3jbk

Cryo-EM reconstruction of the metavinculin-actin interface

Method: ELECTRON MICROSCOPY Dmax: 124.2 Å Quality: GOOD

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

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68135

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 3–377 Chain B; UniProt 3–377 Not recorded Metavinculin × 1 (P18206) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 10 mM imidazole;pH 7;50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 10 mM imidazole cryo-EM vitrification conditions:3 microliters of 0.3 micromolar actin was applied to the grid and incubated for 60 seconds at 25 degrees C. 3 microliters of 10 micromolar MVt was then applied and incubated for 60 seconds. 3 microliters of solution was removed, then an additional 3 microliters of MVt applied. After 60 seconds, 3 microliters of solution was removed, then the grid was blotted for 2 seconds before plunging.;Cryogen ETHANE;3 microliters of 0.3 micromolar actin was applied to the grid and incubated for 60 seconds at 25 degrees C. 3 microliters of 10 micromolar MVt was then applied and incubated for 60 seconds. 3 microliters of solution was removed, then an additional 3 microliters of MVt applied. After 60 seconds, 3 microliters of solution was removed, then the grid was blotted for 2 seconds before plunging into liquid ethane (LEICA EM GP). Resolution 8.20 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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–375; UniProt 3–377 Author chain B; PDBConstruct 1–375; UniProt 3–377

Metavinculin

Homo sapiens

UniProt P18206

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 858–1129 Fragment:tail domain (UNP residues 858-1129) Actin, alpha skeletal muscle × 2 (P68135) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 10 mM imidazole;pH 7;50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 10 mM imidazole cryo-EM vitrification conditions:3 microliters of 0.3 micromolar actin was applied to the grid and incubated for 60 seconds at 25 degrees C. 3 microliters of 10 micromolar MVt was then applied and incubated for 60 seconds. 3 microliters of solution was removed, then an additional 3 microliters of MVt applied. After 60 seconds, 3 microliters of solution was removed, then the grid was blotted for 2 seconds before plunging.;Cryogen ETHANE;3 microliters of 0.3 micromolar actin was applied to the grid and incubated for 60 seconds at 25 degrees C. 3 microliters of 10 micromolar MVt was then applied and incubated for 60 seconds. 3 microliters of solution was removed, then an additional 3 microliters of MVt applied. After 60 seconds, 3 microliters of solution was removed, then the grid was blotted for 2 seconds before plunging into liquid ethane (LEICA EM GP). Resolution 8.20 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.

32 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VINC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 2–273; UniProt 858–1129

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 3jbk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3jbk
Deposition date deposition_date2015-09-03
Structure title titleCryo-EM reconstruction of the metavinculin-actin interface
Keywords keywordsactin, metavinculin, vinculin, cell migration, adhesion, mechanosensation, cytoskeleton, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.80
Radius of gyration Rg (electron density) rg_electron34.62
Forward intensity I(0) i0150351000.00
Molecular weight molecular_weight96821.0 kDa
Excluded volume excluded_volume120680 ų
Envelope volume envelope_volume160560 ų
Hydration-shell volume shell_volume39747 ų
Envelope diameter envelope_diameter133.2
Shell Rg shell_rg39.66
Envelope Rg envelope_rg34.85
Shape Rg shape_rg34.64
Total Rg total_rg34.94
Total atoms total_atoms6776
Residues n_residues865
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 dmax124.2
Rg (real space) rg_real34.96
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real1.5040e+08
I(0) uncertainty (real space) i0_real_error2.5390e+06
Rg (reciprocal space) rg_reciprocal34.86
I(0) (reciprocal space) i0_reciprocal150300000.0000
Solution quality estimate total_estimate0.8530
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.9
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27020000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.751; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.856; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)