BMRB Entry 10251
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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/BMR10251
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Title: Solution structure of the C-terminal PH domain of human pleckstrin 2
Deposition date: 2008-11-20 Original release date: 2009-11-20
Authors: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal PH domain of human pleckstrin 2" . ., .-..
Assembly members:
PH domain, polymer, 129 residues,  Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: Cell free synthesis
Entity Sequences (FASTA):
PH domain: GSSGSSGSLSTVELSGTVVK
QGYLAKQGHKRKNWKVRRFV
LRKDPAFLHYYDPSKEENRP
VGGFSLRGSLVSALEDNGVP
TGVKGNVQGNLFKVITKDDT
HYYIQASSKAERAEWIEAIK
KLTSGPSSG
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 550 | 
| 15N chemical shifts | 124 | 
| 1H chemical shifts | 855 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | PH domain | 1 | 
Entities:
Entity 1, PH domain 129 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | SER | LEU | SER | ||||
| 2 | THR | VAL | GLU | LEU | SER | GLY | THR | VAL | VAL | LYS | ||||
| 3 | GLN | GLY | TYR | LEU | ALA | LYS | GLN | GLY | HIS | LYS | ||||
| 4 | ARG | LYS | ASN | TRP | LYS | VAL | ARG | ARG | PHE | VAL | ||||
| 5 | LEU | ARG | LYS | ASP | PRO | ALA | PHE | LEU | HIS | TYR | ||||
| 6 | TYR | ASP | PRO | SER | LYS | GLU | GLU | ASN | ARG | PRO | ||||
| 7 | VAL | GLY | GLY | PHE | SER | LEU | ARG | GLY | SER | LEU | ||||
| 8 | VAL | SER | ALA | LEU | GLU | ASP | ASN | GLY | VAL | PRO | ||||
| 9 | THR | GLY | VAL | LYS | GLY | ASN | VAL | GLN | GLY | ASN | ||||
| 10 | LEU | PHE | LYS | VAL | ILE | THR | LYS | ASP | ASP | THR | ||||
| 11 | HIS | TYR | TYR | ILE | GLN | ALA | SER | SER | LYS | ALA | ||||
| 12 | GLU | ARG | ALA | GLU | TRP | ILE | GLU | ALA | ILE | LYS | ||||
| 13 | LYS | LEU | THR | SER | GLY | PRO | SER | SER | GLY | 
Samples:
sample_1: PH domain, [U-13C; U-15N], 1.24 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 | 
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 | 
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.913, Kobayashi, N. - data analysis
CYANA v1.0.7, Guentert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
 
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