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 16490

Title: Solution structure of protein sf3929 from Shigella flexneri 2a. Northeast Structural Genomics Consortium target SfR81/Ontario Center for Structural Proteomics Target sf3929

Deposition date: 2009-09-10 Original release date: 2009-10-06

Authors: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Semest, Anthony; Arrowsmith, Cheryl

Citation: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Semest, Anthony; Arrowsmith, Cheryl. "Solution Structure of protein sf3929 from Shigella flexneri 2a. Northeast Structural Genomics Consortium target SfR81/Ontario Center for Structural Proteomics Target sf3929"  .

Assembly members:
sf3929, polymer, 89 residues, 10322.015 Da.

Natural source:   Common Name: shigella flexneri 2a   Taxonomy ID: 42897   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Shigella flexneri

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p15Tvlic

Entity Sequences (FASTA):
sf3929: MKCKRLNEVIELLQPAWQKE PDFNLLQFLQKLAKESGFDG ELADLTDDILIYHLKMRDSA KDAVIPGLQKDYEEDFKTAL LRARGVIKE

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts88
1H chemical shifts612

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sf39291

Entities:

Entity 1, sf3929 89 residues - 10322.015 Da.

1   METLYSCYSLYSARGLEUASNGLUVALILE
2   GLULEULEUGLNPROALATRPGLNLYSGLU
3   PROASPPHEASNLEULEUGLNPHELEUGLN
4   LYSLEUALALYSGLUSERGLYPHEASPGLY
5   GLULEUALAASPLEUTHRASPASPILELEU
6   ILETYRHISLEULYSMETARGASPSERALA
7   LYSASPALAVALILEPROGLYLEUGLNLYS
8   ASPTYRGLUGLUASPPHELYSTHRALALEU
9   LEUARGALAARGGLYVALILELYSGLU

Samples:

sample_1: sf3929, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

MDDGUI v1.0, Gutmanas and Arrowsmith - processing

SPARKY v3.95, Goddard - data analysis, peak picking

FAWN v1.0, Lemak and Arrowsmith - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment

PSVS, Bhattacharya and Montelione - NMR structure quality assessment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB38204 BAE77450 BAG79663 BAI27894 BAI33017
EMBL CAP78316 CAQ34210 CAQ91090 CAR00828 CAR05492
GB AAB02993 AAC76856 AAG59047 AAN45364 AAN83233
REF NP_312808 NP_418295 NP_709657 WP_001295263 WP_001329922
SP P0ADP9 P0ADQ0 P0ADQ1
AlphaFold P0ADP9

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts