BMRB Entry 30136

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30136
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Recognition and targeting mechanisms by chaperones in flagella assembly and operation
Deposition date:
2016-07-07
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:
entity_1, polymer, 122 residues, 13715.621 Da.

Natural source:

Natural source:   Common Name: Salmonella enterica   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):
entity_1: MTSTVEFINRWQRIALLSQS LLELAQRGEWDLLLQQEVSY LQSIETVMEKQTPPGITRSI QDMVAGYIKQTLDNEQLLKG LLQQRLDELSSLIGQSTRQK SLNNAYGRLSGMLLVPDAPG AS

Data sets:
Data typeCount
13C chemical shifts194
15N chemical shifts103
1H chemical shifts332

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 122 residues - 13715.621 Da.

1   METTHRSERTHRVALGLUPHEILEASNARG
2   TRPGLNARGILEALALEULEUSERGLNSER
3   LEULEUGLULEUALAGLNARGGLYGLUTRP
4   ASPLEULEULEUGLNGLNGLUVALSERTYR
5   LEUGLNSERILEGLUTHRVALMETGLULYS
6   GLNTHRPROPROGLYILETHRARGSERILE
7   GLNASPMETVALALAGLYTYRILELYSGLN
8   THRLEUASPASNGLUGLNLEULEULYSGLY
9   LEULEUGLNGLNARGLEUASPGLULEUSER
10   SERLEUILEGLYGLNSERTHRARGGLNLYS
11   SERLEUASNASNALATYRGLYARGLEUSER
12   GLYMETLEULEUVALPROASPALAPROGLY
13   ALASER

Samples:

sample_1: EDTA 0.5 mM; FliT, [U-99% 13C; U-99% 15N; U-99% 2H], 0.5 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05%

sample_2: EDTA 0.5 mM; FliT, U-[2H,15N] 1H-13C-IVLMAT, 1H-13C-15N FY, 0.08 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_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
  • Bruker AvanceIII 900 MHz

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