BMRB Entry 25553

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25553
MolProbity Validation Chart

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Title:
Docked structure between SUMO1 and ZZ-domain from CBP
Deposition date:
2015-03-26
Original release date:
2016-06-01
Authors:
Diehl, C.
Citation:

Citation: Diehl, C.; Akke, M.; Bekker-Jensen, S.; Mailand, N.; Streicher, W.; Wikstrom, M.. "Structural Analysis of a Complex between Small Ubiquitin-like Modifier 1 (SUMO1) and the ZZ Domain of CREB-binding Protein (CBP/p300) Reveals a New Interaction Surface on SUMO"  J. Biol. Chem. 291, 12658-12672 (2016).
PubMed: 27129204

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, 11518.051 Da.
entity_2, polymer, 53 residues, 6315.152 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pNIC28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSDQEAKPSTEDLGDKKEGE YIKLKVIGQDSSEIHFKVKM TTHLKKLKESYCQRQGVPMN SLRFLFEGQRIADNHTPKEL GMEEEDVIEVYQEQTGHSTV
entity_2: GQDRFVYTCNECKHHVETRW HCTVCEDYDLCINCYNTKSH AHKMVKWGLGLDD

Data sets:
Data typeCount
13C chemical shifts14
15N chemical shifts92
1H chemical shifts92

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3ZN_13
4ZN_23

Entities:

Entity 1, entity_1 100 residues - 11518.051 Da.

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

Entity 2, entity_2 53 residues - 6315.152 Da.

1   GLYGLNASPARGPHEVALTYRTHRCYSASN
2   GLUCYSLYSHISHISVALGLUTHRARGTRP
3   HISCYSTHRVALCYSGLUASPTYRASPLEU
4   CYSILEASNCYSTYRASNTHRLYSSERHIS
5   ALAHISLYSMETVALLYSTRPGLYLEUGLY
6   LEUASPASP

Entity 3, ZN_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1 mM; entity_2 mM; MES 20 mM; H2O 93%; D2O, [U-2H], 7%

sample_2: entity_1 mM; entity_2 mM; MES 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N IPAP-HSQCsample_1isotropicsample_conditions_1
15N IPAP-HSQCsample_2anisotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

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