1afp

SOLUTION STRUCTURE OF THE ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS. EVIDENCE FOR DISULPHIDE CONFIGURATIONAL ISOMERISM

Method: SOLUTION NMR D_max: 32.6 Å Quality: REASONABLE

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

ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS

Aspergillus giganteus

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 44–94	Not recorded	No other associated polymer	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	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	AFP_ASPGI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–51； UniProt 44–94

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1afp
Deposition date deposition_date	1994-11-11
Structure title title	SOLUTION STRUCTURE OF THE ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS. EVIDENCE FOR DISULPHIDE CONFIGURATIONAL ISOMERISM
Keywords keywords	ANTIFUNGAL PROTEIN; ANTIFUNGAL PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	9.59 Å
Radius of gyration Rg (electron density) rg_electron	10.25 Å
Forward intensity I(0) i0	786310000.00
Molecular weight molecular_weight	231920.0 kDa
Excluded volume excluded_volume	287810 Å³
Envelope volume envelope_volume	13447 Å³
Hydration-shell volume shell_volume	9623 Å³
Envelope diameter envelope_diameter	38.2 Å
Shell Rg shell_rg	17.66 Å
Envelope Rg envelope_rg	12.42 Å
Shape Rg shape_rg	10.25 Å
Total Rg total_rg	10.35 Å
Total atoms total_atoms	31480
Residues n_residues	2040
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	32.6 Å
Rg (real space) rg_real	9.59 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	7.8630e+08
I(0) uncertainty (real space) i0_real_error	7.1430e+06
Rg (reciprocal space) rg_reciprocal	9.59 Å
I(0) (reciprocal space) i0_reciprocal	786300000.0000
Solution quality estimate total_estimate	0.7279
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	11.1 Å
Skewness Skewness skewness	0.342
Kurtosis Kurtosis kurtosis	-0.308
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	43100.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.943; Smooth: 0.907

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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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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1afpa_
Class class	g — Small proteins
Fold Fold fold	g.26 — Antifungal protein (AGAFP)
Superfamily Superfamily superfamily	g.26.1 — Antifungal protein (AGAFP)
Family Family family	g.26.1.1 — Antifungal protein (AGAFP)

CATH v4.4 (1 domains)

Domain ID domain_id	1afpA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	60 — Antifungal protein domain

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS
Molecular weight formula_weight	5818.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	31480

来源生物 organism	Aspergillus giganteus
NCBI Class编号 ncbi_taxonomy_id	5060

SOLUTION STRUCTURE OF THE ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS. EVIDENCE FOR DISULPHIDE CONFIGURATIONAL ISOMERISM

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

ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/af/1afp/1afp.fit
pddf	/app/data/pr_computation/af/1afp/1afp.pr.out
profile	/app/data/saxs_computation/af/1afp/1afp.dat