BMRB Entry 19411

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19411

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Title:
Conformation and dynamics of the periplasmic membrane-protein chaperone complexes OmpX Skp and tOmpA Skp
Deposition date:
2013-08-03
Original release date:
2013-09-10
Authors:
Burmann, Bjoern; Wang, Congwei; Hiller, Sebastian
Citation:

Citation: Burmann, Bjoern; Wang, Congwei; Hiller, Sebastian. "Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp"  Nat. Struct. Mol. Biol. 20, 1265-1272 (2013).
PubMed: 24077225

Assembly members:

Assembly members:
Escherichia_Coli_OmpX, polymer, 149 residues, Formula weight is not available
Escherichia_Coli_Skp, polymer, 234 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-OmpX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Escherichia_Coli_OmpX: MATSTVTGGYAQSDMQGVMN KTNGFNLKYRYEQQNNPLGV IGSFTYTEKDRTASSGDYNK NQYYGITAGPAYRINDWASI YGVVGVGYGKFQTTEYPTYK HDTSDYGFSYGAGLQFNPME NVALDFSYEQSRIRSVDVGT WIAGVGYRF
Escherichia_Coli_Skp: MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVANSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VKIYGVVGVGYGKFQQTENQ GLNRTASNSDYGFSYGAGMQ FNPIENVALDFSYEQSRIRN VDVGTWIAGVGYRF

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts129
1H chemical shifts129

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OmpX1
2Skp, chain 12
3Skp, chain 22
4Skp, chain 32

Entities:

Entity 1, OmpX 149 residues - Formula weight is not available

native processed E. coli OmpX (rseidues 24 - 172) + initiator methionine

1   METALATHRSERTHRVALTHRGLYGLYTYR
2   ALAGLNSERASPMETGLNGLYVALMETASN
3   LYSTHRASNGLYPHEASNLEULYSTYRARG
4   TYRGLUGLNGLNASNASNPROLEUGLYVAL
5   ILEGLYSERPHETHRTYRTHRGLULYSASP
6   ARGTHRALASERSERGLYASPTYRASNLYS
7   ASNGLNTYRTYRGLYILETHRALAGLYPRO
8   ALATYRARGILEASNASPTRPALASERILE
9   TYRGLYVALVALGLYVALGLYTYRGLYLYS
10   PHEGLNTHRTHRGLUTYRPROTHRTYRLYS
11   HISASPTHRSERASPTYRGLYPHESERTYR
12   GLYALAGLYLEUGLNPHEASNPROMETGLU
13   ASNVALALALEUASPPHESERTYRGLUGLN
14   SERARGILEARGSERVALASPVALGLYTHR
15   TRPILEALAGLYVALGLYTYRARGPHE

Entity 2, Skp, chain 1 234 residues - Formula weight is not available

native processed E. coli SKP (residues 21 - 161) hexahistidin-tag and Thrombin cleavage site (coming from pET28b)

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALAASPLYSILEALAILEVALASNMET
4   GLYSERLEUPHEGLNGLNVALALAGLNLYS
5   THRGLYVALSERASNTHRLEUGLUASNGLU
6   PHELYSGLYARGALASERGLULEUGLNARG
7   METGLUTHRASPLEUGLNALALYSMETLYS
8   LYSLEUGLNSERMETLYSALAGLYSERASP
9   ARGTHRLYSLEUGLULYSASPVALMETALA
10   GLNARGGLNTHRPHEALAGLNLYSALAGLN
11   ALAPHEGLUGLNASPARGALAARGARGSER
12   ASNGLUGLUARGGLYLYSLEUVALTHRARG
13   ILEGLNTHRALAVALLYSSERVALALAASN
14   SERGLNASPILEASPLEUVALVALASPALA
15   ASNALAVALALATYRASNSERSERASPVAL
16   LYSASPILETHRALAASPVALLEULYSGLN
17   VALLYSILETYRGLYVALVALGLYVALGLY
18   TYRGLYLYSPHEGLNGLNTHRGLUASNGLN
19   GLYLEUASNARGTHRALASERASNSERASP
20   TYRGLYPHESERTYRGLYALAGLYMETGLN
21   PHEASNPROILEGLUASNVALALALEUASP
22   PHESERTYRGLUGLNSERARGILEARGASN
23   VALASPVALGLYTHRTRPILEALAGLYVAL
24   GLYTYRARGPHE

Samples:

sample_1: Escherichia Coli OmpX, [U-13C; U-15N; U-2H], 0.6 – 1.05 mM; Escherichia Coli Skp (trimer), [U-99% 2H], 0.6 – 1.05 mM; H2O 95%; D2O 5%; MES 25 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bartels et al., Bruker Biospin, Guntert, Keller and Wuthrich - chemical shift assignment, collection, data analysis, processing

NMR spectrometers:

  • Bruker AscendII 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP P25253 P0AEU7
EMBL CSY35436
GB KFS26214
AlphaFold P25253 P11457

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