SAXSdb — 2j2j

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

FIBER PROTEIN

CANINE ADENOVIRUS 2

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 358–542 Chain B； UniProt 358–542 Chain D； UniProt 358–542	Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：0.15 M KBR, 30% PEG MONOMETHYL-ETHER 2000	Resolution 1.50 Å R-free 0.206
2	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 358–542 Chain E； UniProt 358–542 Chain F； UniProt 358–542	Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：0.15 M KBR, 30% PEG MONOMETHYL-ETHER 2000	Resolution 1.50 Å R-free 0.206

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 2J2J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2J1K CAV-2 fibre head in complex with CAR D1 Deposited 2006-08-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain H 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain I 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.220
2J1K CAV-2 fibre head in complex with CAR D1 Deposited 2006-08-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain E 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain F 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.220
2J1K CAV-2 fibre head in complex with CAR D1 Deposited 2006-08-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain M 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain N 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.220
2J1K CAV-2 fibre head in complex with CAR D1 Deposited 2006-08-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain Q 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain R 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542 Chain S 358–542（185 aa） Fragment：FIBRE HEAD DOMAIN, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.220
2W9L CANINE ADENOVIRUS TYPE 2 FIBRE HEAD IN COMPLEX WITH CAR DOMAIN D1 AND SIALIC ACID Deposited 2009-01-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain Q 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain R 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain S 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 20% POLYETHYLENE GLYCOL MONOMETHYL-ETHER 550, 0.1 M BICINE, PH 9, 0.1 M NACL	Resolution 2.91 Å R-free 0.254
2W9L CANINE ADENOVIRUS TYPE 2 FIBRE HEAD IN COMPLEX WITH CAR DOMAIN D1 AND SIALIC ACID Deposited 2009-01-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain E 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain F 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 20% POLYETHYLENE GLYCOL MONOMETHYL-ETHER 550, 0.1 M BICINE, PH 9, 0.1 M NACL	Resolution 2.91 Å R-free 0.254
2W9L CANINE ADENOVIRUS TYPE 2 FIBRE HEAD IN COMPLEX WITH CAR DOMAIN D1 AND SIALIC ACID Deposited 2009-01-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain H 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain I 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 20% POLYETHYLENE GLYCOL MONOMETHYL-ETHER 550, 0.1 M BICINE, PH 9, 0.1 M NACL	Resolution 2.91 Å R-free 0.254
2W9L CANINE ADENOVIRUS TYPE 2 FIBRE HEAD IN COMPLEX WITH CAR DOMAIN D1 AND SIALIC ACID Deposited 2009-01-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain M 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain N 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 20% POLYETHYLENE GLYCOL MONOMETHYL-ETHER 550, 0.1 M BICINE, PH 9, 0.1 M NACL	Resolution 2.91 Å R-free 0.254
2WBV Canine adenovirus 2 fibre head in complex with sialic acid Deposited 2009-03-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain B 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain D 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542	Not recorded	GOL GLYCEROL × 3 SIA N-acetyl-alpha-neuraminic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions 5% PEG 4000, 5% ISOPROPANOL, 0.1 M HEPES PH 7.4	Resolution 1.90 Å R-free 0.195
2WBV Canine adenovirus 2 fibre head in complex with sialic acid Deposited 2009-03-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain C 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain E 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542 Chain F 358–542（185 aa） Fragment：FIBRE HEAD, RESIDUES 358-542	Not recorded	GOL GLYCEROL × 3 SIA N-acetyl-alpha-neuraminic acid × 3	X-RAY DIFFRACTION X-ray crystallization conditions 5% PEG 4000, 5% ISOPROPANOL, 0.1 M HEPES PH 7.4	Resolution 1.90 Å R-free 0.195

3 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FIBP_ADECT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–197； UniProt 358–542 Author chain B； PDBConstruct 13–197； UniProt 358–542 Author chain C； PDBConstruct 13–197； UniProt 358–542 Author chain D； PDBConstruct 13–197； UniProt 358–542 Author chain E； PDBConstruct 13–197； UniProt 358–542 Author chain F； PDBConstruct 13–197； UniProt 358–542

