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 19836

Title: NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150   PubMed: 24812405

Deposition date: 2014-03-05 Original release date: 2014-05-20

Authors: Saio, Tomohide; Guan, Xiao; Rossi, Paolo; Economou, Anastassios; Kalodimos, Charalampos

Citation: Saio, Tomohide; Guan, Xiao; Rossi, Paolo; Economou, Anastassios; Kalodimos, Charalampos. "Structural basis for protein antiaggregation activity of the trigger factor chaperone"  Science 344, 1250494-1250494 (2014).

Assembly members:
entity_1, polymer, 151 residues, 16862.254 Da.
entity_2, polymer, 443 residues, 48256.020 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 469008   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: HMKQSTIALALLPLLFTPVT KARTPEMPVLENRAAQGDIT APGGARRLTGDQTAALRDSL SDKPAKNIILLIGDGMGDSE ITAARNYAEGAGGFFKGIDA LPLTGQYTHYALNKKTGKPD YVTDSAASATAWSTGVKTYN GALGVDIHEKD
entity_2: MNHKVHHHHHHMQVSVETTQ GLGRRVTITIAADSIETAVK SELVNVAKKVRIDGFRKGKV PMNIVAQRYGASVRQDVLGD LMSRNFIDAIIKEKINPAGA PTYVPGEYKLGEDFTYSVEF EVYPEVELQGLEAIEVEKPI VEVTDADVDGMLDTLRKQQA TWKEKDGAVEAEDRVTIDFT GSVDGEEFEGGKASDFVLAM GQGRMIPGFEDGIKGHKAGE EFTIDVTFPEEYHAENLKGK AAKFAINLKKVEERELPELT AEFIKRFGVEDGSVEGLRAE VRKNMERELKSAIRNRVKSQ AIEGLVKANDIDVPAALIDS EIDVLRRQAAQRFGGNEKQA LELPRELFEEQAKRRVVVGL LLGEVIRTNELKADEERVKG LIEEMASAYEDPKEVIEFYS KNKELMDNMRNVALEEQAVE AVLAKAKVTEKETTFNELMN QQA

Data typeCount
13C chemical shifts565
15N chemical shifts479
1H chemical shifts1638

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 151 residues - 16862.254 Da.

1   HISMETLYSGLNSERTHRILEALALEUALA
2   LEULEUPROLEULEUPHETHRPROVALTHR
3   LYSALAARGTHRPROGLUMETPROVALLEU
4   GLUASNARGALAALAGLNGLYASPILETHR
5   ALAPROGLYGLYALAARGARGLEUTHRGLY
6   ASPGLNTHRALAALALEUARGASPSERLEU
7   SERASPLYSPROALALYSASNILEILELEU
8   LEUILEGLYASPGLYMETGLYASPSERGLU
9   ILETHRALAALAARGASNTYRALAGLUGLY
10   ALAGLYGLYPHEPHELYSGLYILEASPALA
11   LEUPROLEUTHRGLYGLNTYRTHRHISTYR
12   ALALEUASNLYSLYSTHRGLYLYSPROASP
13   TYRVALTHRASPSERALAALASERALATHR
14   ALATRPSERTHRGLYVALLYSTHRTYRASN
15   GLYALALEUGLYVALASPILEHISGLULYS
16   ASP

Entity 2, entity_2 443 residues - 48256.020 Da.

1   METASNHISLYSVALHISHISHISHISHIS
2   HISMETGLNVALSERVALGLUTHRTHRGLN
3   GLYLEUGLYARGARGVALTHRILETHRILE
4   ALAALAASPSERILEGLUTHRALAVALLYS
5   SERGLULEUVALASNVALALALYSLYSVAL
6   ARGILEASPGLYPHEARGLYSGLYLYSVAL
7   PROMETASNILEVALALAGLNARGTYRGLY
8   ALASERVALARGGLNASPVALLEUGLYASP
9   LEUMETSERARGASNPHEILEASPALAILE
10   ILELYSGLULYSILEASNPROALAGLYALA
11   PROTHRTYRVALPROGLYGLUTYRLYSLEU
12   GLYGLUASPPHETHRTYRSERVALGLUPHE
13   GLUVALTYRPROGLUVALGLULEUGLNGLY
14   LEUGLUALAILEGLUVALGLULYSPROILE
15   VALGLUVALTHRASPALAASPVALASPGLY
16   METLEUASPTHRLEUARGLYSGLNGLNALA
17   THRTRPLYSGLULYSASPGLYALAVALGLU
18   ALAGLUASPARGVALTHRILEASPPHETHR
19   GLYSERVALASPGLYGLUGLUPHEGLUGLY
20   GLYLYSALASERASPPHEVALLEUALAMET
21   GLYGLNGLYARGMETILEPROGLYPHEGLU
22   ASPGLYILELYSGLYHISLYSALAGLYGLU
23   GLUPHETHRILEASPVALTHRPHEPROGLU
24   GLUTYRHISALAGLUASNLEULYSGLYLYS
25   ALAALALYSPHEALAILEASNLEULYSLYS
26   VALGLUGLUARGGLULEUPROGLULEUTHR
27   ALAGLUPHEILELYSARGPHEGLYVALGLU
28   ASPGLYSERVALGLUGLYLEUARGALAGLU
29   VALARGLYSASNMETGLUARGGLULEULYS
30   SERALAILEARGASNARGVALLYSSERGLN
31   ALAILEGLUGLYLEUVALLYSALAASNASP
32   ILEASPVALPROALAALALEUILEASPSER
33   GLUILEASPVALLEUARGARGGLNALAALA
34   GLNARGPHEGLYGLYASNGLULYSGLNALA
35   LEUGLULEUPROARGGLULEUPHEGLUGLU
36   GLNALALYSARGARGVALVALVALGLYLEU
37   LEULEUGLYGLUVALILEARGTHRASNGLU
38   LEULYSALAASPGLUGLUARGVALLYSGLY
39   LEUILEGLUGLUMETALASERALATYRGLU
40   ASPPROLYSGLUVALILEGLUPHETYRSER
41   LYSASNLYSGLULEUMETASPASNMETARG
42   ASNVALALALEUGLUGLUGLNALAVALGLU
43   ALAVALLEUALALYSALALYSVALTHRGLU
44   LYSGLUTHRTHRPHEASNGLULEUMETASN
45   GLNGLNALA

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; entity_2, [U-100% 13C; U-100% 15N], 0.5 mM; potassium chloride 100 mM; BME 3 mM; potassium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C HMQC-NOESY_HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

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

SPARKY v3.113, Goddard - chemical shift assignment

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

OLIVIA v1.16, Olivia, Yokochi Masashi - chemical shift assignment

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v3.1, Bruker Biospin - collection

VNMRJ, Varian - collection

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TALOSN, Shen and Bax - geometry optimization

PSVS v1.5, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAB33856 BAE76164 BAG75928 BAI23756 BAI29227 BAB33913 BAD98926 BAE76216 BAG75986 BAI23810
EMBL CAA28257 CAP74918 CAQ30851 CAQ97255 CAR01727 CAP74970 CAQ30908 CAQ97312 CAR01780 CAR06670
GB AAA24359 AAA24363 AAA24364 AAA24365 AAA24366 AAA62791 AAB40192 AAC73539 AAG54786 AAN42037
REF NP_308460 NP_414917 NP_706185 WP_000089619 WP_000089625 NP_286178 NP_308517 NP_414970 NP_706330 NP_752485
SP P00634 A1A8A5 A7ZIJ4 A7ZX94 B1J012 B1LJJ3
BMRB 19835 19837

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