SAXSdb — 1f0c

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

ICE INHIBITOR

Cowpox virus

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–305 Chain B； UniProt 306–341	Fragment：RESIDUES 1-305 Fragment：RESIDUES 306-341	DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；296 K；0.1 M Na-Acetate, 15% PEG 4000, 0.1 M MgCl2, VAPOR DIFFUSION, temperature 296K	Resolution 2.26 Å R-free 0.272

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 1F0C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1C8O 2.9 A STRUCTURE OF CLEAVED VIRAL SERPIN CRMA Deposited 2000-06-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–300（300 aa） Fragment：RESIDUES 1-300 Chain B 301–341（41 aa） Fragment：RESIDUES 301-341	Mutation：C93S,C102S,C124S,C223S,C269S,C298S Mutation：C304S,C313S,C336S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.4；298 K；sodium/potassium phosphate 1.6M, pH 5.4, vapor diffusion/hanging drop, temperature 298K	Resolution 2.90 Å R-free 0.287
1M93 1.65 A Structure of Cleaved Viral Serpin CRMA Deposited 2002-07-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–55（55 aa） Fragment：RESIDUES 1-55 Chain B 56–300（245 aa） Fragment：RESIDUES 56-300 Chain C 301–341（41 aa） Fragment：RESIDUES 301-341	Mutation：C93S, C102S, C124S, C223S, C269S, C298S Mutation：C304S, C313S, C336S	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium/potassium phosphate 1.6M, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.65 Å R-free 0.245

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SPI2_CWPXB
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–305； UniProt 1–305 Author chain B； PDBConstruct 1–36； UniProt 306–341

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	1f0c
Deposition date deposition_date	2000-05-15
Structure title title	STRUCTURE OF THE VIRAL SERPIN CRMA
Keywords keywords	Apoptosis, caspase inhibitor, protease inhibitor, serpin, Viral protein; VIRAL PROTEIN
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	22.36 Å
Radius of gyration Rg (electron density) rg_electron	21.16 Å
Forward intensity I(0) i0	23094800.00
Molecular weight molecular_weight	37217.0 kDa
Excluded volume excluded_volume	46696 Å³
Envelope volume envelope_volume	53344 Å³
Hydration-shell volume shell_volume	21508 Å³
Envelope diameter envelope_diameter	70.3 Å
Shell Rg shell_rg	27.28 Å
Envelope Rg envelope_rg	21.31 Å
Shape Rg shape_rg	21.15 Å
Total Rg total_rg	21.98 Å
Total atoms total_atoms	2609
Residues n_residues	333
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	69.8 Å
Rg (real space) rg_real	22.36 Å
Rg uncertainty (real space) rg_real_error	0.38 Å
I(0) (real space) i0_real	2.3090e+07
I(0) uncertainty (real space) i0_real_error	2.8240e+05
Rg (reciprocal space) rg_reciprocal	22.36 Å
I(0) (reciprocal space) i0_reciprocal	23090000.0000
Solution quality estimate total_estimate	0.9018
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.4 Å
Skewness Skewness skewness	0.355
Kurtosis Kurtosis kurtosis	-0.434
Angular range angular_range	— – 0.3550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4905000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.992

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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	ICE INHIBITOR
Molecular weight formula_weight	34021.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2776

MDIFREIASSMKGENVFISPPSISSVLTILYYGANGSTAEQLSKYVEKEADKNKDDISFKSMNKVYGRYSAVFKDSFLRKIGDNFQTVDFTDCRTVDAINKCVDIFTEGKINPLLDEPLSPDTCLLAISAVYFKAKWLMPFEKEFTSDYPFYVSPTEMVDVSMMSMYGEAFNHASVKESFGNFSIIELPYVGDTSMVVILPDNIDGLESIEQNLTDTNFKKWCDSMDAMFIDVHIPKFKVTGSYNLVDALVKLGLTEVFGSTGDYSNMCNSDVSVDAMIHKTYIDVNEEYTEAAAATCALVADCA

来源 Source

来源生物 organism	Cowpox virus
NCBI Class编号 ncbi_taxonomy_id	10243
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	ICE INHIBITOR
Molecular weight formula_weight	4106.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

STVTNEFCADHPFIYVIRHVDGKILFVGRYCSPTTN

来源 Source

来源生物 organism	Cowpox virus
NCBI Class编号 ncbi_taxonomy_id	10243
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	2,3-DIHYDROXY-1,4-DITHIOBUTANE
Molecular weight formula_weight	154.3 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	167

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1f0c.1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.1 — Serpins
Superfamily Superfamily superfamily	e.1.1 — Serpins
Family Family family	e.1.1.1 — Serpins

CATH v4.4 (2 domains)

Domain ID domain_id	1f0cA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	497 — Antithrombin; Chain I, domain 2
Homologous superfamily homologous superfamily	10 — Antithrombin, subunit I, domain 2

Domain ID domain_id	1f0cA02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	39 — Alpha-1-antitrypsin; domain 1
Homologous superfamily homologous superfamily	10 — Alpha-1-antitrypsin, domain 1

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8. Citations (1)

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Unit-cell length a length_a	49.203 Å
Unit-cell length b length_b	92.455 Å
Unit-cell length c length_c	100.454 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	2.260 Å
Low-resolution limit resolution_low	500.000 Å
R factor r_factor	—
R_work r_work	0.2280
R_free r_free	0.2720

fit	/app/data/saxs_computation/f0/1f0c/1f0c.fit
pddf	/app/data/pr_computation/f0/1f0c/1f0c.pr.out
profile	/app/data/saxs_computation/f0/1f0c/1f0c.dat

STRUCTURE OF THE VIRAL SERPIN CRMA

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

ICE INHIBITOR

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)