BMRB Entry 11427

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11427

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Title:
NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice
Deposition date:
2011-02-10
Original release date:
2011-05-29
Authors:
Suzuki, Rintaro; Tsuchiya, Wataru; Shindo, Heisaburo; Yamazaki, Toshimasa
Citation:

Citation: Suzuki, Rintaro; Tsuchiya, Wataru; Shindo, Heisaburo; Yamazaki, Toshimasa. "NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice."  Biomol. NMR Assignments ., .-. (2011).
PubMed: 21523438

Assembly members:

Assembly members:
SAE2, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: rice   Taxonomy ID: 4530   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Oryza sativa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P-3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SAE2: GPLGSSETPLLLEVNTKTTK LREVIEKIIKSKLGMNLPLV MIGSTLVFEDGEGLEEDEAA NYALNLEKVLAELPAPVVND TKLTVEDFQQELSCSINIKH RDEFDEEKEPDGMVLSGWSA

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts124
1H chemical shifts865

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SAE21

Entities:

Entity 1, SAE2 120 residues - Formula weight is not available

Residues 431-435 represent a non-native sequence from affinity tag.

1   GLYPROLEUGLYSERSERGLUTHRPROLEU
2   LEULEUGLUVALASNTHRLYSTHRTHRLYS
3   LEUARGGLUVALILEGLULYSILEILELYS
4   SERLYSLEUGLYMETASNLEUPROLEUVAL
5   METILEGLYSERTHRLEUVALPHEGLUASP
6   GLYGLUGLYLEUGLUGLUASPGLUALAALA
7   ASNTYRALALEUASNLEUGLULYSVALLEU
8   ALAGLULEUPROALAPROVALVALASNASP
9   THRLYSLEUTHRVALGLUASPPHEGLNGLN
10   GLULEUSERCYSSERILEASNILELYSHIS
11   ARGASPGLUPHEASPGLUGLULYSGLUPRO
12   ASPGLYMETVALLEUSERGLYTRPSERALA

Samples:

sample_1: SAE2, [U-13C; U-15N], 1.28 mM; potassium phosphate 10 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: SAE2, [U-13C; U-15N], 1.18 mM; potassium phosphate 10 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 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 CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 15N-separated NOESY-HSQCsample_1isotropicsample_conditions_1
3D 13C/15N-separated NOESY-HSQCsample_1isotropicsample_conditions_1
3D 13C-separated NOESY-HSQCsample_2isotropicsample_conditions_1

Software:

xwinnmr v3.1, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DMX 750 MHz

Related Database Links:

GB EEC82353 EEE67493

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