SAXSdb — 1feo

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

OMEGA-CONOTOXIN MVIIA-GLY

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 1–25	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6；283 K；Pressure ambient NMR sample composition：2 mM omega-MVIIA-Gly \| 93% H2O, 7% D20 NMR sample composition：2 mM omega-MVIIA-Gly U-15N \| 93% H2O, 7% D20	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 1FEO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DW4 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: CONSTRAINTS ON DISULPHIDE BRIDGES Deposited 2000-01-24	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–25（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1 \| H2O (10% D2O) NMR sample composition 1 \| D2O	Resolution not provided
1DW5 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES Deposited 2000-01-24	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–25（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT NMR sample composition 1	Resolution not provided
1MVI N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES Deposited 1996-08-02	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–25（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；293 K	Resolution not provided
1OMG NMR STUDY OF OMEGA-CONOTOXIN MVIIA Deposited 1995-04-26	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–25（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TT3 NMR soulution structure of omega-conotoxin [K10]MVIIA Deposited 2004-06-21	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 46–70（25 aa）	Mutation：R10K Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；293 K；Pressure ambient NMR measurement conditions pH 3.5；280 K；Pressure ambient NMR sample composition 2mM [K10]MVIIA, 95% H2O, 5% D2O, DSS \| 95% H2O/5% D2O NMR sample composition 2mM [K10]MVIIA, 100% D2O, DSS \| 100% D2O	Resolution not provided
1TTK NMR solution structure of omega-conotoxin MVIIA, a N-type calcium channel blocker Deposited 2004-06-22	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 46–70（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；293 K；Pressure ambient NMR measurement conditions pH 3.5；280 K；Pressure ambient NMR sample composition 2mM MVIIA, 95% H2O, D2O, DSS \| 95% H2O/5% D2O NMR sample composition 2mM MVIIA, 100% D2O \| 100% D2O	Resolution not provided
7MIX Human N-type voltage-gated calcium channel Cav2.2 in the presence of ziconotide at 3.0 Angstrom resolution Deposited 2021-04-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 46–70（25 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2 Y01 CHOLESTEROL HEMISUCCINATE × 2 CLR CHOLESTEROL × 5 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；blot for 6 seconds before plunging	Resolution 3.00 Å
7VFU Human N-type voltage gated calcium channel CaV2.2-alpha2/delta1-beta1 complex, bound to ziconotide Deposited 2021-09-13	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 46–70（25 aa）	Not recorded	R16 HEXADECANE × 18 Y01 CHOLESTEROL HEMISUCCINATE × 3 PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 1 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CXO7A_CONMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–25； UniProt 1–25

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	1feo
Deposition date deposition_date	2000-07-21
Structure title title	Solution structure of omega-conotoxin MVIIA with C-terminal Gly
Keywords keywords	beta sheet, disulfide knot, 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	6.98 Å
Radius of gyration Rg (electron density) rg_electron	7.48 Å
Forward intensity I(0) i0	59710900.00
Molecular weight molecular_weight	54165.0 kDa
Excluded volume excluded_volume	63943 Å³
Envelope volume envelope_volume	5743 Å³
Hydration-shell volume shell_volume	5826 Å³
Envelope diameter envelope_diameter	29.8 Å
Shell Rg shell_rg	13.78 Å
Envelope Rg envelope_rg	9.32 Å
Shape Rg shape_rg	7.43 Å
Total Rg total_rg	7.83 Å
Total atoms total_atoms	7200
Residues n_residues	520
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	24.9 Å
Rg (real space) rg_real	6.97 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	5.9710e+07
I(0) uncertainty (real space) i0_real_error	5.6530e+05
Rg (reciprocal space) rg_reciprocal	6.97 Å
I(0) (reciprocal space) i0_reciprocal	59710000.0000
Solution quality estimate total_estimate	0.8398
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	8.8 Å
Skewness Skewness skewness	0.392
Kurtosis Kurtosis kurtosis	0.235
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6775.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.683; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.913

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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	d1feoa_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.6 — omega toxin-like
Family Family family	g.3.6.1 — Conotoxin

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8. Citations (2)

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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	OMEGA-CONOTOXIN MVIIA-GLY
Molecular weight formula_weight	2709.3 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	7200

fit	/app/data/saxs_computation/fe/1feo/1feo.fit
pddf	/app/data/pr_computation/fe/1feo/1feo.pr.out
profile	/app/data/saxs_computation/fe/1feo/1feo.dat

Solution structure of omega-conotoxin MVIIA with C-terminal Gly

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

OMEGA-CONOTOXIN MVIIA-GLY

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 (2)

9. Files and Curves (10)

Files (7)

Curves (3)