3nbh

Crystal structure of human RMI1C-RMI2 complex

Method: X-RAY DIFFRACTION Dmax: 70.2 Å Quality: REASONABLE

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

RecQ-mediated genome instability protein 1

Homo sapiens

UniProt Q9H9A7

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 475–625 Fragment:RMI1C, residues 475-625 Non-standard monomer:Yes (specific site not provided by mmCIF) RecQ-mediated genome instability protein 2 × 1 (Q96E14) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277.15 K;The precipitant/well solution contained 18% PEG 3350, 300 mM NaSCN, and 10 mM DTT. , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 2.00 Å R-free 0.258

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.

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

View Construct and Data Evidence
UniProt name RMI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–155; UniProt 475–625

RecQ-mediated genome instability protein 2

Homo sapiens

UniProt Q96E14

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 6–147 Fragment:RMI2, residues 6-147 Non-standard monomer:Yes (specific site not provided by mmCIF) RecQ-mediated genome instability protein 1 × 1 (Q9H9A7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277.15 K;The precipitant/well solution contained 18% PEG 3350, 300 mM NaSCN, and 10 mM DTT. , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 2.00 Å R-free 0.258

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RMI2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–147; UniProt 6–147

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 3nbh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3nbh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3nbh
Deposition date deposition_date2010-06-03
Structure title titleCrystal structure of human RMI1C-RMI2 complex
Keywords keywordstwo OB-folds containing complex, RPA-like complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.80
Radius of gyration Rg (electron density) rg_electron19.86
Forward intensity I(0) i018171400.00
Molecular weight molecular_weight31646.0 kDa
Excluded volume excluded_volume39272 ų
Envelope volume envelope_volume46333 ų
Hydration-shell volume shell_volume19933 ų
Envelope diameter envelope_diameter70.8
Shell Rg shell_rg25.97
Envelope Rg envelope_rg20.22
Shape Rg shape_rg19.89
Total Rg total_rg20.62
Total atoms total_atoms2173
Residues n_residues269
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 dmax70.2
Rg (real space) rg_real20.77
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.8170e+07
I(0) uncertainty (real space) i0_real_error2.5090e+05
Rg (reciprocal space) rg_reciprocal20.77
I(0) (reciprocal space) i0_reciprocal18170000.0000
Solution quality estimate total_estimate0.6887
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.232
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5276000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 0.990; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3nbhA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily510
Domain ID domain_id3nbhA02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily770
Domain ID domain_id3nbhB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)