3ipd

Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21

Method: X-RAY DIFFRACTION Dmax: 118.9 Å Quality: REASONABLE

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

Vesicle-associated membrane protein 2

Rattus norvegicus

UniProt P63045

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 30–116 Fragment:C-terminal fragment, UNP Residues 30-116 Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;16% MPD, 0.1M TRIS, 0.05M MAGNESIUM CHLORIDE, 3% SORBITOL, pH 8.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.80 Å R-free 0.332
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 30–116 Fragment:C-terminal fragment, UNP Residues 30-116 Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;16% MPD, 0.1M TRIS, 0.05M MAGNESIUM CHLORIDE, 3% SORBITOL, pH 8.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.80 Å R-free 0.332

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.

22 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAMP2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–91; UniProt 30–116 Author chain E; PDBConstruct 5–91; UniProt 30–116

Syntaxin-1A

Rattus norvegicus

UniProt P32851

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 183–288 Fragment:C-terminal fragment, UNP Residues 183-288 Vesicle-associated membrane protein 2 × 1 (P63045) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;16% MPD, 0.1M TRIS, 0.05M MAGNESIUM CHLORIDE, 3% SORBITOL, pH 8.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.80 Å R-free 0.332
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 183–288 Fragment:C-terminal fragment, UNP Residues 183-288 Vesicle-associated membrane protein 2 × 1 (P63045) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;16% MPD, 0.1M TRIS, 0.05M MAGNESIUM CHLORIDE, 3% SORBITOL, pH 8.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.80 Å R-free 0.332

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.

53 other PDB entries and 71 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STX1A_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–109; UniProt 183–288 Author chain F; PDBConstruct 4–109; UniProt 183–288

Synaptosomal-associated protein 25

Rattus norvegicus

UniProt P60881

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 7–83 Chain D; UniProt 141–204 Fragment:N-terminal fragment, UNP Residues 7-83 Fragment:C-terminal fragment, UNP Residues 141-204 Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;16% MPD, 0.1M TRIS, 0.05M MAGNESIUM CHLORIDE, 3% SORBITOL, pH 8.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.80 Å R-free 0.332
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 7–83 Chain H; UniProt 141–204 Fragment:N-terminal fragment, UNP Residues 7-83 Fragment:C-terminal fragment, UNP Residues 141-204 Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;293 K;16% MPD, 0.1M TRIS, 0.05M MAGNESIUM CHLORIDE, 3% SORBITOL, pH 8.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.80 Å R-free 0.332

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.

39 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNP25_RAT
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 4–80; UniProt 7–83 Author chain G; PDBConstruct 4–80; UniProt 7–83 Author chain D; PDBConstruct 5–68; UniProt 141–204 Author chain H; PDBConstruct 5–68; UniProt 141–204

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3ipd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ipd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ipd
Deposition date deposition_date2009-08-17
Structure title titleHelical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21
Keywords keywords;MEMBRANE PROTEIN, COILED COIL, 4-HELICAL BUNDLE, MEMBRANE FUSION, CYTOPLASMIC VESICLE, MEMBRANE, PHOSPHOPROTEIN, SYNAPSE, SYNAPTOSOME, TRANSMEMBRANE, NEUROTRANSMITTER TRANSPORT, TRANSPORT, CELL MEMBRANE, CYTOPLASM, LIPOPROTEIN, PALMITATE, TRANSPORT PROTEIN, Acetylation, Cell junction, Alternative splicing, EXOCYTOSIS ;; EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.38
Radius of gyration Rg (electron density) rg_electron49.12
Forward intensity I(0) i094511500.00
Molecular weight molecular_weight75244.0 kDa
Excluded volume excluded_volume93077 ų
Envelope volume envelope_volume136990 ų
Hydration-shell volume shell_volume29193 ų
Envelope diameter envelope_diameter216.7
Shell Rg shell_rg39.91
Envelope Rg envelope_rg51.45
Shape Rg shape_rg49.07
Total Rg total_rg48.76
Total atoms total_atoms5242
Residues n_residues654
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax118.9
Rg (real space) rg_real40.23
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real8.9740e+07
I(0) uncertainty (real space) i0_real_error1.3330e+06
Rg (reciprocal space) rg_reciprocal44.39
I(0) (reciprocal space) i0_reciprocal94360000.0000
Solution quality estimate total_estimate0.6625
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.659
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.8469
Highest regularization parameter α highest_alpha2619000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.013; Oscil: 0.972; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.754; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)