2a93

NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES

Method: SOLUTION NMR

▼

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

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER × 1 （P28574）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MYC_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–33； UniProt 406–434

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

OrganismNot specified

UniProt P28574

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER × 1 （P01106）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MAX_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 5–33； UniProt 74–102

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2a93
Deposition date deposition_date	1998-06-09
Structure title title	NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES
Keywords keywords	LEUCINE ZIPPERS, 2D NMR, SOLUTION STRUCTURE, H-BONDS, BURIED SALT BRIDGE; LEUCINE ZIPPERS
Experimental Method method	SOLUTION NMR

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2a93__assembly_1__model_21

Assembly 1 · Model 21 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2a93__assembly_1__model_21 | I(q)

100 plotted points; both axes use logarithmic scales.

2a93__assembly_1__model_21 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	15.65 Å
Rg (electron density)	15.08 Å
Total Rg	16.16 Å
Atom count	1078
Residues	64
Excluded volume	9341 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2a93__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`2a93__assembly_1__model_2`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`2a93__assembly_1__model_3`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`2a93__assembly_1__model_4`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`2a93__assembly_1__model_5`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`2a93__assembly_1__model_6`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`2a93__assembly_1__model_7`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`2a93__assembly_1__model_8`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`2a93__assembly_1__model_9`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`2a93__assembly_1__model_10`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`2a93__assembly_1__model_11`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`2a93__assembly_1__model_12`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`2a93__assembly_1__model_13`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`2a93__assembly_1__model_14`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`2a93__assembly_1__model_15`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`2a93__assembly_1__model_16`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`2a93__assembly_1__model_17`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`2a93__assembly_1__model_18`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`2a93__assembly_1__model_19`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`2a93__assembly_1__model_20`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	21	`2a93__assembly_1__model_21`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	22	`2a93__assembly_1__model_22`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	23	`2a93__assembly_1__model_23`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	24	`2a93__assembly_1__model_24`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	25	`2a93__assembly_1__model_25`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	26	`2a93__assembly_1__model_26`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	27	`2a93__assembly_1__model_27`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	28	`2a93__assembly_1__model_28`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	29	`2a93__assembly_1__model_29`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	30	`2a93__assembly_1__model_30`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	31	`2a93__assembly_1__model_31`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	32	`2a93__assembly_1__model_32`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	33	`2a93__assembly_1__model_33`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	34	`2a93__assembly_1__model_34`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	35	`2a93__assembly_1__model_35`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	36	`2a93__assembly_1__model_36`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	37	`2a93__assembly_1__model_37`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	38	`2a93__assembly_1__model_38`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	39	`2a93__assembly_1__model_39`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	40	`2a93__assembly_1__model_40`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

▼

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2a93a1
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.3 — Leucine zipper domain
Family Family family	h.1.3.1 — Leucine zipper domain

Domain ID domain_id	d2a93a2
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	d2a93b_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.3 — Leucine zipper domain
Family Family family	h.1.3.1 — Leucine zipper domain

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER
Molecular weight formula_weight	3837.4 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	43120

Description description	C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER
Molecular weight formula_weight	3782.3 kDa
Source method src_method	syn
Copy count entity_count	1

NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES

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

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

State in the Current Structure

Other States of the Same Protein in the Database

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2a93__assembly_1__model_21

2a93__assembly_1__model_21 | I(q)

2a93__assembly_1__model_21 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

7. Citations (1)

NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES

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

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2a93__assembly_1__model_21

2a93__assembly_1__model_21 | I(q)

2a93__assembly_1__model_21 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

7. Citations (1)