BMRB Entry 17425
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17425
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: Staphylococcus aureus pathogenicity island 1 protein gp6, an internal scaffold in size determination PubMed: 21821042
Deposition date: 2011-01-31 Original release date: 2011-08-17
Authors: Dearborn, Altaira; Spilman, Michael; Damle, Priyadarshan; Chang, Jenny; Monroe, Eric; Saad, Jamil; Christie, Gail; Dokland, Terje
Citation: Dearborn, Altaira; Spilman, Michael; Damle, Priyadarshan; Chang, Jenny; Monroe, Eric; Saad, Jamil; Christie, Gail; Dokland, Terje. "The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination." J. Mol. Biol. 412, 710-722 (2011).
Assembly members:
entity, polymer, 71 residues, 8150.116 Da.
Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: ETKYELNNTKKVANAFGLNE
EDTNLLINAVDLDIKNNMQE
ISSELQQSEQSKQKQYGTTL
QNLAKQNRIIK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 212 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 419 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | island 1 protein gp6 | 1 |
Entities:
Entity 1, island 1 protein gp6 71 residues - 8150.116 Da.
| 1 | GLU | THR | LYS | TYR | GLU | LEU | ASN | ASN | THR | LYS | ||||
| 2 | LYS | VAL | ALA | ASN | ALA | PHE | GLY | LEU | ASN | GLU | ||||
| 3 | GLU | ASP | THR | ASN | LEU | LEU | ILE | ASN | ALA | VAL | ||||
| 4 | ASP | LEU | ASP | ILE | LYS | ASN | ASN | MET | GLN | GLU | ||||
| 5 | ILE | SER | SER | GLU | LEU | GLN | GLN | SER | GLU | GLN | ||||
| 6 | SER | LYS | GLN | LYS | GLN | TYR | GLY | THR | THR | LEU | ||||
| 7 | GLN | ASN | LEU | ALA | LYS | GLN | ASN | ARG | ILE | ILE | ||||
| 8 | LYS |
Samples:
sample_1: entity, [U-99% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 200 mM; H2O 90%; D2O 10%
sample_2: entity, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 200 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
ProcheckNMR, Laskowski and MacArthur - data analysis
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Ultrashield Plus 700 MHz
Related Database Links:
| PDB | |
| DBJ | BAB43103 BAB56959 BAB58178 BAF77676 BAF78884 |
| EMBL | CBI48784 CEH25196 CEH25509 CEZ61431 CFA52483 |
| GB | AAC28957 AAL04130 AAW37873 ABJ97292 ACY10719 |
| REF | WP_000404187 WP_000448101 WP_000448770 WP_000448771 WP_000448772 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts