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8zbm

RAT skeletal muscle ATM complex

Method: ELECTRON MICROSCOPY Dmax: 273.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68136

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 × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain E； UniProt 7–377 Chain H； UniProt 7–377 Chain O； UniProt 7–377 Chain P； UniProt 7–377 Chain Q； UniProt 7–377 Chain R； UniProt 7–377 Not recorded Tropomyosin beta chain × 4 （P58775） Myosin heavy chain 4 × 6 （F1LRV9） ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.32 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 8ZBM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3U9D Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP Deposited 2011-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 3–377（375 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop；pH 6.5；298 K；18% PEG3350, 0.05M NaAcetate pH4.7, 0.1M MgAcetate pH6.5, 0.32M Guanidine HCl, 0.8% Dioxane, hanging drop, temperature 298K
Resolution 2.50 Å R-free 0.240
3U9D Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP Deposited 2011-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 3–377（375 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop；pH 6.5；298 K；18% PEG3350, 0.05M NaAcetate pH4.7, 0.1M MgAcetate pH6.5, 0.32M Guanidine HCl, 0.8% Dioxane, hanging drop, temperature 298K
Resolution 2.50 Å R-free 0.240
8ZIX RAT skeletal muscle F-actin Deposited 2024-05-14 Different oligomeric state Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 7–377（371 aa）
Chain B 7–377（371 aa）
Chain E 7–377（371 aa）
Chain F 7–377（371 aa）
Chain P 7–377（371 aa）
Chain R 7–377（371 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.54 Å

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain E； PDBConstruct 1–371； UniProt 7–377 Author chain H； PDBConstruct 1–371； UniProt 7–377 Author chain O； PDBConstruct 1–371； UniProt 7–377 Author chain P； PDBConstruct 1–371； UniProt 7–377 Author chain Q； PDBConstruct 1–371； UniProt 7–377 Author chain R； PDBConstruct 1–371； UniProt 7–377

Tropomyosin beta chain

OrganismNot specified

UniProt P58775

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 × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain B； UniProt 45–210 Chain C； UniProt 45–210 Chain F； UniProt 45–210 Chain G； UniProt 45–210 Not recorded Actin, alpha skeletal muscle × 6 （P68136） Myosin heavy chain 4 × 6 （F1LRV9） ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.32 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name TPM2_RAT
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–166； UniProt 45–210 Author chain C； PDBConstruct 1–166； UniProt 45–210 Author chain F； PDBConstruct 1–166； UniProt 45–210 Author chain G； PDBConstruct 1–166； UniProt 45–210

Myosin heavy chain 4

OrganismNot specified

UniProt F1LRV9

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 × 16 PDB declaration: 16-meric（16） Consistent with protein copy count Chain A； UniProt 8–787 Chain D； UniProt 8–787 Chain J； UniProt 8–787 Chain K； UniProt 8–787 Chain L； UniProt 8–787 Chain N； UniProt 8–787 Not recorded Actin, alpha skeletal muscle × 6 （P68136） Tropomyosin beta chain × 4 （P58775） ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.32 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name F1LRV9_RAT
Isoform —
PDB entities 3
Chains and sequence ranges Author chain A； PDBConstruct 1–780； UniProt 8–787 Author chain D； PDBConstruct 1–780； UniProt 8–787 Author chain J； PDBConstruct 1–780； UniProt 8–787 Author chain K； PDBConstruct 1–780； UniProt 8–787 Author chain L； PDBConstruct 1–780； UniProt 8–787 Author chain N； PDBConstruct 1–780； UniProt 8–787

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 8zbm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zbm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zbm
Deposition date deposition_date2024-04-26
最后修订 last_revision2025-01-29
Structure title titleRAT skeletal muscle ATM complex
Keywords keywordsProtein fibril, Protein complex; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier77.50 Å
Radius of gyration Rg (electron density) rg_electron77.71 Å
Forward intensity I(0) i09418190000.00
Molecular weight molecular_weight829340.0 kDa
Excluded volume excluded_volume1039800 ų
Envelope volume envelope_volume1661300 ų
Hydration-shell volume shell_volume177960 ų
Envelope diameter envelope_diameter298.2 Å
Shell Rg shell_rg75.03 Å
Envelope Rg envelope_rg75.83 Å
Shape Rg shape_rg77.74 Å
Total Rg total_rg77.60 Å
Total atoms total_atoms58286
Residues n_residues7306
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 dmax273.1 Å
Rg (real space) rg_real81.03 Å
Rg uncertainty (real space) rg_real_error1.57 Å
I(0) (real space) i0_real9.4420e+09
I(0) uncertainty (real space) i0_real_error1.7920e+08
Rg (reciprocal space) rg_reciprocal77.46 Å
I(0) (reciprocal space) i0_reciprocal9417000000.0000
Solution quality estimate total_estimate0.8995
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.9 Å
Skewness Skewness skewness0.457
Kurtosis Kurtosis kurtosis-0.104
Angular range angular_range— – 0.1000 Å−1
Current regularization parameter α current_alpha1.1230
Highest regularization parameter α highest_alpha518400000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 0.865; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.529
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)