1ccv

NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHYMOTRYPSIN INHIBITOR (AMCI).

Method: SOLUTION NMR D_max: 36.6 Å Quality: GOOD

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

CHYMOTRYPSIN INHIBITOR

OrganismNot specified

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 1–56	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 2.5；288 K	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	AMCI_APIME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–56； UniProt 1–56

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	1ccv
Deposition date deposition_date	1999-03-02
Structure title title	NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHYMOTRYPSIN INHIBITOR (AMCI).
Keywords keywords	PROTEIN INHIBITOR, HEMOLYMPH, APIS MELLIFERA, CANONICAL INHIBITOR, HYDROLASE INHIBITOR; HYDROLASE INHIBITOR
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	11.09 Å
Radius of gyration Rg (electron density) rg_electron	11.32 Å
Forward intensity I(0) i0	271909000.00
Molecular weight molecular_weight	119420.0 kDa
Excluded volume excluded_volume	141500 Å³
Envelope volume envelope_volume	12950 Å³
Hydration-shell volume shell_volume	9107 Å³
Envelope diameter envelope_diameter	41.4 Å
Shell Rg shell_rg	17.70 Å
Envelope Rg envelope_rg	13.04 Å
Shape Rg shape_rg	11.26 Å
Total Rg total_rg	11.61 Å
Total atoms total_atoms	15620
Residues n_residues	1120
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	36.6 Å
Rg (real space) rg_real	11.08 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	2.7190e+08
I(0) uncertainty (real space) i0_real_error	2.8060e+06
Rg (reciprocal space) rg_reciprocal	11.08 Å
I(0) (reciprocal space) i0_reciprocal	271900000.0000
Solution quality estimate total_estimate	0.8971
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	13.9 Å
Skewness Skewness skewness	0.253
Kurtosis Kurtosis kurtosis	-0.312
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	36620.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.976

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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	d1ccva_
Class class	g — Small proteins
Fold Fold fold	g.22 — Serine protease inhibitors
Superfamily Superfamily superfamily	g.22.1 — Serine protease inhibitors
Family Family family	g.22.1.1 — ATI-like

CATH v4.4 (1 domains)

Domain ID domain_id	1ccvA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	25 — Laminin
Homologous superfamily homologous superfamily	10 — Laminin

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8. Citations (2)

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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	CHYMOTRYPSIN INHIBITOR
Molecular weight formula_weight	5976.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	15620

fit	/app/data/saxs_computation/cc/1ccv/1ccv.fit
pddf	/app/data/pr_computation/cc/1ccv/1ccv.pr.out
profile	/app/data/saxs_computation/cc/1ccv/1ccv.dat

NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHYMOTRYPSIN INHIBITOR (AMCI).

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

CHYMOTRYPSIN INHIBITOR

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

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)