SAXSdb — 1hlo

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

PROTEIN (TRANSCRIPTION FACTOR MAX)

Homo sapiens

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 Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric（4） Consistent with all polymer counts	Chain A； UniProt 20–92 Chain B； UniProt 20–92	Not recorded	;DNA (5'-D(CPAPCPCPAPCPGPTPGPGPT)-3') ; × 1 ;DNA (5'-D(APCPCPAPCPGPTPGPGPTPG)-3') ; × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 2.80 Å R-free 0.273

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.

Other PDB	Difference from Current Entry 1HLO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AN2 RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN Deposited 1996-09-06	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 22–107（86 aa） Fragment：DNA BINDING DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；pH 5.50, VAPOR DIFFUSION, SITTING DROP, temperature 277.00K	Resolution 2.90 Å
1NKP Crystal structure of Myc-Max recognizing DNA Deposited 2003-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain B 23–102（80 aa） Fragment：bHLHZ region	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.263
1NKP Crystal structure of Myc-Max recognizing DNA Deposited 2003-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain E 23–102（80 aa） Fragment：bHLHZ region	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å R-free 0.263
1NLW Crystal structure of Mad-Max recognizing DNA Deposited 2003-01-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain B 24–99（76 aa） Fragment：bHLHZ region	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；288 K；20% MPD, 5mM magnesium chloride, 50 mM sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K	Resolution 2.00 Å R-free 0.324
1NLW Crystal structure of Mad-Max recognizing DNA Deposited 2003-01-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain E 24–99（76 aa） Fragment：bHLHZ region	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；288 K；20% MPD, 5mM magnesium chloride, 50 mM sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K	Resolution 2.00 Å R-free 0.324
1R05 Solution Structure of Max B-HLH-LZ Deposited 2003-09-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–103（82 aa） Chain B 22–103（82 aa）	Mutation：N58V, H61L Mutation：N58V, H61L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；308 K；Ionic strength (raw mmCIF value) 250mM KCl；Pressure ambient NMR sample composition 25mM Max 15N, 50mM Phosphate buffer, 250mM KCl \| 90% H2O/10% D2O NMR sample composition 25mM Max 13C,15N, 50mM Phosphate buffer, 250mM KCl \| 90% H2O/10% D2O	Resolution not provided
5EYO The crystal structure of the Max bHLH domain in complex with 5-carboxyl cytosine DNA Deposited 2015-11-25	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 22–107（86 aa） Fragment：UNP residues 22-107	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；289 K；0.2 M Ammonium Sulfate, 0.1 M Sodium Citrate-HCl pH 5.6, 25% (w/v) PEG 4000	Resolution 2.39 Å R-free 0.229
5EYO The crystal structure of the Max bHLH domain in complex with 5-carboxyl cytosine DNA Deposited 2015-11-25	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain C 22–107（86 aa） Fragment：UNP residues 22-107	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；289 K；0.2 M Ammonium Sulfate, 0.1 M Sodium Citrate-HCl pH 5.6, 25% (w/v) PEG 4000	Resolution 2.39 Å R-free 0.229
6G6J The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 22–103（82 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% (w/v) PEG 3350 0.2M sodium sulfate decahydrate, pH 7	Resolution 2.25 Å R-free 0.236
6G6J The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 22–103（82 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；20% (w/v) PEG 3350 0.2M sodium sulfate decahydrate, pH 7	Resolution 2.25 Å R-free 0.236
6G6K The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 22–103（82 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 0.075 %(w/v) of each Additive, 5 %(v/v) EtOH, 0.1 M MOPS/HEPES-Na, pH 7.5, Additive: 0.75 %(w/v) menthol, 0.75 %(w/v) caffeic acid, 0.75 %(w/v) D-quinic acid, 0.75 %(w/v) shikimic acid, 0.75 %(w/v) gallic acid monohydrate, 0.75 %(w/v) N-vanillylnonanamide.	Resolution 1.35 Å R-free 0.203
6G6K The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 22–103（82 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 0.075 %(w/v) of each Additive, 5 %(v/v) EtOH, 0.1 M MOPS/HEPES-Na, pH 7.5, Additive: 0.75 %(w/v) menthol, 0.75 %(w/v) caffeic acid, 0.75 %(w/v) D-quinic acid, 0.75 %(w/v) shikimic acid, 0.75 %(w/v) gallic acid monohydrate, 0.75 %(w/v) N-vanillylnonanamide.	Resolution 1.35 Å R-free 0.203
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 22–103（82 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 22–103（82 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 22–103（82 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
6G6L The crystal structures of Human MYC:MAX bHLHZip complex Deposited 2018-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 22–103（82 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% w/v PEG 8000, 20% v/v ethylene glycol, 15% PEG 8000 15, 0.2M ammonium sulfate, pH 7	Resolution 2.20 Å R-free 0.268
8OTS OCT4 and MYC-MAX co-bound to a nucleosome Deposited 2023-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: tridecameric	Chain N 22–102（81 aa）	Not recorded	PTD PENTANEDIAL × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8OTT MYC-MAX bound to a nucleosome at SHL+5.8 Deposited 2023-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 10 PDB declaration: dodecameric	Chain N 23–73（51 aa）	Not recorded	PTD PENTANEDIAL × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å

