BMRB Entry 17028

Title:
The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein   PubMed: 20826161
Deposition date:
2010-06-30
Original release date:
2010-09-24
Authors:
Pell, Lisa; Gasmi-Seabrook, Genevieve; Donaldson, Logan; Howell, P Lynne; Davidson, Alan; Maxwell, Karen
Citation:

Citation: Pell, Lisa; Gasmi-Seabrook, Genevieve; Morais, Marc; Neudecker, Philipp; Kanelis, Voula; Bona, Diane; Donaldson, Logan; Edwards, Aled; Howell, P. Lynne; Davidson, Alan; Maxwell, Karen. "The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage Tail Tube Protein."  J. Mol. Biol. 403, 468-479 (2010).

Assembly members:

Assembly members:
gpV-C, polymer, 91 residues, 8882.101 Da.

Natural source:

Natural source:   Common Name: Bacteriophage lambda   Taxonomy ID: 10710   Superkingdom: Viruses   Kingdom: not available   Genus/species: Bacteriophage lambda

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32b

Experimental source:

Natural source:   Common Name: Bacteriophage lambda   Taxonomy ID: 10710   Superkingdom: Viruses   Kingdom: not available   Genus/species: Bacteriophage lambda

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32b

Data sets:
Data typeCount
13C chemical shifts343
15N chemical shifts91
1H chemical shifts566

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1gpV-C1

Entities:

Entity 1, gpV-C 91 residues - 8882.101 Da.

1   GLYALAMETALAALAALATHRGLYMETTHR
2   VALTHRPROALASERTHRSERVALVALLYS
3   GLYGLNSERTHRTHRLEUTHRVALALAPHE
4   GLNPROGLUGLYVALTHRASPLYSSERPHE
5   ARGALAVALSERALAASPLYSTHRLYSALA
6   THRVALSERVALSERGLYMETTHRILETHR
7   VALASNGLYVALALAALAGLYLYSVALASN
8   ILEPROVALVALSERGLYASNGLYGLUPHE
9   ALAALAVALALAGLUILETHRVALTHRALA
10   SER

Samples:

sample_1: gpV-C, 15N, 13C, 0.71 – 2.5 mM; sodium phosphate 50 mM; sodium chloride 200 mM; H20 90%; D20 10%

sample_2: sodium phosphate 50 mM; sodium chloride 200 mM; D20 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; 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 HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAG77580 BAI29415
EMBL CAP75673 CAQ31259 CAR01926 CAR02528 CAR16659
GB AAA96545 ACF32394 ACR63704 ACT29881 ACT42628
REF NP_040592 WP_000056728 WP_000306529 WP_000419939 WP_001297108
SP P03733

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