1hui

INSULIN MUTANT (B1, B10, B16, B27)GLU, DES-B30, NMR, 25 STRUCTURES

Method: SOLUTION NMR Dmax: 45.1 Å Quality: GOOD

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

INSULIN

Homo sapiens

UniProt P01308

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 90–110 Chain B; UniProt 26–53 Mutation:CHAIN B, F1E, H10E, Y16E, T27E, DEL(T30) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;307 K Resolution not provided

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.

369 other PDB entries and 583 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 90–110 Author chain B; PDBConstruct 2–29; UniProt 26–53

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 1hui

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1hui
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1hui
Deposition date deposition_date1996-03-29
Structure title titleINSULIN MUTANT (B1, B10, B16, B27)GLU, DES-B30, NMR, 25 STRUCTURES
Keywords keywordsHORMONE, HUMAN INSULIN MUTANT, MONOMER, NEUTRAL PH; HORMONE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.23
Radius of gyration Rg (electron density) rg_electron10.85
Forward intensity I(0) i0306272000.00
Molecular weight molecular_weight141010.0 kDa
Excluded volume excluded_volume173340 ų
Envelope volume envelope_volume21989 ų
Hydration-shell volume shell_volume12966 ų
Envelope diameter envelope_diameter49.9
Shell Rg shell_rg20.26
Envelope Rg envelope_rg14.79
Shape Rg shape_rg10.84
Total Rg total_rg11.14
Total atoms total_atoms18950
Residues n_residues1250
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 dmax45.1
Rg (real space) rg_real11.24
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real3.0630e+08
I(0) uncertainty (real space) i0_real_error3.7730e+06
Rg (reciprocal space) rg_reciprocal11.24
I(0) (reciprocal space) i0_reciprocal306300000.0000
Solution quality estimate total_estimate0.7792
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.7
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis0.063
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha91900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.486; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.672; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1hui.1
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like

8. Citations (1)

9. Files and Curves (10)