7ra9

Designed StabIL-2 seq1

Method: X-RAY DIFFRACTION Dmax: 52.1 Å Quality: REASONABLE

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

Interleukin-2

Homo sapiens

UniProt P60568

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 21–153 Mutation:G27M, I28L, K32D, M39L, E52S, V69A, L72A, Q74G, S75D, K76D, N77P, F78K, H79T, L80I, delta81-82, L85V, I86V, I92F, V115I PO4 PHOSPHATE ION × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10.5;295 K;0.2 M Li2SO4, 0.1 M CAPS pH 10.5, 1.2 M NaH2PO4, and 0.8 M K2HPO4 Resolution 2.20 Å R-free 0.293

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 77 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–132; UniProt 21–153

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 7ra9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ra9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ra9
Deposition date deposition_date2021-06-30
Structure title titleDesigned StabIL-2 seq1
Keywords keywordssynthetic protein, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.06
Radius of gyration Rg (electron density) rg_electron14.66
Forward intensity I(0) i04459700.00
Molecular weight molecular_weight15046.0 kDa
Excluded volume excluded_volume18863 ų
Envelope volume envelope_volume21624 ų
Hydration-shell volume shell_volume12655 ų
Envelope diameter envelope_diameter52.4
Shell Rg shell_rg20.33
Envelope Rg envelope_rg15.09
Shape Rg shape_rg14.61
Total Rg total_rg15.93
Total atoms total_atoms1048
Residues n_residues126
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 dmax52.1
Rg (real space) rg_real16.33
Rg uncertainty (real space) rg_real_error0.11
I(0) (real space) i0_real4.4000e+06
I(0) uncertainty (real space) i0_real_error4.4280e+04
Rg (reciprocal space) rg_reciprocal15.99
I(0) (reciprocal space) i0_reciprocal4460000.0000
Solution quality estimate total_estimate0.6760
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.130
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha8.7910
Highest regularization parameter α highest_alpha609500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 0.925; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.397

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)