6dbj

Cryo-EM structure of RAG in complex with 12-RSS and 23-RSS nicked DNA intermediates

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: GOOD

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

Recombination activating gene 1 - MBP chimera

Danio rerio

UniProt O13033

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 DNA 6 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 271–1031 Chain C; UniProt 271–1031 Not recorded Recombination activating gene 2 × 2 (Q1RLW7) Forward stand of RSS signal end × 2 Reverse stand of RSS × 2 Forward strand of coding flank × 2 ZN ZINC ION × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were made fresh from concentrated to avoid microbial contamination. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å R-free 0.384

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAG1_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 399–1159; UniProt 271–1031 Author chain C; PDBConstruct 399–1159; UniProt 271–1031

Recombination activating gene 1 - MBP chimera

Danio rerio

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 DNA 6 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 29–392 Chain C; UniProt 29–392 Not recorded Recombination activating gene 2 × 2 (Q1RLW7) Forward stand of RSS signal end × 2 Reverse stand of RSS × 2 Forward strand of coding flank × 2 ZN ZINC ION × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were made fresh from concentrated to avoid microbial contamination. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å R-free 0.384

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–378; UniProt 29–392 Author chain C; PDBConstruct 15–378; UniProt 29–392

Recombination activating gene 2

Danio rerio

UniProt Q1RLW7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 DNA 6 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 1–530 Chain D; UniProt 1–530 Not recorded Recombination activating gene 1 - MBP chimera × 2 (P0AEX9,O13033) Forward stand of RSS signal end × 2 Reverse stand of RSS × 2 Forward strand of coding flank × 2 ZN ZINC ION × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Solutions were made fresh from concentrated to avoid microbial contamination. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å R-free 0.384

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q1RLW7_DANRE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–533; UniProt 1–530 Author chain D; PDBConstruct 4–533; UniProt 1–530

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 6dbj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6dbj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6dbj
Deposition date deposition_date2018-05-03
Structure title titleCryo-EM structure of RAG in complex with 12-RSS and 23-RSS nicked DNA intermediates
Keywords keywordsSynaptic RAG complex, V(D)J recombination, RSS, Paired complex, RECOMBINATION-DNA complex; RECOMBINATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.70
Radius of gyration Rg (electron density) rg_electron40.43
Forward intensity I(0) i01101800000.00
Molecular weight molecular_weight243210.0 kDa
Excluded volume excluded_volume291570 ų
Envelope volume envelope_volume395430 ų
Hydration-shell volume shell_volume78227 ų
Envelope diameter envelope_diameter144.8
Shell Rg shell_rg48.51
Envelope Rg envelope_rg40.16
Shape Rg shape_rg40.44
Total Rg total_rg40.75
Total atoms total_atoms16896
Residues n_residues1932
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 dmax130.1
Rg (real space) rg_real40.53
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.1020e+09
I(0) uncertainty (real space) i0_real_error1.8780e+07
Rg (reciprocal space) rg_reciprocal40.70
I(0) (reciprocal space) i0_reciprocal1102000000.0000
Solution quality estimate total_estimate0.8871
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.4
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha130200000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)