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 17768

Title: Structure of bacteriophage SPP1 gp17 protein   PubMed: 22072538

Deposition date: 2011-07-07 Original release date: 2012-05-09

Authors: Chagot, Benjamin; Auzat, Isabelle; Gallopin, Matthieu; Petitpas, Isabelle; Gilquin, Bernard; Tavares, Paulo; Zinn-Justin, Sophie

Citation: Chagot, Benjamin; Auzat, Isabelle; Gallopin, Matthieu; Petitpas, Isabelle; Gilquin, Bernard; Tavares, Paulo; Zinn-Justin, Sophie. "Solution structure of gp17 from the Siphoviridae bacteriophage SPP1: insights into its role in virion assembly."  Proteins 80, 319-326 (2012).

Assembly members:
gp17, polymer, 139 residues, 15478.582 Da.

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

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

Entity Sequences (FASTA):
gp17: QGLQTWKLASRALQKATVEN LESYQPLMEMVNQVTESPGK DDPYPYVVIGDQSSTPFETK SSFGENITMDFHVWGGTTRA EAQDISSRVLEALTYKPLMF EGFTFVAKKLVLAQVITDTD GVTKHGIIKVRFTINNNTG

Data sets:
Data typeCount
13C chemical shifts282
15N chemical shifts102
1H chemical shifts708

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gp171

Entities:

Entity 1, gp17 139 residues - 15478.582 Da.

First four residues (QGLQ) and the two last (TG) are cloning artefacts

1   GLNGLYLEUGLNTHRTRPLYSLEUALASER
2   ARGALALEUGLNLYSALATHRVALGLUASN
3   LEUGLUSERTYRGLNPROLEUMETGLUMET
4   VALASNGLNVALTHRGLUSERPROGLYLYS
5   ASPASPPROTYRPROTYRVALVALILEGLY
6   ASPGLNSERSERTHRPROPHEGLUTHRLYS
7   SERSERPHEGLYGLUASNILETHRMETASP
8   PHEHISVALTRPGLYGLYTHRTHRARGALA
9   GLUALAGLNASPILESERSERARGVALLEU
10   GLUALALEUTHRTYRLYSPROLEUMETPHE
11   GLUGLYPHETHRPHEVALALALYSLYSLEU
12   VALLEUALAGLNVALILETHRASPTHRASP
13   GLYVALTHRLYSHISGLYILEILELYSVAL
14   ARGPHETHRILEASNASNASNTHRGLY

Samples:

sample_1: gp17, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%; TRIS 50 mM; sodium chloride 50 mM

sample_2: gp17 0.3 mM; H2O 90%; D2O 10%; MES 50 mM; sodium chloride 500 mM

sample_3: gp17, [U-100% 13C; U-100% 15N], 0.6 mM; H2O 90%; D2O 10%; MES 50 mM; sodium chloride 500 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.5 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2
2D 1H-1H COSYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
T1 relaxationsample_3isotropicsample_conditions_2
T2 relaxationsample_3isotropicsample_conditions_2
heteronuclear NOEsample_3isotropicsample_conditions_2

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

SPARKY v1.3, Goddard - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker AMX 700 MHz
  • Bruker AMX 600 MHz

Related Database Links:

PDB
EMBL CAA66549
REF NP_690679

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