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BMRB Entry 25461

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25461
MolProbity Validation Chart

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Title: Structure of the CUE domain of yeast Cue1

Deposition date: 2015-02-02 Original release date: 2016-03-21

Authors: Kniss, Andreas; Rogov, Vladimir; Loehr, Frank; Guentert, Peter; Doetsch, Volker

Citation: von Delbrueck, Maximilian; Kniss, Andreas; Rogov, Vladimir; Pluska, Lukas; Bagola, Katrin; Loehr, Frank; Guentert, Peter; Sommer, Thomas; Doetsch, Volker. "Dynamic binding of a ubiquitin binding domain to polyubiquitin stimulates chain elongation by an E2 enzyme"  Not known ., .-..

Assembly members:
Coupling_of_ubiquitin_conjugation_to_ER_degradation_protein_1_(Cue1), polymer, 75 residues, 8266.121 Da.

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
Coupling_of_ubiquitin_conjugation_to_ER_degradation_protein_1_(Cue1): GAMGPQGSTQNALRRTGRVN GGHPVTTQMVETVQNLAPNL HPEQIRYSLENTGSVEETVE RYLRGDEFSFPPGFE

Data sets:
Data typeCount
13C chemical shifts305
15N chemical shifts81
1H chemical shifts498

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 75 residues - 8266.121 Da.

Residues 41-44 represent non-native residues (cloning artifacts). Residues 45-115 represent native amino acids of yeast Cue1.

1   GLYALAMETGLYPROGLNGLYSERTHRGLN
2   ASNALALEUARGARGTHRGLYARGVALASN
3   GLYGLYHISPROVALTHRTHRGLNMETVAL
4   GLUTHRVALGLNASNLEUALAPROASNLEU
5   HISPROGLUGLNILEARGTYRSERLEUGLU
6   ASNTHRGLYSERVALGLUGLUTHRVALGLU
7   ARGTYRLEUARGGLYASPGLUPHESERPHE
8   PROPROGLYPHEGLU

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; D2O 5%; sodium azide 0.01%; protease inhibitor cocktail 4.6 mM; CUE domain of Cue1, [U-98% 13C; U-98% 15N], 1.2 mM; DSS 100 uM; H2O 95%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D long range 1H-15N TROSY HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C ct TROSY H(C)Nsample_1isotropicsample_conditions_1
2D (H)CB(CG)CCH-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D H(CC)(CO)NH TOCSYsample_1isotropicsample_conditions_1
3D (H)C(C)(CO)NH TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N BEST TROSY H(N)Nsample_1isotropicsample_conditions_1

Software:

CYANA v3.96, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v3.1, Bruker Biospin - processing

SPARKY v3.115, Goddard - chemical shift assignment

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TALOS, Cornilescu, Delaglio and Bax - dihedral angle constraints

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts