SAXSdb — 1b1u

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

PROTEIN (ALPHA-AMYLASE/TRYPSIN INHIBITOR RATI)

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 1–122	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；1.15M AMMONIUM SULFATE, 0.2M AMMONIUM PHOSPHATE PH 8.0	Resolution 2.20 Å R-free 0.321

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 1B1U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BIP BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI) Deposited 1995-03-31	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–122（122 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1TMQ STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR Deposited 1998-01-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–117（117 aa）	Not recorded	CL CHLORIDE ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 200MM AMMONIUM PHOSPHATE, 100MM TRIS-HCL, PH 8.5, 50% (W/V) 2-METHYL-2,4- PENTANEDIOL	Resolution 2.50 Å R-free 0.261

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IAAT_ELECO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–122； UniProt 1–122

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	1b1u
Deposition date deposition_date	1998-11-23
Structure title title	CRYSTAL STRUCTURE OF THE BIFUNCTIONAL INHIBITOR RAGI
Keywords keywords	ALPHA-AMYLASE/TRYPSIN INHIBITOR (RATI), BIFUNCTIONAL, HYDROLASE INHIBITOR; HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	14.37 Å
Radius of gyration Rg (electron density) rg_electron	13.24 Å
Forward intensity I(0) i0	3538130.00
Molecular weight molecular_weight	12681.0 kDa
Excluded volume excluded_volume	15666 Å³
Envelope volume envelope_volume	16846 Å³
Hydration-shell volume shell_volume	10972 Å³
Envelope diameter envelope_diameter	46.7 Å
Shell Rg shell_rg	18.85 Å
Envelope Rg envelope_rg	13.60 Å
Shape Rg shape_rg	13.26 Å
Total Rg total_rg	14.35 Å
Total atoms total_atoms	880
Residues n_residues	117
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	46.7 Å
Rg (real space) rg_real	14.29 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	3.5380e+06
I(0) uncertainty (real space) i0_real_error	3.5680e+04
Rg (reciprocal space) rg_reciprocal	14.29 Å
I(0) (reciprocal space) i0_reciprocal	3538000.0000
Solution quality estimate total_estimate	0.8859
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	45.5 Å
Skewness Skewness skewness	0.151
Kurtosis Kurtosis kurtosis	-0.362
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	578700.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.851; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.961

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1b1ua_
Class class	a — All alpha proteins
Fold Fold fold	a.52 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Superfamily Superfamily superfamily	a.52.1 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Family Family family	a.52.1.2 — Proteinase/alpha-amylase inhibitors

CATH v4.4 (1 domains)

Domain ID domain_id	1b1uA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily	10 — Plant lipid-transfer and hydrophobic proteins

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8. Citations (4)

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Unit-cell length a length_a	47.380 Å
Unit-cell length b length_b	54.480 Å
Unit-cell length c length_c	40.350 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2220
R_work r_work	0.2220
R_free r_free	0.3210

Description description	PROTEIN (ALPHA-AMYLASE/TRYPSIN INHIBITOR RATI)
Molecular weight formula_weight	13153.3 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	968

CRYSTAL STRUCTURE OF THE BIFUNCTIONAL INHIBITOR RAGI

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

PROTEIN (ALPHA-AMYLASE/TRYPSIN INHIBITOR RATI)

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	88

fit	/app/data/saxs_computation/b1/1b1u/1b1u.fit
pddf	/app/data/pr_computation/b1/1b1u/1b1u.pr.out
profile	/app/data/saxs_computation/b1/1b1u/1b1u.dat