BMRB Entry 17550

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17550

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Title:
Backbone assignments of the IDOL RING domain
Deposition date:
2011-03-24
Original release date:
2011-07-05
Authors:
GOULT, BENJAMIN; Fairall, Louise; Tontonoz, Peter; Schwabe, John
Citation:

Citation: Zhang, Li; Fairall, Louise; Goult, Benjamin; Calkin, Anna; Hong, Cynthia; Millard, Christopher; Tontonoz, Peter; Schwabe, John. "The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor"  Genes Dev. 25, 1262-1274 (2011).
PubMed: 21685362

Assembly members:

Assembly members:
RING, polymer, 79 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: pLEICS-7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RING: GAQQTRVLQEKLRKLKEAML CMVCCEEEINSTFCPCGHTV CCESCAAQLQSCPVCRSRVE HVQHVYLPTHTSLLNLTVI

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts72
1H chemical shifts119

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RING1

Entities:

Entity 1, RING 79 residues - Formula weight is not available

Residues 1-2 represent a non-native affinity tag

1   GLYALAGLNGLNTHRARGVALLEUGLNGLU
2   LYSLEUARGLYSLEULYSGLUALAMETLEU
3   CYSMETVALCYSCYSGLUGLUGLUILEASN
4   SERTHRPHECYSPROCYSGLYHISTHRVAL
5   CYSCYSGLUSERCYSALAALAGLNLEUGLN
6   SERCYSPROVALCYSARGSERARGVALGLU
7   HISVALGLNHISVALTYRLEUPROTHRHIS
8   THRSERLEULEUASNLEUTHRVALILE

Samples:

sample_1: RING, [U-100% 13C; U-100% 15N], 0.6 ± 0.05 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 100 ± 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; 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 HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

CCPN v2.1.5, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAC28868 BAC30716 BAE35115 BAE42721 BAG37209
GB AAF18974 AAG23789 AAH02860 AAH10206 AAP35704
REF NP_001100814 NP_001267155 NP_037394 NP_722484 XP_002746247
SP D3ZDI6 Q8BM54 Q8WY64
AlphaFold Q8WY64 D3ZDI6 Q8BM54

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