BMRB Entry 16611

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16611

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Title:
Phosphorylation of SUMO-interacting motif by CK2 enhances Daxx SUMO binding activity.
Deposition date:
2009-11-17
Original release date:
2010-10-14
Authors:
Naik, Mandar; Huang, Tai-Huang; Shih, Hsiu-Ming
Citation:

Citation: Naik, Mandar; Chang, Che-Chang; Naik, Nandita; Kung, Camy C-H; Shih, Hsiu-Ming; Huang, Tai-Huang. "NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx."  Biomol. NMR Assignments 5, 75-77 (2011).
PubMed: 20927612

Assembly members:

Assembly members:
SUMO1, polymer, 97 residues, 11149.640 Da.
DAXX20, polymer, 20 residues, 2151.341 Da.

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: pGex-4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SUMO1: MSDQEAKPSTEDLGDKKEGE YIKLKVIGQDSSEIHFKVKM TTHLKKLKESYCQRQGVPMN SLRFLFEGQRIADNHTPKEL GMEEEDVIEVYQEQTGG
DAXX20: KTSVATQCDPEEIIVLSDSD

Data sets:
Data typeCount
13C chemical shifts493
15N chemical shifts120
1H chemical shifts797

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SUMO11
2DAXX202

Entities:

Entity 1, SUMO1 97 residues - 11149.640 Da.

Mature form of Small Ubiquitin like Modifier 1.

1   METSERASPGLNGLUALALYSPROSERTHR
2   GLUASPLEUGLYASPLYSLYSGLUGLYGLU
3   TYRILELYSLEULYSVALILEGLYGLNASP
4   SERSERGLUILEHISPHELYSVALLYSMET
5   THRTHRHISLEULYSLYSLEULYSGLUSER
6   TYRCYSGLNARGGLNGLYVALPROMETASN
7   SERLEUARGPHELEUPHEGLUGLYGLNARG
8   ILEALAASPASNHISTHRPROLYSGLULEU
9   GLYMETGLUGLUGLUASPVALILEGLUVAL
10   TYRGLNGLUGLNTHRGLYGLY

Entity 2, DAXX20 20 residues - 2151.341 Da.

Last 20 amino acids of the Death-associated protein -6 (Daxx), comprising one of the two SUMO Interacting Motif (SIM).

1   LYSTHRSERVALALATHRGLNCYSASPPRO
2   GLUGLUILEILEVALLEUSERASPSERASP

Samples:

sample_1: SUMO1, [U-100% 15N], 0.27 – 0.5 mM; DAXX200 – 1.7 mM; potassium phosphate 10 mM; potassium chloride 100 mM; DTT 2 mM; EDTA 0.1 mM; sodium azide 0.001%; H2O 90%; D2O 10%

sample_2: SUMO1, [U-100% 13C; U-100% 15N], 0.5 mM; DAXX20 2 mM; potassium phosphate 10 mM; potassium chloride 100 mM; DTT 2 mM; EDTA 0.1 mM; sodium azide 0.001%; H2O 90%; D2O 10%

sample_3: SUMO1 2 mM; DAXX20, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 10 mM; potassium chloride 100 mM; DTT 2 mM; EDTA 0.1 mM; sodium azide 0.001%; H2O 90%; D2O 10%

sample_4: SUMO1, [U-100% 13C; U-100% 15N], 0.5 mM; DAXX20, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 10 mM; potassium chloride 100 mM; DTT 2 mM; EDTA 0.1 mM; sodium azide 0.001%; Pf1 phage 0.0066 w/v; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESY - F1 filteredsample_2isotropicsample_conditions_1
3D 1H-13C NOESY - F1 filteredsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-15N HSQC - IPAPsample_4anisotropicsample_conditions_1

Software:

CNS v1.2, Brunger A. T. et.al. - refinement, structure solution

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement, structure solution

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

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

Related Database Links:

BMRB 17536 25299
PDB
DBJ BAB22172 BAB27379 BAB93477 BAC40739 BAE35024 BAA34295 BAB83524 BAD97124 BAE02344 BAE21895
EMBL CAA67898 CAG31129 CAG46944 CAG46953 CAH92616 CAE83918 CAG33366 CAH91194
GB AAB39999 AAB40388 AAB40390 AAC39959 AAC50733 AAB63043 AAB66585 AAB66586 AAB92671 AAC39853
REF NP_001005781 NP_001005782 NP_001009672 NP_001030535 NP_001106146 NP_001135441 NP_001135442 NP_001186662 NP_001241646 NP_001341
SP A7WLH8 P63165 P63166 Q2EF74 Q5E9D1 O18805 O35613 Q8VIB2 Q9UER7
TPG DAA32560
AlphaFold A7WLH8 P63165 P63166 Q2EF74 Q5E9D1 O18805 O35613 Q8VIB2 Q9UER7

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