BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27358

Title: DNA binding protein inhibitor ID2 in 8M urea pH2.3   PubMed: 29642431

Authors: Roschger, Cornelia; Schubert, Mario; Cabrele, Chiara

Citation: Roschger, Cornelia; Schubert, Mario; Regl, Christof; Andosch, Ancuela; Marquez Macheda, Augusto; Berger, Thomas; Huber, Christian; Lutz-Meindl, Ursula; Cabrele, Chiara. "The Recombinant Inhibitor of DNA Binding Id2 Forms Multimeric Structures via the Helix-Loop-Helix Domain and the Nuclear Export Signal"  Int. J. Mol. Sci. 19, E1105-E1105 (2018).

Assembly members:
Id2, polymer, 134 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):
Id2: MKAFSPVRSVRKNSLSDHSL GISRSKTPVDDPMSLLYNMN DCYSKLKELVPSIPQNKKVS KMEILQHVIDYILDLQIALD SHPTIVSLHHQRPGQNQASR TPLTTLNTDISILSLQASEF PSELMSNDSKALCG

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts124
1H chemical shifts129

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Id21

Entities:

Entity 1, Id2 134 residues - Formula weight is not available

1   METLYSALAPHESERPROVALARGSERVAL
2   ARGLYSASNSERLEUSERASPHISSERLEU
3   GLYILESERARGSERLYSTHRPROVALASP
4   ASPPROMETSERLEULEUTYRASNMETASN
5   ASPCYSTYRSERLYSLEULYSGLULEUVAL
6   PROSERILEPROGLNASNLYSLYSVALSER
7   LYSMETGLUILELEUGLNHISVALILEASP
8   TYRILELEUASPLEUGLNILEALALEUASP
9   SERHISPROTHRILEVALSERLEUHISHIS
10   GLNARGPROGLYGLNASNGLNALASERARG
11   THRPROLEUTHRTHRLEUASNTHRASPILE
12   SERILELEUSERLEUGLNALASERGLUPHE
13   PROSERGLULEUMETSERASNASPSERLYS
14   ALALEUCYSGLY

Samples:

sample_1: Id2, [U-99% 13C; U-99% 15N], 0.74 mM; urea 8 M; chloride 180 mM

sample_conditions_1: ionic strength: 180 mM; pH: 2.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D (H)NCANHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

SP Q02363