3nbi

Crystal structure of human RMI1 N-terminus

Method: X-RAY DIFFRACTION Dmax: 58.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–213 Fragment:RMI1N, residues 2-213 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277.15 K;The precipitant/well solution contained 100 mM Tris-HCl pH 8.5, 18% PEG 3350, 300 mM NaSCN, 10 mM NiCl2 and 10 mM DTT., VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 2.00 Å R-free 0.255

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 5–216; UniProt 2–213

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 3nbi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3nbi
Deposition date deposition_date2010-06-03
Structure title titleCrystal structure of human RMI1 N-terminus
Keywords keywordsOB-fold, RPA-like, 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_guinier21.57
Radius of gyration Rg (electron density) rg_electron20.99
Forward intensity I(0) i08443680.00
Molecular weight molecular_weight22059.0 kDa
Excluded volume excluded_volume27846 ų
Envelope volume envelope_volume34383 ų
Hydration-shell volume shell_volume15533 ų
Envelope diameter envelope_diameter94.6
Shell Rg shell_rg25.05
Envelope Rg envelope_rg22.57
Shape Rg shape_rg20.97
Total Rg total_rg21.68
Total atoms total_atoms1539
Residues n_residues188
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 dmax58.2
Rg (real space) rg_real19.86
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real8.0220e+06
I(0) uncertainty (real space) i0_real_error8.6070e+04
Rg (reciprocal space) rg_reciprocal21.93
I(0) (reciprocal space) i0_reciprocal8443000.0000
Solution quality estimate total_estimate0.6856
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha2.1050
Highest regularization parameter α highest_alpha1042000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.983; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3nbiA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily1020 — RecQ-mediated genome instability protein 1, N-terminal domain
Domain ID domain_id3nbiA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily770 — RecQ-mediated genome instability protein Rmi1, C-terminal domain

8. Citations (1)

9. Files and Curves (10)