5zdz

Hairpin Forming Complex, RAG1/2-Nicked 12RSS/23RSS complex in Ca2+

Method: X-RAY DIFFRACTION Dmax: 158.7 Å Quality: GOOD

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

mouse RAG1

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 × 3 DNA 3 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 384–1008 Fragment:UNP residues 384-1008 mouse RAG2 × 1 (P21784) HMGB1 A-B box × 1 (P63158) DNA (30-MER) × 1 DNA (39-MER) × 1 DNA chain M × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100mM MES (pH 6.8), 15% PEG 3350, 200mM Potassium formate Resolution 2.80 Å R-free 0.242
2 Protein–DNA Heteromer Protein × 2 DNA 3 PDB declaration: pentameric(5) Consistent with all polymer counts Chain C; UniProt 384–1008 Fragment:UNP residues 384-1008 mouse RAG2 × 1 (P21784) ;DNA (5'-D(*TP*AP*TP*CP*TP*GP*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-3') ; × 1 DNA (54-MER) × 1 DNA chain L × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100mM MES (pH 6.8), 15% PEG 3350, 200mM Potassium formate Resolution 2.80 Å R-free 0.242

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 34 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 3–627; UniProt 384–1008 Author chain C; PDBConstruct 3–627; UniProt 384–1008

mouse RAG2

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 × 3 DNA 3 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–387 Fragment:UNP residues 1-387 Mutation:M1V mouse RAG1 × 1 (P15919) HMGB1 A-B box × 1 (P63158) DNA (30-MER) × 1 DNA (39-MER) × 1 DNA chain M × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100mM MES (pH 6.8), 15% PEG 3350, 200mM Potassium formate Resolution 2.80 Å R-free 0.242
2 Protein–DNA Heteromer Protein × 2 DNA 3 PDB declaration: pentameric(5) Consistent with all polymer counts Chain D; UniProt 1–387 Fragment:UNP residues 1-387 Mutation:M1V mouse RAG1 × 1 (P15919) ;DNA (5'-D(*TP*AP*TP*CP*TP*GP*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-3') ; × 1 DNA (54-MER) × 1 DNA chain L × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100mM MES (pH 6.8), 15% PEG 3350, 200mM Potassium formate Resolution 2.80 Å R-free 0.242

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 42 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 3–389; UniProt 1–387 Author chain D; PDBConstruct 3–389; UniProt 1–387

HMGB1 A-B box

Mus musculus

UniProt P63158

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 × 3 DNA 3 PDB declaration: hexameric(6) Consistent with all polymer counts Chain N; UniProt 1–163 Fragment:UNP residues 1-163 mouse RAG1 × 1 (P15919) mouse RAG2 × 1 (P21784) DNA (30-MER) × 1 DNA (39-MER) × 1 DNA chain M × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100mM MES (pH 6.8), 15% PEG 3350, 200mM Potassium formate Resolution 2.80 Å R-free 0.242

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 HMGB1_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–163; UniProt 1–163

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 5zdz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5zdz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5zdz
Deposition date deposition_date2018-02-25
Structure title titleHairpin Forming Complex, RAG1/2-Nicked 12RSS/23RSS complex in Ca2+
Keywords keywordsV(D)J recombination, RAG1-2-12RSS-23RSS complex, Hairpin forming complex, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier47.35
Radius of gyration Rg (electron density) rg_electron46.53
Forward intensity I(0) i01626160000.00
Molecular weight molecular_weight291620.0 kDa
Excluded volume excluded_volume346590 ų
Envelope volume envelope_volume499290 ų
Hydration-shell volume shell_volume87780 ų
Envelope diameter envelope_diameter165.9
Shell Rg shell_rg51.90
Envelope Rg envelope_rg46.82
Shape Rg shape_rg46.52
Total Rg total_rg46.74
Total atoms total_atoms20222
Residues n_residues2239
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 dmax158.7
Rg (real space) rg_real47.31
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real1.6260e+09
I(0) uncertainty (real space) i0_real_error3.1060e+07
Rg (reciprocal space) rg_reciprocal47.35
I(0) (reciprocal space) i0_reciprocal1626000000.0000
Solution quality estimate total_estimate0.8736
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.7
Skewness Skewness skewness0.337
Kurtosis Kurtosis kurtosis-0.324
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha96640000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)