BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17862

Title: Solution structure of Staphylococcus aureus IsdH linker domain   PubMed: 21917915

Authors: Spirig, Thomas; Clubb, Robert; Malmirchegini, G.; Robson, Scott

Citation: Krishna Kumar, Kaavya; Jacques, David; Pishchany, Gleb; Caradoc-Davies, Tom; Spirig, Thomas; Malmirchegini, G. Reza; Langley, David; Dickson, Claire; Mackay, Joel; Clubb, Robert; Skaar, Eric; Guss, J. Mitchell; Gell, David. "Structural basis for hemoglobin capture by Staphylococcus aureus cell-surface protein, IsdH."  J. Biol. Chem. 286, 38439-38447 (2011).

Assembly members:
entity, polymer, 78 residues, 9280.425 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: SDDYVDEETYNLQKLLAPYH KAKTLERQVYELEKLQEKLP EKYKAEYKKKLDQTRVELAD QVKSAVTEFENVTPTNDQ

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts82
1H chemical shifts568

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Staphylococcus aureus IsdH linker domain1

Entities:

Entity 1, Staphylococcus aureus IsdH linker domain 78 residues - 9280.425 Da.

Residue 1 represents a non-native residue left after cleaving of the affinity tag

1   SERASPASPTYRVALASPGLUGLUTHRTYR
2   ASNLEUGLNLYSLEULEUALAPROTYRHIS
3   LYSALALYSTHRLEUGLUARGGLNVALTYR
4   GLULEUGLULYSLEUGLNGLULYSLEUPRO
5   GLULYSTYRLYSALAGLUTYRLYSLYSLYS
6   LEUASPGLNTHRARGVALGLULEUALAASP
7   GLNVALLYSSERALAVALTHRGLUPHEGLU
8   ASNVALTHRPROTHRASNASPGLN

Samples:

sample_1: IsdH linker, [U-100% 15N], 1.1 mM; potassium phosphate 20 mM; potassium chloride 50 mM; AEBSF protease inhibitor 100 uM; sodium azide 0.01%; D2O 7%; H2O 93%

sample_2: IsdH linker, [U-100% 13C; U-100% 15N], 1.3 mM; potassium phosphate 20 mM; potassium chloride 50 mM; AEBSF protease inhibitor 100 uM; sodium azide 0.01%; D2O 7%; H2O 93%

sample_3: IsdH linker, [U-100% 13C; U-100% 15N], 1.3 mM; potassium phosphate 20 mM; potassium chloride 50 mM; AEBSF protease inhibitor 100 uM; sodium azide 0.01%; D2O 100%

sample_conditions_1: ionic strength: 140 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CC(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
2D CB(CGCD)HDsample_3isotropicsample_conditions_1
2D CB(CGCD)HEsample_3isotropicsample_conditions_1

Software:

PIPP, Garrett - peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment

ProcheckNMR, Laskowski and MacArthur - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

xwinnmr, Bruker Biospin - collection

CARA, Keller - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17820
PDB
DBJ BAB42820 BAB57893 BAB95538 BAF67896 BAF78600
EMBL CAG43459 CAI81279 CAQ50207 CBI49597 CBX34951
GB AAW38309 ABD20516 ABD30910 ABQ49576 ABR52665
REF WP_001032759 WP_001032760 WP_001032761 WP_001032762 WP_001032763
SP Q2FG07 Q2FXJ2 Q2YTF7 Q5HF43 Q6G8J7