BMRB Entry 16297
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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/BMR16297
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Title: AIDA-1 SAM domain tandem PubMed: 19666031
Deposition date: 2009-05-12 Original release date: 2009-09-04
Authors: Donaldson, Logan; Kurabi, Arwa
Citation: Kurabi, Arwa; Brener, Stacey; Mobli, Mehdi; Kwan, Jamie; Donaldson, Logan. "A Nuclear Localization Signal at the SAM-SAM Domain Interface of AIDA-1 Suggests a Requirement for Domain Uncoupling Prior to Nuclear Import" J. Mol. Biol. 392, 1168-1177 (2009).
Assembly members:
AIDA-1 SAM domain, polymer, 148 residues, 15101.473 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):
AIDA-1 SAM domain: MHHHHHHLVPRGSVQTVGQW
LESIGLPQYENHLMANGFDN
VQAMGSNVMEDQDLLEIGIL
NSGHRQRILQAIQLLPKMRP
IGHDGAHPTSVAEWLDSIEL
GDYTKAFLINGYTSMDLLKK
IAEVELINVLKINLIGHRKR
ILASLGDR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 510 |
| 15N chemical shifts | 121 |
| 1H chemical shifts | 791 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AIDA-1 SAM domain | 1 |
Entities:
Entity 1, AIDA-1 SAM domain 148 residues - 15101.473 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | LEU | VAL | PRO | ||||
| 2 | ARG | GLY | SER | VAL | GLN | THR | VAL | GLY | GLN | TRP | ||||
| 3 | LEU | GLU | SER | ILE | GLY | LEU | PRO | GLN | TYR | GLU | ||||
| 4 | ASN | HIS | LEU | MET | ALA | ASN | GLY | PHE | ASP | ASN | ||||
| 5 | VAL | GLN | ALA | MET | GLY | SER | ASN | VAL | MET | GLU | ||||
| 6 | ASP | GLN | ASP | LEU | LEU | GLU | ILE | GLY | ILE | LEU | ||||
| 7 | ASN | SER | GLY | HIS | ARG | GLN | ARG | ILE | LEU | GLN | ||||
| 8 | ALA | ILE | GLN | LEU | LEU | PRO | LYS | MET | ARG | PRO | ||||
| 9 | ILE | GLY | HIS | ASP | GLY | ALA | HIS | PRO | THR | SER | ||||
| 10 | VAL | ALA | GLU | TRP | LEU | ASP | SER | ILE | GLU | LEU | ||||
| 11 | GLY | ASP | TYR | THR | LYS | ALA | PHE | LEU | ILE | ASN | ||||
| 12 | GLY | TYR | THR | SER | MET | ASP | LEU | LEU | LYS | LYS | ||||
| 13 | ILE | ALA | GLU | VAL | GLU | LEU | ILE | ASN | VAL | LEU | ||||
| 14 | LYS | ILE | ASN | LEU | ILE | GLY | HIS | ARG | LYS | ARG | ||||
| 15 | ILE | LEU | ALA | SER | LEU | GLY | ASP | ARG |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 1.1 mM; D2O 10%; H2O 90%; sodium azide 0.05%; sodium phosphate 5 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian Uniform NMR System 600 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts