BMRB Entry 16824
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16824
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Title: Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector PubMed: 18650809
Deposition date: 2010-04-01 Original release date: 2010-05-05
Authors: Cheng, Hui-Chun; Skehan, Brian; Campellone, Kenneth; Leong, John; Rosen, Michael
Citation: Cheng, Hui-Chun; Skehan, Brian; Campellone, Kenneth; Leong, John; Rosen, Michael. "Structural Mechanism of WASP Activation by the Enterohaemorrhagic E. coli Effector EspFU" Nature 454, 1009-1013 (2008).
Assembly members:
GBD, polymer, 72 residues, 8128.980 Da.
R33, polymer, 36 residues, 4070.712 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
GBD: GHMSGFKHVSHVGWDPQNGF
DVNNLDPDLRSLFSRAGISE
AQLTDAETSKLIYDFIEDQG
GLEAVRQEMRRQ
R33: GHMLPDVAQRLMQHLAEHGI
QPARNMAEHIPPAPNW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 444 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 728 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GBD | 1 |
| 2 | R33 | 2 |
Entities:
Entity 1, GBD 72 residues - 8128.980 Da.
| 1 | GLY | HIS | MET | SER | GLY | PHE | LYS | HIS | VAL | SER | ||||
| 2 | HIS | VAL | GLY | TRP | ASP | PRO | GLN | ASN | GLY | PHE | ||||
| 3 | ASP | VAL | ASN | ASN | LEU | ASP | PRO | ASP | LEU | ARG | ||||
| 4 | SER | LEU | PHE | SER | ARG | ALA | GLY | ILE | SER | GLU | ||||
| 5 | ALA | GLN | LEU | THR | ASP | ALA | GLU | THR | SER | LYS | ||||
| 6 | LEU | ILE | TYR | ASP | PHE | ILE | GLU | ASP | GLN | GLY | ||||
| 7 | GLY | LEU | GLU | ALA | VAL | ARG | GLN | GLU | MET | ARG | ||||
| 8 | ARG | GLN |
Entity 2, R33 36 residues - 4070.712 Da.
| 1 | GLY | HIS | MET | LEU | PRO | ASP | VAL | ALA | GLN | ARG | ||||
| 2 | LEU | MET | GLN | HIS | LEU | ALA | GLU | HIS | GLY | ILE | ||||
| 3 | GLN | PRO | ALA | ARG | ASN | MET | ALA | GLU | HIS | ILE | ||||
| 4 | PRO | PRO | ALA | PRO | ASN | TRP |
Samples:
sample_1: GBD/R33 complex, [U-100% 13C; U-100% 15N], 1 – 1.5 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_2: GBD/R33 complex, [U-100% 13C; U-100% 15N], 1 – 1.5 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; D2O 100%
sample_3: R33 1 mM; GBD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; NaCl 100 mM; DTT 1 mM; EDTA 1 mM; D2O 100%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 13C-filtered NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
ARIA v2.1, Linge, O, . - refinement, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRView, Johnson, One Moon Scientific - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts