BMRB Entry 26730

Title:
Structural and dynamics studies of Pax5 reveal asymmetry in stability and DNA binding by the Paired domain
Deposition date:
2016-01-14
Original release date:
2016-07-14
Authors:
Perez-Borrajero, Cecilia; McIntosh, Lawrence
Citation:

Citation: Perez-Borrajero, Cecilia; Okon, Mark; McIntosh, Lawrence. "Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain"  J. Mol. Biol. 428, 2372-2391 (2016).
PubMed: 27067111

Assembly members:

Assembly members:
Paired_domain_of_Pax5, polymer, 151 residues, Formula weight is not available

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: pET28-MHL

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts137
1H chemical shifts137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Paired domain of Pax51

Entities:

Entity 1, Paired domain of Pax5 151 residues - Formula weight is not available

1   GLYHISMETASPLEUGLULYSASNTYRPRO
2   THRPROARGTHRSERARGTHRGLYHISGLY
3   GLYVALASNGLNLEUGLYGLYVALPHEVAL
4   ASNGLYARGPROLEUPROASPVALVALARG
5   GLNARGILEVALGLULEUALAHISGLNGLY
6   VALARGPROCYSASPILESERARGGLNLEU
7   ARGVALSERHISGLYCYSVALSERLYSILE
8   LEUGLYARGTYRTYRGLUTHRGLYSERILE
9   LYSPROGLYVALILEGLYGLYSERLYSPRO
10   LYSVALALATHRPROLYSVALVALGLULYS
11   ILEALAGLUTYRLYSARGGLNASNPROTHR
12   METPHEALATRPGLUILEARGASPARGLEU
13   LEUALAGLUARGVALCYSASPASNASPTHR
14   VALPROSERVALSERSERILEASNARGILE
15   ILEARGTHRLYSVALGLNGLNPROPROASN
16   GLN

Samples:

sample_1: Paired domain of Pax5, [U-100% 13C; U-100% 15N], 0.35 mM; MES 20 mM; NaCl 200 mM; DTT 2 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 850 MHz

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