SAXSdb — 7bwn

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

Chimera of Green fluorescent protein and p53dim

Aequorea victoria

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	Cellular tumor antigen p53 × 1 （P04637） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A059PIQ0_AEQVI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–238； UniProt 1–238 Author chain C； PDBConstruct 1–238； UniProt 1–238 Author chain E； PDBConstruct 1–238； UniProt 1–238 Author chain F； PDBConstruct 1–238； UniProt 1–238 Author chain H； PDBConstruct 1–238； UniProt 1–238 Author chain J； PDBConstruct 1–238； UniProt 1–238 Author chain M； PDBConstruct 1–238； UniProt 1–238 Author chain O； PDBConstruct 1–238； UniProt 1–238

Cellular tumor antigen p53

Homo sapiens

UniProt P04637

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 2	Chimera of Green fluorescent protein and p53dim × 1 （A0A059PIQ0） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P53_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 11–41； UniProt 326–356 Author chain D； PDBConstruct 11–41； UniProt 326–356 Author chain G； PDBConstruct 11–41； UniProt 326–356 Author chain I； PDBConstruct 11–41； UniProt 326–356 Author chain K； PDBConstruct 11–41； UniProt 326–356 Author chain L； PDBConstruct 11–41； UniProt 326–356 Author chain N； PDBConstruct 11–41； UniProt 326–356 Author chain P； PDBConstruct 11–41； UniProt 326–356

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	7bwn
Deposition date deposition_date	2020-04-15
Structure title title	Crystal Structure of a Designed Protein Heterocatenane
Keywords keywords	Heterocatenane, RECOMBINATION; RECOMBINATION
Experimental Method method	X-RAY DIFFRACTION

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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.

7bwn__assembly_1__model_1

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

Download this curve (.dat)

7bwn__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7bwn__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.47 Å
Rg (electron density)	22.79 Å
Total Rg	23.52 Å
Atom count	2499
Residues	312
Excluded volume	44119 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7bwn__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`7bwn__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`7bwn__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`7bwn__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`7bwn__assembly_5__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`7bwn__assembly_6__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`7bwn__assembly_7__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`7bwn__assembly_8__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Chimera of Green fluorescent protein and p53dim
Molecular weight formula_weight	31618.5 kDa
Mutation mutation	R2S,S30R,A72S,Q80R,A206V,M340E,L344K
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,A,C,E,H,J,M,O
Atom count atom_count	20596

MSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKKLGGEYFTLQIRGRERFEEFREKNEALELKDAQAGGTCFNAS

Source Source

Source organism organism	Aequorea victoria
Common name common_name	Jellyfish
NCBI taxonomy ID ncbi_taxonomy_id	6100
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Cellular tumor antigen p53
Molecular weight formula_weight	5518.0 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,B,D,G,I,K,N,P

GGHHHHHHELEYFTLQIRGRERFEEFREKNEALELKDAQAGTSCFN

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	565

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6. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id	7bwnA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnC01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnC02
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	7bwnE01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnF01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnH01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnJ01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnM01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

Domain ID domain_id	7bwnO01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily	10 — Green fluorescent protein

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Unit-cell length a length_a	108.897 Å
Unit-cell length b length_b	108.897 Å
Unit-cell length c length_c	684.966 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	72

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.396 Å
Low-resolution limit resolution_low	49.145 Å
R factor r_factor	0.1879
R_work r_work	0.1870
R_free r_free	0.2386

Crystal Structure of a Designed Protein Heterocatenane

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

Chimera of Green fluorescent protein and p53dim

State in the Current Structure

Other States of the Same Protein in the Database

Cellular tumor antigen p53

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

7bwn__assembly_1__model_1

7bwn__assembly_1__model_1 | I(q)

7bwn__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

7. Citations (1)

Crystal Structure of a Designed Protein Heterocatenane

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

Chimera of Green fluorescent protein and p53dim

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cellular tumor antigen p53

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

7bwn__assembly_1__model_1

7bwn__assembly_1__model_1 | I(q)

7bwn__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

7. Citations (1)