BMRB Entry 19835

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19835
MolProbity Validation Chart

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Title:
NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310
Deposition date:
2014-03-05
Original release date:
2014-05-20
Authors:
Saio, Tomohide; Guan, Xiao; Rossi, Paolo; Economou, Anastassios; Kalodimos, Charalampos
Citation:

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).
PubMed: 24812405

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 9596.792 Da.
entity_2, polymer, 443 residues, 48256.020 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HMARADVTLGGGAKTFAETA TAGEWQGKTLREQAQARGYQ LVSDAASLNSVTEANQQKPL LGLFADGNMPVRWLGPKATY HGNIDKPAVTCTP
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 sets:
Data typeCount
13C chemical shifts481
15N chemical shifts444
1H chemical shifts1537

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 93 residues - 9596.792 Da.

1   HISMETALAARGALAASPVALTHRLEUGLY
2   GLYGLYALALYSTHRPHEALAGLUTHRALA
3   THRALAGLYGLUTRPGLNGLYLYSTHRLEU
4   ARGGLUGLNALAGLNALAARGGLYTYRGLN
5   LEUVALSERASPALAALASERLEUASNSER
6   VALTHRGLUALAASNGLNGLNLYSPROLEU
7   LEUGLYLEUPHEALAASPGLYASNMETPRO
8   VALARGTRPLEUGLYPROLYSALATHRTYR
9   HISGLYASNILEASPLYSPROALAVALTHR
10   CYSTHRPRO

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 AAA24363 AAA24364 AAA24365 AAA24366 AAA24367 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 19836 19837
AlphaFold P00634 A1A8A5 A7ZIJ4 A7ZX94 B1J012 B1LJJ3

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