SAXSdb — 1beg

▼

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

BETA-ELICITIN CRYPTOGEIN

OrganismNot specified

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 21–118	Not recorded	No other associated polymer	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	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 1BEG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BEO BETA-CRYPTOGEIN Deposited 1996-08-02	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 21–118（98 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；4.85 M NACL, PH 7.5	Resolution 2.20 Å R-free 0.279
1BXM ENGINEERED BETA-CRYPTOGEIN COMPLEXED WITH ERGOSTEROL Deposited 1998-10-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 23–118（96 aa）	Mutation：T1G, A2T, K13H	ERG ERGOSTEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.5；pH 4.5	Resolution 2.15 Å R-free 0.229
1LRI BETA-CRYPTOGEIN-CHOLESTEROL COMPLEX Deposited 2002-05-15	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–118（98 aa）	Not recorded	CL CHLORIDE ION × 1 CLR CHOLESTEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；sodium chloride, cholesterol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.45 Å R-free 0.188

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ELIB_PHYCR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–98； UniProt 21–118

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	1beg
Deposition date deposition_date	1996-11-26
Structure title title	STRUCTURE OF FUNGAL ELICITOR, NMR, 18 STRUCTURES
Keywords keywords	FUNGAL ELICITOR, SIGNALLING PROTEIN, FUNGAL TOXIN; SIGNAL
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	13.11 Å
Radius of gyration Rg (electron density) rg_electron	12.92 Å
Forward intensity I(0) i0	492173000.00
Molecular weight molecular_weight	185490.0 kDa
Excluded volume excluded_volume	231400 Å³
Envelope volume envelope_volume	20948 Å³
Hydration-shell volume shell_volume	12750 Å³
Envelope diameter envelope_diameter	45.4 Å
Shell Rg shell_rg	19.79 Å
Envelope Rg envelope_rg	14.05 Å
Shape Rg shape_rg	12.91 Å
Total Rg total_rg	13.09 Å
Total atoms total_atoms	25794
Residues n_residues	1764
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	42.2 Å
Rg (real space) rg_real	13.00 Å
Rg uncertainty (real space) rg_real_error	0.23 Å
I(0) (real space) i0_real	4.9220e+08
I(0) uncertainty (real space) i0_real_error	4.8160e+06
Rg (reciprocal space) rg_reciprocal	13.00 Å
I(0) (reciprocal space) i0_reciprocal	492200000.0000
Solution quality estimate total_estimate	0.7155
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.7 Å
Skewness Skewness skewness	-0.078
Kurtosis Kurtosis kurtosis	-0.570
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	82500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.998; Smooth: 0.970

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bega_
Class class	a — All alpha proteins
Fold Fold fold	a.134 — Fungal elicitin
Superfamily Superfamily superfamily	a.134.1 — Fungal elicitin
Family Family family	a.134.1.1 — Fungal elicitin

CATH v4.4 (1 domains)

Domain ID domain_id	1begA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	239 — Beta-cryptogein
Homologous superfamily homologous superfamily	10 — Elicitin domain

▶

8. Citations (2)

▶

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	BETA-ELICITIN CRYPTOGEIN
Molecular weight formula_weight	10340.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	25794

fit	/app/data/saxs_computation/be/1beg/1beg.fit
pddf	/app/data/pr_computation/be/1beg/1beg.pr.out
profile	/app/data/saxs_computation/be/1beg/1beg.dat

STRUCTURE OF FUNGAL ELICITOR, NMR, 18 STRUCTURES

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

BETA-ELICITIN CRYPTOGEIN

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)