SAXSdb — 4qxx

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

Bone marrow proteoglycan

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain Z； UniProt 131–135	Fragment：GNLVS peptide (UNP residues 131-135)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.2；291 K；2 M ammonium sulfate, 0.1 M phosphate/citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.45 Å R-free 0.192

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 4QXX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H8U Crystal Structure of the Eosinophil Major Basic Protein at 1.8A: An Atypical Lectin with a Paradigm Shift in Specificity Deposited 2001-02-15	Different construct 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 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 5 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100MM MALONIC ACID PH6, 140MM POTTASIUM DIHYDROGEN PHOSPHATE., pH 6.00	Resolution 1.80 Å R-free 0.264
1H8U Crystal Structure of the Eosinophil Major Basic Protein at 1.8A: An Atypical Lectin with a Paradigm Shift in Specificity Deposited 2001-02-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100MM MALONIC ACID PH6, 140MM POTTASIUM DIHYDROGEN PHOSPHATE., pH 6.00	Resolution 1.80 Å R-free 0.264
2BRS EMBP Heparin complex Deposited 2005-05-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.291
2BRS EMBP Heparin complex Deposited 2005-05-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.291
7Y5N Structure of 1:1 PAPP-A.ProMBP complex(half map) Deposited 2022-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–222（222 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ZN ZINC ION × 1 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
8HGG Structure of 2:2 PAPP-A.ProMBP complex Deposited 2022-11-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.64 Å
9DKZ In situ microED structure of the Eosinophil major basic protein-1 Deposited 2024-09-10	Different construct 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 107–222（116 aa）	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7；secretory granule matrix cryo-EM vitrification conditions Cryogen ETHANE；Blot time of 6~8 sec, single-side back blotting	Resolution 3.20 Å R-free 0.311
9PPV In situ MicroED structure of human eosinophil major basic protein-1 Deposited 2025-07-22	Different construct 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 106–222（117 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å R-free 0.313
9PPV In situ MicroED structure of human eosinophil major basic protein-1 Deposited 2025-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å R-free 0.313
9PSE In situ MicroED structure of IL-5 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct 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 B 107–222（116 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested from human donor peripheral blood and rested in 1640 RPMI medium supplemented with 0.1% human serum albumin (HSA) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.320
9PSE In situ MicroED structure of IL-5 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 107–222（116 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested from human donor peripheral blood and rested in 1640 RPMI medium supplemented with 0.1% human serum albumin (HSA) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.320
9PSK In situ MicroED structure of IL-33 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct 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 106–222（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested eosinophiles resting in 1640 RPMI medium (Sigma-Aldrich) supplemented with 0.1% human serum albumin (HSA) (Sigma-Aldrich) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.340
9PSK In situ MicroED structure of IL-33 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested eosinophiles resting in 1640 RPMI medium (Sigma-Aldrich) supplemented with 0.1% human serum albumin (HSA) (Sigma-Aldrich) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.340

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PRG2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain Z； PDBConstruct 1–5； UniProt 131–135

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	4qxx
Deposition date deposition_date	2014-07-22
Structure title title	Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP)
Keywords keywords	amyloid-like protofibril, PROTEIN FIBRIL; PROTEIN FIBRIL
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	6.92 Å
Radius of gyration Rg (electron density) rg_electron	5.17 Å
Forward intensity I(0) i0	16436.30
Molecular weight molecular_weight	488.5 kDa
Excluded volume excluded_volume	603 Å³
Envelope volume envelope_volume	702 Å³
Hydration-shell volume shell_volume	1644 Å³
Envelope diameter envelope_diameter	19.0 Å
Shell Rg shell_rg	8.47 Å
Envelope Rg envelope_rg	5.63 Å
Shape Rg shape_rg	5.10 Å
Total Rg total_rg	7.19 Å
Total atoms total_atoms	34
Residues n_residues	5
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	24.4 Å
Rg (real space) rg_real	6.99 Å
Rg uncertainty (real space) rg_real_error	0.21 Å
I(0) (real space) i0_real	1.6440e+04
I(0) uncertainty (real space) i0_real_error	1.6090e+02
Rg (reciprocal space) rg_reciprocal	6.99 Å
I(0) (reciprocal space) i0_reciprocal	16440.0000
Solution quality estimate total_estimate	0.8445
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	7.1 Å
Skewness Skewness skewness	0.428
Kurtosis Kurtosis kurtosis	-0.342
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1027.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.566; Smooth: 0.802

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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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8. Citations (1)

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Unit-cell length a length_a	4.755 Å
Unit-cell length b length_b	16.816 Å
Unit-cell length c length_c	35.759 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	4

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

Resolution resolution	1.445 Å
Low-resolution limit resolution_low	17.879 Å
R factor r_factor	0.1674
R_work r_work	0.1641
R_free r_free	0.1918

Description description	Bone marrow proteoglycan
Molecular weight formula_weight	488.5 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	Z
Atom count atom_count	37

Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP)

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

Bone marrow proteoglycan

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

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2

fit	/app/data/saxs_computation/qx/4qxx/4qxx.fit
pddf	/app/data/pr_computation/qx/4qxx/4qxx.pr.out
profile	/app/data/saxs_computation/qx/4qxx/4qxx.dat