SAXSdb — 1imx

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

Insulin-like Growth Factor 1A

Homo sapiens

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 49–118	Not recorded	BR BROMIDE ION × 1 CPQ N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；PEG 3350, deoxy big CHAPS, sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.82 Å R-free 0.258

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 1IMX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B9G INSULIN-LIKE-GROWTH-FACTOR-1 Deposited 1999-02-11	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–57（57 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 1.9；293 K	Resolution not provided
1GZR Human Insulin-like growth factor; ESRF data Deposited 2002-05-28	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 49–118（70 aa）	Not recorded	C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.	Resolution 2.00 Å R-free 0.295
1GZY Human Insulin-like growth factor; In-house data Deposited 2002-06-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 49–118（70 aa）	Not recorded	C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.	Resolution 2.54 Å R-free 0.265
1GZZ Human Insulin-like growth factor; Hamburg data Deposited 2002-06-10	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 49–118（70 aa）	Not recorded	C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.	Resolution 2.30 Å R-free 0.275
1H02 Human Insulin-like growth factor; SRS Daresbury data Deposited 2002-06-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 49–118（70 aa）	Not recorded	C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.	Resolution 2.00 Å R-free 0.300
1H59 Complex of IGFBP-5 with IGF-I Deposited 2001-05-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 49–118（70 aa） Fragment：RESIDUES 49-118	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.60	Resolution 2.10 Å R-free 0.262
1TGR Crystal Structure of mini-IGF-1(2) Deposited 2004-05-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 49–77（29 aa） Fragment：residues 1-52 Chain A 90–110（21 aa） Fragment：residues 1-52	Mutation：T29K Mutation：T29K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.65；289 K；Citrate, ethanol, pH 6.65, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.42 Å R-free 0.224
1TGR Crystal Structure of mini-IGF-1(2) Deposited 2004-05-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 49–77（29 aa） Fragment：residues 1-52 Chain B 90–110（21 aa） Fragment：residues 1-52	Mutation：T29K Mutation：T29K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.65；289 K；Citrate, ethanol, pH 6.65, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.42 Å R-free 0.224
1TGR Crystal Structure of mini-IGF-1(2) Deposited 2004-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 49–77（29 aa） Fragment：residues 1-52 Chain A 90–110（21 aa） Fragment：residues 1-52 Chain B 49–77（29 aa） Fragment：residues 1-52 Chain B 90–110（21 aa） Fragment：residues 1-52	Mutation：T29K Mutation：T29K Mutation：T29K Mutation：T29K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.65；289 K；Citrate, ethanol, pH 6.65, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 1.42 Å R-free 0.224
2GF1 SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY Deposited 1991-01-23	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 49–118（70 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3GF1 SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY Deposited 1991-01-24	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 49–118（70 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IGF1A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–70； UniProt 49–118

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	1imx
Deposition date deposition_date	2001-05-11
Structure title title	1.8 Angstrom crystal structure of IGF-1
Keywords keywords	insulin/relaxin, detergent, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
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	13.54 Å
Radius of gyration Rg (electron density) rg_electron	12.34 Å
Forward intensity I(0) i0	1201170.00
Molecular weight molecular_weight	7144.0 kDa
Excluded volume excluded_volume	8869 Å³
Envelope volume envelope_volume	10733 Å³
Hydration-shell volume shell_volume	8025 Å³
Envelope diameter envelope_diameter	53.5 Å
Shell Rg shell_rg	17.12 Å
Envelope Rg envelope_rg	13.35 Å
Shape Rg shape_rg	12.36 Å
Total Rg total_rg	13.53 Å
Total atoms total_atoms	492
Residues n_residues	56
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	55.0 Å
Rg (real space) rg_real	13.60 Å
Rg uncertainty (real space) rg_real_error	0.62 Å
I(0) (real space) i0_real	1.2010e+06
I(0) uncertainty (real space) i0_real_error	1.6030e+04
Rg (reciprocal space) rg_reciprocal	13.59 Å
I(0) (reciprocal space) i0_reciprocal	1201000.0000
Solution quality estimate total_estimate	0.7561
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.0 Å
Skewness Skewness skewness	0.523
Kurtosis Kurtosis kurtosis	0.360
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	143100.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.409; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.606; Smooth: 0.992

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Insulin-like Growth Factor 1A
Molecular weight formula_weight	7663.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	539

GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	BROMIDE ION
Molecular weight formula_weight	79.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE
Molecular weight formula_weight	862.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	47

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1imxa_
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

CATH v4.4 (1 domains)

Domain ID domain_id	1imxA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily	10 — Insulin-like

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8. Citations (1)

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Unit-cell length a length_a	31.831 Å
Unit-cell length b length_b	71.055 Å
Unit-cell length c length_c	65.996 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	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.820 Å
Low-resolution limit resolution_low	19.000 Å
R factor r_factor	—
R_work r_work	0.2450
R_free r_free	0.2580

fit	/app/data/saxs_computation/im/1imx/1imx.fit
pddf	/app/data/pr_computation/im/1imx/1imx.pr.out
profile	/app/data/saxs_computation/im/1imx/1imx.dat

1.8 Angstrom crystal structure of IGF-1

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

Insulin-like Growth Factor 1A

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