BMRB Entry 19479
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19479
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Title: Solution Structure of an Active Site Mutant Pepitdyl Carrier Protein PubMed: 24704508
Deposition date: 2013-09-06 Original release date: 2014-04-22
Authors: Tufar, Peter; Rahighi, Simin; Kraas, Femke; Kirchner, Donata; Loehr, Frank; Henrich, Erik; Koepke, Juergen; Dikic, Ivan; Guentert, Peter; Marahiel, Mohamed; Doetsch, Volker
Citation: Tufar, Peter; Rahighi, Simin; Kraas, Femke; Kirchner, Donata; Lohr, Frank; Henrich, Erik; Kopke, Jurgen; Dikic, Ivan; Guntert, Peter; Marahiel, Mohamed; Dotsch, Volker. "Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification." Chem. Biol. 21, 552-562 (2014).
Assembly members:
PCP, polymer, 90 residues, 9972.533 Da.
Natural source: Common Name: Bacillus brevis Taxonomy ID: 1393 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus brevis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PCP: PVTEAQYVAPTNAVESKLAE
IWERVLGVSGIGILDNFFQI
GGHALKAMAVAAQVHREYQV
ELPLKVLFAQPTIKALAQYV
ATRSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 292 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 610 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Active Site Mutant Pepitdyl Carrier Protein | 1 |
Entities:
Entity 1, Active Site Mutant Pepitdyl Carrier Protein 90 residues - 9972.533 Da.
M1 is cleaved in vivo during expression. R84-H91 are a non-native.
| 1 | PRO | VAL | THR | GLU | ALA | GLN | TYR | VAL | ALA | PRO | |
| 2 | THR | ASN | ALA | VAL | GLU | SER | LYS | LEU | ALA | GLU | |
| 3 | ILE | TRP | GLU | ARG | VAL | LEU | GLY | VAL | SER | GLY | |
| 4 | ILE | GLY | ILE | LEU | ASP | ASN | PHE | PHE | GLN | ILE | |
| 5 | GLY | GLY | HIS | ALA | LEU | LYS | ALA | MET | ALA | VAL | |
| 6 | ALA | ALA | GLN | VAL | HIS | ARG | GLU | TYR | GLN | VAL | |
| 7 | GLU | LEU | PRO | LEU | LYS | VAL | LEU | PHE | ALA | GLN | |
| 8 | PRO | THR | ILE | LYS | ALA | LEU | ALA | GLN | TYR | VAL | |
| 9 | ALA | THR | ARG | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: PCP, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 50 mM; DSS 0.15 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
SPARKY v3.114, Goddard - chemical shift assignment, peak picking
TOPSPIN v3.0, Bruker Biospin - collection, processing
CYANA v3.96, Guntert, Mumenthaler and Wuthrich - structure solution
OPALp v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 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