BMRB Entry 11267

Title:
Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein
Deposition date:
2010-08-09
Original release date:
2011-08-18
Authors:
Zhao, C.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Zhao, C.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein"  .

Assembly members:

Assembly members:
ubiquitin-like molecule, polymer, 104 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040510-09

Experimental source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040510-09

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts399
15N chemical shifts94
1H chemical shifts635

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin-like molecule1

Entities:

Entity 1, ubiquitin-like molecule 104 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETALAASP
2   GLULYSPROLYSGLUGLYVALLYSTHRGLU
3   ASNASNASPHISILEASNLEULYSVALALA
4   GLYGLNASPGLYSERVALVALGLNPHELYS
5   ILELYSARGHISTHRPROLEUSERLYSLEU
6   METLYSALATYRCYSGLUARGGLNGLYLEU
7   SERMETARGGLNILEARGPHEARGPHEASP
8   GLYGLNPROILEASNGLUTHRASPTHRPRO
9   ALAGLNLEUGLUMETGLUASPGLUASPTHR
10   ILEASPVALPHEGLNGLNGLNTHRSERGLY
11   PROSERSERGLY

Samples:

sample_1: ubiquitin-like molecule, [U-13C; U-15N], 1.21 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.921, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 19961
PDB
DBJ BAB28360 BAC39397 BAE21037 BAE35772 BAE39412
EMBL CAA67897 CAG32064 CAL37097
GB AAB49682 AAB92355 AAD45399 AAH08450 AAH16775
REF NP_001003422 NP_001074186 NP_001185620 NP_001231073 NP_001239218
SP P61955 P61956 P61957 P61958 P61959
TPG DAA13334 DAA18189
AlphaFold P61957

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