← Back to search
11tg

NMR solution structure of Manduca sexta pro-moricin-6

Method: SOLUTION NMR Dmax: 72.3 Å Quality: REASONABLE
▼

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

Pro-moricin-6

OrganismNot specified

UniProt A0A922CLZ4

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 24–65 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 0；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition：1.2 mM pro-moricin-6, methanol | methanol 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.

Other PDB Difference from Current Entry 11TG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
11TJ NMR solution structure of Manduca sexta moricin-6 Deposited 2026-03-12 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–65（38 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 0；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR sample composition 1.2 mM moricin-6, methanol | methanol
Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A922CLZ4_MANSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–42； UniProt 24–65

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 11tg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11tg
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id11tg
Deposition date deposition_date2026-03-12
最后修订 last_revision2026-04-22
Structure title titleNMR solution structure of Manduca sexta pro-moricin-6
Keywords keywordsantimicrobial peptide, AMP, insect immunity, proteolytic activation, S8 serine protease, DPP4, ANTIMICROBIAL PROTEIN; ANTIMICROBIAL PROTEIN
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier19.44 Å
Radius of gyration Rg (electron density) rg_electron19.67 Å
Forward intensity I(0) i028579700.00
Molecular weight molecular_weight44172.0 kDa
Excluded volume excluded_volume55792 ų
Envelope volume envelope_volume14861 ų
Hydration-shell volume shell_volume7682 ų
Envelope diameter envelope_diameter71.3 Å
Shell Rg shell_rg22.95 Å
Envelope Rg envelope_rg21.42 Å
Shape Rg shape_rg19.66 Å
Total Rg total_rg19.84 Å
Total atoms total_atoms6510
Residues n_residues420
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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 dmax72.3 Å
Rg (real space) rg_real20.15 Å
Rg uncertainty (real space) rg_real_error0.88 Å
I(0) (real space) i0_real2.8580e+07
I(0) uncertainty (real space) i0_real_error4.1660e+05
Rg (reciprocal space) rg_reciprocal20.05 Å
I(0) (reciprocal space) i0_reciprocal28580000.0000
Solution quality estimate total_estimate0.6163
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary7.1 Å
Skewness Skewness skewness0.540
Kurtosis Kurtosis kurtosis-0.769
Angular range angular_range— – 0.4100 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11450.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.004; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.996
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▶

8. Citations (1)

▶

9. Files and Curves (10)