BMRB Entry 6057

Title:
Sequence-specific resonance assignments of the tandem SH3 domains in autoinhibitory form of p47phox
Deposition date:
2003-12-27
Original release date:
2004-06-28
Authors:
Yuzawa, Satoru; Yokochi, Masashi; Fujioka, Yuko; Ogura, Kenji; Sumimoto, Hideki; Inagaki, Fuyuhiko
Citation:

Citation: Yuzawa, Satoru; Ogura, Kenji; Horiuchi, M.; Suzuki, N.; Fujioka, Yuko; Kataoka, M.; Sumimoto, Hideki; Inagaki, Fuyuhiko. "Solution structure of the tandem SH3 domains of p47phox in an autoinhibited form. "  J. Biol. Chem. 29, 451-452 (2004).
PubMed: 15123602

Assembly members:

Assembly members:
p47phox, polymer, 193 residues, 21988.85 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pPRO EX HTb

Data sets:
Data typeCount
13C chemical shifts551
1H chemical shifts179
15N chemical shifts179

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p47phox1

Entities:

Entity 1, p47phox 193 residues - 21988.85 Da.

1   GLYALAMETASPILETHRGLYPROILEILE
2   LEUGLNTHRTYRARGALAILEALAASPTYR
3   GLULYSTHRSERGLYSERGLUMETALALEU
4   SERTHRGLYASPVALVALGLUVALVALGLU
5   LYSSERGLUSERGLYTRPTRPPHECYSGLN
6   METLYSALALYSARGGLYTRPILEPROALA
7   SERPHELEUGLUPROLEUASPSERPROASP
8   GLUTHRGLUASPPROGLUPROASNTYRALA
9   GLYGLUPROTYRVALALAILELYSALATYR
10   THRALAVALGLUGLYASPGLUVALSERLEU
11   LEUGLUGLYGLUALAVALGLUVALILEHIS
12   LYSLEULEUASPGLYTRPTRPVALILEARG
13   LYSASPASPVALTHRGLYTYRPHEPROSER
14   METTYRLEUGLNLYSSERGLYGLNASPVAL
15   SERGLNALAGLNARGGLNILELYSARGGLY
16   ALAPROPROARGARGSERSERILEARGASN
17   ALAHISSERILEHISGLNARGSERARGLYS
18   ARGLEUSERGLNASPALATYRARGARGASN
19   SERVALARGPHELEUGLNGLNARGARGARG
20   GLNALAARG

Samples:

sample_1: p47phox, [U-90% 2H; U-98% 13C; U-98% 15N], 1.0 mM

Ex-cond_1: pH: 6.5; temperature: 298 K; ionic strength: 0.20 M

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availableEx-cond_1
HNCOsample_1not availableEx-cond_1
HN(CA)COsample_1not availableEx-cond_1
HNCAsample_1not availableEx-cond_1
HN(CO)CAsample_1not availableEx-cond_1
NH(CO)CACBsample_1not availableEx-cond_1
HNCACBsample_1not availableEx-cond_1

Software:

nmrPipe - raw spectral data processing

Olivia - data processing, assignment analysis

NMR spectrometers:

  • Varian INOVAplus 600 MHz

Related Database Links:

PDB

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