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7t7x

Munc13-1 C1-C2B-MUN-C2C Upright conformation spanning two lipid bilayers

Method: ELECTRON MICROSCOPY Dmax: 216.4 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein unc-13 homolog A

Rattus norvegicus

UniProt Q4KUS2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1448–1712 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE；blot for 5 sec before plunging, blot force -1 Resolution 10.00 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.

Other PDB Difference from Current Entry 7T7X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7T7C The hexagonal organization of Munc13-1 C1-C2B-MUN-C2C domains between lipid bilayers Deposited 2021-12-15 Different construct Different mutation/modification Different oligomeric state Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric
Chain A 1448–1712（265 aa）
Chain B 1448–1712（265 aa）
Chain C 1448–1712（265 aa）
Chain D 1448–1712（265 aa）
Chain E 1448–1712（265 aa）
Chain F 1448–1712（265 aa）
Chain G 1448–1712（265 aa）
Chain H 1448–1712（265 aa）
Chain I 1448–1712（265 aa）
Chain J 1448–1712（265 aa）
Chain K 1448–1712（265 aa）
Chain L 1448–1712（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 5 sec before plunging, blot force -1
Resolution 10.00 Å
7T7R Structure of Munc13-1 C1-C2B-MUN-C2C trimer between lipid bilayers Deposited 2021-12-15 Different construct Different mutation/modification Different oligomeric state Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 525–1403（879 aa）
Chain A 1448–1712（265 aa）
Chain B 525–1403（879 aa）
Chain B 1448–1712（265 aa）
Chain C 525–1403（879 aa）
Chain C 1448–1712（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 5 sec before plunging, blot force -1
Resolution 10.00 Å
7T7V Munc13-1 C1-C2B-MUN-C2C Lateral conformation on lipid bilayer surface Deposited 2021-12-15 Different construct Different mutation/modification Different oligomeric state Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 525–1403（879 aa）
Chain A 1448–1712（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 5 sec before plunging, blot force -1
Resolution 10.00 Å
7T81 Model of Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers. Deposited 2021-12-15 Different construct Different mutation/modification Different oligomeric state Assembly 1 Insufficient information Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1448–1712（265 aa）
Chain C 1448–1712（265 aa）
Chain D 1448–1712（265 aa）
Chain E 1448–1712（265 aa）
Chain F 1448–1712（265 aa）
Chain G 1448–1712（265 aa）
Chain H 1448–1712（265 aa）
Chain I 1448–1712（265 aa）
Chain J 1448–1712（265 aa）
Chain K 1448–1712（265 aa）
Chain L 1448–1712（265 aa）
Chain M 1448–1712（265 aa）
Chain N 1448–1712（265 aa）
Chain O 1448–1712（265 aa）
Chain P 1448–1712（265 aa）
Chain Q 1448–1712（265 aa）
Chain R 1448–1712（265 aa）
Chain S 1448–1712（265 aa）
Chain T 1448–1712（265 aa）
Chain U 1448–1712（265 aa）
Chain V 1448–1712（265 aa）
Chain W 1448–1712（265 aa）
Chain X 1448–1712（265 aa）
Chain Y 1448–1712（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 5 sec before plunging, blot force -1
Resolution 10.00 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UN13A_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 890–1154； UniProt 1448–1712

Protein unc-13 homolog A

Rattus norvegicus

UniProt Q62768

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 529–1407 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE；blot for 5 sec before plunging, blot force -1 Resolution 10.00 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.

Other PDB Difference from Current Entry 7T7X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1Y8F Solution structure of the munc13-1 C1-domain Deposited 2004-12-12 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 567–616（50 aa） Fragment：C1-domain (residues 567-616)
Not recorded ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 150mM NaCl；Pressure ambient
NMR sample composition 1.5mM munc13-1 C1-domain U-15N, 40mM HEPES (pH 7.0), 150mM NaCl, 50uM ZnCl2 | 40mM HEPES (pH 7.0), 150mM NaCl, 50uM ZnCl2
NMR sample composition 1.5mM munc13-1 C1-domain U-15N,13C, 40mM HEPES (pH 7.0), 150mM NaCl, 50uM ZnCl2 | 40 mM HEPES (pH 7.0), 150 mM NaCl, 50 uM ZnCl2
Resolution not provided
2CJS Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch: C2-domains as Versatile Protein-Protein Interaction Modules Deposited 2006-04-06 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 × 3 PDB declaration: trimeric
Chain A 2–150（149 aa） Fragment：C2A DOMAIN, RESIDUES 2-150
Chain B 2–150（149 aa） Fragment：C2A DOMAIN, RESIDUES 2-150
Mutation：YES Mutation：YES EDO 1,2-ETHANEDIOL × 5 GOL GLYCEROL × 6 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；VAPOR DIFFUSION; HANGING DROP; PROTEIN: 10 MG/ML MUNC13-1/RIM2ALPHA IN 30 MM TRIS, 150 MM NACL AND 1 MM TCEP, PH 7.4); RESERVOIR: 0.3 M AMMONIUM TARTRATE (PH 7.0); DROP: 1 MICROLITER PROTEIN PLUS 1 MICROLITER RESERVOIR; TEMPERATURE: 20 DEGREES CELSIUS; CRYSTALS APPEARED OVERNIGHT AND GREW TO A FINAL SIZE OF ABOUT 0.06 MM X 0.06 MM X 0.25 MM WITHIN 4 DAYS.
Resolution 1.78 Å R-free 0.219
2CJT Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch: C2-domains as Versatile Protein-Protein Interaction Modules Deposited 2006-04-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–128（128 aa） Fragment：C2A DOMAIN, RESIDUES 1-128
Chain C 1–128（128 aa） Fragment：C2A DOMAIN, RESIDUES 1-128
Not recorded EDO 1,2-ETHANEDIOL × 11 FMT FORMIC ACID × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；VAPOR DIFFUSION; HANGING DROP; PROTEIN: 12 MG/ML MUNC13-1 IN 30 MM TRIS, 150 MM NACL AND 1 MM TCEP, PH 7.4; RESERVOIR: 0.4 M MAGNESIUM FORMATE, 0.1 M SODIUM ACETATE (PH 4.5); DROP: 1 MICROLITER PROTEIN PLUS 1 MICROLITER RESERVOIR; TEMPERATURE: 20 DEGREES CELSIUS; CRYSTALS APPEARED OVERNIGHT AND GREW TO A FINAL SIZE OF ABOUT 0.05 MM X 0.05 MM X 0.35 MM WITHIN 3 DAYS.
Resolution 1.44 Å R-free 0.188
2CJT Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch: C2-domains as Versatile Protein-Protein Interaction Modules Deposited 2006-04-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 1–128（128 aa） Fragment：C2A DOMAIN, RESIDUES 1-128
Chain D 1–128（128 aa） Fragment：C2A DOMAIN, RESIDUES 1-128
Not recorded EDO 1,2-ETHANEDIOL × 12 FMT FORMIC ACID × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；VAPOR DIFFUSION; HANGING DROP; PROTEIN: 12 MG/ML MUNC13-1 IN 30 MM TRIS, 150 MM NACL AND 1 MM TCEP, PH 7.4; RESERVOIR: 0.4 M MAGNESIUM FORMATE, 0.1 M SODIUM ACETATE (PH 4.5); DROP: 1 MICROLITER PROTEIN PLUS 1 MICROLITER RESERVOIR; TEMPERATURE: 20 DEGREES CELSIUS; CRYSTALS APPEARED OVERNIGHT AND GREW TO A FINAL SIZE OF ABOUT 0.05 MM X 0.05 MM X 0.35 MM WITHIN 3 DAYS.
Resolution 1.44 Å R-free 0.188
2KDU Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode Deposited 2009-01-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 458–492（35 aa） Fragment：UNP residues 458-492, Calmodulin binding domain
Not recorded CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 6.8；308 K
NMR sample composition 10 mM calcium, 1.5 mM [U-99% 13C; U-99% 15N] calmodulin, 1.8 mM Munc13-1, 150 mM potassium chloride, 20 mM BIS-TRIS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 10 mM calcium, 0.5 mM [U-99% 13C; U-99% 15N] Munc13-1, 0.6 mM calmodulin, 150 mM potassium chloride, 20 mM BIS-TRIS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 10 mM calcium, 1.5 mM [U-99% 13C; U-99% 15N] calmodulin, 1.8 mM Munc13, 150 mM potassium chloride, 20 mM BIS-TRIS, 100% D2O | 100% D2O
Resolution not provided
3SWH Munc13-1, MUN domain, C-terminal module Deposited 2011-07-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1148–1407（260 aa） Fragment：SEE REMARK 999
Chain A 1453–1531（79 aa） Fragment：SEE REMARK 999
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；18-25% PEG400, 0.1 M MES, pH 6.0, 0.15 M sodium chloride, 10% glycerol, 5 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.65 Å R-free 0.302
3SWH Munc13-1, MUN domain, C-terminal module Deposited 2011-07-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1148–1407（260 aa） Fragment：SEE REMARK 999
Chain B 1453–1531（79 aa） Fragment：SEE REMARK 999
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；18-25% PEG400, 0.1 M MES, pH 6.0, 0.15 M sodium chloride, 10% glycerol, 5 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.65 Å R-free 0.302
4Y21 Crystal Structure of Munc13-1 MUN domain Deposited 2015-02-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 942–1407（466 aa） Fragment：MUN domain
Chain A 1453–1523（71 aa） Fragment：MUN domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；277 K；PEG 3350, Mg(NO3)2, MES
Resolution 2.90 Å R-free 0.252
5UE8 The crystal structure of Munc13-1 C1C2BMUN domain Deposited 2016-12-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 529–1407（879 aa） Fragment：C1C2BMUN domain (UNP residues 529-1407 and 1452-1531)
Chain A 1452–1531（80 aa） Fragment：C1C2BMUN domain (UNP residues 529-1407 and 1452-1531)
Mutation：;L756W mutation. Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact. ; Mutation：;L756W mutation. Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact. ; ZN ZINC ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M LiCl, 0.1 M Tris-HCl pH 8.0, 0.15 M NaCl, 12% PEG 10,000, 10% glycerol, 5 mM TCEP, 25% ethylene glycol
Resolution 3.35 Å R-free 0.290
5UE8 The crystal structure of Munc13-1 C1C2BMUN domain Deposited 2016-12-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 529–1407（879 aa） Fragment：C1C2BMUN domain (UNP residues 529-1407 and 1452-1531)
Chain B 1452–1531（80 aa） Fragment：C1C2BMUN domain (UNP residues 529-1407 and 1452-1531)
Mutation：;L756W mutation. Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact. ; Mutation：;L756W mutation. Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact. ; ZN ZINC ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M LiCl, 0.1 M Tris-HCl pH 8.0, 0.15 M NaCl, 12% PEG 10,000, 10% glycerol, 5 mM TCEP, 25% ethylene glycol
Resolution 3.35 Å R-free 0.290
5UF7 CRYSTAL STRUCTURE OF MUNC13-1 MUN DOMAIN Deposited 2017-01-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 942–1407（466 aa） Fragment：MUN DOMAIN (UNP residues 942-1407 and 1453-1531)
Chain A 1453–1531（79 aa） Fragment：MUN DOMAIN (UNP residues 942-1407 and 1453-1531)
Mutation：Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact. Mutation：Removal of alternatively spliced loop between residues 1407 and 1453, addition of two residues (EF) as cloning artifact. No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.2 M Mg(NO3)2, 0.1 M MES pH 5.8 - 6.3, 0.15 M NaCl, 18-25% PEG 3350, 10% glycerol, 5 mM DTT, 30% ethylene glycol
Resolution 2.90 Å R-free 0.253
6A30 Crystal Structure of Munc13-1 MUN Domain and Synaptobrevin-2 Juxtamembrane Linker Region Deposited 2018-06-14 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 944–1407（464 aa） Fragment：MUN domain
Chain A 1453–1523（71 aa） Fragment：MUN domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；PEG 3350, magnesium nitrate, 2-(N-Morpholino)ethanesulfonic acid (MES)
Resolution 2.79 Å R-free 0.239
6NYC Munc13-1 C2B-domain, calcium free Deposited 2019-02-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 675–820（146 aa） Fragment：C2B domain, residues 675-820
Mutation：L756W CL CHLORIDE ION × 2 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；298 K；30% PEG-MME 2000, 0.1 M bis-tris propane pH 6.8, 0.1 M NaCl, 0.5 mM TCEP
Resolution 1.89 Å R-free 0.248
6NYT Munc13-1 C2B-domain, calcium bound Deposited 2019-02-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 675–820（146 aa） Fragment：C2B
Mutation：L756W CA CALCIUM ION × 2 CL CHLORIDE ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；298 K；30% PEG-MME 2000, 0.1 M bis-tris propane pH 6.8, 0.1 M NaCl, 0.1 MM CaCl2, 0.5 mM TCEP
Resolution 1.37 Å R-free 0.169
7T81 Model of Munc13-1 C1-C2B-MUN-C2C 2D crystal between lipid bilayers. Deposited 2021-12-15 Different construct Different mutation/modification Different oligomeric state Assembly 1 Insufficient information Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 529–1407（879 aa）
Chain C 529–1407（879 aa）
Chain D 529–1407（879 aa）
Chain E 529–1407（879 aa）
Chain F 529–1407（879 aa）
Chain G 529–1407（879 aa）
Chain H 529–1407（879 aa）
Chain I 529–1407（879 aa）
Chain J 529–1407（879 aa）
Chain K 529–1407（879 aa）
Chain L 529–1407（879 aa）
Chain M 529–1407（879 aa）
Chain N 529–1407（879 aa）
Chain O 529–1407（879 aa）
Chain P 529–1407（879 aa）
Chain Q 529–1407（879 aa）
Chain R 529–1407（879 aa）
Chain S 529–1407（879 aa）
Chain T 529–1407（879 aa）
Chain U 529–1407（879 aa）
Chain V 529–1407（879 aa）
Chain W 529–1407（879 aa）
Chain X 529–1407（879 aa）
Chain Y 529–1407（879 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 5 sec before plunging, blot force -1
Resolution 10.00 Å

12 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UN13A_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 9–887； UniProt 529–1407

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 7t7x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7t7x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7t7x
Deposition date deposition_date2021-12-15
Structure title titleMunc13-1 C1-C2B-MUN-C2C Upright conformation spanning two lipid bilayers
Keywords keywordsSynaptic Transmission, Munc13, Membrane Fusion, EXOCYTOSIS; EXOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier72.72 Å
Radius of gyration Rg (electron density) rg_electron73.91 Å
Forward intensity I(0) i0237662000.00
Molecular weight molecular_weight128600.0 kDa
Excluded volume excluded_volume160910 ų
Envelope volume envelope_volume265320 ų
Hydration-shell volume shell_volume35523 ų
Envelope diameter envelope_diameter249.9 Å
Shell Rg shell_rg51.25 Å
Envelope Rg envelope_rg72.68 Å
Shape Rg shape_rg73.89 Å
Total Rg total_rg73.39 Å
Total atoms total_atoms18010
Residues n_residues1132
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax216.4 Å
Rg (real space) rg_real73.44 Å
Rg uncertainty (real space) rg_real_error2.03 Å
I(0) (real space) i0_real2.3730e+08
I(0) uncertainty (real space) i0_real_error5.6480e+06
Rg (reciprocal space) rg_reciprocal68.78 Å
I(0) (reciprocal space) i0_reciprocal235400000.0000
Solution quality estimate total_estimate0.6321
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4 Å
Skewness Skewness skewness0.473
Kurtosis Kurtosis kurtosis-0.872
Angular range angular_range— – 0.1100 Å−1
Current regularization parameter α current_alpha0.0015
Highest regularization parameter α highest_alpha5443000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.273; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.230; Smooth: 0.185
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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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8. Citations (1)

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9. Files and Curves (10)