BMRB Entry 7427
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7427
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Title: Yersinia pseudotuberculosis type III secretion effector YopE. PubMed: 18502763
Deposition date: 2008-07-17 Original release date: 2008-08-13
Authors: Rodgers, Loren; Gamez, Alicia; Riek, Roland; Ghosh, Partho
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).
Assembly members:
YopE, polymer, 227 residues, 24052.1 Da.
YopE_effector_domain, polymer, 149 residues, 15876.0 Da.
Natural source: Common Name: Yersinia pseudotuberculosis Taxonomy ID: 633 Superkingdom: Bacteria Kingdom: not available Genus/species: Yersinia pseudotuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
YopE: MKISSFISTSLPLPTSVSGS
SSVGEMSGRSVSQQTSDQYA
NNLAGRTESPQGSSLASRII
ERLSSVAHSVIGFIQRMFSE
GSHKPVVTPAPTPAQMPSPT
SFSDSIKQLAAETLPKYMQQ
LNSLDAEMLQKNHDQFATGS
GPLRGSITQCQGLMQFCGGE
LQAEASAILNTPVCGIPFSQ
WGTIGGAASAYVASGVDLTQ
AANEIKGLAQQMQKLLSLML
EHHHHHH
YopE_effector_domain: MEGSHKPVVTPAPTPAQMPS
PTSFSDSIKQLAAETLPKYM
QQLNSLDAEMLQKNHDQFAT
GSGPLRGSITQCQGLMQFCG
GELQAEASAILNTPVCGIPF
SQWGTIGGAASAYVASGVDL
TQAANEIKGLAQQMQKLLSL
MLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 129 |
| 1H chemical shifts | 129 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YopE | 1 |
| 2 | YopE effector domain | 2 |
Entities:
Entity 1, YopE 227 residues - 24052.1 Da.
| 1 | MET | LYS | ILE | SER | SER | PHE | ILE | SER | THR | SER | ||||
| 2 | LEU | PRO | LEU | PRO | THR | SER | VAL | SER | GLY | SER | ||||
| 3 | SER | SER | VAL | GLY | GLU | MET | SER | GLY | ARG | SER | ||||
| 4 | VAL | SER | GLN | GLN | THR | SER | ASP | GLN | TYR | ALA | ||||
| 5 | ASN | ASN | LEU | ALA | GLY | ARG | THR | GLU | SER | PRO | ||||
| 6 | GLN | GLY | SER | SER | LEU | ALA | SER | ARG | ILE | ILE | ||||
| 7 | GLU | ARG | LEU | SER | SER | VAL | ALA | HIS | SER | VAL | ||||
| 8 | ILE | GLY | PHE | ILE | GLN | ARG | MET | PHE | SER | GLU | ||||
| 9 | GLY | SER | HIS | LYS | PRO | VAL | VAL | THR | PRO | ALA | ||||
| 10 | PRO | THR | PRO | ALA | GLN | MET | PRO | SER | PRO | THR | ||||
| 11 | SER | PHE | SER | ASP | SER | ILE | LYS | GLN | LEU | ALA | ||||
| 12 | ALA | GLU | THR | LEU | PRO | LYS | TYR | MET | GLN | GLN | ||||
| 13 | LEU | ASN | SER | LEU | ASP | ALA | GLU | MET | LEU | GLN | ||||
| 14 | LYS | ASN | HIS | ASP | GLN | PHE | ALA | THR | GLY | SER | ||||
| 15 | GLY | PRO | LEU | ARG | GLY | SER | ILE | THR | GLN | CYS | ||||
| 16 | GLN | GLY | LEU | MET | GLN | PHE | CYS | GLY | GLY | GLU | ||||
| 17 | LEU | GLN | ALA | GLU | ALA | SER | ALA | ILE | LEU | ASN | ||||
| 18 | THR | PRO | VAL | CYS | GLY | ILE | PRO | PHE | SER | GLN | ||||
| 19 | TRP | GLY | THR | ILE | GLY | GLY | ALA | ALA | SER | ALA | ||||
| 20 | TYR | VAL | ALA | SER | GLY | VAL | ASP | LEU | THR | GLN | ||||
| 21 | ALA | ALA | ASN | GLU | ILE | LYS | GLY | LEU | ALA | GLN | ||||
| 22 | GLN | MET | GLN | LYS | LEU | LEU | SER | LEU | MET | LEU | ||||
| 23 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Entity 2, YopE effector domain 149 residues - 15876.0 Da.
| 1 | MET | GLU | GLY | SER | HIS | LYS | PRO | VAL | VAL | THR | ||||
| 2 | PRO | ALA | PRO | THR | PRO | ALA | GLN | MET | PRO | SER | ||||
| 3 | PRO | THR | SER | PHE | SER | ASP | SER | ILE | LYS | GLN | ||||
| 4 | LEU | ALA | ALA | GLU | THR | LEU | PRO | LYS | TYR | MET | ||||
| 5 | GLN | GLN | LEU | ASN | SER | LEU | ASP | ALA | GLU | MET | ||||
| 6 | LEU | GLN | LYS | ASN | HIS | ASP | GLN | PHE | ALA | THR | ||||
| 7 | GLY | SER | GLY | PRO | LEU | ARG | GLY | SER | ILE | THR | ||||
| 8 | GLN | CYS | GLN | GLY | LEU | MET | GLN | PHE | CYS | GLY | ||||
| 9 | GLY | GLU | LEU | GLN | ALA | GLU | ALA | SER | ALA | ILE | ||||
| 10 | LEU | ASN | THR | PRO | VAL | CYS | GLY | ILE | PRO | PHE | ||||
| 11 | SER | GLN | TRP | GLY | THR | ILE | GLY | GLY | ALA | ALA | ||||
| 12 | SER | ALA | TYR | VAL | ALA | SER | GLY | VAL | ASP | LEU | ||||
| 13 | THR | GLN | ALA | ALA | ASN | GLU | ILE | LYS | GLY | LEU | ||||
| 14 | ALA | GLN | GLN | MET | GLN | LYS | LEU | LEU | SER | LEU | ||||
| 15 | MET | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
YopE_effector_domain_sample: YopE, [U-95% 15N], 2.8 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | YopE_effector_domain_sample | isotropic | all_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 7426 |
| 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 | P31493 P08008 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts