SAXSdb — 3shi

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

Interstitial collagenase

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	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 106–261	Fragment：UNP residues 106-261	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；30% PEG8000, 0.1 M Tris-HCl, pH 8.5	Resolution 2.20 Å R-free 0.278
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain G； UniProt 106–261	Fragment：UNP residues 106-261	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；30% PEG8000, 0.1 M Tris-HCl, pH 8.5	Resolution 2.20 Å R-free 0.278
3	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain M； UniProt 106–261	Fragment：UNP residues 106-261	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；30% PEG8000, 0.1 M Tris-HCl, pH 8.5	Resolution 2.20 Å R-free 0.278

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 3SHI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AYK INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, 30 STRUCTURES Deposited 1997-11-06	Different construct 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 101–269（169 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 6.5；308 K；Pressure 1	Resolution not provided
1CGE CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF Deposited 1994-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 102–269（168 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å
1CGF CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF Deposited 1994-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 102–263（162 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1CGF CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF Deposited 1994-02-03	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 102–263（162 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1HFC 1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE Deposited 1994-09-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 101–269（169 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 1 PLH METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å
1SU3 X-ray structure of human proMMP-1: New insights into collagenase action Deposited 2004-03-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 20–469（450 aa）	Not recorded	CA CALCIUM ION × 4 CL CHLORIDE ION × 1 NA SODIUM ION × 1 ZN ZINC ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；1.5M Li2SO4, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP	Resolution 2.20 Å R-free 0.252
1SU3 X-ray structure of human proMMP-1: New insights into collagenase action Deposited 2004-03-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 20–469（450 aa）	Not recorded	CA CALCIUM ION × 4 CL CHLORIDE ION × 1 NA SODIUM ION × 1 ZN ZINC ION × 2 SO4 SULFATE ION × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；1.5M Li2SO4, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP	Resolution 2.20 Å R-free 0.252
1SU3 X-ray structure of human proMMP-1: New insights into collagenase action Deposited 2004-03-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain B 20–469（450 aa）	Not recorded	CA CALCIUM ION × 32 CL CHLORIDE ION × 8 NA SODIUM ION × 8 ZN ZINC ION × 16 SO4 SULFATE ION × 32 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；1.5M Li2SO4, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP	Resolution 2.20 Å R-free 0.252
2AYK INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1997-11-06	Different construct 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 101–269（169 aa）	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 10 mM TRIS BASE, 100 mM NACL, 5 mM CACL2, 0.1 mM ZNCL2, 2mM NAN3, 10 mM DEUTERATED DTT, 90% H2O/10%D2O OR 100% D2O；Pressure 1	Resolution not provided
2CLT Crystal structure of the active form (full-length) of human fibroblast collagenase. Deposited 2006-04-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 100–466（367 aa）	Mutation：YES	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1M TRIS (7.5); 10% PEG 8000; 1.5M AMMONIUM FORMATE, pH 7.50	Resolution 2.67 Å R-free 0.259
2CLT Crystal structure of the active form (full-length) of human fibroblast collagenase. Deposited 2006-04-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 100–466（367 aa）	Mutation：YES	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1M TRIS (7.5); 10% PEG 8000; 1.5M AMMONIUM FORMATE, pH 7.50	Resolution 2.67 Å R-free 0.259
2J0T Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1 Deposited 2006-08-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 101–269（169 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 101-269	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10% PEG 8000, 8% ETHYLENE GLYCOL, 0.1M HEPES (PH 7.5).	Resolution 2.54 Å R-free 0.275
2J0T Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1 Deposited 2006-08-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 101–269（169 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 101-269	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10% PEG 8000, 8% ETHYLENE GLYCOL, 0.1M HEPES (PH 7.5).	Resolution 2.54 Å R-free 0.275
2J0T Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1 Deposited 2006-08-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 101–269（169 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 101-269	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；10% PEG 8000, 8% ETHYLENE GLYCOL, 0.1M HEPES (PH 7.5).	Resolution 2.54 Å R-free 0.275
2TCL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR Deposited 1994-09-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 101–269（169 aa） Fragment：CATALYTIC DOMAIN	Not recorded	ZN ZINC ION × 2 SM SAMARIUM (III) ION × 1 CA CALCIUM ION × 2 RO4 [[1-[N-HYDROXY-ACETAMIDYL]-3-METHYL-BUTYL]-CARBONYL-LEUCINYL]-ALANINE ETHYL ESTER × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
3AYK CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1999-02-01	Different construct 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 101–269（169 aa） Fragment：CATALYTIC FRAGMENT	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 1 CGS N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE × 1	SOLUTION NMR NMR measurement conditions pH 6.5；308 K；Pressure 1	Resolution not provided
4AUO Crystal structure of MMP-1(E200A) in complex with a triple-helical collagen peptide Deposited 2012-05-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 100–466（367 aa）	Mutation：YES	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8	Resolution 3.00 Å R-free 0.273
4AUO Crystal structure of MMP-1(E200A) in complex with a triple-helical collagen peptide Deposited 2012-05-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 100–466（367 aa）	Mutation：YES	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8	Resolution 3.00 Å R-free 0.273
4AYK CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, 30 STRUCTURES Deposited 1999-02-01	Different construct 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 101–269（169 aa） Fragment：CATALYTIC FRAGMENT	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 1 CGS N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE × 1	SOLUTION NMR NMR measurement conditions pH 6.5；308 K；Pressure 1	Resolution not provided
966C CRYSTAL STRUCTURE OF FIBROBLAST COLLAGENASE-1 COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID Deposited 1998-08-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 108–264（157 aa） Fragment：CATALYTIC DOMAIN	Not recorded	ZN ZINC ION × 2 CA CALCIUM ION × 3 RS2 N-HYDROXY-2-[4-(4-PHENOXY-BENZENESULFONYL)-TETRAHYDRO-PYRAN-4-YL]-ACETAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 1.90 Å R-free 0.330

