BMRB Entry 18216
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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/BMR18216
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Title: NMR structure of an acyl-carrier protein from Rickettsia prowazekii.(Seattle Structural Genomics Center for Infectious Disease (SSGCID)) PubMed: 21904063
Deposition date: 2012-01-25 Original release date: 2012-02-10
Authors: Barnwal, Ravi P; Gonen, Shane; Varani, Gabriele
Citation: Barnwal, Ravi; Van Voorhis, Wesley; Varani, G.. "NMR structure of an acyl-carrier protein from Borrelia burgdorferi." Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 1137-1140 (2011).
Assembly members:
acyl_carrier_protein, polymer, 81 residues, 9250.662 Da.
Natural source: Common Name: Rickettsia prowazekii Taxonomy ID: 782 Superkingdom: Bacteria Kingdom: not available Genus/species: Rickettsia prowazekii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
acyl_carrier_protein: MSTTDKIEQKVIEMVAEKLN
KDKAIITTDSRFIEDLKADS
LDTVELMMAIEVEYGIDIPD
DEATKIKTVSDVIKYIKERQ
S
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 350 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 513 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | acyl-carrier protein from Rickettsia prowazekii | 1 |
Entities:
Entity 1, acyl-carrier protein from Rickettsia prowazekii 81 residues - 9250.662 Da.
| 1 | MET | SER | THR | THR | ASP | LYS | ILE | GLU | GLN | LYS | ||||
| 2 | VAL | ILE | GLU | MET | VAL | ALA | GLU | LYS | LEU | ASN | ||||
| 3 | LYS | ASP | LYS | ALA | ILE | ILE | THR | THR | ASP | SER | ||||
| 4 | ARG | PHE | ILE | GLU | ASP | LEU | LYS | ALA | ASP | SER | ||||
| 5 | LEU | ASP | THR | VAL | GLU | LEU | MET | MET | ALA | ILE | ||||
| 6 | GLU | VAL | GLU | TYR | GLY | ILE | ASP | ILE | PRO | ASP | ||||
| 7 | ASP | GLU | ALA | THR | LYS | ILE | LYS | THR | VAL | SER | ||||
| 8 | ASP | VAL | ILE | LYS | TYR | ILE | LYS | GLU | ARG | GLN | ||||
| 9 | SER |
Samples:
sample_1: acyl carrier protein, [U-98% 13C; U-98% 15N], 1.7 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7; 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 | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts