8ott

MYC-MAX bound to a nucleosome at SHL+5.8

Method: ELECTRON MICROSCOPY Dmax: 140.0 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 40–134 Chain E; UniProt 40–134 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H2A type 1-K × 1 (Q8CGP7) DNA (144-MER) × 1 DNA (144-MER) × 1 Myc proto-oncogene protein × 1 (P01106) Protein max × 1 (P61244) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–95; UniProt 40–134 Author chain E; PDBConstruct 1–95; UniProt 40–134

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 22–103 Chain F; UniProt 22–103 Not recorded Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H2A type 1-K × 1 (Q8CGP7) DNA (144-MER) × 1 DNA (144-MER) × 1 Myc proto-oncogene protein × 1 (P01106) Protein max × 1 (P61244) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 1–82; UniProt 22–103 Author chain F; PDBConstruct 1–82; UniProt 22–103

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 9–117 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-J × 2 (P06899) Histone H2A type 1-K × 1 (Q8CGP7) DNA (144-MER) × 1 DNA (144-MER) × 1 Myc proto-oncogene protein × 1 (P01106) Protein max × 1 (P61244) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–109; UniProt 9–117

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 33–125 Chain H; UniProt 33–125 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2A type 1-K × 1 (Q8CGP7) DNA (144-MER) × 1 DNA (144-MER) × 1 Myc proto-oncogene protein × 1 (P01106) Protein max × 1 (P61244) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–93; UniProt 33–125 Author chain H; PDBConstruct 1–93; UniProt 33–125

Histone H2A type 1-K

Homo sapiens

UniProt Q8CGP7

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain G; UniProt 11–118 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (144-MER) × 1 DNA (144-MER) × 1 Myc proto-oncogene protein × 1 (P01106) Protein max × 1 (P61244) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name H2A1K_MOUSE
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–108; UniProt 11–118

Myc proto-oncogene protein

Homo sapiens

UniProt P01106

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain M; UniProt 368–420 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H2A type 1-K × 1 (Q8CGP7) DNA (144-MER) × 1 DNA (144-MER) × 1 Protein max × 1 (P61244) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name MYC_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain M; PDBConstruct 1–53; UniProt 368–420

Protein max

Homo sapiens

UniProt P61244

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain N; UniProt 23–73 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 2 (P06899) Histone H2A type 1-K × 1 (Q8CGP7) DNA (144-MER) × 1 DNA (144-MER) × 1 Myc proto-oncogene protein × 1 (P01106) PTD PENTANEDIAL × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

10 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAX_HUMAN
Isoform P61244-3
PDB entities 9
Chains and sequence ranges Author chain N; PDBConstruct 1–51; UniProt 23–73

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 8ott

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ott
Deposition date deposition_date2023-04-21
Structure title titleMYC-MAX bound to a nucleosome at SHL+5.8
Keywords keywordsE-box, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.16
Radius of gyration Rg (electron density) rg_electron39.57
Forward intensity I(0) i0878398000.00
Molecular weight molecular_weight182150.0 kDa
Excluded volume excluded_volume202570 ų
Envelope volume envelope_volume313340 ų
Hydration-shell volume shell_volume65287 ų
Envelope diameter envelope_diameter141.4
Shell Rg shell_rg45.90
Envelope Rg envelope_rg39.37
Shape Rg shape_rg39.43
Total Rg total_rg40.13
Total atoms total_atoms12448
Residues n_residues1147
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 dmax140.0
Rg (real space) rg_real42.06
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real8.7840e+08
I(0) uncertainty (real space) i0_real_error1.4460e+07
Rg (reciprocal space) rg_reciprocal42.16
I(0) (reciprocal space) i0_reciprocal878500000.0000
Solution quality estimate total_estimate0.8847
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.2
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58310000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id8ottA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottF01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottG01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id8ottH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)