BMRB Entry 16271
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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/BMR16271
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Title: A PH domain within OCRL bridges clathrin mediated membrane trafficking to phosphoinositide metabolis PubMed: 19536138
Deposition date: 2009-05-03 Original release date: 2009-06-25
Authors: Mao, Yuxin; Balkin, Daniel; Zoncu, Roberto; Erdmann, Kai; Tomasini, Livia; Hu, Fenghua; Jin, Moonsoon; Hodsdon, Michael; De Camilli, Pietro
Citation: Mao, Yuxin; Balkin, Daniel; Zoncu, Roberto; Erdmann, Kai; Tomasini, Livia; Hu, Fenghua; Jin, Moonsoon; Hodsdon, Michael; De Camilli, Pietro. "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism" EMBO J. 28, 1831-1842 (2009).
Assembly members:
PH domain, polymer, 372 residues, 41573.961 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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 424 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 899 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PH domain | 1 |
Entities:
Entity 1, PH domain 372 residues - 41573.961 Da.
| 1 | GLY | PRO | LEU | GLY | SER | MET | GLU | PRO | PRO | LEU | ||||
| 2 | PRO | VAL | GLY | ALA | GLN | PRO | LEU | ALA | THR | VAL | ||||
| 3 | GLU | GLY | MET | GLU | MET | LYS | GLY | PRO | LEU | ARG | ||||
| 4 | GLU | PRO | CYS | ALA | LEU | THR | LEU | ALA | GLN | ARG | ||||
| 5 | ASN | GLY | GLN | TYR | GLU | LEU | ILE | ILE | GLN | LEU | ||||
| 6 | HIS | GLU | LYS | GLU | GLN | HIS | VAL | GLN | ASP | ILE | ||||
| 7 | ILE | PRO | ILE | ASN | SER | HIS | PHE | ARG | CYS | VAL | ||||
| 8 | GLN | GLU | ALA | GLU | GLU | THR | LEU | LEU | ILE | ASP | ||||
| 9 | ILE | ALA | SER | ASN | SER | GLY | CYS | LYS | ILE | ARG | ||||
| 10 | VAL | GLN | GLY | ASP | TRP | ILE | ARG | GLU | ARG | ARG | ||||
| 11 | PHE | GLU | ILE | PRO | ASP | GLU | GLU | HIS | CYS | LEU | ||||
| 12 | LYS | PHE | LEU | SER | ALA | VAL | LEU | ALA | ALA | GLN | ||||
| 13 | LYS | ALA | GLN | SER | GLY | PRO | LEU | GLY | SER | MET | ||||
| 14 | GLU | PRO | PRO | LEU | PRO | VAL | GLY | ALA | GLN | PRO | ||||
| 15 | LEU | ALA | THR | VAL | GLU | GLY | MET | GLU | MET | LYS | ||||
| 16 | GLY | PRO | LEU | ARG | GLU | PRO | CYS | ALA | LEU | THR | ||||
| 17 | LEU | ALA | GLN | ARG | ASN | GLY | GLN | TYR | GLU | LEU | ||||
| 18 | ILE | ILE | GLN | LEU | HIS | GLU | LYS | GLU | GLN | HIS | ||||
| 19 | VAL | GLN | ASP | ILE | ILE | PRO | ILE | ASN | SER | HIS | ||||
| 20 | PHE | ARG | CYS | VAL | GLN | GLU | ALA | GLU | GLU | THR | ||||
| 21 | LEU | LEU | ILE | ASP | ILE | ALA | SER | ASN | SER | GLY | ||||
| 22 | CYS | LYS | ILE | ARG | VAL | GLN | GLY | ASP | TRP | ILE | ||||
| 23 | ARG | GLU | ARG | ARG | PHE | GLU | ILE | PRO | ASP | GLU | ||||
| 24 | GLU | HIS | CYS | LEU | LYS | PHE | LEU | SER | ALA | VAL | ||||
| 25 | LEU | ALA | ALA | GLN | LYS | ALA | GLN | SER | GLY | PRO | ||||
| 26 | LEU | GLY | SER | MET | GLU | PRO | PRO | LEU | PRO | VAL | ||||
| 27 | GLY | ALA | GLN | PRO | LEU | ALA | THR | VAL | GLU | GLY | ||||
| 28 | MET | GLU | MET | LYS | GLY | PRO | LEU | ARG | GLU | PRO | ||||
| 29 | CYS | ALA | LEU | THR | LEU | ALA | GLN | ARG | ASN | GLY | ||||
| 30 | GLN | TYR | GLU | LEU | ILE | ILE | GLN | LEU | HIS | GLU | ||||
| 31 | LYS | GLU | GLN | HIS | VAL | GLN | ASP | ILE | ILE | PRO | ||||
| 32 | ILE | ASN | SER | HIS | PHE | ARG | CYS | VAL | GLN | GLU | ||||
| 33 | ALA | GLU | GLU | THR | LEU | LEU | ILE | ASP | ILE | ALA | ||||
| 34 | SER | ASN | SER | GLY | CYS | LYS | ILE | ARG | VAL | GLN | ||||
| 35 | GLY | ASP | TRP | ILE | ARG | GLU | ARG | ARG | PHE | GLU | ||||
| 36 | ILE | PRO | ASP | GLU | GLU | HIS | CYS | LEU | LYS | PHE | ||||
| 37 | LEU | SER | ALA | VAL | LEU | ALA | ALA | GLN | LYS | ALA | ||||
| 38 | GLN | SER |
Samples:
sample_1: entity 1 mM; potassium phosphate 20 mM
sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-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 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts