BMRB Entry 25886
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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/BMR25886
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Title: Solution structure of acyl carrier protein LipD from Actinoplanes friuliensis PubMed: 28187530
Deposition date: 2015-11-10 Original release date: 2016-11-14
Authors: Paul, Subrata; Ishida, Hiroaki; Liu, Zhihong; Nguyen, Leonard; Vogel, Hans
Citation: Paul, Subrata; Ishida, Hiroaki; Nguyen, Leonard; Liu, Zhihong; Vogel, Hans. "Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics" Protein Sci. 26, 946-959 (2017).
Assembly members:
entity, polymer, 90 residues, 9504.713 Da.
Natural source: Common Name: high GC gram+ Taxonomy ID: 196914 Superkingdom: Bacteria Kingdom: not available Genus/species: Actinoplanes friuliensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GHMSDLSTAPTLDSLRVWLV
DCVAGHLGLDAATIATDLPL
TSYGLDSVYALSIAAELEDH
LDVSLDPTLIWDHPTIDALS
TALVAELRSA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 375 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 599 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 90 residues - 9504.713 Da.
| 1 | GLY | HIS | MET | SER | ASP | LEU | SER | THR | ALA | PRO | |
| 2 | THR | LEU | ASP | SER | LEU | ARG | VAL | TRP | LEU | VAL | |
| 3 | ASP | CYS | VAL | ALA | GLY | HIS | LEU | GLY | LEU | ASP | |
| 4 | ALA | ALA | THR | ILE | ALA | THR | ASP | LEU | PRO | LEU | |
| 5 | THR | SER | TYR | GLY | LEU | ASP | SER | VAL | TYR | ALA | |
| 6 | LEU | SER | ILE | ALA | ALA | GLU | LEU | GLU | ASP | HIS | |
| 7 | LEU | ASP | VAL | SER | LEU | ASP | PRO | THR | LEU | ILE | |
| 8 | TRP | ASP | HIS | PRO | THR | ILE | ASP | ALA | LEU | SER | |
| 9 | THR | ALA | LEU | VAL | ALA | GLU | LEU | ARG | SER | ALA |
Samples:
sample_1: entity, [U-15N], 0.5 mM; D2O, [U-2H], 10%; H2O 90%; sodium azide 0.03%; potassium chloride 100 mM; DTT 10 mM; DSS 0.5 mM; potassium phosphate 50 mM
sample_2: entity, [U-13C; U-15N], 0.5 mM; potassium chloride 100 mM; DTT 10 mM; sodium azide 0.03%; D2O, [U-2H], 10%; H2O 90%; DSS 0.5 mM; potassium phosphate 50 mM
sample_3: entity, [U-13C; U-15N], 0.5 mM; potassium phosphate 50 mM; potassium chloride 100 mM; DTT 10 mM; sodium azide 0.03%; DSS 0.5 mM; D2O, [U-2H], 100%
sample_4: entity 1 mM; potassium phosphate 50 mM; potassium chloride 100 mM; sodium azide 0.03%; DTT 10 mM; DSS 0.5 mM; D2O, [U-2H], 100%
sample_5: entity, [U-15N], 0.5 mM; D2O, [U-2H], 10%; H2O 90%; potassium chloride 130 mM; potassium phosphate 50 mM; DTT 10 mM; DSS 0.5 mM; PMSF 0.03%; Pf1 phage 15 mg/mL
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 297 K
sample_conditions_2: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 297 K
sample_conditions_3: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 297 K
sample_conditions_4: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 297 K
sample_conditions_5: ionic strength: 130 mM; pH*: 6.0; pressure: 1 atm; temperature: 297 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_2 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_4 |
| 2D DQF-COSY | sample_4 | isotropic | sample_conditions_4 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_4 |
| IPAP-1H-15N-HSQC | sample_5 | anisotropic | sample_conditions_5 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_3 |
| IPAP-1H-15N-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution
X-PLOR_NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts