BMRB Entry 16068

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16068
MolProbity Validation Chart

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NMR-STAR v3 text file.
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All files associated with the entry

Title:
gp16
Deposition date:
2008-12-18
Original release date:
2009-05-20
Authors:
Gallopin, Matthieu; Gilquin, Bernard; Zinn-Justin, Sophie
Citation:

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).
PubMed: 19433794

Assembly members:

Assembly members:
gp16, polymer, 109 residues, 12615.187 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gp16: MYEEFRDVITFQSYVEQSNG EGGKTYKWVDEFTAAAHVQP ISQEEYYKAQQLQTPIGYNI YTPYDDRIDKKMRVIYRGKI VTFIGDPVDLSGLQEITRIK GKEDGAYVG

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts97
1H chemical shifts459

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gp161

Entities:

Entity 1, gp16 109 residues - 12615.187 Da.

1   METTYRGLUGLUPHEARGASPVALILETHR
2   PHEGLNSERTYRVALGLUGLNSERASNGLY
3   GLUGLYGLYLYSTHRTYRLYSTRPVALASP
4   GLUPHETHRALAALAALAHISVALGLNPRO
5   ILESERGLNGLUGLUTYRTYRLYSALAGLN
6   GLNLEUGLNTHRPROILEGLYTYRASNILE
7   TYRTHRPROTYRASPASPARGILEASPLYS
8   LYSMETARGVALILETYRARGGLYLYSILE
9   VALTHRPHEILEGLYASPPROVALASPLEU
10   SERGLYLEUGLNGLUILETHRARGILELYS
11   GLYLYSGLUASPGLYALATYRVALGLY

Samples:

sample_1: gp16 0.35 mM; HEPES 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_2: gp16, [U-100% 15N], 0.35 mM; HEPES 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_3: gp16, [U-100% 13C; U-100% 15N], 0.35 mM; HEPES 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_4: gp16, [U-100% 13C; U-100% 15N; U-80% 2H], 0.35 mM; HEPES 5 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
1H-2H exchange experimentssample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
1H-15N nOe transfersample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCACONHsample_3isotropicsample_conditions_1
3D HBHACONHsample_3isotropicsample_conditions_1
3D HCCH COSYsample_3isotropicsample_conditions_1
3D HCCH TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
HNCACBsample_4isotropicsample_conditions_1
HNCACOsample_4isotropicsample_conditions_1
HNCOCACBsample_4isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

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

INCA, Bernard Gilquin - chemical shift assignment

NMR spectrometers:

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

Related Database Links:

PDB
EMBL CAA66547
REF NP_690677

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks