8rdu

Conformational Landscape of the Type V-K CRISPR-associated TransposonIntegration Assembly CAST V-K composite map

Method: ELECTRON MICROSCOPY Dmax: 236.1 Å Quality: EXCELLENT

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

ShCas12k

Scytonema hofmannii

UniProt A0A8X6EH11

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 × 25 DNA 6 RNA 1 PDB declaration: 32-meric(32) Consistent with all polymer counts Chain A; UniProt 4–641 Not recorded sgRNA × 1 Non-target strand - LE × 1 Target strand -LE × 1 LE × 1 RE × 1 Non-target strand - RE × 1 Target strand × 1 Small ribosomal subunit protein uS15 × 1 (A0A139X9A4) TniQ × 1 (A0A8J0PCL5) ShTnsC × 14 (A0A8J0PCL3) TnsB × 8 (A0A979HMQ2) MG MAGNESIUM ION × 17 ZN ZINC ION × 2 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.

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

View Construct and Data Evidence
UniProt name A0A8X6EH11_9CYAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain A; PDBConstruct 61–698; UniProt 4–641

Small ribosomal subunit protein uS15

Scytonema hofmannii

UniProt A0A139X9A4

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 × 25 DNA 6 RNA 1 PDB declaration: 32-meric(32) Consistent with all polymer counts Chain B; UniProt 1–89 Not recorded sgRNA × 1 Non-target strand - LE × 1 Target strand -LE × 1 LE × 1 RE × 1 Non-target strand - RE × 1 Target strand × 1 ShCas12k × 1 (A0A8X6EH11) TniQ × 1 (A0A8J0PCL5) ShTnsC × 14 (A0A8J0PCL3) TnsB × 8 (A0A979HMQ2) MG MAGNESIUM ION × 17 ZN ZINC ION × 2 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A139X9A4_9CYAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain B; PDBConstruct 2–90; UniProt 1–89

TniQ

Scytonema hofmannii

UniProt A0A8J0PCL5

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 × 25 DNA 6 RNA 1 PDB declaration: 32-meric(32) Consistent with all polymer counts Chain C; UniProt 1–167 Not recorded sgRNA × 1 Non-target strand - LE × 1 Target strand -LE × 1 LE × 1 RE × 1 Non-target strand - RE × 1 Target strand × 1 ShCas12k × 1 (A0A8X6EH11) Small ribosomal subunit protein uS15 × 1 (A0A139X9A4) ShTnsC × 14 (A0A8J0PCL3) TnsB × 8 (A0A979HMQ2) MG MAGNESIUM ION × 17 ZN ZINC ION × 2 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.

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

View Construct and Data Evidence
UniProt name A0A8J0PCL5_9CYAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain C; PDBConstruct 1–167; UniProt 1–167

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 Other combination Heteromer Protein × 25 DNA 6 RNA 1 PDB declaration: 32-meric(32) 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 sgRNA × 1 Non-target strand - LE × 1 Target strand -LE × 1 LE × 1 RE × 1 Non-target strand - RE × 1 Target strand × 1 ShCas12k × 1 (A0A8X6EH11) Small ribosomal subunit protein uS15 × 1 (A0A139X9A4) TniQ × 1 (A0A8J0PCL5) TnsB × 8 (A0A979HMQ2) MG MAGNESIUM ION × 17 ZN ZINC ION × 2 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 11
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

TnsB

Scytonema hofmannii

UniProt A0A979HMQ2

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 × 25 DNA 6 RNA 1 PDB declaration: 32-meric(32) Consistent with all polymer counts Chain R; UniProt 2–584 Chain S; UniProt 2–584 Chain T; UniProt 2–584 Chain U; UniProt 2–584 Chain r; UniProt 2–584 Chain s; UniProt 2–584 Chain t; UniProt 2–584 Chain u; UniProt 2–584 Not recorded sgRNA × 1 Non-target strand - LE × 1 Target strand -LE × 1 LE × 1 RE × 1 Non-target strand - RE × 1 Target strand × 1 ShCas12k × 1 (A0A8X6EH11) Small ribosomal subunit protein uS15 × 1 (A0A139X9A4) TniQ × 1 (A0A8J0PCL5) ShTnsC × 14 (A0A8J0PCL3) MG MAGNESIUM ION × 17 ZN ZINC ION × 2 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A979HMQ2_9CYAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain R; PDBConstruct 2–584; UniProt 2–584 Author chain S; PDBConstruct 2–584; UniProt 2–584 Author chain T; PDBConstruct 2–584; UniProt 2–584 Author chain U; PDBConstruct 2–584; UniProt 2–584 Author chain r; PDBConstruct 2–584; UniProt 2–584 Author chain s; PDBConstruct 2–584; UniProt 2–584 Author chain t; PDBConstruct 2–584; UniProt 2–584 Author chain u; PDBConstruct 2–584; UniProt 2–584

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 8rdu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rdu
Deposition date deposition_date2023-12-08
Structure title titleConformational Landscape of the Type V-K CRISPR-associated TransposonIntegration Assembly CAST V-K composite 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_guinier81.44
Radius of gyration Rg (electron density) rg_electron80.47
Forward intensity I(0) i013836600000.00
Molecular weight molecular_weight872440.0 kDa
Excluded volume excluded_volume1041900 ų
Envelope volume envelope_volume1688900 ų
Hydration-shell volume shell_volume185860 ų
Envelope diameter envelope_diameter315.9
Shell Rg shell_rg71.28
Envelope Rg envelope_rg80.62
Shape Rg shape_rg80.42
Total Rg total_rg80.49
Total atoms total_atoms60568
Residues n_residues6629
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 dmax236.1
Rg (real space) rg_real76.80
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real1.3320e+10
I(0) uncertainty (real space) i0_real_error2.7230e+08
Rg (reciprocal space) rg_reciprocal77.82
I(0) (reciprocal space) i0_reciprocal13700000000.0000
Solution quality estimate total_estimate0.9023
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.5
Skewness Skewness skewness0.523
Kurtosis Kurtosis kurtosis-0.344
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.5192
Highest regularization parameter α highest_alpha1402000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 0.982; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.079

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)