4nin

DSVISLS segment 101-107 from Human Superoxide Dismutase

Method: X-RAY DIFFRACTION Dmax: 25.0 Å Quality: REASONABLE

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

DSVISLS segment from Superoxide dismutase [Cu-Zn]

OrganismNot specified

UniProt P00441

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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 102–108 Fragment:UNP residues 102-108 ZN ZINC ION × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.1 M MES pH 6.0, 20% PEG 6000, and 5 mM ZnCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.40 Å R-free 0.228

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.

153 other PDB entries and 375 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SODC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–7; UniProt 102–108

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 4nin

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4nin
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4nin
Deposition date deposition_date2013-11-06
Structure title titleDSVISLS segment 101-107 from Human Superoxide Dismutase
Keywords keywordssteric zipper, cross-beta spine, amyloid fiber, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier9.16
Radius of gyration Rg (electron density) rg_electron7.82
Forward intensity I(0) i034424.10
Molecular weight molecular_weight784.2 kDa
Excluded volume excluded_volume932 ų
Envelope volume envelope_volume1186 ų
Hydration-shell volume shell_volume1981 ų
Envelope diameter envelope_diameter27.0
Shell Rg shell_rg10.36
Envelope Rg envelope_rg7.92
Shape Rg shape_rg7.39
Total Rg total_rg9.61
Total atoms total_atoms51
Residues n_residues7
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 dmax25.0
Rg (real space) rg_real8.73
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real3.3110e+04
I(0) uncertainty (real space) i0_real_error2.3410e+02
Rg (reciprocal space) rg_reciprocal9.34
I(0) (reciprocal space) i0_reciprocal34420.0000
Solution quality estimate total_estimate0.6243
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary6.6
Skewness Skewness skewness0.321
Kurtosis Kurtosis kurtosis-0.867
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha6.0280
Highest regularization parameter α highest_alpha1344.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 0.962; Sysdev: 0.000; Positv: 1.000; Valcen: 0.372; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)