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 15111

Title: Solution Structure of the UBA Domain from Cbl-b   PubMed: 18596201

Authors: Zhou, Chen-Jie; Zhou, Zi-Ren; Lin, Dong-Hai; Hu, Hong-Yu

Citation: Zhou, Zi-Ren; Gao, Hong-Chang; Zhou, Chen-Jie; Chang, Yong-Gang; Hong, Jing; Song, Ai-Xin; Lin, Dong-Hai; Hu, Hong-Yu. "Differential Ubiquitin Binding of the UBA Domains from Human c-Cbl and Cbl-b: NMR Structural and Biochemical Insights"  Protein Sci. 17, 1805-1814 (2008).

Assembly members:
UBA domain of Cbl-b, polymer, 46 residues, 5113.846 Da.

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):
UBA domain of Cbl-b: EAALENVDAKIAKLMGEGYA FEEVKRALEIAQNNVEVARS ILREFA

Data sets:
Data typeCount
13C chemical shifts113
15N chemical shifts42
1H chemical shifts258

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBA domain of Cbl-b1

Entities:

Entity 1, UBA domain of Cbl-b 46 residues - 5113.846 Da.

1   GLUALAALALEUGLUASNVALASPALALYS
2   ILEALALYSLEUMETGLYGLUGLYTYRALA
3   PHEGLUGLUVALLYSARGALALEUGLUILE
4   ALAGLNASNASNVALGLUVALALAARGSER
5   ILELEUARGGLUPHEALA

Samples:

sample_1: entity, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%

sample_conditions_1: pH: 6.5; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_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

Software:

NMRDraw v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

ARIA v2.0, Linge, O, . - data analysis, refinement, structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB 2DO6 2JNH 2OOA 2OOB
DBJ BAC05498 BAE36418 BAF85481 BAG52839 BAG53874
EMBL CAH18449 CAH56175
GB AAB09291 AAF13271 AAH32851 AAI50935 AAI50939
REF NP_001028410 NP_001192852 NP_598285 NP_733762 XP_001503404
SP Q13191 Q3TTA7 Q8K4S7
TPG DAA33541