BMRB Entry 11029

Title:
Solution Structure of the N-terminal SAP Domain of SUMO E3 Ligases from Saccharomyces cerevisiae
Deposition date:
2008-01-29
Original release date:
2008-11-11
Authors:
Suzuki, Rintaro; Shindo, Heisaburo; Tase, Akira; Yamazaki, Toshimasa
Citation:

Citation: Suzuki, Rintaro; Shindo, Heisaburo; Tase, Akira; Kikuchi, Yoshiko; Shimizu, Mitsuhiro; Yamazaki, Toshimasa. "Solution Structures and DNA Binding Properties of the N-terminal SAP Domains of SUMO E3 Ligases from Saccharomyces cerevisiae and Oryza sativa."  Proteins 75, 336-347 (2008).
PubMed: 18831036

Assembly members:

Assembly members:
Siz1 1-111, polymer, 114 residues, 13249.319 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28b(+)

Data sets:
Data typeCount
13C chemical shifts505
15N chemical shifts125
1H chemical shifts861

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Siz1 1-1111

Entities:

Entity 1, Siz1 1-111 114 residues - 13249.319 Da.

Residues (-3)-(-1) represent a non-native sequence from affinity tag.

1   GLYSERHISMETILEASNLEUGLUASPTYR
2   TRPGLUASPGLUTHRPROGLYPROASPARG
3   GLUPROTHRASNGLULEUARGASNGLUVAL
4   GLUGLUTHRILETHRLEUMETGLULEULEU
5   LYSVALSERGLULEULYSASPILECYSARG
6   SERVALSERPHEPROVALSERGLYARGLYS
7   ALAVALLEUGLNASPLEUILEARGASNPHE
8   LEUGLNASNALALEUVALVALGLYLYSSER
9   ASPPROTYRARGVALGLNALAVALLYSPHE
10   LEUILEGLUARGILEARGLYSASNGLUPRO
11   LEUPROVALTYRLYSASPLEUTRPASNALA
12   LEUARGLYSGLY

Samples:

15N_in_8%_D2O: Siz1 1-111, [U-15N], 0.55 mM; potassium phosphate 20 mM; sodium chloride 300 mM; DTT 3 mM; H2O 92%; D2O 8%

13C_15N_in_8%_D2O: Siz1 1-111, [U-13C; U-15N], 0.6 mM; potassium phosphate 20 mM; sodium chloride 300 mM; DTT 3 mM; H2O 92%; D2O 8%

13C_15N_in_100%_D2O: Siz1 1-111, [U-13C; U-15N], 0.69 mM; potassium phosphate 20 mM; sodium chloride 300 mM; DTT 3 mM; D2O 100%

pH_6.1: pH: 6.1; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_in_8%_D2OisotropicpH_6.1
3D 1H-15N NOESY15N_in_8%_D2OisotropicpH_6.1
2D 1H-15N HSQC13C_15N_in_8%_D2OisotropicpH_6.1
3D HNCO13C_15N_in_8%_D2OisotropicpH_6.1
3D HNCA13C_15N_in_8%_D2OisotropicpH_6.1
3D CBCA(CO)NH13C_15N_in_8%_D2OisotropicpH_6.1
3D 13C-edited 1H-15N NOESY13C_15N_in_8%_D2OisotropicpH_6.1
2D 1H-13C HSQC13C_15N_in_100%_D2OisotropicpH_6.1
3D HCCH-TOCSY13C_15N_in_100%_D2OisotropicpH_6.1
4D 1H-13C NOESY13C_15N_in_100%_D2OisotropicpH_6.1

Software:

xwinnmr v3.1, Bruker Biospin - collection

NMRPipe vreleased at Feb 10, 2006, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis

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

PIPP v4.3.6, Garrett - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

AQUA v3.2, Rullmann, Doreleijers and Kaptein - data analysis

ProcheckNMR v3.5.4, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker DMX 750 MHz

Related Database Links:

PDB
DBJ GAA22629
GB AAB64849 AHY75365 AJP38091 AJU58213 AJU58906
REF NP_010697
SP Q04195
TPG DAA12251
AlphaFold Q04195

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