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 26730

Title: Structural and dynamics studies of Pax5 reveal asymmetry in stability and DNA binding by the Paired domain   PubMed: 27067111

Deposition date: 2016-01-14 Original release date: 2016-07-14

Authors: Perez-Borrajero, Cecilia; McIntosh, Lawrence

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).

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

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

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

Entity Sequences (FASTA):
Paired_domain_of_Pax5: GHMDLEKNYPTPRTSRTGHG GVNQLGGVFVNGRPLPDVVR QRIVELAHQGVRPCDISRQL RVSHGCVSKILGRYYETGSI KPGVIGGSKPKVATPKVVEK IAEYKRQNPTMFAWEIRDRL LAERVCDNDTVPSVSSINRI IRTKVQQPPNQ

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts