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 30985

Title: Solution structure of the phosphatidylinositol 3-phosphate binding domain from the Legionella effector SetA

Deposition date: 2022-01-24 Original release date: 2023-01-31

Authors: Beck, W.; Enoki, T.; Feigenson, G.; Nicholson, L.; Oswald, R.; Mao, Y.

Citation: Beck, W.; Enoki, T.; Feigenson, G.; Nicholson, L.; Oswald, R.; Mao, Y.. "Solution structure of the phosphatidylinositol 3-phosphate binding domain from the Legionella effector SetA"  .

Assembly members:
entity_1, polymer, 108 residues, 12192.811 Da.

Natural source:   Common Name: Legionella pneumophila   Taxonomy ID: 446   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Legionella pneumophila

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: SDEKIKTAHDLIDEIIQDVI QLDGKLGLLGGNTRQLEDGR VINIPNGAAMIFDDYKKYKQ GELTAESALESMIKIAKLSN QLNRHTFFNQRQPETGQFYK KVAAIDLQ

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts122
1H chemical shifts797

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 108 residues - 12192.811 Da.

1   SERASPGLULYSILELYSTHRALAHISASP
2   LEUILEASPGLUILEILEGLNASPVALILE
3   GLNLEUASPGLYLYSLEUGLYLEULEUGLY
4   GLYASNTHRARGGLNLEUGLUASPGLYARG
5   VALILEASNILEPROASNGLYALAALAMET
6   ILEPHEASPASPTYRLYSLYSTYRLYSGLN
7   GLYGLULEUTHRALAGLUSERALALEUGLU
8   SERMETILELYSILEALALYSLEUSERASN
9   GLNLEUASNARGHISTHRPHEPHEASNGLN
10   ARGGLNPROGLUTHRGLYGLNPHETYRLYS
11   LYSVALALAALAILEASPLEUGLN

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N; U-80% 2H], 6 ± 0.3 mg/mL; sodium phosphate buffer 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N-NOESYHSQCsample_1isotropicsample_conditions_1
3D 1H-13C-NOESYHSQC (aromatic)sample_1isotropicsample_conditions_1
3D 1H-13C-NOESYHSQC (aliphatic)sample_1isotropicsample_conditions_1

Software:

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

PONDEROSA-C/S, Woonghee Lee - refinement, structure calculation

Sparky, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 500 MHz

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