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 25577

Title: Solution structure of human SUMO2

Deposition date: 2015-04-24 Original release date: 2016-04-18

Authors: Naik, Mandar; Naik, Nandita; Shih, Hsiu-Ming; Huang, Tai-huang

Citation: Naik, Mandar; Naik, Nandita; Shih, Hsiu-Ming; Huang, Tai-huang. "Structures of human SUMO"  Not known ., .-..

Assembly members:
SUMO2, polymer, 107 residues, 11149.640 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):
SUMO2: MGSSHHHHHHSQDPMADEKP KEGVKTENNDHINLKVAGQD GSVVQFKIKRHTPLSKLMKA YCERQGLSMRQIRFRFDGQP INETDTPAQLEMEDEDTIDV FQQQTGG

Data sets:
Data typeCount
13C chemical shifts411
15N chemical shifts106
1H chemical shifts666

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human SUMO21

Entities:

Entity 1, human SUMO2 107 residues - 11149.640 Da.

Residues 1-14 (MGSSHHHHHHSQDP) represent a non-native purification tag. These residues were neither assigned nor included in structure calculation.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERGLNASPPROMETALAASPGLULYSPRO
3   LYSGLUGLYVALLYSTHRGLUASNASNASP
4   HISILEASNLEULYSVALALAGLYGLNASP
5   GLYSERVALVALGLNPHELYSILELYSARG
6   HISTHRPROLEUSERLYSLEUMETLYSALA
7   TYRCYSGLUARGGLNGLYLEUSERMETARG
8   GLNILEARGPHEARGPHEASPGLYGLNPRO
9   ILEASNGLUTHRASPTHRPROALAGLNLEU
10   GLUMETGLUASPGLUASPTHRILEASPVAL
11   PHEGLNGLNGLNTHRGLYGLY

Samples:

CN: SUMO2, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%

N: SUMO2, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%

Phage: SUMO2, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; Pf1 phage 10 ± 0.1 w/v; H2O 90%; D2O 10%

Unlabeled: SUMO20.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%

Default: pH: 6.5; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNisotropicDefault
2D 1H-13C HSQCCNisotropicDefault
3D HNCOCNisotropicDefault
3D HNCACNisotropicDefault
3D HN(CO)CACNisotropicDefault
3D HNCACBCNisotropicDefault
3D CBCA(CO)NHCNisotropicDefault
3D HCCH-TOCSYCNisotropicDefault
3D HCCH-COSYCNisotropicDefault
3D HBHAcoNHCNisotropicDefault
2D-hbCBcgcdHDCNisotropicDefault
2D-hbCBcgcdceHECNisotropicDefault
3D 1H-15N TOCSYCNisotropicDefault
2D 1H-1H NOESYUnlabeledisotropicDefault
3D 1H-15N NOESYCNisotropicDefault
3D 1H-13C NOESYCNisotropicDefault
2D 1H-15N HSQC IPAPPhageanisotropicDefault

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

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

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 850 MHz

Related Database Links:

UNP P61956
PDB

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