13 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MMP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–156； UniProt 106–261 Author chain G； PDBConstruct 1–156； UniProt 106–261 Author chain M； PDBConstruct 1–156； UniProt 106–261

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	3shi
Deposition date deposition_date	2011-06-16
Structure title title	Crystal structure of human MMP1 catalytic domain at 2.2 A resolution
Keywords keywords	;matrix metalloproteinase, paramagnetic restraints, paramagnetic tag, lanthanides, protein refinement, residual dipolar couplings, HYDROLASE ;; HYDROLASE
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	30.80 Å
Radius of gyration Rg (electron density) rg_electron	30.58 Å
Forward intensity I(0) i0	50580400.00
Molecular weight molecular_weight	53031.0 kDa
Excluded volume excluded_volume	64757 Å³
Envelope volume envelope_volume	83199 Å³
Hydration-shell volume shell_volume	24637 Å³
Envelope diameter envelope_diameter	105.3 Å
Shell Rg shell_rg	34.66 Å
Envelope Rg envelope_rg	30.27 Å
Shape Rg shape_rg	30.56 Å
Total Rg total_rg	30.99 Å
Total atoms total_atoms	3723
Residues n_residues	468
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	105.6 Å
Rg (real space) rg_real	31.11 Å
Rg uncertainty (real space) rg_real_error	1.26 Å
I(0) (real space) i0_real	5.0580e+07
I(0) uncertainty (real space) i0_real_error	8.9150e+05
Rg (reciprocal space) rg_reciprocal	30.98 Å
I(0) (reciprocal space) i0_reciprocal	50580000.0000
Solution quality estimate total_estimate	0.7888
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	22.8 Å
Skewness Skewness skewness	0.467
Kurtosis Kurtosis kurtosis	-0.527
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	18920000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.438; Smooth: 0.822

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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	Interstitial collagenase
Molecular weight formula_weight	17458.0 kDa
EC 编号 ec_number	3.4.24.7
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,G,M
Atom count atom_count	4024

NPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYG

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	Escherichia coli

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	6

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	301

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d3shia_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family family	d.92.1.11 — Matrix metalloproteases, catalytic domain

Domain ID domain_id	d3shig_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family family	d.92.1.11 — Matrix metalloproteases, catalytic domain

Domain ID domain_id	d3shim_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family family	d.92.1.11 — Matrix metalloproteases, catalytic domain

CATH v4.4 (3 domains)

Domain ID domain_id	3shiA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	3shiG00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

Domain ID domain_id	3shiM00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily	10 — Collagenase (Catalytic Domain)

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8. Citations (4)

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Unit-cell length a length_a	147.694 Å
Unit-cell length b length_b	54.528 Å
Unit-cell length c length_c	94.905 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	120.69 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	81.650 Å
R factor r_factor	0.2153
R_work r_work	0.2090
R_free r_free	0.2781

fit	/app/data/saxs_computation/sh/3shi/3shi.fit
pddf	/app/data/pr_computation/sh/3shi/3shi.pr.out
profile	/app/data/saxs_computation/sh/3shi/3shi.dat

Crystal structure of human MMP1 catalytic domain at 2.2 A resolution

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

Interstitial collagenase

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