7u4d

CryoEM structure of CENP-N promoted nucleosome stacks with CENP-A and 601 DNA sequence

Method: ELECTRON MICROSCOPY Dmax: 162.0 Å Quality: GOOD

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

Histone H3-like centromeric protein A

Homo sapiens

UniProt P49450

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 × 18 DNA 4 PDB declaration: 22-meric(22) Consistent with all polymer counts Chain A; UniProt 1–140 Chain E; UniProt 1–140 Chain L; UniProt 1–140 Chain P; UniProt 1–140 Not recorded Histone H4 × 4 (P62805) Histone H2A × 4 (Q93077) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (147-MER) × 2 DNA (147-MER) × 2 Centromere protein N × 2 (Q96H22) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 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.

33 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–140; UniProt 1–140 Author chain E; PDBConstruct 1–140; UniProt 1–140 Author chain L; PDBConstruct 1–140; UniProt 1–140 Author chain P; PDBConstruct 1–140; UniProt 1–140

Histone H4

Homo sapiens

UniProt P62805

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 × 18 DNA 4 PDB declaration: 22-meric(22) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Chain M; UniProt 1–103 Chain Q; UniProt 1–103 Not recorded Histone H3-like centromeric protein A × 4 (P49450) Histone H2A × 4 (Q93077) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (147-MER) × 2 DNA (147-MER) × 2 Centromere protein N × 2 (Q96H22) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
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 Author chain M; PDBConstruct 1–103; UniProt 1–103 Author chain Q; PDBConstruct 1–103; UniProt 1–103

Histone H2A

Homo sapiens

UniProt Q93077

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 × 18 DNA 4 PDB declaration: 22-meric(22) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Chain N; UniProt 1–130 Chain R; UniProt 1–130 Not recorded Histone H3-like centromeric protein A × 4 (P49450) Histone H4 × 4 (P62805) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (147-MER) × 2 DNA (147-MER) × 2 Centromere protein N × 2 (Q96H22) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1C_HUMAN
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 Author chain N; PDBConstruct 1–130; UniProt 1–130 Author chain R; PDBConstruct 1–130; UniProt 1–130

Histone H2B type 1-C/E/F/G/I

Homo sapiens

UniProt P62807

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 × 18 DNA 4 PDB declaration: 22-meric(22) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Chain O; UniProt 1–126 Chain S; UniProt 1–126 Not recorded Histone H3-like centromeric protein A × 4 (P49450) Histone H4 × 4 (P62805) Histone H2A × 4 (Q93077) DNA (147-MER) × 2 DNA (147-MER) × 2 Centromere protein N × 2 (Q96H22) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126 Author chain O; PDBConstruct 1–126; UniProt 1–126 Author chain S; PDBConstruct 1–126; UniProt 1–126

Centromere protein N

Homo sapiens

UniProt Q96H22

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 × 18 DNA 4 PDB declaration: 22-meric(22) Consistent with all polymer counts Chain K; UniProt 1–289 Chain V; UniProt 1–289 Not recorded Histone H3-like centromeric protein A × 4 (P49450) Histone H4 × 4 (P62805) Histone H2A × 4 (Q93077) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (147-MER) × 2 DNA (147-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.10 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.

19 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPN_HUMAN
Isoform Q96H22-3
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–289; UniProt 1–289 Author chain V; PDBConstruct 1–289; UniProt 1–289

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 7u4d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7u4d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7u4d
Deposition date deposition_date2022-02-28
Structure title titleCryoEM structure of CENP-N promoted nucleosome stacks with CENP-A and 601 DNA sequence
Keywords keywordsnucleosome, CENP-A, kinetochore, CENP-N, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.06
Radius of gyration Rg (electron density) rg_electron50.79
Forward intensity I(0) i03510690000.00
Molecular weight molecular_weight382770.0 kDa
Excluded volume excluded_volume432310 ų
Envelope volume envelope_volume732670 ų
Hydration-shell volume shell_volume115870 ų
Envelope diameter envelope_diameter164.6
Shell Rg shell_rg59.17
Envelope Rg envelope_rg48.60
Shape Rg shape_rg50.66
Total Rg total_rg51.30
Total atoms total_atoms26240
Residues n_residues2406
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 dmax162.0
Rg (real space) rg_real52.78
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real3.5110e+09
I(0) uncertainty (real space) i0_real_error7.2680e+07
Rg (reciprocal space) rg_reciprocal53.28
I(0) (reciprocal space) i0_reciprocal3513000000.0000
Solution quality estimate total_estimate0.8251
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.6
Skewness Skewness skewness0.070
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha640800000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)