BMRB Entry 27239

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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/BMR27239
MolProbity Validation Chart

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Title:
Trigger factor
Deposition date:
2017-08-29
Original release date:
2017-11-20
Authors:
Morgado, Leonor; Burmann, Bjorn; Hiller, Sebastian
Citation:

Citation: Morgado, Leonor; Burmann, Bjorn; Sharpe, Timothy; Mazur, Adam; Hiller, Sebastian. "The dynamic dimer structure of the chaperone Trigger Factor."  Nat. Commun. 8, 1992-1992 (2017).
PubMed: 29222465

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

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 typeCount
13C chemical shifts1108
15N chemical shifts981
1H chemical shifts981

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RBD1
2SBD1
3PPD1
4RBD-SBD1
5SBD-PPD1

Entities:

Entity 1, RBD 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:

RBD-SBD: RBD-SBD, [U-15N; U-2H], 5 – 500 uM; potassium phosphate 20 mM; potassium chloride 100 mM; EDTA 0.5 mM

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

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

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

PPD: PPD, [U-15N], 100 uM; 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 HSQCRBDisotropicsample_conditions_1
2D 1H-15N HSQCSBDisotropicsample_conditions_1
2D 1H-15N HSQCPPDisotropicsample_conditions_1
2D 1H-15N HSQCRBD-SBDisotropicsample_conditions_1
2D 1H-15N HSQCSBD-PPDisotropicsample_conditions_1
3D HNCACBRBDisotropicsample_conditions_1
3D HNCACBSBDisotropicsample_conditions_1
3D HNCACBSBD-PPDisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

PROSA, Guntert - processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Ascend 700 MHz
  • Bruker Avance 900 MHz

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