9xao

Spatial structure of the antimicrobial peptide Ap9

Method: SOLUTION NMR Dmax: 27.1 Å Quality: REASONABLE

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

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息,但缺少统一蛋白身份时,不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly Oligomeric State 实体与Construct证据 Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer 蛋白 1 / DNA 0 / RNA 0 / 其他Polymer 0 PDB declaration: monomeric Entity 1:antimicrobial peptide Ap9 × 1 缺少 UniProt 身份时不显示参考序列区间 Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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 9xao

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xao
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9xao
Deposition date deposition_date2025-10-22
最后修订 last_revision2026-06-10
Structure title titleSpatial structure of the antimicrobial peptide Ap9
Keywords keywordsantibiotic, antimicrobial peptides, protein; ANTIBIOTIC
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier9.94
Radius of gyration Rg (electron density) rg_electron9.91
Forward intensity I(0) i012179500.00
Molecular weight molecular_weight24709.0 kDa
Excluded volume excluded_volume29542 ų
Envelope volume envelope_volume5972 ų
Hydration-shell volume shell_volume5308 ų
Envelope diameter envelope_diameter40.0
Shell Rg shell_rg15.11
Envelope Rg envelope_rg11.55
Shape Rg shape_rg9.92
Total Rg total_rg10.21
Total atoms total_atoms3330
Residues n_residues210
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 dmax27.1
Rg (real space) rg_real9.50
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real1.1710e+07
I(0) uncertainty (real space) i0_real_error7.2890e+04
Rg (reciprocal space) rg_reciprocal10.14
I(0) (reciprocal space) i0_reciprocal12180000.0000
Solution quality estimate total_estimate0.6530
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary8.6
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.731
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha7.0280
Highest regularization parameter α highest_alpha4078.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.984; Stabil: 0.966; Sysdev: 0.000; Positv: 1.000; Valcen: 0.641; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)