SAXSdb — 1g2g

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

ALPHA-CONOTOXIN IMI

OrganismNot specified

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 1–12	Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.8；278 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition：5-6 mM alpha-ImI; 90 % H2O, 10 % D2O; 0.1 M potassium phosphate buffer pH 5.8 \| 90 % H2O, 10 % D2O; 0.1 M potassium phosphate buffer pH 5.8	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 1G2G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CNL ALPHA-CONOTOXIN IMI Deposited 1999-05-20	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.1；280 K NMR sample composition 10% D2O/90% H2O	Resolution not provided
1E74 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT R11E Deposited 2000-08-24	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.1；298 K	Resolution not provided
1E75 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT R7L Deposited 2000-08-24	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.7；298 K	Resolution not provided
1E76 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT D5N Deposited 2000-08-24	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.1；298 K	Resolution not provided
1IM1 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1, 20 STRUCTURES Deposited 1998-11-18	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K NMR sample composition 90% H2O/10% D2O OR 100% D2O	Resolution not provided
1IMI SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 Deposited 1998-11-27	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；278 K；Pressure 1 NMR sample composition 90% H2O/ 10% D2O	Resolution not provided
2BC7 Solution structure of [Sec2,8]-ImI Deposited 2005-10-18	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 5–16（12 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；290 K；Ionic strength (raw mmCIF value) 1；Pressure ambient NMR sample composition 1mM peptide \| 90% H2O/10% D2O	Resolution not provided
2BC8 [Sec2,3,8,12]-ImI Deposited 2005-10-18	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 5–16（12 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；290 K；Ionic strength (raw mmCIF value) 1；Pressure ambient NMR sample composition 2mM [Sec2,3,8,12]-ImI \| 90% D2O, 10% H2O NMR sample composition 2mM [Sec2,3,8,12]-ImI \| 100% D2O	Resolution not provided
2BYP Crystal structure of Aplysia californica AChBP in complex with alpha- conotoxin ImI Deposited 2005-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain F 5–16（12 aa） Chain G 5–16（12 aa） Chain H 5–16（12 aa） Chain I 5–16（12 aa） Chain J 5–16（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；11-14% PEG-4000, 0.1 M TRIS, PH 7.5, 0.4 M MGCL2	Resolution 2.07 Å R-free 0.214
2C9T Crystal Structure Of Acetylcholine Binding Protein (AChBP) From Aplysia Californica In Complex With alpha-Conotoxin ImI Deposited 2005-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain K 5–16（12 aa） Fragment：RESIDUES 5-16 Chain M 5–16（12 aa） Fragment：RESIDUES 5-16 Chain O 5–16（12 aa） Fragment：RESIDUES 5-16 Chain P 5–16（12 aa） Fragment：RESIDUES 5-16 Chain Q 5–16（12 aa） Fragment：RESIDUES 5-16 Chain R 5–16（12 aa） Fragment：RESIDUES 5-16 Chain S 5–16（12 aa） Fragment：RESIDUES 5-16 Chain T 5–16（12 aa） Fragment：RESIDUES 5-16	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 100 MM SODIUM ACETATE PH 5.5, 12.5% PEG5000 MME	Resolution 2.25 Å R-free 0.227
2MOA Solution NMR structure of peptide ImI1 (peak 2) Deposited 2014-04-24	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 5–16（12 aa） Fragment：UNP residues 5-16	Mutation：C2(81S), C3A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；278 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 1 mM ImI1, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
9NX0 Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImI Deposited 2025-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain F 5–16（12 aa） Fragment：residues 5-16 Chain G 5–16（12 aa） Fragment：residues 5-16 Chain H 5–16（12 aa） Fragment：residues 5-16 Chain I 5–16（12 aa） Fragment：residues 5-16 Chain J 5–16（12 aa） Fragment：residues 5-16	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CXA1_CONIM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–12； UniProt 1–12

