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 17536

Title: Molecular Determinants of Paralogue-Specific SUMO-SIM Recognition   PubMed: 22147707

Deposition date: 2011-03-20 Original release date: 2011-12-14

Authors: Namanja, Andrew; Li, Yi-Jia; Su, Yang; Wong, Steven; Lu, Jingjun; Colson, Loren; Wu, Chenggang; Li, Shawn; Chen, Yuan

Citation: Namanja, Andrew; Li, Yi-Jia; Su, Yang; Wong, Steven; Lu, Jingjun; Colson, Loren; Wu, Chenggang; Li, Shawn; Chen, Yuan. "Insights into High Affinity Small Ubiquitin-like Modifier (SUMO) Recognition by SUMO-interacting Motifs (SIMs) Revealed by a Combination of NMR and Peptide Array Analysis."  J. Biol. Chem. 287, 3231-3240 (2012).

Assembly members:
SUMO1, polymer, 97 residues, 9099.442 Da.
M-IR2_peptide, polymer, 13 residues, 1616.870 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

Entity Sequences (FASTA):
SUMO1: MSDQEAKPSTEDLGDKKEGE YIKLKVIGQDSSEIHFKVKM TTHLKKLKESYCQRQGVPMN SLRFLFEGQRIADNHTPKEL GMEEEDVIEVYQEQTGG
M-IR2_peptide: DNEIEVIIVWEKK

Data sets:
Data typeCount
13C chemical shifts225
15N chemical shifts92
1H chemical shifts198

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SUMO11
2M-IR22

Entities:

Entity 1, SUMO1 97 residues - 9099.442 Da.

1   METSERASPGLNGLUALALYSPROSERTHR
2   GLUASPLEUGLYASPLYSLYSGLUGLYGLU
3   TYRILELYSLEULYSVALILEGLYGLNASP
4   SERSERGLUILEHISPHELYSVALLYSMET
5   THRTHRHISLEULYSLYSLEULYSGLUSER
6   TYRCYSGLNARGGLNGLYVALPROMETASN
7   SERLEUARGPHELEUPHEGLUGLYGLNARG
8   ILEALAASPASNHISTHRPROLYSGLULEU
9   GLYMETGLUGLUGLUASPVALILEGLUVAL
10   TYRGLNGLUGLNTHRGLYGLY

Entity 2, M-IR2 13 residues - 1616.870 Da.

1   ASPASNGLUILEGLUVALILEILEVALTRP
2   GLULYSLYS

Samples:

sample_1: SUMO1, [U-13C; U-15N; U-2H], 0.5 mM; M-IR2 peptide 1.0 mM; H2O 90%; D2O 10%

sample_2: SUMO1, [U-15N]; perdeuterated, 0.5 mM; M-IR2 peptide 0.6 mM; H2O 90%; D2O 10%

sample_3: SUMO1, [U-15N; U-2H], 0.6 mM; M-IR2 peptide 0.4 mM; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 15N-edited NOESYHSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC-TOCSYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment

HADDOCK v2.0, Bonvin - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - analysis, refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16611 25299
PDB
DBJ BAB22172 BAB27379 BAB93477 BAC40739 BAE35024
EMBL CAA67898 CAG31129 CAG46944 CAG46953 CAH92616
GB AAB39999 AAB40388 AAB40390 AAC39959 AAC50733
REF NP_001005781 NP_001005782 NP_001009672 NP_001030535 NP_001106146
SP A7WLH8 P63165 P63166 Q2EF74 Q5E9D1
TPG DAA32560

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