SAXSdb — 1r05

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

Max protein

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 22–103 Chain B； UniProt 22–103	Mutation：N58V, H61L	No other associated polymer	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

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 1R05	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 oligomeric state Different experimental method 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
1HLO THE CRYSTAL STRUCTURE OF AN INTACT HUMAN MAX-DNA COMPLEX: NEW INSIGHTS INTO MECHANISMS OF TRANSCRIPTIONAL CONTROL Deposited 1997-09-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 20–92（73 aa） Chain B 20–92（73 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 2.80 Å R-free 0.273
1NKP Crystal structure of Myc-Max recognizing DNA Deposited 2003-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental method 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 method 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 method 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 method 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
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 oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–83； UniProt 22–103 Author chain B； PDBConstruct 2–83； UniProt 22–103

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	1r05
Deposition date deposition_date	2003-09-19
Structure title title	Solution Structure of Max B-HLH-LZ
Keywords keywords	Basic-Helix-Loop-Helix-LeucineZipper Homodimer, TRANSCRIPTION; TRANSCRIPTION
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	26.72 Å
Radius of gyration Rg (electron density) rg_electron	26.47 Å
Forward intensity I(0) i0	251270000.00
Molecular weight molecular_weight	121870.0 kDa
Excluded volume excluded_volume	149000 Å³
Envelope volume envelope_volume	56625 Å³
Hydration-shell volume shell_volume	19008 Å³
Envelope diameter envelope_diameter	108.4 Å
Shell Rg shell_rg	30.93 Å
Envelope Rg envelope_rg	30.65 Å
Shape Rg shape_rg	26.35 Å
Total Rg total_rg	27.00 Å
Total atoms total_atoms	17124
Residues n_residues	1044
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	101.7 Å
Rg (real space) rg_real	27.41 Å
Rg uncertainty (real space) rg_real_error	1.19 Å
I(0) (real space) i0_real	2.5130e+08
I(0) uncertainty (real space) i0_real_error	4.2800e+06
Rg (reciprocal space) rg_reciprocal	27.19 Å
I(0) (reciprocal space) i0_reciprocal	251200000.0000
Solution quality estimate total_estimate	0.6849
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.0 Å
Skewness Skewness skewness	0.726
Kurtosis Kurtosis kurtosis	-0.047
Angular range angular_range	— – 0.2950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	629500.0000
Real-space data points n_real_points	60
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.327; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.037; Smooth: 0.882

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1r05a1
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	d1r05a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1r05b1
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	d1r05b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	1r05A00
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	1r05B00
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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Description description	Max protein
Molecular weight formula_weight	10173.5 kDa
Mutation mutation	N58V, H61L
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	17124

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

fit	/app/data/saxs_computation/r0/1r05/1r05.fit
pddf	/app/data/pr_computation/r0/1r05/1r05.pr.out
profile	/app/data/saxs_computation/r0/1r05/1r05.dat

Solution Structure of Max B-HLH-LZ

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

Max protein

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)