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	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 8–80； UniProt 20–92 Author chain B； PDBConstruct 8–80； UniProt 20–92

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1hlo
Deposition date deposition_date	1997-09-10
Structure title title	THE CRYSTAL STRUCTURE OF AN INTACT HUMAN MAX-DNA COMPLEX: NEW INSIGHTS INTO MECHANISMS OF TRANSCRIPTIONAL CONTROL
Keywords keywords	TRANSCRIPTIONAL REGULATION, DNA BINDING, COMPLEX (TRANSCRIPTION FACTOR MAX-DNA), TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	22.54 Å
Radius of gyration Rg (electron density) rg_electron	22.37 Å
Forward intensity I(0) i0	17146800.00
Molecular weight molecular_weight	24923.0 kDa
Excluded volume excluded_volume	28491 Å³
Envelope volume envelope_volume	38259 Å³
Hydration-shell volume shell_volume	16254 Å³
Envelope diameter envelope_diameter	81.9 Å
Shell Rg shell_rg	26.36 Å
Envelope Rg envelope_rg	23.21 Å
Shape Rg shape_rg	22.36 Å
Total Rg total_rg	22.85 Å
Total atoms total_atoms	1728
Residues n_residues	175
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	81.0 Å
Rg (real space) rg_real	22.86 Å
Rg uncertainty (real space) rg_real_error	0.84 Å
I(0) (real space) i0_real	1.7150e+07
I(0) uncertainty (real space) i0_real_error	2.4200e+05
Rg (reciprocal space) rg_reciprocal	22.78 Å
I(0) (reciprocal space) i0_reciprocal	17150000.0000
Solution quality estimate total_estimate	0.7904
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.9 Å
Skewness Skewness skewness	0.697
Kurtosis Kurtosis kurtosis	0.012
Angular range angular_range	— – 0.3500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1642000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.588; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.576; Smooth: 0.934

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(CPAPCPCPAPCPGPTPGPGP*T)-3') ;
Molecular weight formula_weight	3334.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	C
Atom count atom_count	1746

CACCACGTGGT

Entity 2 Entity 2 polymer

Description description	;DNA (5'-D(APCPCPAPCPGPTPGPGPTP*G)-3') ;
Molecular weight formula_weight	3374.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	D

ACCACGTGGTG

Entity 3 Entity 3 polymer

Description description	PROTEIN (TRANSCRIPTION FACTOR MAX)
Molecular weight formula_weight	9542.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B

NDDIEVESDADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQN

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	18

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1hloa_
Class class	a — All alpha proteins
Fold Fold fold	a.38 — HLH-like
Superfamily Superfamily superfamily	a.38.1 — HLH, helix-loop-helix DNA-binding domain
Family Family family	a.38.1.1 — HLH, helix-loop-helix DNA-binding domain

Domain ID domain_id	d1hlob_
Class class	a — All alpha proteins
Fold Fold fold	a.38 — HLH-like
Superfamily Superfamily superfamily	a.38.1 — HLH, helix-loop-helix DNA-binding domain
Family Family family	a.38.1.1 — HLH, helix-loop-helix DNA-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id	1hloA00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily	10 — Helix-loop-helix DNA-binding domain

Domain ID domain_id	1hloB00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily	10 — Helix-loop-helix DNA-binding domain

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8. Citations (1)

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Unit-cell length a length_a	108.000 Å
Unit-cell length b length_b	108.000 Å
Unit-cell length c length_c	127.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2130
R_work r_work	0.2130
R_free r_free	0.2730

fit	/app/data/saxs_computation/hl/1hlo/1hlo.fit
pddf	/app/data/pr_computation/hl/1hlo/1hlo.pr.out
profile	/app/data/saxs_computation/hl/1hlo/1hlo.dat

THE CRYSTAL STRUCTURE OF AN INTACT HUMAN MAX-DNA COMPLEX: NEW INSIGHTS INTO MECHANISMS OF TRANSCRIPTIONAL CONTROL

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

PROTEIN (TRANSCRIPTION FACTOR MAX)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)