2n1t

Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution

Method: SOLUTION NMR Dmax: 115.8 Å Quality: GOOD

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 25–93 Fragment:UNP residues 25-93 Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60880) Synaptosomal-associated protein 25 × 1 (P60880) Synaptotagmin-1 × 1 (P21579) SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Pressure ambient NMR sample composition:30 uM [U-100% 13C; U-100% 15N] protein, 25 mM Tris-HCl, 125 mM KSCN, 1 mM CaCl2, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–69; UniProt 25–93

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 188–259 Fragment:UNP residues 188-259 Vesicle-associated membrane protein 2 × 1 (P63045) Synaptosomal-associated protein 25 × 1 (P60880) Synaptosomal-associated protein 25 × 1 (P60880) Synaptotagmin-1 × 1 (P21579) SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Pressure ambient NMR sample composition:30 uM [U-100% 13C; U-100% 15N] protein, 25 mM Tris-HCl, 125 mM KSCN, 1 mM CaCl2, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–72; UniProt 188–259

Synaptosomal-associated protein 25

Homo sapiens

UniProt P60880

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 7–83 Chain D; UniProt 131–204 Fragment:N-terminal domain (UNP residues 7-83) Fragment:C-terminal domain (UNP residues 131-204) Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptotagmin-1 × 1 (P21579) SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Pressure ambient NMR sample composition:30 uM [U-100% 13C; U-100% 15N] protein, 25 mM Tris-HCl, 125 mM KSCN, 1 mM CaCl2, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

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

View Construct and Data Evidence
UniProt name SNP25_HUMAN
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 1–77; UniProt 7–83 Author chain D; PDBConstruct 1–74; UniProt 131–204

Synaptotagmin-1

Homo sapiens

UniProt P21579

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 272–419 Fragment:C2B domain (UNP residues 272-419) Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60880) Synaptosomal-associated protein 25 × 1 (P60880) SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Pressure ambient NMR sample composition:30 uM [U-100% 13C; U-100% 15N] protein, 25 mM Tris-HCl, 125 mM KSCN, 1 mM CaCl2, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

21 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYT1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 9–156; UniProt 272–419

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 2n1t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n1t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n1t
Deposition date deposition_date2015-04-21
Structure title titleDynamic binding mode of a synaptotagmin-1-SNARE complex in solution
Keywords keywordsSynaptotagmin-1, C2B domain, Syntaxin-1A, Synaptobrevin-2, SNAP-25, SNAP-25A, SNARE complex, EXOCYTOSIS; EXOCYTOSIS
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier31.08
Radius of gyration Rg (electron density) rg_electron30.98
Forward intensity I(0) i01025400000.00
Molecular weight molecular_weight256630.0 kDa
Excluded volume excluded_volume317500 ų
Envelope volume envelope_volume150280 ų
Hydration-shell volume shell_volume40681 ų
Envelope diameter envelope_diameter129.0
Shell Rg shell_rg37.44
Envelope Rg envelope_rg32.04
Shape Rg shape_rg30.97
Total Rg total_rg31.24
Total atoms total_atoms35980
Residues n_residues2240
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 dmax115.8
Rg (real space) rg_real31.33
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real1.0250e+09
I(0) uncertainty (real space) i0_real_error1.9070e+07
Rg (reciprocal space) rg_reciprocal31.22
I(0) (reciprocal space) i0_reciprocal1025000000.0000
Solution quality estimate total_estimate0.8113
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.533
Kurtosis Kurtosis kurtosis0.040
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7849000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.652; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.658; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2n1ta_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd2n1tb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd2n1tc_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd2n1td_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd2n1te1
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.1 — C2 domain (Calcium/lipid-binding domain, CaLB)
Family Family familyb.7.1.2 — Synaptotagmin-like (S variant)
Domain ID domain_idd2n1te2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (5 domains)

Domain ID domain_id2n1tA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id2n1tB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id2n1tC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id2n1tD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id2n1tE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain

8. Citations (1)

9. Files and Curves (10)