BMRB Entry 17934
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17934
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Title: AIDA1 PTB domain PubMed: 23799029
Deposition date: 2011-09-12 Original release date: 2012-09-17
Authors: Donaldson, Logan
Citation: Smirnova, Ekaterina; Shanbhag, Riya; Kurabi, Arwa; Mobli, Mehdi; Kwan, Jamie; Donaldson, Logan. "Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein." PLoS ONE 8, e65605-e65605 (2013).
Assembly members:
AIDA1 PTB domain, polymer, 153 residues,   15011.303 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):
AIDA1 PTB domain: STPVQAWQHHPEKLIAQSCD
YKAAYLGSMLIKELRGTEST
QDACAKMRANCQKSTEQMKK
VPTIILSVSAKGVKFIDATN
KNIIAEHEIRNISCAAQDPE
DLSTFAYITKDLKSNHHYCH
VFTAFDVNLAAEIILTLGQA
FEVAYQLALQARK
- assigned_chemical_shifts
| Data type | Count | 
| 13C chemical shifts | 561 | 
| 15N chemical shifts | 134 | 
| 1H chemical shifts | 858 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | AIDA1 PTB domain | 1 | 
Entities:
Entity 1, AIDA1 PTB domain 153 residues - 15011.303 Da.
| 1 | SER | THR | PRO | VAL | GLN | ALA | TRP | GLN | HIS | HIS | ||||
| 2 | PRO | GLU | LYS | LEU | ILE | ALA | GLN | SER | CYS | ASP | ||||
| 3 | TYR | LYS | ALA | ALA | TYR | LEU | GLY | SER | MET | LEU | ||||
| 4 | ILE | LYS | GLU | LEU | ARG | GLY | THR | GLU | SER | THR | ||||
| 5 | GLN | ASP | ALA | CYS | ALA | LYS | MET | ARG | ALA | ASN | ||||
| 6 | CYS | GLN | LYS | SER | THR | GLU | GLN | MET | LYS | LYS | ||||
| 7 | VAL | PRO | THR | ILE | ILE | LEU | SER | VAL | SER | ALA | ||||
| 8 | LYS | GLY | VAL | LYS | PHE | ILE | ASP | ALA | THR | ASN | ||||
| 9 | LYS | ASN | ILE | ILE | ALA | GLU | HIS | GLU | ILE | ARG | ||||
| 10 | ASN | ILE | SER | CYS | ALA | ALA | GLN | ASP | PRO | GLU | ||||
| 11 | ASP | LEU | SER | THR | PHE | ALA | TYR | ILE | THR | LYS | ||||
| 12 | ASP | LEU | LYS | SER | ASN | HIS | HIS | TYR | CYS | HIS | ||||
| 13 | VAL | PHE | THR | ALA | PHE | ASP | VAL | ASN | LEU | ALA | ||||
| 14 | ALA | GLU | ILE | ILE | LEU | THR | LEU | GLY | GLN | ALA | ||||
| 15 | PHE | GLU | VAL | ALA | TYR | GLN | LEU | ALA | LEU | GLN | ||||
| 16 | ALA | ARG | LYS | 
Samples:
sample_1: AIDA1 PTB domain 0.8 mM; sodium azide 0.05%; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 | 
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 | 
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 | 
Software:
CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian Uniform NMR System 600 MHz
- Bruker Avance 900 MHz
Related Database Links:
| BMRB | 17428 | 
| PDB | |
| DBJ | BAE87950 | 
| GB | EDL21516 EDL21517 EDL21518 EDM16964 EDM16965 | 
| REF | XP_003126745 XP_005658157 XP_006077488 XP_013846696 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts
    
