BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 36008

Title: SOLUTION STRUCTURE OF LYS39 ACETYLATED HUMAN SUMO1

Deposition date: 2016-06-19 Original release date: 2017-06-05

Authors: Naik, M.; Naik, N.; Shih, H.; Huang, T.

Citation: Naik, M.; Naik, N.; Shih, H.; Huang, T.. "Structures of Human Sumo"  . ., .-..

Assembly members:
Small ubiquitin-related modifier 1, polymer, 111 residues, 12809.266 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 BL21(DE3)

Entity Sequences (FASTA):
Small ubiquitin-related modifier 1: MGSSHHHHHHSQDPMSDQEA KPSTEDLGDKKEGEYIKLKV IGQDSSEIHFKVXMTTHLKK LKESYCQRQGVPMNSLRFLF EGQRIADNHTPKELGMEEED VIEVYQEQTGG

Data sets:
Data typeCount
13C chemical shifts426
15N chemical shifts103
1H chemical shifts701

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 111 residues - 12809.266 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERGLNASPPROMETSERASPGLNGLUALA
3   LYSPROSERTHRGLUASPLEUGLYASPLYS
4   LYSGLUGLYGLUTYRILELYSLEULYSVAL
5   ILEGLYGLNASPSERSERGLUILEHISPHE
6   LYSVALALYMETTHRTHRHISLEULYSLYS
7   LEULYSGLUSERTYRCYSGLNARGGLNGLY
8   VALPROMETASNSERLEUARGPHELEUPHE
9   GLUGLYGLNARGILEALAASPASNHISTHR
10   PROLYSGLULEUGLYMETGLUGLUGLUASP
11   VALILEGLUVALTYRGLNGLUGLNTHRGLY
12   GLY

Samples:

sample_1: DTT 2 mM; EDTA 0.1 mM; SUMO1 K39Ac, [U-100% 13C; U-100% 15N], 1 mM; potassium chloride 100 mM; potassium phosphate 10 mM; sodium azide 0.001%; H2O 90%; D2O, [U-2H], 10%

sample_2: DTT 2 mM; EDTA 0.1 mM; SUMO1 K39Ac, [U-100% 15N], 1 mM; potassium chloride 100 mM; potassium phosphate 10 mM; sodium azide 0.001%; H2O 90%; D2O, [U-2H], 10%

sample_3: DTT 2 mM; EDTA 0.1 mM; Pf1 phage 10 mg/mL; SUMO1 K39Ac, [U-100% 15N], 1 mM; potassium chloride 100 mM; potassium phosphate 10 mM; sodium azide 0.001%; H2O 90%; D2O, [U-2H], 10%

sample_4: DTT 2 mM; EDTA 0.1 mM; SUMO1 K39Ac 1 mM; potassium chloride 100 mM; potassium phosphate 10 mM; sodium azide 0.001%; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH- TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HBHACONHsample_1isotropicsample_conditions_1
2D-HBCBCGCDHDsample_1isotropicsample_conditions_1
2D-HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_4anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_3anisotropicsample_conditions_1
2D NOESY F1 FILTEREDsample_1isotropicsample_conditions_1
2D NOESY F2 FILTEREDsample_1isotropicsample_conditions_1
2D NOESY F1/F2 FILTEREDsample_1isotropicsample_conditions_1
2D TOCSY F1/F2 FILTEREDsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY v3.113, Goddard - data analysis

TOPSPIN v3.2, Bruker Biospin - processing

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

NMR spectrometers:

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

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