SAXSdb — 3cev

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

PROTEIN (ARGINASE)

Bacillus caldovelox

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 2–299 Chain B； UniProt 2–299 Chain C； UniProt 2–299	Not recorded	MN MANGANESE (II) ION × 6 ARG ARGININE × 12	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 10 MM EDTA, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.05 M BISTRISPROPANE/HCL, PH 8. THE CRYSTALS WERE THEN SOAKED IN 42.5% MMPEG 2000, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-ARGININE, 10 MM EDTA, 0.05M BISTRISPROPANE/HCL, PH 8.5 FOR 8 HOURS, VAPOR DIFFUSION, HANGING DROP	Resolution 2.40 Å R-free 0.243
2	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 2–299 Chain E； UniProt 2–299 Chain F； UniProt 2–299	Not recorded	MN MANGANESE (II) ION × 3 ARG ARGININE × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 10 MM EDTA, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.05 M BISTRISPROPANE/HCL, PH 8. THE CRYSTALS WERE THEN SOAKED IN 42.5% MMPEG 2000, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-ARGININE, 10 MM EDTA, 0.05M BISTRISPROPANE/HCL, PH 8.5 FOR 8 HOURS, VAPOR DIFFUSION, HANGING DROP	Resolution 2.40 Å R-free 0.243
3	Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain D； UniProt 2–299 Chain E； UniProt 2–299 Chain F； UniProt 2–299	Not recorded	MN MANGANESE (II) ION × 6 ARG ARGININE × 12	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 10 MM EDTA, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.05 M BISTRISPROPANE/HCL, PH 8. THE CRYSTALS WERE THEN SOAKED IN 42.5% MMPEG 2000, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-ARGININE, 10 MM EDTA, 0.05M BISTRISPROPANE/HCL, PH 8.5 FOR 8 HOURS, VAPOR DIFFUSION, HANGING DROP	Resolution 2.40 Å R-free 0.243

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 3CEV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CEV ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6 Deposited 1999-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–299（299 aa） Chain B 1–299（299 aa） Chain C 1–299（299 aa） Chain D 1–299（299 aa） Chain E 1–299（299 aa） Chain F 1–299（299 aa）	Not recorded	MN MANGANESE (II) ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；3-6% N-BUTANOL,IN 0.1 M SODIUM CITRATE BUFFER, PH 5.6 PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.40 Å R-free 0.265
1CEV ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6 Deposited 1999-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–299（299 aa） Chain B 1–299（299 aa） Chain C 1–299（299 aa） Chain D 1–299（299 aa） Chain E 1–299（299 aa） Chain F 1–299（299 aa）	Not recorded	MN MANGANESE (II) ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；3-6% N-BUTANOL,IN 0.1 M SODIUM CITRATE BUFFER, PH 5.6 PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.40 Å R-free 0.265
2CEV ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5 Deposited 1999-03-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 2–299（298 aa） Chain B 2–299（298 aa） Chain C 2–299（298 aa）	Not recorded	MN MANGANESE (II) ION × 12 GAI GUANIDINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP VAPOUR DIFFUSION, MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION. PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5. RESERVOIR SOLUTION 27-30% MONOMETHYLPEG 5000, 10 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.1 M BISTRISPROPANE/HCL, PH 8.5., VAPOR DIFFUSION, HANGING DROP	Resolution 2.15 Å R-free 0.238
2CEV ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5 Deposited 1999-03-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 2–299（298 aa） Chain E 2–299（298 aa） Chain F 2–299（298 aa）	Not recorded	MN MANGANESE (II) ION × 6 GAI GUANIDINE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP VAPOUR DIFFUSION, MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION. PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5. RESERVOIR SOLUTION 27-30% MONOMETHYLPEG 5000, 10 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.1 M BISTRISPROPANE/HCL, PH 8.5., VAPOR DIFFUSION, HANGING DROP	Resolution 2.15 Å R-free 0.238
2CEV ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5 Deposited 1999-03-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain D 2–299（298 aa） Chain E 2–299（298 aa） Chain F 2–299（298 aa）	Not recorded	MN MANGANESE (II) ION × 12 GAI GUANIDINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP VAPOUR DIFFUSION, MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION. PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5. RESERVOIR SOLUTION 27-30% MONOMETHYLPEG 5000, 10 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.1 M BISTRISPROPANE/HCL, PH 8.5., VAPOR DIFFUSION, HANGING DROP	Resolution 2.15 Å R-free 0.238
4CEV ARGINASE FROM BACILLUS CALDEVELOX, L-ORNITHINE COMPLEX Deposited 1999-03-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–299（299 aa） Chain B 1–299（299 aa） Chain C 1–299（299 aa） Chain D 1–299（299 aa）	Not recorded	MN MANGANESE (II) ION × 16 ORN L-ornithine × 12 GAI GUANIDINE × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM D/L-ORNITHINE,IN 0.05 M BISTRISPROPANE/HCL,PH 8.5 27 MG/ML PROTEIN, 10 MM MOPSm, PH 7.5 , VAPOR DIFFUSION, HANGING DROP	Resolution 2.70 Å R-free 0.274
4CEV ARGINASE FROM BACILLUS CALDEVELOX, L-ORNITHINE COMPLEX Deposited 1999-03-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain D 1–299（299 aa） Chain E 1–299（299 aa） Chain F 1–299（299 aa）	Not recorded	MN MANGANESE (II) ION × 12 GAI GUANIDINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM D/L-ORNITHINE,IN 0.05 M BISTRISPROPANE/HCL,PH 8.5 27 MG/ML PROTEIN, 10 MM MOPSm, PH 7.5 , VAPOR DIFFUSION, HANGING DROP	Resolution 2.70 Å R-free 0.274
5CEV ARGINASE FROM BACILLUS CALDEVELOX, L-LYSINE COMPLEX Deposited 1999-03-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 2–299（298 aa） Chain B 2–299（298 aa） Chain C 2–299（298 aa）	Not recorded	MN MANGANESE (II) ION × 12 LYS LYSINE × 6 GAI GUANIDINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-LYSINE, IN 0.05 M BISTRISPROPANE/HCL, PH 8.5 , VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.261
5CEV ARGINASE FROM BACILLUS CALDEVELOX, L-LYSINE COMPLEX Deposited 1999-03-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain D 2–299（298 aa） Chain E 2–299（298 aa） Chain F 2–299（298 aa）	Not recorded	MN MANGANESE (II) ION × 12 LYS LYSINE × 6 GAI GUANIDINE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-LYSINE, IN 0.05 M BISTRISPROPANE/HCL, PH 8.5 , VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.261

