SAXSdb — 1bxm

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

BETA-CRYPTOGEIN

Phytophthora cryptogea

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 23–118	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

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 1BXM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BEG STRUCTURE OF FUNGAL ELICITOR, NMR, 18 STRUCTURES Deposited 1996-11-26	Different construct Different mutation/modification Different oligomeric state 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	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BEO BETA-CRYPTOGEIN Deposited 1996-08-02	Different construct Different mutation/modification Different ligand/ion 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
1LRI BETA-CRYPTOGEIN-CHOLESTEROL COMPLEX Deposited 2002-05-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion 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 4–99； UniProt 23–118

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bxm
Deposition date deposition_date	1998-10-05
Structure title title	ENGINEERED BETA-CRYPTOGEIN COMPLEXED WITH ERGOSTEROL
Keywords keywords	FUNGAL TOXIC ELICITOR MUTANT, ELICITIN, PHYTOPHTHORA, STEROL, PLANT PATHOGEN, FUNGAL TOXIC ELICITOR; FUNGAL TOXIC ELICITOR
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	14.20 Å
Radius of gyration Rg (electron density) rg_electron	12.67 Å
Forward intensity I(0) i0	2399270.00
Molecular weight molecular_weight	10854.0 kDa
Excluded volume excluded_volume	13659 Å³
Envelope volume envelope_volume	14941 Å³
Hydration-shell volume shell_volume	10275 Å³
Envelope diameter envelope_diameter	42.1 Å
Shell Rg shell_rg	18.10 Å
Envelope Rg envelope_rg	12.87 Å
Shape Rg shape_rg	12.67 Å
Total Rg total_rg	13.93 Å
Total atoms total_atoms	755
Residues n_residues	99
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	45.0 Å
Rg (real space) rg_real	14.10 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	2.3990e+06
I(0) uncertainty (real space) i0_real_error	2.4820e+04
Rg (reciprocal space) rg_reciprocal	14.11 Å
I(0) (reciprocal space) i0_reciprocal	2399000.0000
Solution quality estimate total_estimate	0.8903
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.9 Å
Skewness Skewness skewness	0.040
Kurtosis Kurtosis kurtosis	-0.418
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	184600.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.962

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	BETA-CRYPTOGEIN
Molecular weight formula_weight	10493.0 kDa
Mutation mutation	T1G, A2T, K13H
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	812

RGTCTATQQTAAYHTLVSILSDASFNQCSTDSGYSMLTAKALPTTAQYKLMCASTACNTMIKKIVTLNPPNCDLTVPTSGLVLNVYSYANGFSNKCSSL

来源 Source

来源生物 organism	Phytophthora cryptogea
NCBI Class编号 ncbi_taxonomy_id	4786
宿主生物 host_organism	Pichia pastoris

Entity 2 Entity 2 non-polymer

Description description	ERGOSTEROL
Molecular weight formula_weight	396.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	57

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bxma_
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	1bxmA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	239 — Beta-cryptogein
Homologous superfamily homologous superfamily	10 — Elicitin domain

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8. Citations (4)

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Unit-cell length a length_a	31.130 Å
Unit-cell length b length_b	95.230 Å
Unit-cell length c length_c	65.700 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	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1890
R_work r_work	0.1890
R_free r_free	0.2290

fit	/app/data/saxs_computation/bx/1bxm/1bxm.fit
pddf	/app/data/pr_computation/bx/1bxm/1bxm.pr.out
profile	/app/data/saxs_computation/bx/1bxm/1bxm.dat

ENGINEERED BETA-CRYPTOGEIN COMPLEXED WITH ERGOSTEROL

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

BETA-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

Refinement Refinement

Diffraction experiment Diffraction