BMRB Entry 34175
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34175
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 lipase binding domain LID1 of foldase from Pseudomonas aeruginosa PubMed: 32107397
Deposition date: 2017-08-29 Original release date: 2018-12-05
Authors: Viegas, A.; Jaeger, K.; Etzkorn, M.; Gohlke, H.; Verma, N.; Dollinger, P.; Kovacic, F.
Citation: Viegas, Aldino; Dollinger, Peter; Verma, Neha; Kubiak, Jakub; Viennet, Thibault; Seidel, Claus; Gohlke, Holger; Etzkorn, Manuel; Kovacic, Filip; Jaeger, Karl-Erich. "Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation" Sci. Rep. 10, 3578-3578 (2020).
Assembly members:
entity_1, polymer, 89 residues, 10108.320 Da.
Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 208964 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MGHHHHHHLPTSFRGTSVDG
SFSVDASGNLLITRDIRNLF
DYFLSAVGEEPLQQSLDRLR
AYIAAELQEPARGQALALMQ
QYIDYKKEL
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 314 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 547 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 89 residues - 10108.320 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | LEU | PRO | ||||
| 2 | THR | SER | PHE | ARG | GLY | THR | SER | VAL | ASP | GLY | ||||
| 3 | SER | PHE | SER | VAL | ASP | ALA | SER | GLY | ASN | LEU | ||||
| 4 | LEU | ILE | THR | ARG | ASP | ILE | ARG | ASN | LEU | PHE | ||||
| 5 | ASP | TYR | PHE | LEU | SER | ALA | VAL | GLY | GLU | GLU | ||||
| 6 | PRO | LEU | GLN | GLN | SER | LEU | ASP | ARG | LEU | ARG | ||||
| 7 | ALA | TYR | ILE | ALA | ALA | GLU | LEU | GLN | GLU | PRO | ||||
| 8 | ALA | ARG | GLY | GLN | ALA | LEU | ALA | LEU | MET | GLN | ||||
| 9 | GLN | TYR | ILE | ASP | TYR | LYS | LYS | GLU | LEU |
Samples:
sample_1: Lipase-interaction domain 1, [U-13C; U-15N], 450 uM; Sodium Phosphate buffer 20 mM
sample_2: Lipase-interaction domain 1, [U-13C; U-15N], 900 uM; Sodium Phosphate buffer 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 303 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, data analysis, processing
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
AMBER, Case, etc. - geometry optimization, refinement
NMR spectrometers:
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts