7X3T

Cryo-EM structure of ISW1a-dinucleosome


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

ISW1a-dinucleosome

Zhucheng, C.Lifei, L.Kangjing, C.

To be published.

Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H3A,
E,
L [auth K],
P [auth O]
136Xenopus laevisMutation(s): 0 
Gene Names: LOC121398065LOC108703785LOC121398067
UniProt
Find proteins for A0A310TTQ1 (Xenopus laevis)
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UniProt GroupA0A310TTQ1
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H4B,
F,
M [auth L],
Q [auth P]
103Xenopus laevisMutation(s): 0 
UniProt
Find proteins for P62799 (Xenopus laevis)
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H2AC,
G,
N [auth M],
R [auth Q]
130Xenopus laevisMutation(s): 0 
Gene Names: h2ac14.Lh2ac14hist1h2ajhist1h2aj.LLOC494591
UniProt
Find proteins for Q6AZJ8 (Xenopus laevis)
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Histone H2B 1.1D,
H,
O [auth N],
S [auth R]
126Xenopus laevisMutation(s): 0 
UniProt
Find proteins for P02281 (Xenopus laevis)
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
ISWI one complex protein 3K [auth U]624Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: IOC3YFR013W
UniProt
Find proteins for P43596 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
ISWI chromatin-remodeling complex ATPase ISW1T [auth V]1,062Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: ISW1YBR245CYBR1633
EC: 3.6.4
UniProt
Find proteins for P38144 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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Entity ID: 5
MoleculeChains LengthOrganismImage
DNA (343-MER)354synthetic construct
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Entity ID: 6
MoleculeChains LengthOrganismImage
DNA(343-MER)354synthetic construct
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China--

Revision History  (Full details and data files)

  • Version 1.0: 2023-09-20
    Type: Initial release