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.
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
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:

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).
PubMed: 21821042

Assembly members:

Assembly members:
entity, polymer, 71 residues, 8150.116 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHis6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: ETKYELNNTKKVANAFGLNE EDTNLLINAVDLDIKNNMQE ISSELQQSEQSKQKQYGTTL QNLAKQNRIIK

Data sets:
Data typeCount
13C chemical shifts212
15N chemical shifts70
1H chemical shifts419

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1island 1 protein gp61

Entities:

Entity 1, island 1 protein gp6 71 residues - 8150.116 Da.

1   GLUTHRLYSTYRGLULEUASNASNTHRLYS
2   LYSVALALAASNALAPHEGLYLEUASNGLU
3   GLUASPTHRASNLEULEUILEASNALAVAL
4   ASPLEUASPILELYSASNASNMETGLNGLU
5   ILESERSERGLULEUGLNGLNSERGLUGLN
6   SERLYSGLNLYSGLNTYRGLYTHRTHRLEU
7   GLNASNLEUALALYSGLNASNARGILEILE
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks