BMRB Entry 16362

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16362

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 13C and 15N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II.
Deposition date:
2009-06-24
Original release date:
2009-11-16
Authors:
Castrillo, Ines; Bruix, Marta; Santoro, Jorge
Citation:

Citation: Castrillo, Ines; Alegre-Cebollada, Jorge; Martinez-Del-Pozo, Alvaro; Gavilanes, Jose; Bruix, Marta. "(1)H, (13)C, and (15)N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II."  Biomol NMR Assign 3, 239-241 (2009).
PubMed: 19768581

Assembly members:

Assembly members:
R29Q_StnII, polymer, 175 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE60

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R29Q_StnII: ALAGTIIAGASLTFQVLDKV LEELGKVSQKIAVGIDNESG GTWTALNAYFRSGTTDVILP EFVPNTKALLYSGRKDTGPV ATGAVAAFAYYMSSGNTLGV MFSVPFDYNWYSNWWDVKIY SGKRRADQGMYEDLYYGNPY RGDNGWHEKNLGYGLRMKGI MTSAGEAKMQIKISR

Data sets:
Data typeCount
13C chemical shifts412
15N chemical shifts178
1H chemical shifts1142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1

Entities:

Entity 1, monomer 175 residues - Formula weight is not available

1   ALALEUALAGLYTHRILEILEALAGLYALA
2   SERLEUTHRPHEGLNVALLEUASPLYSVAL
3   LEUGLUGLULEUGLYLYSVALSERGLNLYS
4   ILEALAVALGLYILEASPASNGLUSERGLY
5   GLYTHRTRPTHRALALEUASNALATYRPHE
6   ARGSERGLYTHRTHRASPVALILELEUPRO
7   GLUPHEVALPROASNTHRLYSALALEULEU
8   TYRSERGLYARGLYSASPTHRGLYPROVAL
9   ALATHRGLYALAVALALAALAPHEALATYR
10   TYRMETSERSERGLYASNTHRLEUGLYVAL
11   METPHESERVALPROPHEASPTYRASNTRP
12   TYRSERASNTRPTRPASPVALLYSILETYR
13   SERGLYLYSARGARGALAASPGLNGLYMET
14   TYRGLUASPLEUTYRTYRGLYASNPROTYR
15   ARGGLYASPASNGLYTRPHISGLULYSASN
16   LEUGLYTYRGLYLEUARGMETLYSGLYILE
17   METTHRSERALAGLYGLUALALYSMETGLN
18   ILELYSILESERARG

Samples:

sample_1: R29Q StnII, [U-13C]; [U-15N], 0.5 ± 0.1 mM; H2O 90%; D2O 10%

sample_2: R29Q StnII 0.5 ± 0.1 mM; D2O 100%

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AV800 800.2 MHz

Related Database Links:

BMRB 16630
PDB
EMBL CAC20912
SP P07845
AlphaFold P07845

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks