SAXSdb — 1bw4

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

BARWIN, BASIC BARLEY SEED PROTEIN

Hordeum vulgare

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 2–125	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.

Other PDB	Difference from Current Entry 1BW4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BW3 THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM BARLEY SEED Deposited 1992-07-06	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–125（124 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	BARW_HORVU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–125； UniProt 2–125

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	1bw4
Deposition date deposition_date	1992-07-06
Structure title title	THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM BARLEY SEED
Keywords keywords	LECTIN; LECTIN
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	14.16 Å
Radius of gyration Rg (electron density) rg_electron	13.91 Å
Forward intensity I(0) i0	1180090000.00
Molecular weight molecular_weight	274760.0 kDa
Excluded volume excluded_volume	336090 Å³
Envelope volume envelope_volume	29121 Å³
Hydration-shell volume shell_volume	15614 Å³
Envelope diameter envelope_diameter	48.0 Å
Shell Rg shell_rg	21.70 Å
Envelope Rg envelope_rg	15.65 Å
Shape Rg shape_rg	13.90 Å
Total Rg total_rg	14.05 Å
Total atoms total_atoms	37260
Residues n_residues	2500
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	41.0 Å
Rg (real space) rg_real	14.07 Å
Rg uncertainty (real space) rg_real_error	0.20 Å
I(0) (real space) i0_real	1.1800e+09
I(0) uncertainty (real space) i0_real_error	1.2490e+07
Rg (reciprocal space) rg_reciprocal	14.07 Å
I(0) (reciprocal space) i0_reciprocal	1180000000.0000
Solution quality estimate total_estimate	0.8291
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.1 Å
Skewness Skewness skewness	0.138
Kurtosis Kurtosis kurtosis	-0.453
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	543300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.000

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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	d1bw4a_
Class class	b — All beta proteins
Fold Fold fold	b.52 — Double psi beta-barrel
Superfamily Superfamily superfamily	b.52.1 — Barwin-like endoglucanases
Family Family family	b.52.1.2 — Barwin

CATH v4.4 (1 domains)

Domain ID domain_id	1bw4A00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily	10 — RlpA-like domain

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8. Citations (3)

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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	BARWIN, BASIC BARLEY SEED PROTEIN
Molecular weight formula_weight	13751.2 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	37260

来源生物 organism	Hordeum vulgare
NCBI Class编号 ncbi_taxonomy_id	4513

THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF BARWIN, A PROTEIN FROM BARLEY SEED

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

BARWIN, BASIC BARLEY SEED PROTEIN

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 (3)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/bw/1bw4/1bw4.fit
pddf	/app/data/pr_computation/bw/1bw4/1bw4.pr.out
profile	/app/data/saxs_computation/bw/1bw4/1bw4.dat