SAXSdb — 1au1

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

INTERFERON-BETA

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	Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 22–187 Chain B； UniProt 22–187	Not recorded	;beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-[alpha-D-quinovopyranose-(1-6)]beta-D-glucopyranose ; × 1 alpha-D-quinovopyranose-(1-6)-beta-D-glucopyranose × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；pH 7.5	Resolution 2.20 Å R-free 0.283

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	INB_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–166； UniProt 22–187 Author chain B； PDBConstruct 1–166； UniProt 22–187

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	1au1
Deposition date deposition_date	1997-09-09
Structure title title	HUMAN INTERFERON-BETA CRYSTAL STRUCTURE
Keywords keywords	INTERFERON, HELICAL CYTOKINE, IMMUNE SYSTEM, CYTOKINE; INTERFERON
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	25.98 Å
Radius of gyration Rg (electron density) rg_electron	25.22 Å
Forward intensity I(0) i0	27773900.00
Molecular weight molecular_weight	41160.0 kDa
Excluded volume excluded_volume	51837 Å³
Envelope volume envelope_volume	64486 Å³
Hydration-shell volume shell_volume	22226 Å³
Envelope diameter envelope_diameter	96.2 Å
Shell Rg shell_rg	30.93 Å
Envelope Rg envelope_rg	25.66 Å
Shape Rg shape_rg	25.18 Å
Total Rg total_rg	26.07 Å
Total atoms total_atoms	3623
Residues n_residues	329
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	93.6 Å
Rg (real space) rg_real	26.12 Å
Rg uncertainty (real space) rg_real_error	0.84 Å
I(0) (real space) i0_real	2.7770e+07
I(0) uncertainty (real space) i0_real_error	3.8900e+05
Rg (reciprocal space) rg_reciprocal	26.08 Å
I(0) (reciprocal space) i0_reciprocal	27770000.0000
Solution quality estimate total_estimate	0.8309
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.5 Å
Skewness Skewness skewness	0.465
Kurtosis Kurtosis kurtosis	-0.235
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	9525000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.712; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.728; Smooth: 0.932

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	INTERFERON-BETA
Molecular weight formula_weight	20054.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3866

MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN

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	Cricetulus griseus

Entity 2 Entity 2 branched

Description description	;beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-[alpha-D-quinovopyranose-(1-6)]beta-D-glucopyranose ;
Molecular weight formula_weight	1137.0 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 branched

Description description	alpha-D-quinovopyranose-(1-6)-beta-D-glucopyranose
Molecular weight formula_weight	326.3 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	81

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1au1a_
Class class	a — All alpha proteins
Fold Fold fold	a.26 — 4-helical cytokines
Superfamily Superfamily superfamily	a.26.1 — 4-helical cytokines
Family Family family	a.26.1.3 — Interferons/interleukin-10 (IL-10)

Domain ID domain_id	d1au1b_
Class class	a — All alpha proteins
Fold Fold fold	a.26 — 4-helical cytokines
Superfamily Superfamily superfamily	a.26.1 — 4-helical cytokines
Family Family family	a.26.1.3 — Interferons/interleukin-10 (IL-10)

CATH v4.4 (2 domains)

Domain ID domain_id	1au1A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1au1B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Unit-cell length a length_a	55.300 Å
Unit-cell length b length_b	65.900 Å
Unit-cell length c length_c	121.500 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2230
R_work r_work	0.2230
R_free r_free	0.2830

fit	/app/data/saxs_computation/au/1au1/1au1.fit
pddf	/app/data/pr_computation/au/1au1/1au1.pr.out
profile	/app/data/saxs_computation/au/1au1/1au1.dat

HUMAN INTERFERON-BETA CRYSTAL STRUCTURE

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

INTERFERON-BETA

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