1bh4

CIRCULIN A FROM CHASSALIA PARVIFLORA, NMR, 12 STRUCTURES

Method: SOLUTION NMR D_max: 30.9 Å Quality: GOOD

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

CIRCULIN A

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 1–27	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3.5；285 K NMR sample composition：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	CIRA_CHAPA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–30； UniProt 1–27

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	1bh4
Deposition date deposition_date	1998-06-12
Structure title title	CIRCULIN A FROM CHASSALIA PARVIFLORA, NMR, 12 STRUCTURES
Keywords keywords	CYCLIC PEPTIDE, CYSTINE KNOT, ANTI-HIV ACTIVITY; CYCLIC PEPTIDE
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	7.69 Å
Radius of gyration Rg (electron density) rg_electron	8.49 Å
Forward intensity I(0) i0	24135600.00
Molecular weight molecular_weight	37930.0 kDa
Excluded volume excluded_volume	46577 Å³
Envelope volume envelope_volume	8480 Å³
Hydration-shell volume shell_volume	7358 Å³
Envelope diameter envelope_diameter	32.7 Å
Shell Rg shell_rg	15.39 Å
Envelope Rg envelope_rg	10.53 Å
Shape Rg shape_rg	8.57 Å
Total Rg total_rg	8.70 Å
Total atoms total_atoms	5112
Residues n_residues	360
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	30.9 Å
Rg (real space) rg_real	7.69 Å
Rg uncertainty (real space) rg_real_error	0.45 Å
I(0) (real space) i0_real	2.4140e+07
I(0) uncertainty (real space) i0_real_error	2.5810e+05
Rg (reciprocal space) rg_reciprocal	7.69 Å
I(0) (reciprocal space) i0_reciprocal	24140000.0000
Solution quality estimate total_estimate	0.7638
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	9.8 Å
Skewness Skewness skewness	0.414
Kurtosis Kurtosis kurtosis	0.396
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23850.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.401; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.787; Smooth: 0.939

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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bh4a_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.3 — Cyclotides
Family Family family	g.3.3.3 — Circulin A

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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	CIRCULIN A
Molecular weight formula_weight	3178.8 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	5112

fit	/app/data/saxs_computation/bh/1bh4/1bh4.fit
pddf	/app/data/pr_computation/bh/1bh4/1bh4.pr.out
profile	/app/data/saxs_computation/bh/1bh4/1bh4.dat

CIRCULIN A FROM CHASSALIA PARVIFLORA, NMR, 12 STRUCTURES

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

CIRCULIN A

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) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)