SAXSdb — 1cev

▼

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 1–299 Chain B； UniProt 1–299 Chain C； UniProt 1–299 Chain D； UniProt 1–299 Chain E； UniProt 1–299 Chain F； UniProt 1–299	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
2	Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 1–299 Chain B； UniProt 1–299 Chain C； UniProt 1–299 Chain D； UniProt 1–299 Chain E； UniProt 1–299 Chain F； UniProt 1–299	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

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 1CEV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2CEV ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5 Deposited 1999-03-10	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 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 construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification 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
3CEV ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE Deposited 1999-03-15	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 2–299（298 aa） Chain B 2–299（298 aa） Chain C 2–299（298 aa）	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
3CEV ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE Deposited 1999-03-15	Different construct Different mutation/modification Different oligomeric state 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 × 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
3CEV ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE Deposited 1999-03-15	Different construct Different mutation/modification 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 × 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
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 mutation/modification 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 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 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 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 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 10 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 1–299； UniProt 1–299 Author chain B； PDBConstruct 1–299； UniProt 1–299 Author chain C； PDBConstruct 1–299； UniProt 1–299 Author chain D； PDBConstruct 1–299； UniProt 1–299 Author chain E； PDBConstruct 1–299； UniProt 1–299 Author chain F； PDBConstruct 1–299； UniProt 1–299

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cev
Deposition date deposition_date	1999-03-12
Structure title title	ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6
Keywords keywords	ENZYME, HYDROLASE, ARGININE HYDROLYSIS, NITROGEN METABOLISM, MANGANESE METALLOENZYME; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	37.19 Å
Radius of gyration Rg (electron density) rg_electron	36.12 Å
Forward intensity I(0) i0	583294000.00
Molecular weight molecular_weight	195200.0 kDa
Excluded volume excluded_volume	243900 Å³
Envelope volume envelope_volume	300210 Å³
Hydration-shell volume shell_volume	65779 Å³
Envelope diameter envelope_diameter	124.9 Å
Shell Rg shell_rg	44.78 Å
Envelope Rg envelope_rg	36.08 Å
Shape Rg shape_rg	36.15 Å
Total Rg total_rg	36.53 Å
Total atoms total_atoms	13668
Residues n_residues	1794
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	115.3 Å
Rg (real space) rg_real	36.90 Å
Rg uncertainty (real space) rg_real_error	0.63 Å
I(0) (real space) i0_real	5.8330e+08
I(0) uncertainty (real space) i0_real_error	8.7400e+06
Rg (reciprocal space) rg_reciprocal	37.08 Å
I(0) (reciprocal space) i0_reciprocal	583400000.0000
Solution quality estimate total_estimate	0.8907
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	51.0 Å
Skewness Skewness skewness	0.053
Kurtosis Kurtosis kurtosis	-0.469
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	387900000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.973

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

▼

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1ceva_
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	d1cevb_
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	d1cevc_
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	d1cevd_
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	d1ceve_
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	d1cevf_
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	1cevA00
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	1cevB00
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	1cevC00
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	1cevD00
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	1cevE00
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	1cevF00
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

▶

8. Citations (1)

▶

Unit-cell length a length_a	83.600 Å
Unit-cell length b length_b	145.600 Å
Unit-cell length c length_c	155.400 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	24

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	—
R_work r_work	0.2050
R_free r_free	0.2650

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 type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	13668

ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	12

fit	/app/data/saxs_computation/ce/1cev/1cev.fit
pddf	/app/data/pr_computation/ce/1cev/1cev.pr.out
profile	/app/data/saxs_computation/ce/1cev/1cev.dat