SAXSdb — 3ci2

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

CHYMOTRYPSIN INHIBITOR 2

Hordeum vulgare

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ICI2_HORVU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–66； UniProt 18–83

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3ci2
Deposition date deposition_date	1991-09-10
Structure title title	REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF BARLEY SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE STRUCTURES IN CRYSTALS
Keywords keywords	SERINE PROTEASE INHIBITOR; SERINE PROTEASE INHIBITOR
Experimental Method method	SOLUTION NMR

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3ci2__assembly_1__model_17

Assembly 1 · Model 17 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3ci2__assembly_1__model_17 | I(q)

100 plotted points; both axes use logarithmic scales.

3ci2__assembly_1__model_17 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	11.89 Å
Rg (electron density)	10.77 Å
Total Rg	12.51 Å
Atom count	1060
Residues	63
Excluded volume	9509 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3ci2__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`3ci2__assembly_1__model_2`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`3ci2__assembly_1__model_3`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`3ci2__assembly_1__model_4`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`3ci2__assembly_1__model_5`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`3ci2__assembly_1__model_6`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`3ci2__assembly_1__model_7`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`3ci2__assembly_1__model_8`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`3ci2__assembly_1__model_9`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`3ci2__assembly_1__model_10`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`3ci2__assembly_1__model_11`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`3ci2__assembly_1__model_12`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`3ci2__assembly_1__model_13`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`3ci2__assembly_1__model_14`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`3ci2__assembly_1__model_15`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`3ci2__assembly_1__model_16`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`3ci2__assembly_1__model_17`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`3ci2__assembly_1__model_18`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`3ci2__assembly_1__model_19`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`3ci2__assembly_1__model_20`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (1)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3ci2a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.40 — CI-2 family of serine protease inhibitors
Superfamily Superfamily superfamily	d.40.1 — CI-2 family of serine protease inhibitors
Family Family family	d.40.1.1 — CI-2 family of serine protease inhibitors

CATH v4.4 (1 domains)

Domain ID domain_id	3ci2A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	10 — Trypsin Inhibitor V; Chain A
Homologous superfamily homologous superfamily	10 — Trypsin Inhibitor V, subunit A

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7. Citations (8)

;Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. ;

J.Mol.Biol. (1991)

PMID: 1748996 · DOI: 10.1016/0022-2836(91)90500-6 PRIMARY

;Accurate Measurements of Coupling Constants from Two-Dimensional Nuclear Magnetic Resonance Spectra of Proteins and Determination of Phi-Angles ;

J.Mol.Biol. (1991)

Application of Symmetry Projection Operators to Measurements of Coupling Constants in 2D NMR Spectra of Proteins

J.Magn.Reson. (1990)

;The Three-Dimensional Structure of Barley Serine Proteinase Inhibitor-2 in Solution as Determined by Proton Nuclear Magnetic Resonance Spectroscopy ;

Alfred Benzon Symp. (1988)

;The Determination of the Three-Dimensional Structure of Barley Serine Proteinase Inhibitor 2 by Nuclear Magnetic Resonance, Distance Geometry and Restrained Molecular Dynamics ;

Protein Eng. (1987)

Comparison of the Solution and X-Ray Structures of Barley Serine Proteinase Inhibitor 2

Protein Eng. (1987)

Secondary Structure of Barley Serine Proteinase Inhibitor 2 Determined by Proton Nuclear Magnetic Resonance Spectroscopy

Carlsberg Res.Commun. (1987)

Sequence Specific Assignment of the Proton Nuclear Magnetic Resonance Spectrum of Barley Serine Proteinase Inhibitor 2

Carlsberg Res.Commun. (1987)

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 2
Molecular weight formula_weight	7547.8 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	21220

Source organism organism	Hordeum vulgare
NCBI taxonomy ID ncbi_taxonomy_id	4513

REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF BARLEY SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE STRUCTURES IN CRYSTALS

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

CHYMOTRYPSIN INHIBITOR 2

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3ci2__assembly_1__model_17

3ci2__assembly_1__model_17 | I(q)

3ci2__assembly_1__model_17 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (8)

REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF BARLEY SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE STRUCTURES IN CRYSTALS

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

CHYMOTRYPSIN INHIBITOR 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3ci2__assembly_1__model_17

3ci2__assembly_1__model_17 | I(q)

3ci2__assembly_1__model_17 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (8)