8rup

Chromosome Passenger Complex (CPC) localization module in complex with H3.T3p-nucleosome

Method: ELECTRON MICROSCOPY Dmax: 149.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H3.2

Xenopus laevis

UniProt P84233

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain A; UniProt 1–136 Not recorded Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Borealin × 1 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136

Histone H4

Xenopus laevis

UniProt P62799

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.2 × 1 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Borealin × 1 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Borealin × 1 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–130; UniProt 1–130 Author chain G; PDBConstruct 1–130; UniProt 1–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Borealin × 1 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–123; UniProt 5–126 Author chain H; PDBConstruct 2–123; UniProt 5–126

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain E; UniProt 2–136 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Borealin × 1 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 2–136

Baculoviral IAP repeat-containing protein 5

Homo sapiens

UniProt O15392

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain K; UniProt 1–142 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Borealin × 1 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

35 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BIRC5_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain K; PDBConstruct 3–144; UniProt 1–142

Borealin

Homo sapiens

UniProt Q53HL2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain L; UniProt 1–76 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BOREA_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain L; PDBConstruct 1–76; UniProt 1–76

Inner centromere protein

Homo sapiens

UniProt Q9NQS7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain M; UniProt 1–80 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H3 × 1 (A0A310TTQ1) DNA (147-MER) × 1 DNA (147-MER) × 1 Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Borealin × 1 (Q53HL2) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM TRIS-HCl, pH 7.5, 150 mM NaCl, 2 mM DTT, 0.3% n-octyl-beta-D-glucoside cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting time, -10 force, no wait time. Resolution 2.42 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INCE_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain M; PDBConstruct 3–82; UniProt 1–80

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8rup

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rup
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rup
Deposition date deposition_date2024-01-31
Structure title titleChromosome Passenger Complex (CPC) localization module in complex with H3.T3p-nucleosome
Keywords keywordsCPC, nucleosome, cell cycle, chromosome segregation, histone modification, cryoEM; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier44.46
Radius of gyration Rg (electron density) rg_electron43.52
Forward intensity I(0) i01043000000.00
Molecular weight molecular_weight204700.0 kDa
Excluded volume excluded_volume230670 ų
Envelope volume envelope_volume366560 ų
Hydration-shell volume shell_volume70987 ų
Envelope diameter envelope_diameter156.4
Shell Rg shell_rg48.11
Envelope Rg envelope_rg42.93
Shape Rg shape_rg43.46
Total Rg total_rg43.84
Total atoms total_atoms25466
Residues n_residues1314
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax149.0
Rg (real space) rg_real44.39
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real1.0430e+09
I(0) uncertainty (real space) i0_real_error1.8360e+07
Rg (reciprocal space) rg_reciprocal44.46
I(0) (reciprocal space) i0_reciprocal1043000000.0000
Solution quality estimate total_estimate0.8747
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.1
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.286
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha91190000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.829

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (2)

9. Files and Curves (10)