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 17322

Title: High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH   PubMed: 22087227

Deposition date: 2010-11-24 Original release date: 2012-09-20

Authors: Sborgi, Lorenzo; Verma, Abhinav; Munoz, Victor; de Alba, Eva

Citation: Sborgi, Lorenzo; Verma, Abhinav; Munoz, Victor; de Alba, Eva. "Revisiting the NMR structure of the ultrafast downhill folding protein gpW from bacteriophage ."  PLoS ONE 6, e26409-e26409 (2011).

Assembly members:
gpW, polymer, 62 residues, 6989.108 Da.

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

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

Entity Sequences (FASTA):
gpW: MVRQEELAAARAALHDLMTG KRVATVQKDGRRVEFTATSV SDLKKYIAELEVQTGMTQRR RG

Data sets:
Data typeCount
13C chemical shifts206
15N chemical shifts62
1H chemical shifts432

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1W protein of bacteriophage lambda1

Entities:

Entity 1, W protein of bacteriophage lambda 62 residues - 6989.108 Da.

1   METVALARGGLNGLUGLULEUALAALAALA
2   ARGALAALALEUHISASPLEUMETTHRGLY
3   LYSARGVALALATHRVALGLNLYSASPGLY
4   ARGARGVALGLUPHETHRALATHRSERVAL
5   SERASPLEULYSLYSTYRILEALAGLULEU
6   GLUVALGLNTHRGLYMETTHRGLNARGARG
7   ARGGLY

Samples:

sample_1: gpW, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%; glycine buffer 20 mM

sample_2: gpW, [U-13C; U-15N], 1 mM; D2O 100%; glycine buffer 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 3.5; pressure: 1 atm; temperature: 293.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

PIPP, Garrett - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17321
PDB
DBJ BAG76119 BAG77589 BAI23937 BAI29406 GAL55727
EMBL CAP75664 CAQ31249 CAQ97648 CAQ98444 CAR11829
GB AAA96535 AAG55981 AAN81624 AAZ89070 ABG69179
REF NP_040582 WP_000198149 WP_000246867 WP_001571330 WP_001657975
SP P68659 P68660
AlphaFold P68659 P68660

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