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BMRB Entry 25927

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25927
MolProbity Validation Chart

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Title: Curli secretion specificity factor CsgE W48A/F79A mutant   PubMed: 27298344

Deposition date: 2015-12-21 Original release date: 2016-06-13

Authors: Shu, Qin; Krezel, Andrzej; Frieden, Carl

Citation: Shu, Qin; Krezel, Andrzej; Hultgren, Scott; Frieden, Carl. "Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation"  Proc. Natl. Acad. Sci. U.S.A. 113, 7130-7135 (2016).

Assembly members:
entity, polymer, 108 residues, 13021.44 Da.

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

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

Entity Sequences (FASTA):
entity: AVEVEVPGLLTDHTVSSIGH DFYRAFSDKWESDYTGNLTI NERPSARAGSWITITVNQDV IFQTFLFPLKRDFEKTVVAA LIQTEEALNRRQINQALLST GDLAHDEF

Data sets:
Data typeCount
13C chemical shifts470
15N chemical shifts116
1H chemical shifts747

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 108 residues - 13021.44 Da.

1   ALAVALGLUVALGLUVALPROGLYLEULEU
2   THRASPHISTHRVALSERSERILEGLYHIS
3   ASPPHETYRARGALAPHESERASPLYSTRP
4   GLUSERASPTYRTHRGLYASNLEUTHRILE
5   ASNGLUARGPROSERALAARGALAGLYSER
6   TRPILETHRILETHRVALASNGLNASPVAL
7   ILEPHEGLNTHRPHELEUPHEPROLEULYS
8   ARGASPPHEGLULYSTHRVALVALALAALA
9   LEUILEGLNTHRGLUGLUALALEUASNARG
10   ARGGLNILEASNGLNALALEULEUSERTHR
11   GLYASPLEUALAHISASPGLUPHE

Samples:

15N: entity, [U-100% 15N], 180 uM; potassium phosphate 10 mM; D2O, [U-100% 13C; U-100% 15N; U-80% 2H], 10%; H2O 90%

15N-13C: entity, [U-99% 13C; U-99% 15N], 180 uM; potassium phosphate 10 mM; D2O, [U-100% 13C; U-100% 15N; U-80% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 10 mM; pH: 5.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC15N-13Cisotropicsample_conditions_1
2D 1H-13C HSQC aromatic15N-13Cisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic15N-13Cisotropicsample_conditions_1
3D CBCA(CO)NH15N-13Cisotropicsample_conditions_1
3D C(CO)NH15N-13Cisotropicsample_conditions_1
3D HNCO15N-13Cisotropicsample_conditions_1
3D HNCACB15N-13Cisotropicsample_conditions_1
3D HN(CO)CA15N-13Cisotropicsample_conditions_1
3D C(CO)NH15N-13Cisotropicsample_conditions_1
3D H(CCO)NH15N-13Cisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESY15N-13Cisotropicsample_conditions_1
3D 1H-13C NOESY aromatic15N-13Cisotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, data analysis, processing

CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - chemical shift assignment, peak picking

Amber v12, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DMX 750 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P0AE95
GB ECK1025 EcoGene:EG13411
NCBI 945711

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