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	1g2g
Deposition date deposition_date	2000-10-19
Structure title title	MINIMAL CONFORMATION OF THE ALPHA-CONOTOXIN IMI FOR THE ALPHA7 NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR RECOGNITION
Keywords keywords	alpha-helix, 3-10 helix, TOXIN; TOXIN
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	5.24 Å
Radius of gyration Rg (electron density) rg_electron	5.76 Å
Forward intensity I(0) i0	38249700.00
Molecular weight molecular_weight	40698.0 kDa
Excluded volume excluded_volume	46429 Å³
Envelope volume envelope_volume	2727 Å³
Hydration-shell volume shell_volume	3783 Å³
Envelope diameter envelope_diameter	21.7 Å
Shell Rg shell_rg	11.30 Å
Envelope Rg envelope_rg	7.26 Å
Shape Rg shape_rg	5.76 Å
Total Rg total_rg	5.94 Å
Total atoms total_atoms	5130
Residues n_residues	360
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	19.5 Å
Rg (real space) rg_real	5.22 Å
Rg uncertainty (real space) rg_real_error	0.33 Å
I(0) (real space) i0_real	3.8250e+07
I(0) uncertainty (real space) i0_real_error	3.0610e+05
Rg (reciprocal space) rg_reciprocal	5.22 Å
I(0) (reciprocal space) i0_reciprocal	38250000.0000
Solution quality estimate total_estimate	0.8242
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	6.9 Å
Skewness Skewness skewness	0.220
Kurtosis Kurtosis kurtosis	-0.064
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	438.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.672; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.896; Smooth: 0.809

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1g2ga_
Class class	j — Peptides
Fold Fold fold	j.30 — Conotoxins
Superfamily Superfamily superfamily	j.30.1 — Conotoxins
Family Family family	j.30.1.2 — alpha-conotoxin

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8. Citations (6)

;Minimal conformation of the alpha-conotoxin ImI for the alpha7 neuronal nicotinic acetylcholine receptor recognition: correlated CD, NMR and binding studies. ;

FEBS Lett. (1999)

PMID: 10431825 · DOI: 10.1016/S0014-5793(99)00831-5 PRIMARY

;NMR Spatial Structure of alpha-Conotoxin ImI Reveals a Common Scaffold in Snail and Snake Toxins Recognizing Neuronal Nicotinic Acetylcholine Receptors ;

FEBS Lett. (1999)

DOI: 10.1016/S0014-5793(99)00069-1

;NMR Solution Structure of alpha-Conotoxin ImI and Comparison to other Conotoxins Specific for Neuronal Nicotinic Acetylcholine Receptors ;

Biochemistry (1999)

DOI: 10.1021/bi9826254

Functional Determinants by which Snake and Cone Snail Toxins Block the alpha 7 Neuronal Nicotinic Acetylcholine Receptors

J.Physiol.(Paris) (1998)

DOI: 10.1016/S0928-4257(98)80146-0

Identification of Residues in the Neuronal alpha7 Acetylcholine Receptor that Confer Selectivity for Conotoxin ImI

J.Biol.Chem. (1998)

DOI: 10.1074/jbc.273.18.11001

A Nicotinic Acetylcholine Receptor Ligand of Unique Specificity, alpha-Conotoxin ImI

J.Biol.Chem. (1994)

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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	—

Description description	ALPHA-CONOTOXIN IMI
Molecular weight formula_weight	1356.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5130

fit	/app/data/saxs_computation/g2/1g2g/1g2g.fit
pddf	/app/data/pr_computation/g2/1g2g/1g2g.pr.out
profile	/app/data/saxs_computation/g2/1g2g/1g2g.dat

MINIMAL CONFORMATION OF THE ALPHA-CONOTOXIN IMI FOR THE ALPHA7 NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR RECOGNITION

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

ALPHA-CONOTOXIN IMI

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (6)

9. Files and Curves (10)

Files (7)

Curves (3)