BMRB Entry 16137
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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/BMR16137
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Title: NMR structure of the first SAM domain from AIDA1
Deposition date: 2009-01-27 Original release date: 2009-10-20
Authors: Donaldson, Logan
Citation: Donaldson, Logan. "NMR structure of the first SAM domain from AIDA1" .
Assembly members:
AIDA1_SAM1, polymer, 103 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: recombinant technology Host organism: Escherichia coli Vector: pDEST586
Entity Sequences (FASTA):
AIDA1_SAM1: GSDITSLYKKAGSEMNGPRC
PVQTVGQWLESIGLPQYENH
LMANGFDNVQFMGSNVMEDQ
DLLEIGILNSGHRQRILQAI
QLLPKMRPIGHDGYHPTSVA
EWL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 257 |
15N chemical shifts | 61 |
1H chemical shifts | 411 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | AIDA1_SAM1 | 1 |
Entities:
Entity 1, AIDA1_SAM1 103 residues - Formula weight is not available
1 | GLY | SER | ASP | ILE | THR | SER | LEU | TYR | LYS | LYS | ||||
2 | ALA | GLY | SER | GLU | MET | ASN | GLY | PRO | ARG | CYS | ||||
3 | PRO | VAL | GLN | THR | VAL | GLY | GLN | TRP | LEU | GLU | ||||
4 | SER | ILE | GLY | LEU | PRO | GLN | TYR | GLU | ASN | HIS | ||||
5 | LEU | MET | ALA | ASN | GLY | PHE | ASP | ASN | VAL | GLN | ||||
6 | PHE | MET | GLY | SER | ASN | VAL | MET | GLU | ASP | GLN | ||||
7 | ASP | LEU | LEU | GLU | ILE | GLY | ILE | LEU | ASN | SER | ||||
8 | GLY | HIS | ARG | GLN | ARG | ILE | LEU | GLN | ALA | ILE | ||||
9 | GLN | LEU | LEU | PRO | LYS | MET | ARG | PRO | ILE | GLY | ||||
10 | HIS | ASP | GLY | TYR | HIS | PRO | THR | SER | VAL | ALA | ||||
11 | GLU | TRP | LEU |
Samples:
NMRsample: AIDA1 SAM1, [U-98% 13C; U-98% 15N], 0.8 mM; D2O 10%; H2O 90%; sodium chloride 150 mM; sodium phosphate 20 mM; sodium azide 0.05%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.8; pressure: 1.0 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | NMRsample | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | NMRsample | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | NMRsample | isotropic | sample_conditions_1 |
3D C(CO)NH | NMRsample | isotropic | sample_conditions_1 |
3D HNCO | NMRsample | isotropic | sample_conditions_1 |
3D HNCACB | NMRsample | isotropic | sample_conditions_1 |
3D H(CCO)NH | NMRsample | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | NMRsample | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | NMRsample | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.21, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMRView v5, Johnson, One Moon Scientific - peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian NMRS 600 MHz
Related Database Links:
GB | AY283057.2 AAF80756 AAH26313 AAH68451 AAH98373 AAI49112 |
PDB | |
DBJ | BAE01854 BAG57507 BAI47262 |
EMBL | CAH91693 |
REF | NP_001095761 NP_001121558 NP_001125990 NP_001170868 NP_001190995 |
TPG | DAA29568 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts