6xny

Structure of RAG1 (R848M/E649V)-RAG2-DNA Strand Transfer Complex (Paired-Form)

Method: ELECTRON MICROSCOPY Dmax: 127.1 Å Quality: GOOD

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

V(D)J recombination-activating protein 1

Mus musculus

UniProt P15919

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 Heteromer Protein × 4 DNA 6 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 261–1008 Chain C; UniProt 261–1008 Mutation:R848M, E649V V(D)J recombination-activating protein 2 × 2 (P21784) 12RSS integration strand (55-mer) × 1 23RSS integration strand (66-mer) × 1 Flanking DNA top strand (16-mer) × 2 23RSS signal DNA top strand (45-mer) × 1 12RSS signal DNA top strand (34-mer) × 1 MG MAGNESIUM ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;20 mM HEPES pH7.6, 0.5 mM TCEP, 5 mM MgCl2 and 150 mM KCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

30 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAG1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–750; UniProt 261–1008 Author chain C; PDBConstruct 3–750; UniProt 261–1008

V(D)J recombination-activating protein 2

Mus musculus

UniProt P21784

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 Heteromer Protein × 4 DNA 6 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 3–361 Chain D; UniProt 3–361 Not recorded V(D)J recombination-activating protein 1 × 2 (P15919) 12RSS integration strand (55-mer) × 1 23RSS integration strand (66-mer) × 1 Flanking DNA top strand (16-mer) × 2 23RSS signal DNA top strand (45-mer) × 1 12RSS signal DNA top strand (34-mer) × 1 MG MAGNESIUM ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;20 mM HEPES pH7.6, 0.5 mM TCEP, 5 mM MgCl2 and 150 mM KCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

33 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAG2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–363; UniProt 3–361 Author chain D; PDBConstruct 5–363; UniProt 3–361

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 6xny

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xny
Deposition date deposition_date2020-07-05
Structure title titleStructure of RAG1 (R848M/E649V)-RAG2-DNA Strand Transfer Complex (Paired-Form)
Keywords keywordsDNA Transposase, RECOMBINATION; RECOMBINATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.92
Radius of gyration Rg (electron density) rg_electron37.84
Forward intensity I(0) i01041790000.00
Molecular weight molecular_weight239780.0 kDa
Excluded volume excluded_volume288990 ų
Envelope volume envelope_volume341400 ų
Hydration-shell volume shell_volume71533 ų
Envelope diameter envelope_diameter143.8
Shell Rg shell_rg46.35
Envelope Rg envelope_rg38.03
Shape Rg shape_rg37.88
Total Rg total_rg38.13
Total atoms total_atoms16681
Residues n_residues1909
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 dmax127.1
Rg (real space) rg_real37.74
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real1.0420e+09
I(0) uncertainty (real space) i0_real_error1.7860e+07
Rg (reciprocal space) rg_reciprocal37.85
I(0) (reciprocal space) i0_reciprocal1042000000.0000
Solution quality estimate total_estimate0.8747
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.4
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.270
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha167500000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)