BMRB Entry 16610
Click here to enlarge.
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/BMR16610
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the N-terminal domain (residues 1-111) of Brugia malayi asparaginyl-tRNA synthetase
Deposition date: 2009-11-16 Original release date: 2012-08-03
Authors: Volkman, B.; Peterson, F.; Kron, M.
Citation: Kron, Michael; Volkman, Brian; Peterson, Francis. "TBD" To be published ., .-..
Assembly members:
AsnRS, polymer, 113 residues, 12667.689 Da.
Natural source: Common Name: B. malayi Taxonomy ID: 6279 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Brugia malayi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
AsnRS: GSMTVYICPETGDDGNDGSE
LKPLRTLYQAMIITKSSKGD
FLIRTKKDGKQVWEAASKTA
LKKSWKRYEQEMLKNEKVAA
KMLEKDATEVGVKAALEEAK
KVQIELDTSLSYI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 505 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 846 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AsnRS | 1 |
Entities:
Entity 1, AsnRS 113 residues - 12667.689 Da.
| 1 | GLY | SER | MET | THR | VAL | TYR | ILE | CYS | PRO | GLU | ||||
| 2 | THR | GLY | ASP | ASP | GLY | ASN | ASP | GLY | SER | GLU | ||||
| 3 | LEU | LYS | PRO | LEU | ARG | THR | LEU | TYR | GLN | ALA | ||||
| 4 | MET | ILE | ILE | THR | LYS | SER | SER | LYS | GLY | ASP | ||||
| 5 | PHE | LEU | ILE | ARG | THR | LYS | LYS | ASP | GLY | LYS | ||||
| 6 | GLN | VAL | TRP | GLU | ALA | ALA | SER | LYS | THR | ALA | ||||
| 7 | LEU | LYS | LYS | SER | TRP | LYS | ARG | TYR | GLU | GLN | ||||
| 8 | GLU | MET | LEU | LYS | ASN | GLU | LYS | VAL | ALA | ALA | ||||
| 9 | LYS | MET | LEU | GLU | LYS | ASP | ALA | THR | GLU | VAL | ||||
| 10 | GLY | VAL | LYS | ALA | ALA | LEU | GLU | GLU | ALA | LYS | ||||
| 11 | LYS | VAL | GLN | ILE | GLU | LEU | ASP | THR | SER | LEU | ||||
| 12 | SER | TYR | ILE |
Samples:
sample_1: AsnRS, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 53 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY (AROMATIC) | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis
GARANT v2.2, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
TOPSPIN v2.1, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance III 500 MHz
Related Database Links:
| PDB | |
| EMBL | CDQ01803 CDQ01804 CDQ05032 CDQ06500 |
| GB | AAA27849 AAA27852 |
| REF | XP_001898693 XP_002372115 |
| SP | P10723 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts