SAXSdb — 1a92

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

DELTA ANTIGEN

Hepatitis delta virus

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 12–60 Chain B； UniProt 12–60 Chain C； UniProt 12–60 Chain D； UniProt 12–60	Fragment：OLIGOMERIZATION DOMAIN Mutation：INS (K60-Y)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.2；pH 5.2	Resolution 1.80 Å R-free 0.279
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 12–60 Chain C； UniProt 12–60	Fragment：OLIGOMERIZATION DOMAIN Mutation：INS (K60-Y)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.2；pH 5.2	Resolution 1.80 Å R-free 0.279
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 12–60 Chain D； UniProt 12–60	Fragment：OLIGOMERIZATION DOMAIN Mutation：INS (K60-Y)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.2；pH 5.2	Resolution 1.80 Å R-free 0.279

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 1A92	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BY0 N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN Deposited 1998-10-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–50（27 aa） Fragment：RESIDUES 24-50	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Pressure 1	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AANT_HDVAM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–49； UniProt 12–60 Author chain B； PDBConstruct 1–49； UniProt 12–60 Author chain C； PDBConstruct 1–49； UniProt 12–60 Author chain D； PDBConstruct 1–49； UniProt 12–60

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	1a92
Deposition date deposition_date	1998-04-15
Structure title title	OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN
Keywords keywords	LEUCINE ZIPPER, COILED-COIL, OLIGOMERIZATION, HEPATITIS DELTA, HDV; LEUCINE ZIPPER
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	22.09 Å
Radius of gyration Rg (electron density) rg_electron	21.31 Å
Forward intensity I(0) i0	9478460.00
Molecular weight molecular_weight	23670.0 kDa
Excluded volume excluded_volume	30256 Å³
Envelope volume envelope_volume	39571 Å³
Hydration-shell volume shell_volume	16778 Å³
Envelope diameter envelope_diameter	71.8 Å
Shell Rg shell_rg	26.21 Å
Envelope Rg envelope_rg	20.84 Å
Shape Rg shape_rg	21.34 Å
Total Rg total_rg	22.03 Å
Total atoms total_atoms	1670
Residues n_residues	199
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	74.9 Å
Rg (real space) rg_real	22.12 Å
Rg uncertainty (real space) rg_real_error	0.66 Å
I(0) (real space) i0_real	9.4780e+06
I(0) uncertainty (real space) i0_real_error	1.2750e+05
Rg (reciprocal space) rg_reciprocal	22.12 Å
I(0) (reciprocal space) i0_reciprocal	9478000.0000
Solution quality estimate total_estimate	0.8811
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	73.8 Å
Skewness Skewness skewness	0.330
Kurtosis Kurtosis kurtosis	-0.345
Angular range angular_range	— – 0.3600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	772400.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.862; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.930

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1a92a_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.6 — Oligomerization domain of hepatitis delta antigen
Family Family family	h.4.6.1 — Oligomerization domain of hepatitis delta antigen

Domain ID domain_id	d1a92b_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.6 — Oligomerization domain of hepatitis delta antigen
Family Family family	h.4.6.1 — Oligomerization domain of hepatitis delta antigen

Domain ID domain_id	d1a92c_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.6 — Oligomerization domain of hepatitis delta antigen
Family Family family	h.4.6.1 — Oligomerization domain of hepatitis delta antigen

Domain ID domain_id	d1a92d_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.6 — Oligomerization domain of hepatitis delta antigen
Family Family family	h.4.6.1 — Oligomerization domain of hepatitis delta antigen

CATH v4.4 (4 domains)

Domain ID domain_id	1a92A00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	220 — Light-harvesting Protein
Homologous superfamily homologous superfamily	40 — Delta antigen, N-terminal

Domain ID domain_id	1a92B00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	220 — Light-harvesting Protein
Homologous superfamily homologous superfamily	40 — Delta antigen, N-terminal

Domain ID domain_id	1a92C00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	220 — Light-harvesting Protein
Homologous superfamily homologous superfamily	40 — Delta antigen, N-terminal

Domain ID domain_id	1a92D00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	220 — Light-harvesting Protein
Homologous superfamily homologous superfamily	40 — Delta antigen, N-terminal

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8. Citations (2)

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Unit-cell length a length_a	109.220 Å
Unit-cell length b length_b	85.300 Å
Unit-cell length c length_c	29.360 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	16

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2270
R_work r_work	0.2270
R_free r_free	0.2790

Description description	DELTA ANTIGEN
Molecular weight formula_weight	6006.1 kDa
Mutation mutation	INS (K60-Y)
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	1784

OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN

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

DELTA ANTIGEN

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Hepatitis delta virus
NCBI Class编号 ncbi_taxonomy_id	12475

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	114

fit	/app/data/saxs_computation/a9/1a92/1a92.fit
pddf	/app/data/pr_computation/a9/1a92/1a92.pr.out
profile	/app/data/saxs_computation/a9/1a92/1a92.dat