4 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ARGI_BACCD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–299； UniProt 2–299 Author chain B； PDBConstruct 2–299； UniProt 2–299 Author chain C； PDBConstruct 2–299； UniProt 2–299 Author chain D； PDBConstruct 2–299； UniProt 2–299 Author chain E； PDBConstruct 2–299； UniProt 2–299 Author chain F； PDBConstruct 2–299； UniProt 2–299

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	3cev
Deposition date deposition_date	1999-03-15
Structure title title	ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE
Keywords keywords	ENZYME, HYDROLASE, ARGININE HYDROLYSIS, NITROGEN METABOLISM, MANGANESE METALLOENZYME; 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	53.01 Å
Radius of gyration Rg (electron density) rg_electron	53.40 Å
Forward intensity I(0) i0	565005000.00
Molecular weight molecular_weight	196180.0 kDa
Excluded volume excluded_volume	245160 Å³
Envelope volume envelope_volume	329910 Å³
Hydration-shell volume shell_volume	53455 Å³
Envelope diameter envelope_diameter	173.6 Å
Shell Rg shell_rg	52.13 Å
Envelope Rg envelope_rg	52.28 Å
Shape Rg shape_rg	53.42 Å
Total Rg total_rg	53.28 Å
Total atoms total_atoms	13758
Residues n_residues	1788
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	164.2 Å
Rg (real space) rg_real	53.40 Å
Rg uncertainty (real space) rg_real_error	1.63 Å
I(0) (real space) i0_real	5.6500e+08
I(0) uncertainty (real space) i0_real_error	1.0520e+07
Rg (reciprocal space) rg_reciprocal	52.66 Å
I(0) (reciprocal space) i0_reciprocal	564400000.0000
Solution quality estimate total_estimate	0.7780
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.3 Å
Skewness Skewness skewness	0.382
Kurtosis Kurtosis kurtosis	-0.827
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	16680000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.734; Smooth: 0.001

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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	PROTEIN (ARGINASE)
Molecular weight formula_weight	32476.2 kDa
EC 编号 ec_number	3.5.3.1
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	14395

MKPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIPIGKAERLHEQGDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHSIAIGTLAGVAKHYERLGVIWYDAHGDVNTAETSPSGNIHGMPLAASLGFGHPALTQIGGYSPKIKPEHVVLIGVRSLDEGEKKFIREKGIKIYTMHEVDRLGMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGTPVIGGLTYRESHLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM

来源 Source

来源生物 organism	Bacillus caldovelox
NCBI Class编号 ncbi_taxonomy_id	33931
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 3 Entity 3 non-polymer

Description description	ARGININE
Molecular weight formula_weight	175.2 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	637

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d3ceva_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

Domain ID domain_id	d3cevb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

Domain ID domain_id	d3cevc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

Domain ID domain_id	d3cevd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

Domain ID domain_id	d3ceve_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

Domain ID domain_id	d3cevf_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.42 — Arginase/deacetylase
Superfamily Superfamily superfamily	c.42.1 — Arginase/deacetylase
Family Family family	c.42.1.1 — Arginase-like amidino hydrolases

CATH v4.4 (6 domains)

Domain ID domain_id	3cevA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

Domain ID domain_id	3cevB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

Domain ID domain_id	3cevC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

Domain ID domain_id	3cevD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

Domain ID domain_id	3cevE00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

Domain ID domain_id	3cevF00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	800 — Arginase; Chain A
Homologous superfamily homologous superfamily	10 — Ureohydrolase domain

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8. Citations (1)

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Unit-cell length a length_a	106.800 Å
Unit-cell length b length_b	277.700 Å
Unit-cell length c length_c	140.000 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	48

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	—
R_work r_work	0.1930
R_free r_free	0.2430

fit	/app/data/saxs_computation/ce/3cev/3cev.fit
pddf	/app/data/pr_computation/ce/3cev/3cev.pr.out
profile	/app/data/saxs_computation/ce/3cev/3cev.dat

ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE

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

PROTEIN (ARGINASE)

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