9si9

Chromosomal Passenger Complex in complex with H3T3ph Nucleosome (Class0)

Method: ELECTRON MICROSCOPY Dmax: 144.2 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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 2–136 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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 4
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A type 1

Homo sapiens

UniProt P0C0S8

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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.

49 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B type 1-J

Homo sapiens

UniProt P06899

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain L; UniProt 1–280 Chain O; UniProt 1–280 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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 7
Chains and sequence ranges Author chain L; PDBConstruct 1–280; UniProt 1–280 Author chain O; PDBConstruct 1–280; UniProt 1–280

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain M; UniProt 1–142 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Inner centromere protein × 1 (Q9NQS7) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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 M; PDBConstruct 1–142; UniProt 1–142

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain N; UniProt 1–918 Not recorded DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) H3.4 histone × 1 (S4RAZ3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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 9
Chains and sequence ranges Author chain N; PDBConstruct 1–918; UniProt 1–918

H3.4 histone

Homo sapiens

UniProt S4RAZ3

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain E; UniProt 25–159 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (147-MER) × 1 DNA (147-MER) × 1 Histone H3.2 × 1 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-J × 2 (P06899) Borealin × 2 (Q53HL2) Baculoviral IAP repeat-containing protein 5 × 1 (O15392) Inner centromere protein × 1 (Q9NQS7) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.86 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S4RAZ3_PETMA
Isoform
PDB entities 10
Chains and sequence ranges Author chain E; PDBConstruct 1–135; UniProt 25–159

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 9si9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9si9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9si9
Deposition date deposition_date2025-08-28
Structure title titleChromosomal Passenger Complex in complex with H3T3ph Nucleosome (Class0)
Keywords keywordsNucleosome-binding DNA-binding Stabilising Nucleosome Acidic-patch interaction, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.41
Radius of gyration Rg (electron density) rg_electron42.33
Forward intensity I(0) i01093910000.00
Molecular weight molecular_weight211170.0 kDa
Excluded volume excluded_volume239030 ų
Envelope volume envelope_volume368620 ų
Hydration-shell volume shell_volume72437 ų
Envelope diameter envelope_diameter157.7
Shell Rg shell_rg47.78
Envelope Rg envelope_rg41.78
Shape Rg shape_rg42.26
Total Rg total_rg42.70
Total atoms total_atoms14471
Residues n_residues1346
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 dmax144.2
Rg (real space) rg_real43.31
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real1.0940e+09
I(0) uncertainty (real space) i0_real_error1.9850e+07
Rg (reciprocal space) rg_reciprocal43.41
I(0) (reciprocal space) i0_reciprocal1094000000.0000
Solution quality estimate total_estimate0.8776
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.1
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98770000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)