SAXSdb — 3ppd

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

GGVLVN peptide, amyloid forming segment

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 A； UniProt 260–265	Fragment：Residue 260-265	ZN ZINC ION × 6 ACY ACETIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1M MES pH6.0, 0.2M Zn(OAc)2, 10%(w/v)PEG-8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.219

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 3PPD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CVI CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1999-08-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 33–374（342 aa） Chain B 33–374（342 aa） Chain C 33–374（342 aa） Chain D 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GLY GLYCINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；289 K；PEG 1450, POTASSIUM CHLORIDE, GLYCINE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.20 Å R-free 0.274
1CVI CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1999-08-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 33–374（342 aa） Chain B 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GLY GLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；289 K；PEG 1450, POTASSIUM CHLORIDE, GLYCINE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.20 Å R-free 0.274
1CVI CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1999-08-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–374（342 aa） Chain D 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GLY GLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；289 K；PEG 1450, POTASSIUM CHLORIDE, GLYCINE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 3.20 Å R-free 0.274
1ND5 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 33–386（354 aa） Chain B 33–386（354 aa） Chain C 33–386（354 aa）	Not recorded	2BF ALPHA-BENZYL-AMINOBENZYL-PHOSPHONIC ACID × 3 1PE PENTAETHYLENE GLYCOL × 7 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.279
1ND5 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–386（354 aa） Chain D 33–386（354 aa）	Not recorded	2BF ALPHA-BENZYL-AMINOBENZYL-PHOSPHONIC ACID × 2 1PE PENTAETHYLENE GLYCOL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.279
1ND6 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 33–386（354 aa） Chain B 33–386（354 aa）	Not recorded	PO4 PHOSPHATE ION × 2 1PE PENTAETHYLENE GLYCOL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GLY GLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.40 Å R-free 0.256
1ND6 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–386（354 aa） Chain D 33–386（354 aa）	Not recorded	PO4 PHOSPHATE ION × 2 1PE PENTAETHYLENE GLYCOL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.40 Å R-free 0.256
1ND6 Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design Deposited 2002-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 33–386（354 aa） Chain B 33–386（354 aa） Chain C 33–386（354 aa） Chain D 33–386（354 aa）	Not recorded	PO4 PHOSPHATE ION × 4 1PE PENTAETHYLENE GLYCOL × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GLY GLYCINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；298 K；PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.40 Å R-free 0.256
2HPA STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1998-09-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 33–374（342 aa） Chain B 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PT3 N-PROPYL-TARTRAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；pH 10	Resolution 2.90 Å R-free 0.308
2HPA STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1998-09-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 33–374（342 aa） Chain D 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PT3 N-PROPYL-TARTRAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；pH 10	Resolution 2.90 Å R-free 0.308
2HPA STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE Deposited 1998-09-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 33–374（342 aa） Chain B 33–374（342 aa） Chain C 33–374（342 aa） Chain D 33–374（342 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PT3 N-PROPYL-TARTRAMIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 10；pH 10	Resolution 2.90 Å R-free 0.308
2L3H NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP248-286 Deposited 2010-09-13	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 248–286（39 aa） Fragment：UNP residues 248-286	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.3；310 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 2.5 mM PAP248-286-1, 120 mM sodium chloride-2, 20 mM sodium phosphate-3, 200 mM [U-99% 2H] SDS-4, 10 % [U-99% 2H] D2O-5, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L77 Solution NMR structure of PAP248-286 in 50% TFE Deposited 2010-12-03	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 248–286（39 aa） Fragment：UNP residues 248-286	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Pressure ambient NMR sample composition 1.2 mM PAP248-286-1; 20 mM sodium phosphate-2; 10 % [U-99% 2H] D2O-3; 50 % [U-99% 2H] TFE-4; trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2L79 Solution NMR structure of PAP248-286 in 30% TFE Deposited 2010-12-03	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 248–286（39 aa） Fragment：UNP residues 248-286	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Pressure ambient NMR sample composition 1.2 mM PAP248-286-1; 20 mM sodium phosphate-2; 10 % [U-99% 2H] D2O-3; 30 % [U-99% 2H] TFE-4; trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2MG0 PAP262-270 in SDS micelles Deposited 2013-10-24	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 262–270（9 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K NMR sample composition 300 uM protein_1-1, 50 mM [U-99% 2H] SDS-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
7ZZV Prostatic acid phosphatase (PAP) fragment (85-120) Deposited 2022-05-26	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 85–120（36 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 0.8 mM pap85_120, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8XJ4 Structure of prostatic acid phosphatase in human semen Deposited 2023-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 31–377（347 aa） Chain B 31–377（347 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MAN alpha-D-mannopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.19 Å
9NMU TCR156 bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 7 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；0.2 M Sodium malonate, 0.1 M bis Tris-propane pH 7.5, 17% PEG 3500	Resolution 2.10 Å R-free 0.227
9NMV TCR156 S32Halpha bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；0.2 M Sodium malonate, 0.1 M bis Tris-propane pH 7.5, 20% PEG3500	Resolution 1.97 Å R-free 0.217
9NMW TCR156 S30Ealpha S32Qalpha bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 11 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；0.2 M Na2SO4, bis tris propane pH 7.5, 20% PEG 3350	Resolution 2.11 Å R-free 0.232
9NMX TCR156 S32Malpha variant bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	MLI MALONATE ION × 2 GOL GLYCEROL × 12 NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；295 K；0.2 M Sodium malonate, 0.1 M bis Tris-propane pH 7.5, 17% PEG 3500	Resolution 2.19 Å R-free 0.229
9NMY TCR156 S32Qalpha bound to HLA A*02:01-PAP Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 112–120（9 aa）	Not recorded	GOL GLYCEROL × 9 MLI MALONATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.3；295 K；0.2 M sodium malonat, 20% PEG 3350	Resolution 2.01 Å R-free 0.227
9YTD Designed antibody vAB66 targeting PAP-HLA A*02:01 Deposited 2025-10-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 112–120（9 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å

