1c01

SOLUTION STRUCTURE OF MIAMP1, A PLANT ANTIMICROBIAL PROTEIN

Method: SOLUTION NMR Dmax: 35.0 Å Quality: EXCELLENT

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

ANTIMICROBIAL PEPTIDE 1

OrganismNot specified

UniProt P80915

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 27–102 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5;308 K;Ionic strength (raw mmCIF value) 1.5 mM;Pressure 11 NMR measurement conditions:pH 5;283 K;Ionic strength (raw mmCIF value) 1.5 mM;Pressure 11 NMR sample composition:1.5 MM ANTIMICROBIAL PROTEIN; 90% H2O, 10% D2O NMR sample composition:1.5 MM ANTIMICROBIAL PROTEIN U-15N; 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name AMP1_MACIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 27–102

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 1c01

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c01
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c01
Deposition date deposition_date1999-07-13
Structure title titleSOLUTION STRUCTURE OF MIAMP1, A PLANT ANTIMICROBIAL PROTEIN
Keywords keywordsGREEK KEY, BETA-BARREL, ANTIMICROBIAL PROTEIN; ANTIMICROBIAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.43
Radius of gyration Rg (electron density) rg_electron11.07
Forward intensity I(0) i0433430000.00
Molecular weight molecular_weight162860.0 kDa
Excluded volume excluded_volume197860 ų
Envelope volume envelope_volume14873 ų
Hydration-shell volume shell_volume10380 ų
Envelope diameter envelope_diameter37.1
Shell Rg shell_rg17.96
Envelope Rg envelope_rg12.42
Shape Rg shape_rg10.99
Total Rg total_rg11.44
Total atoms total_atoms21800
Residues n_residues1520
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 dmax35.0
Rg (real space) rg_real11.33
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real4.3340e+08
I(0) uncertainty (real space) i0_real_error4.4450e+06
Rg (reciprocal space) rg_reciprocal11.33
I(0) (reciprocal space) i0_reciprocal433400000.0000
Solution quality estimate total_estimate0.9098
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness-0.060
Kurtosis Kurtosis kurtosis-0.660
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58650.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1c01a_
Class classb — All beta proteins
Fold Fold foldb.11 — gamma-Crystallin-like
Superfamily Superfamily superfamilyb.11.1 — gamma-Crystallin-like
Family Family familyb.11.1.5 — Plant antimicrobial protein MIAMP1

CATH v4.4 (1 domains)

Domain ID domain_id1c01A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)