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 16057

Title: NMR structure of protein gp15 of bacteriophage SPP1   PubMed: 19433794

Authors: Gallopin, Matthieu; Gilquin, Bernard; Zinn-Justin, Sophie

Citation: Lhuillier, Sophie; Gallopin, Matthieu; Gilquin, Bernard; Brasiles, Sandrine; Lancelot, Nathalie; Letellier, Guillaume; Gilles, Mathilde; Dethan, Guillaume; Orlova, Elena; Couprie, Joel; Tavares, Paulo; Zinn-Justin, Sophie. "Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating"  Proc. Natl. Acad. Sci. U.S.A. 106, 8507-8512 (2009).

Assembly members:
gp15, polymer, 99 residues, 11270.051 Da.

Natural source:   Common Name: Bacteriophage SPP1   Taxonomy ID: 10724   Superkingdom: Viruses   Kingdom: not available   Genus/species: Bacteriophage SPP1

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

Entity Sequences (FASTA):
gp15: QRVKRLLSITNDKHDEYLTE MVPLLVEFAKDECHNPFIDK DGNESIPSGVLIFVAKAAQF YMTNAGLTGRSMDTVSYNFA TEIPSTILKKLNPYRKMAR

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts93
1H chemical shifts666

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 99 residues - 11270.051 Da.

1   GLNARGVALLYSARGLEULEUSERILETHR
2   ASNASPLYSHISASPGLUTYRLEUTHRGLU
3   METVALPROLEULEUVALGLUPHEALALYS
4   ASPGLUCYSHISASNPROPHEILEASPLYS
5   ASPGLYASNGLUSERILEPROSERGLYVAL
6   LEUILEPHEVALALALYSALAALAGLNPHE
7   TYRMETTHRASNALAGLYLEUTHRGLYARG
8   SERMETASPTHRVALSERTYRASNPHEALA
9   THRGLUILEPROSERTHRILELEULYSLYS
10   LEUASNPROTYRARGLYSMETALAARG

Samples:

sample_1: gp15, [U-100% 15N], 0.5 mM

sample_2: gp15, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D H-D exchangesample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N nOe transfersample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH COSYsample_2isotropicsample_conditions_1
3D HCCH TOCSYsample_2isotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 2 600 MHz
  • Bruker Avance 2 700 MHz

Related Database Links:

PDB
EMBL CAA61872 CAA66546
REF NP_690676