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11tj

NMR solution structure of Manduca sexta moricin-6

Method: SOLUTION NMR Dmax: 65.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 28–65 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 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 11TJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
11TG NMR solution structure of Manduca sexta pro-moricin-6 Deposited 2026-03-12 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24–65（42 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 pro-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 1–38； UniProt 28–65

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 11tj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11tj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id11tj
Deposition date deposition_date2026-03-12
最后修订 last_revision2026-04-22
Structure title titleNMR solution structure of Manduca sexta moricin-6
Keywords keywords;antimicrobial peptide, AMP, insect immunity, proteolytic activation, S8 serine protease, DPP4, molecular dynamics simulation, ANTIMICROBIAL PROTEIN ;; ANTIMICROBIAL PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.46 Å
Radius of gyration Rg (electron density) rg_electron17.93 Å
Forward intensity I(0) i023722900.00
Molecular weight molecular_weight40238.0 kDa
Excluded volume excluded_volume50903 ų
Envelope volume envelope_volume11835 ų
Hydration-shell volume shell_volume6684 ų
Envelope diameter envelope_diameter66.5 Å
Shell Rg shell_rg21.02 Å
Envelope Rg envelope_rg19.91 Å
Shape Rg shape_rg17.87 Å
Total Rg total_rg18.28 Å
Total atoms total_atoms5980
Residues n_residues380
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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax65.7 Å
Rg (real space) rg_real18.14 Å
Rg uncertainty (real space) rg_real_error0.76 Å
I(0) (real space) i0_real2.3720e+07
I(0) uncertainty (real space) i0_real_error3.6270e+05
Rg (reciprocal space) rg_reciprocal18.06 Å
I(0) (reciprocal space) i0_reciprocal23720000.0000
Solution quality estimate total_estimate0.6164
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary7.0 Å
Skewness Skewness skewness0.609
Kurtosis Kurtosis kurtosis-0.622
Angular range angular_range— – 0.4550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8576.0000
Real-space data points n_real_points76
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: 0.997
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)