SAXSdb — 8jq1

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

Insulinoma-associated protein 1

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 257–320	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition：2.0 % [U-13C; U-15N] ribonuclease, 90% H2O/10% D2O \| 90% H2O/10% D2O	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 8JQ1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2LV2 Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B Deposited 2012-06-27	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 424–497（74 aa） Fragment：C2H2-type zinc fingers 4 and 5	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Pressure ambient NMR sample composition 0.69 mM [U-100% 13C; U-100% 15N] HR7614B.021, 100 mM NaCl, 5 mM DTT, 0.02 % NaN3, 10 mM Tris-HCl pH 7.5, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.25 mM [U-5% 13C; U-100% 15N] HR7614B.023, 100 mM NaCl, 5 mM DTT, 0.02 % NaN3, 10 mM Tris-HCl pH 7.5, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.25 mM [U-5% 13C; U-100% 15N] HR7614B.023, 100 mM NaCl, 5 mM DTT, 0.02 % NaN3, 10 mM Tris-HCl pH 7.5, 100% D2O \| 100% D2O	Resolution not provided
3ZMS LSD1-CoREST in complex with INSM1 peptide Deposited 2013-02-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 2–510（509 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 2.96 Å R-free 0.227
8JPY Solution NMR Structure of Zinc-fingers 1 and 2 (fragment 257-320) from human Insulinoma-associated protein 1(INSM1) Deposited 2023-06-13	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 257–320（64 aa）	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 100；Pressure ambient NMR sample composition 0.69 mM [U-100% 13C; U-100% 15N] ZF3 protein, 0.69 mM [U-100% 13C; U-100% 15N] ZF3 protein, 0.69 mM [U-100% 13C; U-100% 15N] ZF3 protein, 0.69 mM [U-100% 13C; U-100% 15N] ZF3 protein, 0.69 mM [U-100% 13C; U-100% 15N] ZF3 protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	INSM1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–64； UniProt 257–320

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	8jq1
Deposition date deposition_date	2023-06-13
最后修订 last_revision	2024-06-19
Structure title title	Solution NMR Structure of zinc fingers 1-2 (fragment 257-320) from human insulinoma-associated protein 1(INSM1)
Keywords keywords	Zinc fingers, Long flexible linker, C3H/C2H2-type Zinc-fingers, DNA BINDING PROTEIN; DNA BINDING PROTEIN
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	21.94 Å
Radius of gyration Rg (electron density) rg_electron	21.38 Å
Forward intensity I(0) i0	372028000.00
Molecular weight molecular_weight	148190.0 kDa
Excluded volume excluded_volume	181020 Å³
Envelope volume envelope_volume	103600 Å³
Hydration-shell volume shell_volume	32241 Å³
Envelope diameter envelope_diameter	90.3 Å
Shell Rg shell_rg	33.81 Å
Envelope Rg envelope_rg	26.92 Å
Shape Rg shape_rg	21.44 Å
Total Rg total_rg	21.89 Å
Total atoms total_atoms	20200
Residues n_residues	1280
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	84.2 Å
Rg (real space) rg_real	22.10 Å
Rg uncertainty (real space) rg_real_error	0.92 Å
I(0) (real space) i0_real	3.7200e+08
I(0) uncertainty (real space) i0_real_error	5.8280e+06
Rg (reciprocal space) rg_reciprocal	22.07 Å
I(0) (reciprocal space) i0_reciprocal	372000000.0000
Solution quality estimate total_estimate	0.8057
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.9 Å
Skewness Skewness skewness	0.343
Kurtosis Kurtosis kurtosis	-0.335
Angular range angular_range	— – 0.3600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	187200.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.497; Smooth: 0.985

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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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8. Citations (1)

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Description description	Insulinoma-associated protein 1
Molecular weight formula_weight	7287.5 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	20200

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	Homo sapiens

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

fit	/app/data/saxs_computation/jq/8jq1/8jq1.fit
pddf	/app/data/pr_computation/jq/8jq1/8jq1.pr.out
profile	/app/data/saxs_computation/jq/8jq1/8jq1.dat

Solution NMR Structure of zinc fingers 1-2 (fragment 257-320) from human insulinoma-associated protein 1(INSM1)

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

Insulinoma-associated protein 1

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)