BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27242

Title: Trigger Factor   PubMed: 29222465

Deposition date: 2017-09-01 Original release date: 2017-11-20

Authors: Morgado, Leonor; Burmann, Bjoern; Hiller, Sebastian

Citation: Morgado, Leonor; Burmann, Bjoern; Sharpe, Timothy; Mazur, Adam; Hiller, Sebastian. "The dynamic dimer structure of the chaperone Trigger Factor."  Nat. Commun. 8, 1992-1992 (2017).

Assembly members:
TF, polymer, 432 residues, Formula weight is not available

Natural source:   Common Name: E. coli   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):
TF: MQVSVETTQGLGRRVTITIA ADSIETAVKSELVNVAKKVR IDGFRKGKVPMNIVAQRYGA SVRQDVLGDLMSRNFIDAII KEKINPAGAPTYVPGEYKLG EDFTYSVEFEVYPEVELQGL EAIEVEKPIVEVTDADVDGM LDTLRKQQATWKEKDGAVEA EDRVTIDFTGSVDGEEFEGG KASDFVLAMGQGRMIPGFED GIKGHKAGEEFTIDVTFPEE YHAENLKGKAAKFAINLKKV EERELPELTAEFIKRFGVED GSVEGLRAEVRKNMERELKS AIRNRVKSQAIEGLVKANDI DVPAALIDSEIDVLRRQAAQ RFGGNEKQALELPRELFEEQ AKRRVVVGLLLGEVIRTNEL KADEERVKGLIEEMASAYED PKEVIEFYSKNKELMDNMRN VALEEQAVEAVLAKAKVTEK ETTFNELMNQQA

Data sets:
Data typeCount
13C chemical shifts201
15N chemical shifts182
1H chemical shifts181

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TF1

Entities:

Entity 1, TF 432 residues - Formula weight is not available

1   METGLNVALSERVALGLUTHRTHRGLNGLY
2   LEUGLYARGARGVALTHRILETHRILEALA
3   ALAASPSERILEGLUTHRALAVALLYSSER
4   GLULEUVALASNVALALALYSLYSVALARG
5   ILEASPGLYPHEARGLYSGLYLYSVALPRO
6   METASNILEVALALAGLNARGTYRGLYALA
7   SERVALARGGLNASPVALLEUGLYASPLEU
8   METSERARGASNPHEILEASPALAILEILE
9   LYSGLULYSILEASNPROALAGLYALAPRO
10   THRTYRVALPROGLYGLUTYRLYSLEUGLY
11   GLUASPPHETHRTYRSERVALGLUPHEGLU
12   VALTYRPROGLUVALGLULEUGLNGLYLEU
13   GLUALAILEGLUVALGLULYSPROILEVAL
14   GLUVALTHRASPALAASPVALASPGLYMET
15   LEUASPTHRLEUARGLYSGLNGLNALATHR
16   TRPLYSGLULYSASPGLYALAVALGLUALA
17   GLUASPARGVALTHRILEASPPHETHRGLY
18   SERVALASPGLYGLUGLUPHEGLUGLYGLY
19   LYSALASERASPPHEVALLEUALAMETGLY
20   GLNGLYARGMETILEPROGLYPHEGLUASP
21   GLYILELYSGLYHISLYSALAGLYGLUGLU
22   PHETHRILEASPVALTHRPHEPROGLUGLU
23   TYRHISALAGLUASNLEULYSGLYLYSALA
24   ALALYSPHEALAILEASNLEULYSLYSVAL
25   GLUGLUARGGLULEUPROGLULEUTHRALA
26   GLUPHEILELYSARGPHEGLYVALGLUASP
27   GLYSERVALGLUGLYLEUARGALAGLUVAL
28   ARGLYSASNMETGLUARGGLULEULYSSER
29   ALAILEARGASNARGVALLYSSERGLNALA
30   ILEGLUGLYLEUVALLYSALAASNASPILE
31   ASPVALPROALAALALEUILEASPSERGLU
32   ILEASPVALLEUARGARGGLNALAALAGLN
33   ARGPHEGLYGLYASNGLULYSGLNALALEU
34   GLULEUPROARGGLULEUPHEGLUGLUGLN
35   ALALYSARGARGVALVALVALGLYLEULEU
36   LEUGLYGLUVALILEARGTHRASNGLULEU
37   LYSALAASPGLUGLUARGVALLYSGLYLEU
38   ILEGLUGLUMETALASERALATYRGLUASP
39   PROLYSGLUVALILEGLUPHETYRSERLYS
40   ASNLYSGLULEUMETASPASNMETARGASN
41   VALALALEUGLUGLUGLNALAVALGLUALA
42   VALLEUALALYSALALYSVALTHRGLULYS
43   GLUTHRTHRPHEASNGLULEUMETASNGLN
44   GLNALA

Samples:

sample_1: TF, [U-13C; U-15N; U-2H], 1 mM; potassium phosphate 20 mM; potassium chloride 100 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

PROSA, Guntert - processing

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 900 MHz

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