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Biological Magnetic Resonance Data Bank


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BMRB Entry 36006

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36006
MolProbity Validation Chart

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Title: SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2

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 2, polymer, 107 residues, 12283.632 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 2: MGSSHHHHHHSQDPMADEKP KEGVKTENNDHINLKVAGQD GSVVQFKIKRHTPLSXLMKA YCERQGLSMRQIRFRFDGQP INETDTPAQLEMEDEDTIDV FQQQTGG

Data sets:
Data typeCount
13C chemical shifts399
15N chemical shifts105
1H chemical shifts670

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 107 residues - 12283.632 Da.

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

Samples:

sample_1: DTT 2 mM; EDTA 0.1 mM; SUMO2 K42Ac, [U-100% 13C; U-100% 15N; U-80% 2H], 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; SUMO2 K42Ac, [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; SUMO2 K42Ac, [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; K42Ac SUMO2 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_1isotropicsample_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_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_1anisotropicsample_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