8bd6

Cas12k-sgRNA-dsDNA-TnsC non-productive complex.

Method: ELECTRON MICROSCOPY Dmax: 187.0 Å Quality: GOOD

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

Cas12k

Scytonema hofmannii

UniProt A0A8M0FGU0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 10 DNA 4 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain A; UniProt 2–639 Not recorded sgRNA × 1 DNA target strand × 1 DNA non-target strand × 1 TnsC × 9 (A0A8J0PCL3) DNA × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 MG MAGNESIUM ION × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8M0FGU0_9CYAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 61–698; UniProt 2–639

TnsC

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 Other combination Heteromer Protein × 10 DNA 4 RNA 1 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain R; UniProt 1–276 Chain S; UniProt 1–276 Chain T; UniProt 1–276 Chain U; UniProt 1–276 Chain V; UniProt 1–276 Chain W; UniProt 1–276 Chain X; UniProt 1–276 Chain Y; UniProt 1–276 Chain Z; UniProt 1–276 Not recorded Cas12k × 1 (A0A8M0FGU0) sgRNA × 1 DNA target strand × 1 DNA non-target strand × 1 DNA × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 MG MAGNESIUM ION × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 5
Chains and sequence ranges Author chain R; PDBConstruct 1–276; UniProt 1–276 Author chain S; PDBConstruct 1–276; UniProt 1–276 Author chain T; PDBConstruct 1–276; UniProt 1–276 Author chain U; PDBConstruct 1–276; UniProt 1–276 Author chain V; PDBConstruct 1–276; UniProt 1–276 Author chain W; PDBConstruct 1–276; UniProt 1–276 Author chain X; PDBConstruct 1–276; UniProt 1–276 Author chain Y; PDBConstruct 1–276; UniProt 1–276 Author chain Z; PDBConstruct 1–276; UniProt 1–276

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 8bd6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bd6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bd6
Deposition date deposition_date2022-10-18
Structure title titleCas12k-sgRNA-dsDNA-TnsC non-productive complex.
Keywords keywordsCas12k, sgRNA, TnsC, CRISPR-Cas, Tn7-like transposons, transposition, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.17
Radius of gyration Rg (electron density) rg_electron54.30
Forward intensity I(0) i03684510000.00
Molecular weight molecular_weight432650.0 kDa
Excluded volume excluded_volume510340 ų
Envelope volume envelope_volume801510 ų
Hydration-shell volume shell_volume120120 ų
Envelope diameter envelope_diameter190.1
Shell Rg shell_rg60.53
Envelope Rg envelope_rg52.56
Shape Rg shape_rg54.27
Total Rg total_rg54.53
Total atoms total_atoms29951
Residues n_residues3213
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 dmax187.0
Rg (real space) rg_real55.09
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real3.6850e+09
I(0) uncertainty (real space) i0_real_error7.0140e+07
Rg (reciprocal space) rg_reciprocal55.22
I(0) (reciprocal space) i0_reciprocal3685000000.0000
Solution quality estimate total_estimate0.8764
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.5
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha336500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.846

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)