BMRB Entry 31069

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/BMR31069
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:
FliT-FliJ fusion complex
Deposition date:
2023-01-13
Original release date:
2023-06-27
Authors:
Rossi, P.; Kalodimos, C.
Citation:

Citation: Rossi, P.; Xing, Q.; Bini, E.; Portaliou, A.; Clay, M.; Warren, E.; Khanra, N.; Economou, A.; Kalodimos, C.. "Chaperone Recycling in Late-Stage Flagellar Assembly"  J. Mol. Biol. ., 167954-167954 (2023).
PubMed: 37330284

Assembly members:

Assembly members:
entity_1, polymer, 166 residues, 18827.361 Da.

Natural source:

Natural source:   Common Name: Salmonella enterica subsp. enterica serovar Typhimurium   Taxonomy ID: 90371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella enterica

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTSTVEFINRWQRIALLSQS LLELAQRGEWDLLLQQEVSY LQSIETVMEKQTPPGITRSI QDMVAGYIKQTLDNEQLLKG LLQQRLDELSSLIGQVLFQG PSAGLVPRGSGGIEGSNLNT DMGNGIASNRWINYQQFIQT LEKAIEQHRLQLTQWTQKVD LALKSW

Data sets:
Data typeCount
13C chemical shifts562
15N chemical shifts154
1H chemical shifts454

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 166 residues - 18827.361 Da.

1   METTHRSERTHRVALGLUPHEILEASNARG
2   TRPGLNARGILEALALEULEUSERGLNSER
3   LEULEUGLULEUALAGLNARGGLYGLUTRP
4   ASPLEULEULEUGLNGLNGLUVALSERTYR
5   LEUGLNSERILEGLUTHRVALMETGLULYS
6   GLNTHRPROPROGLYILETHRARGSERILE
7   GLNASPMETVALALAGLYTYRILELYSGLN
8   THRLEUASPASNGLUGLNLEULEULYSGLY
9   LEULEUGLNGLNARGLEUASPGLULEUSER
10   SERLEUILEGLYGLNVALLEUPHEGLNGLY
11   PROSERALAGLYLEUVALPROARGGLYSER
12   GLYGLYILEGLUGLYSERASNLEUASNTHR
13   ASPMETGLYASNGLYILEALASERASNARG
14   TRPILEASNTYRGLNGLNPHEILEGLNTHR
15   LEUGLULYSALAILEGLUGLNHISARGLEU
16   GLNLEUTHRGLNTRPTHRGLNLYSVALASP
17   LEUALALEULYSSERTRP

Samples:

sample_1: FliT_1-95-FliJ_51-101_fusion, [U-13C; U-15N; U-2H], 400 uM; potassium phosphate 20 mM; potassium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 5 mM

sample_2: FliT_1-95-FliJ_51-101_fusion, [U-100% 15N], 100% 13C-CH3_ILVMAT, 100%-1H,13C-Phe,Tyr, 400 uM; potassium phosphate 20 mM; potassium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 5 mM

sample_conditions_1: ionic strength: 200 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TopSpin, Bruker Biospin - collection

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

PdbStat, tejero & montelione - processing

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

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

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AVANCE 700 MHz
  • Bruker AVANCE 850 MHz

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