6mti

Synaptotagmin-1 C2A, C2B domains and SNARE-pin proteins (5CCI) individually docked into Cryo-EM map of C2AB-SNARE complexes helically organized on lipid nanotube surface in presence of Mg2+

Method: ELECTRON MICROSCOPY Dmax: 232.5 Å Quality: GOOD

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

Synaptotagmin-1

Rattus norvegicus

UniProt P21707

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 141–267 Chain 2; UniProt 141–421 Chain 3; UniProt 141–421 Chain 4; UniProt 141–421 Chain 5; UniProt 141–421 Chain 6; UniProt 141–267 Fragment:C2A domain, residues 141-267 Fragment:C2A and C2B domains, residues 141-421 Vesicle-associated membrane protein 2 × 6 (P63045) Syntaxin-1A × 6 (P32851) Synaptosomal-associated protein 25 × 6 (P60881) Synaptosomal-associated protein 25 × 6 (P60881) MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.40 Å

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.

19 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYT1_RAT
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–127; UniProt 141–267 Author chain 6; PDBConstruct 1–127; UniProt 141–267 Author chain 2; PDBConstruct 1–281; UniProt 141–421 Author chain 3; PDBConstruct 1–281; UniProt 141–421 Author chain 4; PDBConstruct 1–281; UniProt 141–421 Author chain 5; PDBConstruct 1–281; UniProt 141–421

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 28–89 Chain E; UniProt 28–89 Chain I; UniProt 28–89 Chain M; UniProt 28–89 Chain Q; UniProt 28–89 Chain U; UniProt 28–89 Fragment:residues 28-89 Synaptotagmin-1 × 2 (P21707) Synaptotagmin-1 × 4 (P21707) Syntaxin-1A × 6 (P32851) Synaptosomal-associated protein 25 × 6 (P60881) Synaptosomal-associated protein 25 × 6 (P60881) MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.40 Å

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 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAMP2_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 2–63; UniProt 28–89 Author chain E; PDBConstruct 2–63; UniProt 28–89 Author chain I; PDBConstruct 2–63; UniProt 28–89 Author chain M; PDBConstruct 2–63; UniProt 28–89 Author chain Q; PDBConstruct 2–63; UniProt 28–89 Author chain U; PDBConstruct 2–63; UniProt 28–89

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain B; UniProt 191–256 Chain F; UniProt 191–256 Chain J; UniProt 191–256 Chain N; UniProt 191–256 Chain R; UniProt 191–256 Chain V; UniProt 191–256 Fragment:residues 191-256 Synaptotagmin-1 × 2 (P21707) Synaptotagmin-1 × 4 (P21707) Vesicle-associated membrane protein 2 × 6 (P63045) Synaptosomal-associated protein 25 × 6 (P60881) Synaptosomal-associated protein 25 × 6 (P60881) MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.40 Å

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 72 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STX1A_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 2–67; UniProt 191–256 Author chain F; PDBConstruct 2–67; UniProt 191–256 Author chain J; PDBConstruct 2–67; UniProt 191–256 Author chain N; PDBConstruct 2–67; UniProt 191–256 Author chain R; PDBConstruct 2–67; UniProt 191–256 Author chain V; PDBConstruct 2–67; UniProt 191–256

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain C; UniProt 7–83 Chain D; UniProt 141–204 Chain G; UniProt 7–83 Chain H; UniProt 141–204 Chain K; UniProt 7–83 Chain L; UniProt 141–204 Chain O; UniProt 7–83 Chain P; UniProt 141–204 Chain S; UniProt 7–83 Chain T; UniProt 141–204 Chain W; UniProt 7–83 Chain X; UniProt 141–204 Fragment:residues 7-83 Fragment:residues 141-204 Synaptotagmin-1 × 2 (P21707) Synaptotagmin-1 × 4 (P21707) Vesicle-associated membrane protein 2 × 6 (P63045) Syntaxin-1A × 6 (P32851) MG MAGNESIUM ION × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.40 Å

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 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNP25_RAT
Isoform P60881-2
PDB entities 5, 6
Chains and sequence ranges Author chain C; PDBConstruct 1–77; UniProt 7–83 Author chain G; PDBConstruct 1–77; UniProt 7–83 Author chain K; PDBConstruct 1–77; UniProt 7–83 Author chain O; PDBConstruct 1–77; UniProt 7–83 Author chain S; PDBConstruct 1–77; UniProt 7–83 Author chain W; PDBConstruct 1–77; UniProt 7–83 Author chain D; PDBConstruct 2–65; UniProt 141–204 Author chain H; PDBConstruct 2–65; UniProt 141–204 Author chain L; PDBConstruct 2–65; UniProt 141–204 Author chain P; PDBConstruct 2–65; UniProt 141–204 Author chain T; PDBConstruct 2–65; UniProt 141–204 Author chain X; PDBConstruct 2–65; 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 6mti

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mti
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mti
Deposition date deposition_date2018-10-19
Structure title titleSynaptotagmin-1 C2A, C2B domains and SNARE-pin proteins (5CCI) individually docked into Cryo-EM map of C2AB-SNARE complexes helically organized on lipid nanotube surface in presence of Mg2+
Keywords keywordsSNARE, lipid nanotubes, EXOCYTOSIS; EXOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier75.69
Radius of gyration Rg (electron density) rg_electron76.92
Forward intensity I(0) i01716310000.00
Molecular weight molecular_weight335740.0 kDa
Excluded volume excluded_volume415450 ų
Envelope volume envelope_volume712780 ų
Hydration-shell volume shell_volume90186 ų
Envelope diameter envelope_diameter314.5
Shell Rg shell_rg60.75
Envelope Rg envelope_rg75.05
Shape Rg shape_rg76.88
Total Rg total_rg76.73
Total atoms total_atoms23540
Residues n_residues2966
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 dmax232.5
Rg (real space) rg_real73.61
Rg uncertainty (real space) rg_real_error1.62
I(0) (real space) i0_real1.6930e+09
I(0) uncertainty (real space) i0_real_error3.0510e+07
Rg (reciprocal space) rg_reciprocal72.32
I(0) (reciprocal space) i0_reciprocal1702000000.0000
Solution quality estimate total_estimate0.8510
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.4
Skewness Skewness skewness0.558
Kurtosis Kurtosis kurtosis-0.258
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0619
Highest regularization parameter α highest_alpha69110000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.913; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.256

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)