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 15807

Title: The Solution Structure of gpV, the Major Tail Protein from Bacteriophage Lambda   PubMed: 19251647

Authors: Pell, Lisa; Kanelis, Voula; Howell, P. Lynne; Davidson, Alan

Citation: Pell, Lisa; Kanelis, Voula; Donaldson, Logan; Howell, Lynne; Davidson, Alan. "The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system"  Proc. Natl. Acad. Sci. USA 106, 4160-4165 (2009).

Assembly members:
gpV_protein, polymer, 156 residues, 16896.908 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
gpV_protein: GAMMPVPNPTMPVKGAGTTL WVYKGSGDPYANPLSDVDWS RLAKVKDLTPGELTAESYDD SYLDDEDADWTATGQGQKSA GDTSFTLAWMPGEQGQQALL AWFNEGDTRAYKIRFPNGTV DVFRGWVSSIGKAVTAKEVI TRTVKVTNVGRPSMAE

Data sets:
Data typeCount
13C chemical shifts539
15N chemical shifts149
1H chemical shifts914

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gpV_protein1

Entities:

Entity 1, gpV_protein 156 residues - 16896.908 Da.

1   GLYALAMETMETPROVALPROASNPROTHR
2   METPROVALLYSGLYALAGLYTHRTHRLEU
3   TRPVALTYRLYSGLYSERGLYASPPROTYR
4   ALAASNPROLEUSERASPVALASPTRPSER
5   ARGLEUALALYSVALLYSASPLEUTHRPRO
6   GLYGLULEUTHRALAGLUSERTYRASPASP
7   SERTYRLEUASPASPGLUASPALAASPTRP
8   THRALATHRGLYGLNGLYGLNLYSSERALA
9   GLYASPTHRSERPHETHRLEUALATRPMET
10   PROGLYGLUGLNGLYGLNGLNALALEULEU
11   ALATRPPHEASNGLUGLYASPTHRARGALA
12   TYRLYSILEARGPHEPROASNGLYTHRVAL
13   ASPVALPHEARGGLYTRPVALSERSERILE
14   GLYLYSALAVALTHRALALYSGLUVALILE
15   THRARGTHRVALLYSVALTHRASNVALGLY
16   ARGPROSERMETALAGLU

Samples:

sample_1: sodium phosphate 50 mM; DSS 0.6 mM; sodium chloride 200 mM; D2O 8-10%; sodium azide 0.1%; gpV protein, [U-100% 13C; U-100% 15N], 1 mM

sample_2: gpV protein, [U-100% 13C; U-100% 15N], 1 mM; D2O 90-99%; DSS 0.6 mM; sodium phosphate 50 mM; sodium chloride 200 mM; sodium azide 0.1%

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAG76128 BAG77176 BAG77580 BAI23948 BAI29415
EMBL CAP75673 CAQ31259 CAQ97657 CAQ98435 CAR01926
GB AAA96545 AAN81615 AAZ89061 ABG69188 ACA77741
REF NP_040592 WP_000056697 WP_000056728 WP_000112332 WP_000223313
SP P03733