8rku

Conformational Landscape of the Type V-K CRISPR-associated TransposonIntegration Assembly CAST V-K TnsC domain local-refinement map

Method: ELECTRON MICROSCOPY Dmax: 150.7 Å Quality: GOOD

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

ShTnsC

Scytonema hofmannii

UniProt A0A8J0PCL3

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–DNA Homooligomer Protein × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain D; UniProt 2–276 Chain E; UniProt 2–276 Chain F; UniProt 2–276 Chain G; UniProt 2–276 Chain H; UniProt 2–276 Chain I; UniProt 2–276 Chain J; UniProt 2–276 Chain K; UniProt 2–276 Chain L; UniProt 2–276 Chain M; UniProt 2–276 Chain N; UniProt 2–276 Chain O; UniProt 2–276 Chain P; UniProt 2–276 Chain Q; UniProt 2–276 Not recorded Non-target strand - LE × 1 Target strand - LE × 1 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.30 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0PCL3_9CYAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 2–276; UniProt 2–276 Author chain E; PDBConstruct 2–276; UniProt 2–276 Author chain F; PDBConstruct 2–276; UniProt 2–276 Author chain G; PDBConstruct 2–276; UniProt 2–276 Author chain H; PDBConstruct 2–276; UniProt 2–276 Author chain I; PDBConstruct 2–276; UniProt 2–276 Author chain J; PDBConstruct 2–276; UniProt 2–276 Author chain K; PDBConstruct 2–276; UniProt 2–276 Author chain L; PDBConstruct 2–276; UniProt 2–276 Author chain M; PDBConstruct 2–276; UniProt 2–276 Author chain N; PDBConstruct 2–276; UniProt 2–276 Author chain O; PDBConstruct 2–276; UniProt 2–276 Author chain P; PDBConstruct 2–276; UniProt 2–276 Author chain Q; PDBConstruct 2–276; UniProt 2–276

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 8rku

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rku
Deposition date deposition_date2023-12-30
Structure title titleConformational Landscape of the Type V-K CRISPR-associated TransposonIntegration Assembly CAST V-K TnsC domain local-refinement map
Keywords keywordsCRISPR-associated Transposon genome editing transposition, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.22
Radius of gyration Rg (electron density) rg_electron48.09
Forward intensity I(0) i02778010000.00
Molecular weight molecular_weight431380.0 kDa
Excluded volume excluded_volume537660 ų
Envelope volume envelope_volume730490 ų
Hydration-shell volume shell_volume118580 ų
Envelope diameter envelope_diameter162.6
Shell Rg shell_rg57.81
Envelope Rg envelope_rg47.52
Shape Rg shape_rg48.09
Total Rg total_rg48.39
Total atoms total_atoms30188
Residues n_residues3638
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 dmax150.7
Rg (real space) rg_real47.82
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real2.7780e+09
I(0) uncertainty (real space) i0_real_error4.4410e+07
Rg (reciprocal space) rg_reciprocal48.21
I(0) (reciprocal space) i0_reciprocal2779000000.0000
Solution quality estimate total_estimate0.8860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.9
Skewness Skewness skewness0.099
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0006
Highest regularization parameter α highest_alpha360100000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)