SAXSdb — 1bzv

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

INSULIN

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 31–51	Mutation：CHAIN B, TYR(B26)D-ALA	INSULIN × 1 （P30410）	SOLUTION NMR NMR measurement conditions：pH 2；298 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	INS_BALPH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–21； UniProt 31–51

INSULIN

synthetic construct

UniProt P30410

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 25–49	Mutation：CHAIN B, TYR(B26)D-ALA Non-standard monomer：Yes (specific site not provided by mmCIF)	INSULIN × 1 （P01312）	SOLUTION NMR NMR measurement conditions：pH 2；298 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	INS_PANTR
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–25； UniProt 25–49

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	1bzv
Deposition date deposition_date	1998-11-04
Structure title title	[D-ALAB26]-DES(B27-B30)-INSULIN-B26-AMIDE A SUPERPOTENT SINGLE-REPLACEMENT INSULIN ANALOGUE, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords	INSULIN, SUPERPOTENCY, HORMONE; HORMONE
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	11.63 Å
Radius of gyration Rg (electron density) rg_electron	10.14 Å
Forward intensity I(0) i0	727779.00
Molecular weight molecular_weight	5258.0 kDa
Excluded volume excluded_volume	6503 Å³
Envelope volume envelope_volume	7620 Å³
Hydration-shell volume shell_volume	6784 Å³
Envelope diameter envelope_diameter	35.8 Å
Shell Rg shell_rg	15.05 Å
Envelope Rg envelope_rg	10.53 Å
Shape Rg shape_rg	10.14 Å
Total Rg total_rg	11.64 Å
Total atoms total_atoms	366
Residues n_residues	46
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	39.0 Å
Rg (real space) rg_real	11.60 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	7.2780e+05
I(0) uncertainty (real space) i0_real_error	7.6370e+03
Rg (reciprocal space) rg_reciprocal	11.60 Å
I(0) (reciprocal space) i0_reciprocal	727800.0000
Solution quality estimate total_estimate	0.8874
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	14.3 Å
Skewness Skewness skewness	0.231
Kurtosis Kurtosis kurtosis	-0.284
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	78590.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.972

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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bzv.1
Class class	g — Small proteins
Fold Fold fold	g.1 — Insulin-like
Superfamily Superfamily superfamily	g.1.1 — Insulin-like
Family Family family	g.1.1.1 — Insulin-like

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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	INSULIN
Molecular weight formula_weight	2383.7 kDa
Mutation mutation	CHAIN B, TYR(B26)D-ALA
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	366

Description description	INSULIN
Molecular weight formula_weight	2913.4 kDa
Mutation mutation	CHAIN B, TYR(B26)D-ALA
Source method src_method	man
Copy count entity_count	1

[D-ALAB26]-DES(B27-B30)-INSULIN-B26-AMIDE A SUPERPOTENT SINGLE-REPLACEMENT INSULIN ANALOGUE, NMR, MINIMIZED AVERAGE STRUCTURE

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

INSULIN

State in the Current Structure

Other States of the Same Protein in the Database

INSULIN

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	synthetic construct
NCBI Class编号 ncbi_taxonomy_id	32630

fit	/app/data/saxs_computation/bz/1bzv/1bzv.fit
pddf	/app/data/pr_computation/bz/1bzv/1bzv.pr.out
profile	/app/data/saxs_computation/bz/1bzv/1bzv.dat