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	2j2j
Deposition date deposition_date	2006-08-16
Structure title title	Canine adenovirus fibre head at 1.5 A resolution
Keywords keywords	FIBER PROTEIN, CANINE ADENOVIRUS, AD, CAR, KNOB, HEAD, FIBER FIBRE, ADENOVIRUS, COXSACKIEVIRUS, ADENOVIRUS RECEPTOR, 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	36.12 Å
Radius of gyration Rg (electron density) rg_electron	35.89 Å
Forward intensity I(0) i0	218673000.00
Molecular weight molecular_weight	120010.0 kDa
Excluded volume excluded_volume	150130 Å³
Envelope volume envelope_volume	179970 Å³
Hydration-shell volume shell_volume	42603 Å³
Envelope diameter envelope_diameter	118.9 Å
Shell Rg shell_rg	41.44 Å
Envelope Rg envelope_rg	35.79 Å
Shape Rg shape_rg	35.91 Å
Total Rg total_rg	36.18 Å
Total atoms total_atoms	8436
Residues n_residues	1092
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	117.7 Å
Rg (real space) rg_real	36.31 Å
Rg uncertainty (real space) rg_real_error	0.97 Å
I(0) (real space) i0_real	2.1870e+08
I(0) uncertainty (real space) i0_real_error	3.6210e+06
Rg (reciprocal space) rg_reciprocal	36.20 Å
I(0) (reciprocal space) i0_reciprocal	218600000.0000
Solution quality estimate total_estimate	0.8408
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	34.8 Å
Skewness Skewness skewness	0.405
Kurtosis Kurtosis kurtosis	-0.693
Angular range angular_range	— – 0.2200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	71060000.0000
Real-space data points n_real_points	45
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.888; Smooth: 0.882

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2j2ja_
Class class	b — All beta proteins
Fold Fold fold	b.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamily	b.21.1 — Virus attachment protein globular domain
Family Family family	b.21.1.0 — automated matches

Domain ID domain_id	d2j2jb_
Class class	b — All beta proteins
Fold Fold fold	b.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamily	b.21.1 — Virus attachment protein globular domain
Family Family family	b.21.1.0 — automated matches

Domain ID domain_id	d2j2jc_
Class class	b — All beta proteins
Fold Fold fold	b.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamily	b.21.1 — Virus attachment protein globular domain
Family Family family	b.21.1.0 — automated matches

Domain ID domain_id	d2j2jd_
Class class	b — All beta proteins
Fold Fold fold	b.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamily	b.21.1 — Virus attachment protein globular domain
Family Family family	b.21.1.0 — automated matches

Domain ID domain_id	d2j2je_
Class class	b — All beta proteins
Fold Fold fold	b.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamily	b.21.1 — Virus attachment protein globular domain
Family Family family	b.21.1.0 — automated matches

Domain ID domain_id	d2j2jf_
Class class	b — All beta proteins
Fold Fold fold	b.21 — Virus attachment protein globular domain
Superfamily Superfamily superfamily	b.21.1 — Virus attachment protein globular domain
Family Family family	b.21.1.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id	2j2jA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	10 — Adenovirus pIV-related, attachment domain

Domain ID domain_id	2j2jB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	10 — Adenovirus pIV-related, attachment domain

Domain ID domain_id	2j2jC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	10 — Adenovirus pIV-related, attachment domain

Domain ID domain_id	2j2jD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	10 — Adenovirus pIV-related, attachment domain

Domain ID domain_id	2j2jE00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	10 — Adenovirus pIV-related, attachment domain

Domain ID domain_id	2j2jF00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	90 — Adenovirus Type 5 Fiber Protein (Receptor Binding Domain)
Homologous superfamily homologous superfamily	10 — Adenovirus pIV-related, attachment domain

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8. Citations (1)

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Unit-cell length a length_a	55.834 Å
Unit-cell length b length_b	88.547 Å
Unit-cell length c length_c	106.913 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.40 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	106.000 Å
R factor r_factor	0.1650
R_work r_work	0.1650
R_free r_free	0.2060

Description description	FIBER PROTEIN
Molecular weight formula_weight	21685.5 kDa
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	10007

Canine adenovirus fibre head at 1.5 A resolution

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

FIBER PROTEIN

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 water

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	CANINE ADENOVIRUS 2
通用名 common_name	CADV-2
NCBI Class编号 ncbi_taxonomy_id	10514
宿主生物 host_organism	ESCHERICHIA COLI

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1539

fit	/app/data/saxs_computation/j2/2j2j/2j2j.fit
pddf	/app/data/pr_computation/j2/2j2j/2j2j.pr.out
profile	/app/data/saxs_computation/j2/2j2j/2j2j.dat