9g2n

Trp-cage fortified Tc5b-Exenatide chimera ( Ex-4-Tc5bDR) at 288K

Method: SOLUTION NMR Dmax: 27.8 Å Quality: GOOD

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

Exendin-4

Heloderma suspectum

UniProt P26349

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 62–86 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.1;288 K;Ionic strength (raw mmCIF value) n.d.;Pressure 1 NMR sample composition:0.85 mM non-labeled polypeptide, 1 % non-labeled sodium azide, 1 % non-labeled DSS, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXE4_HELSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–25; UniProt 62–86

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 9g2n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9g2n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9g2n
Deposition date deposition_date2024-07-11
Structure title titleTrp-cage fortified Tc5b-Exenatide chimera ( Ex-4-Tc5bDR) at 288K
Keywords keywordsExenatide, GLP-1R ligand, Trp-Cage DE NOVO PROTEIN, DE NOVO PROTEIN; DE NOVO PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier8.09
Radius of gyration Rg (electron density) rg_electron7.87
Forward intensity I(0) i011954900.00
Molecular weight molecular_weight27681.0 kDa
Excluded volume excluded_volume34354 ų
Envelope volume envelope_volume4335 ų
Hydration-shell volume shell_volume4845 ų
Envelope diameter envelope_diameter28.3
Shell Rg shell_rg12.88
Envelope Rg envelope_rg8.80
Shape Rg shape_rg7.83
Total Rg total_rg8.31
Total atoms total_atoms3850
Residues n_residues250
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 dmax27.8
Rg (real space) rg_real8.16
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.1950e+07
I(0) uncertainty (real space) i0_real_error1.2700e+05
Rg (reciprocal space) rg_reciprocal8.16
I(0) (reciprocal space) i0_reciprocal11950000.0000
Solution quality estimate total_estimate0.8517
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.8
Skewness Skewness skewness0.429
Kurtosis Kurtosis kurtosis-0.448
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2847.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.687; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)