5d53

In meso in situ serial X-ray crystallography structure of insulin at 100 K

Method: X-RAY DIFFRACTION Dmax: 37.9 Å Quality: GOOD

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

Insulin B chain

OrganismNot specified

UniProt P01315

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 88–108 Chain B; UniProt 25–54 Not recorded PO4 PHOSPHATE ION × 2 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;0.1-0.2 M sodium phosphate, pH 5.5-6.1, and 33-38 %(w/v) PEG400 Resolution 1.50 Å R-free 0.170

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.

41 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_PIG
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 88–108 Author chain B; PDBConstruct 1–30; UniProt 25–54

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 5d53

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d53
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5d53
Deposition date deposition_date2015-08-10
Structure title titleIn meso in situ serial X-ray crystallography structure of insulin at 100 K
Keywords keywordsHORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier11.58
Radius of gyration Rg (electron density) rg_electron10.11
Forward intensity I(0) i0970414.00
Molecular weight molecular_weight6132.0 kDa
Excluded volume excluded_volume7498 ų
Envelope volume envelope_volume8189 ų
Hydration-shell volume shell_volume7168 ų
Envelope diameter envelope_diameter35.2
Shell Rg shell_rg15.32
Envelope Rg envelope_rg10.58
Shape Rg shape_rg10.09
Total Rg total_rg11.58
Total atoms total_atoms819
Residues n_residues51
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 dmax37.9
Rg (real space) rg_real11.52
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real9.7040e+05
I(0) uncertainty (real space) i0_real_error1.0290e+04
Rg (reciprocal space) rg_reciprocal11.52
I(0) (reciprocal space) i0_reciprocal970400.0000
Solution quality estimate total_estimate0.8874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.4
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.321
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)