16 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PPAP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–6； UniProt 260–265

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	3ppd
Deposition date deposition_date	2010-11-24
Structure title title	GGVLVN segment from Human Prostatic Acid Phosphatase Residues 260-265, involved in Semen-Derived Enhancer of Viral Infection
Keywords keywords	amyloid-like protofibril, amyloid fibrils, 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	7.96 Å
Radius of gyration Rg (electron density) rg_electron	6.56 Å
Forward intensity I(0) i0	27294.30
Molecular weight molecular_weight	683.1 kDa
Excluded volume excluded_volume	814 Å³
Envelope volume envelope_volume	958 Å³
Hydration-shell volume shell_volume	1850 Å³
Envelope diameter envelope_diameter	21.4 Å
Shell Rg shell_rg	9.37 Å
Envelope Rg envelope_rg	6.68 Å
Shape Rg shape_rg	6.27 Å
Total Rg total_rg	8.32 Å
Total atoms total_atoms	44
Residues n_residues	6
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	26.3 Å
Rg (real space) rg_real	8.09 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	2.7290e+04
I(0) uncertainty (real space) i0_real_error	2.5560e+02
Rg (reciprocal space) rg_reciprocal	8.09 Å
I(0) (reciprocal space) i0_reciprocal	27290.0000
Solution quality estimate total_estimate	0.7903
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	8.3 Å
Skewness Skewness skewness	0.350
Kurtosis Kurtosis kurtosis	-0.737
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	977.8000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.666; Stabil: 0.977; Sysdev: 1.000; Positv: 1.000; Valcen: 0.362; Smooth: 0.979

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GGVLVN peptide, amyloid forming segment
Molecular weight formula_weight	557.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	45

GGVLVN

Entity 2 Entity 2 non-polymer

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

Entity 3 Entity 3 non-polymer

Description description	ACETIC ACID
Molecular weight formula_weight	60.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1

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8. Citations (1)

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Unit-cell length a length_a	4.834 Å
Unit-cell length b length_b	17.682 Å
Unit-cell length c length_c	40.322 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 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	20.160 Å
R factor r_factor	0.1818
R_work r_work	0.1779
R_free r_free	0.2189

fit	/app/data/saxs_computation/pp/3ppd/3ppd.fit
pddf	/app/data/pr_computation/pp/3ppd/3ppd.pr.out
profile	/app/data/saxs_computation/pp/3ppd/3ppd.dat

GGVLVN segment from Human Prostatic Acid Phosphatase Residues 260-265, involved in Semen-Derived Enhancer of Viral Infection

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

GGVLVN peptide, amyloid forming segment

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