BMRB Entry 17906
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17906
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Title: NMR structure of holo-ACPI domain from CurA module from Lyngbya majuscula PubMed: 22103656
Deposition date: 2011-09-01 Original release date: 2011-12-14
Authors: Busche, Alena; Gottstein, Daniel; Hein, Christopher; Ripin, Nina; Pader, Irina; Gu, Liangcai; Walsh, Christopher; Sherman, David; Loehr, Frank; Guentert, Peter; Doetsch, Volker
Citation: Busche, Alena; Gottstein, Daniel; Hein, Christopher; Ripin, Nina; Pader, Irina; Tufar, Peter; Eisman, Eli; Gu, Liangcai; Walsh, Christopher; Sherman, David; Lohr, Frank; Guntert, Peter; Dotsch, Volker. "Characterization of molecular interactions between ACP and halogenase domains in the Curacin A polyketide synthase." ACS Chem. Biol. 7, 378-386 (2012).
Assembly members:
entity, polymer, 99 residues, 11009.415 Da.
Natural source: Common Name: Lyngbya majuscula Taxonomy ID: 158786 Superkingdom: Bacteria Kingdom: not available Genus/species: Lyngbya majuscula
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: SGLVPRGSHMTPQVNQVNLS
EIKQVLKQQLAEALYTEESE
IAEDQKFVDLGLDSIVGVEW
TTTINQTYNLNLKATKLYDY
PTLLELSGYIAQILSSQGT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 418 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 688 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CurA | 1 |
Entities:
Entity 1, CurA 99 residues - 11009.415 Da.
| 1 | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | MET | ||||
| 2 | THR | PRO | GLN | VAL | ASN | GLN | VAL | ASN | LEU | SER | ||||
| 3 | GLU | ILE | LYS | GLN | VAL | LEU | LYS | GLN | GLN | LEU | ||||
| 4 | ALA | GLU | ALA | LEU | TYR | THR | GLU | GLU | SER | GLU | ||||
| 5 | ILE | ALA | GLU | ASP | GLN | LYS | PHE | VAL | ASP | LEU | ||||
| 6 | GLY | LEU | ASP | SER | ILE | VAL | GLY | VAL | GLU | TRP | ||||
| 7 | THR | THR | THR | ILE | ASN | GLN | THR | TYR | ASN | LEU | ||||
| 8 | ASN | LEU | LYS | ALA | THR | LYS | LEU | TYR | ASP | TYR | ||||
| 9 | PRO | THR | LEU | LEU | GLU | LEU | SER | GLY | TYR | ILE | ||||
| 10 | ALA | GLN | ILE | LEU | SER | SER | GLN | GLY | THR |
Samples:
Holo_ACPI_15N: CurA, [U-15N], 1 mM; D2O 5%; DSS 0.15 mM; Arginine 50 mM; Glutamate 50 mM; H2O 95%; D2O 5%
Holo_ACPI_13C: CurA, [U-13C], 1 mM; D2O 5%; DSS 0.15 mM; Arginine 50 mM; Glutamate 50 mM; H2O 95%; D2O 5%
Holo_ACPI_15N_13C: CurA, [U-15N],[U-13C], 1 mM; D2O 5%; DSS 0.15 mM; Arginine 50 mM; Glutamate 50 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 291 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Holo_ACPI_15N | isotropic | sample_conditions_1 |
| 3D HNCACB | Holo_ACPI_15N_13C | isotropic | sample_conditions_1 |
| 3D HNCO | Holo_ACPI_15N_13C | isotropic | sample_conditions_1 |
| 3D HNCACO | Holo_ACPI_15N_13C | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH-TOCSY | Holo_ACPI_15N_13C | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH-TOCSY | Holo_ACPI_15N_13C | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | Holo_ACPI_15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | Holo_ACPI_13C | isotropic | sample_conditions_1 |
| (H)CB(CGCC-TOCSY)Har | Holo_ACPI_15N_13C | isotropic | sample_conditions_1 |
Software:
CYANA v2.1 and 3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 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