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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

Method: SOLUTION NMR Dmax: 59.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Insulinoma-associated protein 1

Homo sapiens

UniProt Q01101

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 424–497 Fragment：C2H2-type zinc fingers 4 and 5 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

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 2LV2 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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 construct 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
8JQ1 Solution NMR Structure of zinc fingers 1-2 (fragment 257-320) from human insulinoma-associated protein 1(INSM1) Deposited 2023-06-13 Different construct 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 1
NMR sample composition 2.0 % [U-13C; U-15N] ribonuclease, 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 12–85； UniProt 424–497

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2lv2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lv2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lv2
Deposition date deposition_date2012-06-27
Structure title titleSolution 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
Keywords keywordsStructural Genomics, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), PSI-Biology, Protein Structure Initiative, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.87 Å
Radius of gyration Rg (electron density) rg_electron22.54 Å
Forward intensity I(0) i0643273000.00
Molecular weight molecular_weight187360.0 kDa
Excluded volume excluded_volume224130 ų
Envelope volume envelope_volume134950 ų
Hydration-shell volume shell_volume34216 ų
Envelope diameter envelope_diameter139.0 Å
Shell Rg shell_rg37.46 Å
Envelope Rg envelope_rg38.69 Å
Shape Rg shape_rg22.65 Å
Total Rg total_rg22.78 Å
Total atoms total_atoms25100
Residues n_residues1700
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax59.5 Å
Rg (real space) rg_real20.11 Å
Rg uncertainty (real space) rg_real_error0.18 Å
I(0) (real space) i0_real6.0640e+08
I(0) uncertainty (real space) i0_real_error6.8070e+06
Rg (reciprocal space) rg_reciprocal23.73 Å
I(0) (reciprocal space) i0_reciprocal643200000.0000
Solution quality estimate total_estimate0.6430
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.6 Å
Skewness Skewness skewness0.441
Kurtosis Kurtosis kurtosis-0.622
Angular range angular_range— – 0.3450 Å−1
Current regularization parameter α current_alpha1.8000
Highest regularization parameter α highest_alpha76250.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.027; Oscil: 0.954; Stabil: 0.989; Sysdev: 0.000; Positv: 1.000; Valcen: 0.561; Smooth: 0.000
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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

CATH v4.4 (1 domains)

Domain ID domain_id2lv2A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily60 — Classic Zinc Finger
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8. Citations (1)

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9. Files and Curves (10)