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 18670

Title: Solution structure of the Sgt2 homodimerization domain   PubMed: 23142665

Authors: Chartron, Justin; VanderVelde, David; Clemons, William

Citation: Chartron, Justin; VanderVelde, David; Clemons, William. "Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface."  Cell Rep. 2, 1620-1632 (2012).

Assembly members:
Sgt2, polymer, 74 residues, 7889.790 Da.

Natural source:   Common Name: Baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Sgt2: SVDSASKEEIAALIVNYFSS IVEKKEISEDGADSLNVAMD CISEAFGFEREAVSGILGKS EFKGQHLADILNSA

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts70
1H chemical shifts426

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sgt2 homodimerization domain, 11
2Sgt2 homodimerization domain, 21

Entities:

Entity 1, Sgt2 homodimerization domain, 1 74 residues - 7889.790 Da.

1   SERVALASPSERALASERLYSGLUGLUILE
2   ALAALALEUILEVALASNTYRPHESERSER
3   ILEVALGLULYSLYSGLUILESERGLUASP
4   GLYALAASPSERLEUASNVALALAMETASP
5   CYSILESERGLUALAPHEGLYPHEGLUARG
6   GLUALAVALSERGLYILELEUGLYLYSSER
7   GLUPHELYSGLYGLNHISLEUALAASPILE
8   LEUASNSERALA

Samples:

sample_1: Sgt2, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 20 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: Sgt2, [U-100% 15N], 2 mM; sodium phosphate 20 mM; sodium azide 0.02%; Polyacrylamide 7%; H2O 90%; D2O 10%

sample_3: Sgt2, [U-100% 15N], 2 mM; sodium phosphate 20 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 6.1; pressure: 1 atm; temperature: 297.5 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

Analysis, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS+, Cornilescu, Delaglio and Bax - data analysis

ARIA v2.3, Linge, O, . - refinement, structure solution

PALES, Zweckstetter and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18341
PDB
DBJ GAA26330
EMBL CAA99195 CAY86295
GB AAC49487 AHY77314 AJP41546 AJT70966 AJT71456
REF NP_014649
SP Q12118
TPG DAA10789