAGLU
7   ASPALAGLYSERTYRLYSVALTHRVALTHR
8   ASPSERLYSGLNVALSERLYSASPSERTHR
9   THRCYSALAVALTHRVALASNPROTHRVAL
10   PROGLYGLYLEUGLUHISHISHISHISHIS
11   HIS

Samples:

sample_1: c72, [U-99% 13C; U-99% 15N], 200 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 25 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D TOCSY-NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(COCA)sample_1isotropicsample_conditions_1
3D HN(CA)NNHsample_1isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CcpNMR, CCPN - data analysis, peak picking

INCA, Savarin P., Zinn-Justin S., Gilquin B., 19,2001, J. Biomol NMR, pp. 49-62 - structure calculation

NMR spectrometers:

  • Bruker DRX(600) 600 MHz
  • Bruker DRX(700) 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts