SAXSdb — 1cs6

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

AXONIN-1

Gallus gallus

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 28–409	Fragment：IG1-4	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；290 K；PEG 10000, sodium formiate, HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K	Resolution 1.80 Å R-free 0.257

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	CNTN2_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–382； UniProt 28–409

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	1cs6
Deposition date deposition_date	1999-08-17
Structure title title	N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN
Keywords keywords	NEURAL CELL ADHESION, CELL ADHESION; CELL ADHESION
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	29.14 Å
Radius of gyration Rg (electron density) rg_electron	28.59 Å
Forward intensity I(0) i0	30883400.00
Molecular weight molecular_weight	42625.0 kDa
Excluded volume excluded_volume	53040 Å³
Envelope volume envelope_volume	69727 Å³
Hydration-shell volume shell_volume	21485 Å³
Envelope diameter envelope_diameter	100.0 Å
Shell Rg shell_rg	34.18 Å
Envelope Rg envelope_rg	28.09 Å
Shape Rg shape_rg	28.56 Å
Total Rg total_rg	29.25 Å
Total atoms total_atoms	3005
Residues n_residues	382
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	97.9 Å
Rg (real space) rg_real	29.30 Å
Rg uncertainty (real space) rg_real_error	1.02 Å
I(0) (real space) i0_real	3.0880e+07
I(0) uncertainty (real space) i0_real_error	4.9600e+05
Rg (reciprocal space) rg_reciprocal	29.23 Å
I(0) (reciprocal space) i0_reciprocal	30880000.0000
Solution quality estimate total_estimate	0.8662
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	27.2 Å
Skewness Skewness skewness	0.388
Kurtosis Kurtosis kurtosis	-0.551
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2669000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.782; Smooth: 0.850

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	AXONIN-1
Molecular weight formula_weight	42602.7 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	3362

RSYGPVFEEQPAHTLFPEGSAEEKVTLTCRARANPPATYRWKMNGTELKMGPDSRYRLVAGDLVISNPVKAKDAGSYQCVATNARGTVVSREASLRFGFLQEFSAEERDPVKITEGWGVMFTCSPPPHYPALSYRWLLNEFPNFIPADGRRFVSQTTGNLYIAKTEASDLGNYSCFATSHIDFITKSVFSKFSQLSLAAEDARQYAPSIKAKFPADTYALTGQMVTLECFAFGNPVPQIKWRKLDGSQTSKWLSSEPLLHIQNVDFEDEGTYECEAENIKGRDTYQGRIIIHAQPDWLDVITDTEADIGSDLRWSCVASGKPRPAVRWLRDGQPLASQNRIEVSGGELRFSKLVLEDSGMYQCVAENKHGTVYASAELTVQA

来源 Source

来源生物 organism	Gallus gallus
通用名 common_name	chicken
NCBI Class编号 ncbi_taxonomy_id	9031
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	357

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1cs6a1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.4 — I set domains

Domain ID domain_id	d1cs6a2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.4 — I set domains

Domain ID domain_id	d1cs6a3
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.4 — I set domains

Domain ID domain_id	d1cs6a4
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.4 — I set domains

CATH v4.4 (4 domains)

Domain ID domain_id	1cs6A01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1cs6A02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1cs6A03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1cs6A04
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	60.583 Å
Unit-cell length b length_b	45.540 Å
Unit-cell length c length_c	99.548 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.14 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2260
R_work r_work	0.2260
R_free r_free	0.2570

fit	/app/data/saxs_computation/cs/1cs6/1cs6.fit
pddf	/app/data/pr_computation/cs/1cs6/1cs6.pr.out
profile	/app/data/saxs_computation/cs/1cs6/1cs6.dat

N-TERMINAL FRAGMENT OF AXONIN-1 FROM CHICKEN

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

AXONIN-1

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