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 34047

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

Deposition date: 2016-09-22 Original release date: 2017-04-13

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, 86 residues, 9758.273 Da.

Natural source:   Common Name: Escherichia phage T5   Taxonomy ID: 10726   Superkingdom: Viruses   Kingdom: not available   Genus/species: T5virus not available

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

Entity Sequences (FASTA):
Decoration protein: MGIDYSGLRTIFGEKLPESH IFFATVAAHKYVPSYAFLRR ELGLSSAHTNRKVWKKFVEA YGKAIPPAPPAPPLTLSKLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts68
1H chemical shifts521

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 86 residues - 9758.273 Da.

1   METGLYILEASPTYRSERGLYLEUARGTHR
2   ILEPHEGLYGLULYSLEUPROGLUSERHIS
3   ILEPHEPHEALATHRVALALAALAHISLYS
4   TYRVALPROSERTYRALAPHELEUARGARG
5   GLULEUGLYLEUSERSERALAHISTHRASN
6   ARGLYSVALTRPLYSLYSPHEVALGLUALA
7   TYRGLYLYSALAILEPROPROALAPROPRO
8   ALAPROPROLEUTHRLEUSERLYSLEUGLU
9   HISHISHISHISHISHIS

Samples:

sample_1: n77, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D HSQCsample_1isotropicsample_conditions_1
3D TOCSY-NOESYsample_1isotropicsample_conditions_1
3D HN-HAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_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 DRX600 600 MHz
  • Bruker DRX700 700 MHz

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