BMRB Entry 30127

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30127
MolProbity Validation Chart

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Title:
Recognition and targeting mechanisms by chaperones in flagella assembly and operation
Deposition date:
2016-07-01
Original release date:
2016-08-11
Authors:
Khanra, N.; Rossi, P.; Economou, A.; Kalodimos, C.
Citation:

Citation: Khanra, N.; Rossi, P.; Economou, A.; Kalodimos, C.. "Recognition and targeting mechanisms by chaperones in flagellum assembly and operation"  Proc. Natl. Acad. Sci. U. S. A. 113, 9798-9803 (2016).
PubMed: 27528687

Assembly members:

Assembly members:
Flagellar protein FliT,Flagellum-specific ATP synthase, polymer, 140 residues, 15656.003 Da.

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 99287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Flagellar protein FliT,Flagellum-specific ATP synthase: MTSTVEFINRWQRIALLSQS LLELAQRGEWDLLLQQEVSY LQSIETVMEKQTPPGITRSI QDMVAGYIKQTLDNEQLLKG LLQQRLDELSSLIGQVLFQG PSAGLVPRGSGGIEGMTTRL TRWLTALDNFEAKMALLPAV

Data sets:
Data typeCount
13C chemical shifts500
15N chemical shifts139
1H chemical shifts480

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 140 residues - 15656.003 Da.

1   METTHRSERTHRVALGLUPHEILEASNARG
2   TRPGLNARGILEALALEULEUSERGLNSER
3   LEULEUGLULEUALAGLNARGGLYGLUTRP
4   ASPLEULEULEUGLNGLNGLUVALSERTYR
5   LEUGLNSERILEGLUTHRVALMETGLULYS
6   GLNTHRPROPROGLYILETHRARGSERILE
7   GLNASPMETVALALAGLYTYRILELYSGLN
8   THRLEUASPASNGLUGLNLEULEULYSGLY
9   LEULEUGLNGLNARGLEUASPGLULEUSER
10   SERLEUILEGLYGLNVALLEUPHEGLNGLY
11   PROSERALAGLYLEUVALPROARGGLYSER
12   GLYGLYILEGLUGLYMETTHRTHRARGLEU
13   THRARGTRPLEUTHRALALEUASPASNPHE
14   GLUALALYSMETALALEULEUPROALAVAL

Samples:

sample_1: EDTA 0.5 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; protein, [U-100% 15N,2H]_[1H,13C]ILVMATFY_[1H]W, 0.5 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_2: EDTA 0.5 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; protein, [U-99% 13C; U-99% 15N; U-99% 2H], 0.5 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7; 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 HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 700 MHz

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