SAXSdb — 1f2r

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

CASPASE-ACTIVATED DNASE

Mus musculus

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–87	Fragment：N-TERMINAL DOMAIN (CAD DOMAIN), RESIDUES 1-87	INHIBITOR OF CASPASE-ACTIVATED DNASE × 1 （O54786）	SOLUTION NMR NMR measurement conditions：pH 6.4；308 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition：0.6mM CAD U-15N,13C/0.6mM ICAD unlabeled; 20mM phophate buffer pH6.4 \| 90% H2O/10% D2O NMR sample composition：0.6mM CAD U-15N,13C/0.6mM ICAD unlabeled; 20mM phophate buffer pH6.4 \| 100% D2O NMR sample composition：0.6mM ICAD U-15N,13C/0.6mM CAD unlabeled; 20mM phophate buffer pH6.4 \| 90% H2O/10% D2O NMR sample composition：0.6mM ICAD U-15N,13C/0.6mM CAD unlabeled; 20mM phophate buffer pH6.4 \| 100% D2O	Resolution not provided

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 1F2R	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1C9F NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE Deposited 1999-08-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–87（87 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-87	Mutation：VPH ADDED AT N-TERMINUS	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.6；298 K；Ionic strength (raw mmCIF value) 50mM；Pressure AMBIENT NMR sample composition U-15N NMR sample composition U-13C;U-15N NMR sample composition U-13C;U-15N NMR sample composition U-15N	Resolution not provided
1V0D Crystal Structure of Caspase-activated DNase (CAD) Deposited 2004-03-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–329（329 aa） Fragment：RESIDUES 1-329	Not recorded	ZN ZINC ION × 2 MG MAGNESIUM ION × 2 PB LEAD (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.00	Resolution 2.60 Å R-free 0.246

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

View Construct and Data Evidence

UniProt name	DFFB_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain C； PDBConstruct 1–87； UniProt 1–87

INHIBITOR OF CASPASE-ACTIVATED DNASE

Mus musculus

UniProt O54786

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain I； UniProt 1–100	Fragment：N-TERMINAL DOMAIN (CAD DOMAIN), RESIDUES 1-100	CASPASE-ACTIVATED DNASE × 1 （O54788）	SOLUTION NMR NMR measurement conditions：pH 6.4；308 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition：0.6mM CAD U-15N,13C/0.6mM ICAD unlabeled; 20mM phophate buffer pH6.4 \| 90% H2O/10% D2O NMR sample composition：0.6mM CAD U-15N,13C/0.6mM ICAD unlabeled; 20mM phophate buffer pH6.4 \| 100% D2O NMR sample composition：0.6mM ICAD U-15N,13C/0.6mM CAD unlabeled; 20mM phophate buffer pH6.4 \| 90% H2O/10% D2O NMR sample composition：0.6mM ICAD U-15N,13C/0.6mM CAD unlabeled; 20mM phophate buffer pH6.4 \| 100% D2O	Resolution not provided

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	DFFA_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain I； PDBConstruct 1–100； UniProt 1–100

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	1f2r
Deposition date deposition_date	2000-05-29
Structure title title	NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD
Keywords keywords	ALPHA-BETA ROLL, PROTEIN-PROTEIN COMPLEX, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	19.54 Å
Radius of gyration Rg (electron density) rg_electron	18.16 Å
Forward intensity I(0) i0	8584980.00
Molecular weight molecular_weight	20658.0 kDa
Excluded volume excluded_volume	25576 Å³
Envelope volume envelope_volume	32950 Å³
Hydration-shell volume shell_volume	15749 Å³
Envelope diameter envelope_diameter	70.7 Å
Shell Rg shell_rg	23.79 Å
Envelope Rg envelope_rg	18.64 Å
Shape Rg shape_rg	18.13 Å
Total Rg total_rg	19.21 Å
Total atoms total_atoms	2870
Residues n_residues	187
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	69.5 Å
Rg (real space) rg_real	19.50 Å
Rg uncertainty (real space) rg_real_error	0.63 Å
I(0) (real space) i0_real	8.5850e+06
I(0) uncertainty (real space) i0_real_error	1.0850e+05
Rg (reciprocal space) rg_reciprocal	19.51 Å
I(0) (reciprocal space) i0_reciprocal	8585000.0000
Solution quality estimate total_estimate	0.7735
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	4
Primary peak position r_peak_primary	21.5 Å
Skewness Skewness skewness	0.278
Kurtosis Kurtosis kurtosis	-0.353
Angular range angular_range	— – 0.4050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2433000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.723; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.905; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	CASPASE-ACTIVATED DNASE
Molecular weight formula_weight	9613.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C
Atom count atom_count	2870

MCAVLRQPKCVKLRALHSACKFGVAARSCQELLRKGCVRFQLPMPGSRLCLYEDGTEVTDDCFPGLPNDAELLLLTAGETWHGYVSD

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	INHIBITOR OF CASPASE-ACTIVATED DNASE
Molecular weight formula_weight	11076.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

MELSRGASAPDPDDVRPLKPCLLRRNHSRDQHGVAASSLEELRSKACELLAIDKSLTPITLVLAEDGTIVDDDDYFLCLPSNTKFVALACNEKWTYNDSD

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1f2rc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.1 — CAD domain

Domain ID domain_id	d1f2ri_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.2 — CAD & PB1 domains
Family Family family	d.15.2.1 — CAD domain

CATH v4.4 (2 domains)

Domain ID domain_id	1f2rC00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	1f2rI00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	10 —

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8. Citations (4)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

fit	/app/data/saxs_computation/f2/1f2r/1f2r.fit
pddf	/app/data/pr_computation/f2/1f2r/1f2r.pr.out
profile	/app/data/saxs_computation/f2/1f2r/1f2r.dat

NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD

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

CASPASE-ACTIVATED DNASE

State in the Current Structure

Other States of the Same Protein in the Database

INHIBITOR OF CASPASE-ACTIVATED DNASE

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)