BMRB Entry 7426

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7426

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Title:
Yersinia pseudotuberculosis type III secretion effector YopE.
Deposition date:
2008-07-17
Original release date:
2008-08-13
Authors:
Rodgers, Loren; Gamez, Alicia; Riek, Roland; Ghosh, Partho
Citation:

Citation: Rodgers, Loren; Gamez, Alicia; Riek, Roland; Ghosh, Partho. "The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE."  J. Biol. Chem. 283, 20857-20863 (2008).
PubMed: 18502763

Assembly members:

Assembly members:
YopE, polymer, 227 residues, 24052.1 Da.

Natural source:

Natural source:   Common Name: Yersinia pseudotuberculosis   Taxonomy ID: 633   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pseudotuberculosis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YopE: MKISSFISTSLPLPTSVSGS SSVGEMSGRSVSQQTSDQYA NNLAGRTESPQGSSLASRII ERLSSVAHSVIGFIQRMFSE GSHKPVVTPAPTPAQMPSPT SFSDSIKQLAAETLPKYMQQ LNSLDAEMLQKNHDQFATGS GPLRGSITQCQGLMQFCGGE LQAEASAILNTPVCGIPFSQ WGTIGGAASAYVASGVDLTQ AANEIKGLAQQMQKLLSLML EHHHHHH

Data sets:
Data typeCount
13C chemical shifts84
15N chemical shifts193
1H chemical shifts193

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YopE1

Entities:

Entity 1, YopE 227 residues - 24052.1 Da.

1   METLYSILESERSERPHEILESERTHRSER
2   LEUPROLEUPROTHRSERVALSERGLYSER
3   SERSERVALGLYGLUMETSERGLYARGSER
4   VALSERGLNGLNTHRSERASPGLNTYRALA
5   ASNASNLEUALAGLYARGTHRGLUSERPRO
6   GLNGLYSERSERLEUALASERARGILEILE
7   GLUARGLEUSERSERVALALAHISSERVAL
8   ILEGLYPHEILEGLNARGMETPHESERGLU
9   GLYSERHISLYSPROVALVALTHRPROALA
10   PROTHRPROALAGLNMETPROSERPROTHR
11   SERPHESERASPSERILELYSGLNLEUALA
12   ALAGLUTHRLEUPROLYSTYRMETGLNGLN
13   LEUASNSERLEUASPALAGLUMETLEUGLN
14   LYSASNHISASPGLNPHEALATHRGLYSER
15   GLYPROLEUARGGLYSERILETHRGLNCYS
16   GLNGLYLEUMETGLNPHECYSGLYGLYGLU
17   LEUGLNALAGLUALASERALAILELEUASN
18   THRPROVALCYSGLYILEPROPHESERGLN
19   TRPGLYTHRILEGLYGLYALAALASERALA
20   TYRVALALASERGLYVALASPLEUTHRGLN
21   ALAALAASNGLUILELYSGLYLEUALAGLN
22   GLNMETGLNLYSLEULEUSERLEUMETLEU
23   GLUHISHISHISHISHISHIS

Samples:

Free_YopE: YopE, [U-95% 13C; U-95% 15N; 90% 2H], 0.08 – 0.2 mM; D2O, [U-99.9% 2H], 5%; H2O 95%; sodium phosphate pH6.1 45 mM

all_samples: pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCFree_YopEisotropicall_samples
3D HNCAFree_YopEisotropicall_samples
3D 1H-15N NOESYFree_YopEisotropicall_samples

Software:

XEASY, Bartels et al., Keller and Wuthrich - chemical shift assignment, chemical shift calculation, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15878 7427
EMBL CAA68609 CAB54883 CAF25368
GB AAA27672 AAC62587 AAC69818 AAS58592 ABG16295
REF NP_395143 NP_857762 NP_857967 NP_995401 WP_002213405
SP P08008 P31493
AlphaFold P08008 P31493

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