BMRB Entry 16375
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16375
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Title: Solution Structure of C-terminal domain of oxidized NleG2-3 (residue 90-191) from Pathogenic E. coli O157:H7. Northeast Structural Genomics Consortium and Midwest Center for Structural Genomics target ET109A
Deposition date: 2009-06-29 Original release date: 2009-09-15
Authors: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Semest, Anthony; Claude, Marie; Singer, Alexander; Edwards, Aled; Savchenko, Alexei; Arrowsmith, Cheryl
Citation: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Semest, Anthony; Claude, Marie; Coomes, Brian; Edwards, Aled; Singer, Alexander; Arrowsmith, Cheryl; Savchenko, Alexei. "Pathogenic E. coli O157:H7 NleG family of Type 3 secretion effectors features a common C-terminal U-box domain and E3 ubiquitin ligase activity" Not known ., .-..
Assembly members:
NleG2-3, polymer, 102 residues, 11290.936 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NleG2-3: SQESIQNKISQCKFSVCPER
LQCPLEAIQCPITLEQPEKG
IFVKNSDGSDVCTLFDAAAF
SRLVGEGLPHPLTREPITAS
IIVKHEECIYDDTRGNFIIK
GN
- assigned_chemical_shifts
- RDCs
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 432 |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 721 |
| residual dipolar couplings | 166 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NleG2-3 | 1 |
Entities:
Entity 1, NleG2-3 102 residues - 11290.936 Da.
| 1 | SER | GLN | GLU | SER | ILE | GLN | ASN | LYS | ILE | SER | ||||
| 2 | GLN | CYS | LYS | PHE | SER | VAL | CYS | PRO | GLU | ARG | ||||
| 3 | LEU | GLN | CYS | PRO | LEU | GLU | ALA | ILE | GLN | CYS | ||||
| 4 | PRO | ILE | THR | LEU | GLU | GLN | PRO | GLU | LYS | GLY | ||||
| 5 | ILE | PHE | VAL | LYS | ASN | SER | ASP | GLY | SER | ASP | ||||
| 6 | VAL | CYS | THR | LEU | PHE | ASP | ALA | ALA | ALA | PHE | ||||
| 7 | SER | ARG | LEU | VAL | GLY | GLU | GLY | LEU | PRO | HIS | ||||
| 8 | PRO | LEU | THR | ARG | GLU | PRO | ILE | THR | ALA | SER | ||||
| 9 | ILE | ILE | VAL | LYS | HIS | GLU | GLU | CYS | ILE | TYR | ||||
| 10 | ASP | ASP | THR | ARG | GLY | ASN | PHE | ILE | ILE | LYS | ||||
| 11 | GLY | ASN |
Samples:
sample_1: NleG, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H20 90%; D20 10%
sample_2: NleG, [U-7% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H20 90%; D20 10%
sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D IPAP-J HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MDDGUI v1.0, Gutmanas and Arrowsmith - processing
SPARKY v3.95, Goddard - data analysis, peak picking
FAWN v1.0, Lemak and Arrowsmith - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment
PSVS, Bhattacharya and Montelione - NMR structure quality assessment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 16374 |
| PDB | |
| DBJ | BAB35417 BAB35579 BAI25254 BAI35676 |
| EMBL | CTT86631 CTZ63346 CTZ65248 CTZ72681 CTZ98837 |
| GB | AAG56215 AAG56388 ACI35420 ACT71854 ADD56326 |
| REF | NP_310021 NP_310183 WP_001131656 WP_001131657 WP_001131658 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts