6cim

Pre-Reaction Complex, RAG1(E962Q)/2-nicked/intact 12/23RSS complex in Mn2+

Method: X-RAY DIFFRACTION Dmax: 147.9 Å Quality: REASONABLE

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 × 5 DNA 5 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 384–1008 Chain C; UniProt 384–1008 Mutation:E962Q V(D)J recombination-activating protein 2 × 2 (P21784) High mobility group protein B1 × 1 (P09429) Nicked 12RSS intermediate reverse strand × 1 ;DNA (5'-D(*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-3') ; × 1 Nicked 12RSS intermediate forward strand × 1 Intact 23RSS substrate reverse strand × 1 Intact 23RSS substrate forward strand × 1 ZN ZINC ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;277 K;18% PEG3350, 200 mM KNO3, 50 mM HEPES pH 6.9 Resolution 3.60 Å R-free 0.254

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 1–625; UniProt 384–1008 Author chain C; PDBConstruct 1–625; UniProt 384–1008

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 × 5 DNA 5 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 1–359 Chain D; UniProt 1–359 Not recorded V(D)J recombination-activating protein 1 × 2 (P15919) High mobility group protein B1 × 1 (P09429) Nicked 12RSS intermediate reverse strand × 1 ;DNA (5'-D(*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-3') ; × 1 Nicked 12RSS intermediate forward strand × 1 Intact 23RSS substrate reverse strand × 1 Intact 23RSS substrate forward strand × 1 ZN ZINC ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;277 K;18% PEG3350, 200 mM KNO3, 50 mM HEPES pH 6.9 Resolution 3.60 Å R-free 0.254

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 1–359; UniProt 1–359 Author chain D; PDBConstruct 1–359; UniProt 1–359

High mobility group protein B1

Homo sapiens

UniProt P09429

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 × 5 DNA 5 PDB declaration: decameric(10) Consistent with all polymer counts Chain N; UniProt 1–163 Not recorded V(D)J recombination-activating protein 1 × 2 (P15919) V(D)J recombination-activating protein 2 × 2 (P21784) Nicked 12RSS intermediate reverse strand × 1 ;DNA (5'-D(*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-3') ; × 1 Nicked 12RSS intermediate forward strand × 1 Intact 23RSS substrate reverse strand × 1 Intact 23RSS substrate forward strand × 1 ZN ZINC ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;277 K;18% PEG3350, 200 mM KNO3, 50 mM HEPES pH 6.9 Resolution 3.60 Å R-free 0.254

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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HMGB1_HUMAN
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 6cim

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6cim
Deposition date deposition_date2018-02-24
Structure title titlePre-Reaction Complex, RAG1(E962Q)/2-nicked/intact 12/23RSS complex in Mn2+
Keywords keywordsVDJ recombination, RSS, RAG1/2, RECOMBINATION, RECOMBINATION-DNA complex; RECOMBINATION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.28
Radius of gyration Rg (electron density) rg_electron45.60
Forward intensity I(0) i01394350000.00
Molecular weight molecular_weight270520.0 kDa
Excluded volume excluded_volume321820 ų
Envelope volume envelope_volume481810 ų
Hydration-shell volume shell_volume85842 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg51.88
Envelope Rg envelope_rg45.26
Shape Rg shape_rg45.62
Total Rg total_rg45.76
Total atoms total_atoms18784
Residues n_residues2156
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 dmax147.9
Rg (real space) rg_real46.07
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.3940e+09
I(0) uncertainty (real space) i0_real_error2.4230e+07
Rg (reciprocal space) rg_reciprocal46.28
I(0) (reciprocal space) i0_reciprocal1395000000.0000
Solution quality estimate total_estimate0.6865
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.6
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.446
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha99520000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.974; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)