SAXSdb — 1ciy

▼

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

CRYIA(A)

Bacillus thuringiensis

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 29–618	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.25 Å R-free 0.248

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	CR1AA_BACTK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–590； UniProt 29–618

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	1ciy
Deposition date deposition_date	1995-06-01
Structure title title	INSECTICIDAL TOXIN: STRUCTURE AND CHANNEL FORMATION
Keywords keywords	TOXIN, DELTA-ENDOTOXIN CRYIA(A), ICP; TOXIN
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	26.39 Å
Radius of gyration Rg (electron density) rg_electron	25.29 Å
Forward intensity I(0) i0	67361600.00
Molecular weight molecular_weight	64542.0 kDa
Excluded volume excluded_volume	80849 Å³
Envelope volume envelope_volume	94367 Å³
Hydration-shell volume shell_volume	31047 Å³
Envelope diameter envelope_diameter	93.2 Å
Shell Rg shell_rg	32.62 Å
Envelope Rg envelope_rg	25.53 Å
Shape Rg shape_rg	25.28 Å
Total Rg total_rg	26.07 Å
Total atoms total_atoms	4571
Residues n_residues	577
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	89.5 Å
Rg (real space) rg_real	26.32 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	6.7360e+07
I(0) uncertainty (real space) i0_real_error	1.0400e+06
Rg (reciprocal space) rg_reciprocal	26.34 Å
I(0) (reciprocal space) i0_reciprocal	67360000.0000
Solution quality estimate total_estimate	0.6820
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.3 Å
Skewness Skewness skewness	0.287
Kurtosis Kurtosis kurtosis	-0.269
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13810000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.818; Stabil: 1.000; Sysdev: 0.145; Positv: 1.000; Valcen: 0.991; Smooth: 0.980

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	CRYIA(A)
Molecular weight formula_weight	66166.9 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	4693

IETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEADPTNPALREEMRIQFNDMNSALTTAIPLLAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRLIGNYTDYAVRWYNTGLERVWGPDSRDWVRYNQFRRELTLTVLDIVALFSNYDSRRYPIRTVSQLTREIYTNPVLENFDGSFRGMAQRIEQNIRQPHLMDILNSITIYTDVHRGFNYWSGHQITASPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIFRTLSSPLYRRIILGSGPNNQELFVLDGTEFSFASLTTNLPSTIYRQRGTVDSLDVIPPQDNSVPPRAGFSHRLSHVTMLSQAAGAVYTLRAPTFSWQHRSAEFNNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQISTLRVNITAPLSQRYRVRIRYASTTNLQFHTSIDGRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVPAEVTFEAEYDLER

来源 Source

来源生物 organism	Bacillus thuringiensis
NCBI Class编号 ncbi_taxonomy_id	1428
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	122

▼

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1ciya1
Class class	b — All beta proteins
Fold Fold fold	b.18 — Galactose-binding domain-like
Superfamily Superfamily superfamily	b.18.1 — Galactose-binding domain-like
Family Family family	b.18.1.3 — delta-Endotoxin, C-terminal domain

Domain ID domain_id	d1ciya2
Class class	b — All beta proteins
Fold Fold fold	b.77 — beta-Prism I
Superfamily Superfamily superfamily	b.77.2 — delta-Endotoxin (insectocide), middle domain
Family Family family	b.77.2.1 — delta-Endotoxin (insectocide), middle domain

Domain ID domain_id	d1ciya3
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamily	f.1.3 — delta-Endotoxin (insectocide), N-terminal domain
Family Family family	f.1.3.1 — delta-Endotoxin (insectocide), N-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id	1ciyA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	10 — Pesticidal crystal protein, N-terminal domain

Domain ID domain_id	1ciyA02
Class class	2 — Mainly Beta
Architecture architecture	100 — Aligned Prism
Topology topology	10 — Vitelline Membrane Outer Layer Protein I, subunit A
Homologous superfamily homologous superfamily	10 — Pesticidal crystal protein, central domain

Domain ID domain_id	1ciyA03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	260 — Galactose-binding domain-like

▶

8. Citations (3)

▶

Unit-cell length a length_a	54.000 Å
Unit-cell length b length_b	111.500 Å
Unit-cell length c length_c	154.600 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	2.250 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1630
R_work r_work	0.1630
R_free r_free	0.2480

fit	/app/data/saxs_computation/ci/1ciy/1ciy.fit
pddf	/app/data/pr_computation/ci/1ciy/1ciy.pr.out
profile	/app/data/saxs_computation/ci/1ciy/1ciy.dat

INSECTICIDAL TOXIN: STRUCTURE AND CHANNEL FORMATION

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

CRYIA(A)

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