3j98

Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIa)

Method: ELECTRON MICROSCOPY Dmax: 214.1 Å Quality: GOOD

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

Vesicle-fusing ATPase

Cricetulus griseus

UniProt P18708

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain A; UniProt 1–744 Chain B; UniProt 1–744 Chain C; UniProt 1–744 Chain D; UniProt 1–744 Chain E; UniProt 1–744 Chain F; UniProt 1–744 Not recorded Alpha-soluble NSF attachment protein × 4 (P54921) Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40;pH 8;50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40 cryo-EM vitrification conditions:Blot for 3.5 seconds before plunging.;90 K;Cryogen ETHANE;Blot for 3.5 seconds before plunging into liquid ethane (FEI VITROBOT MARK I). Resolution 8.40 Å R-free 0.328

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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSF_CRIGR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–747; UniProt 1–744 Author chain B; PDBConstruct 4–747; UniProt 1–744 Author chain C; PDBConstruct 4–747; UniProt 1–744 Author chain D; PDBConstruct 4–747; UniProt 1–744 Author chain E; PDBConstruct 4–747; UniProt 1–744 Author chain F; PDBConstruct 4–747; UniProt 1–744

Alpha-soluble NSF attachment protein

Rattus norvegicus

UniProt P54921

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain G; UniProt 1–295 Chain H; UniProt 1–295 Chain I; UniProt 1–295 Chain J; UniProt 1–295 Not recorded Vesicle-fusing ATPase × 6 (P18708) Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40;pH 8;50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40 cryo-EM vitrification conditions:Blot for 3.5 seconds before plunging.;90 K;Cryogen ETHANE;Blot for 3.5 seconds before plunging into liquid ethane (FEI VITROBOT MARK I). Resolution 8.40 Å R-free 0.328

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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNAA_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 3–297; UniProt 1–295 Author chain H; PDBConstruct 3–297; UniProt 1–295 Author chain I; PDBConstruct 3–297; UniProt 1–295 Author chain J; PDBConstruct 3–297; UniProt 1–295

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain K; UniProt 28–89 Fragment:UNP residues 28-89 Vesicle-fusing ATPase × 6 (P18708) Alpha-soluble NSF attachment protein × 4 (P54921) Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40;pH 8;50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40 cryo-EM vitrification conditions:Blot for 3.5 seconds before plunging.;90 K;Cryogen ETHANE;Blot for 3.5 seconds before plunging into liquid ethane (FEI VITROBOT MARK I). Resolution 8.40 Å R-free 0.328

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 K; 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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain L; UniProt 191–256 Fragment:UNP residues 191-256 Vesicle-fusing ATPase × 6 (P18708) Alpha-soluble NSF attachment protein × 4 (P54921) Vesicle-associated membrane protein 2 × 1 (P63045) Synaptosomal-associated protein 25 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40;pH 8;50 mM Tris-Cl, 150 mM NaCl, 1 mM AMPPNP, 1 mM EDTA, 1 mM DTT, 0.05% v/v Nonident P-40 cryo-EM vitrification conditions:Blot for 3.5 seconds before plunging.;90 K;Cryogen ETHANE;Blot for 3.5 seconds before plunging into liquid ethane (FEI VITROBOT MARK I). Resolution 8.40 Å R-free 0.328

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 L; PDBConstruct 2–67; UniProt 191–256

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 3j98

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j98
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j98
Deposition date deposition_date2014-12-05
Structure title titleStructure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIa)
Keywords keywordsvesicle trafficking, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.00
Radius of gyration Rg (electron density) rg_electron63.66
Forward intensity I(0) i04741300000.00
Molecular weight molecular_weight582930.0 kDa
Excluded volume excluded_volume730500 ų
Envelope volume envelope_volume1175000 ų
Hydration-shell volume shell_volume151660 ų
Envelope diameter envelope_diameter213.8
Shell Rg shell_rg69.22
Envelope Rg envelope_rg60.51
Shape Rg shape_rg63.62
Total Rg total_rg63.88
Total atoms total_atoms40956
Residues n_residues5422
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 dmax214.1
Rg (real space) rg_real63.72
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real4.7410e+09
I(0) uncertainty (real space) i0_real_error8.6540e+07
Rg (reciprocal space) rg_reciprocal64.21
I(0) (reciprocal space) i0_reciprocal4745000000.0000
Solution quality estimate total_estimate0.8615
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.3
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha377100000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.708

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)