SAXSdb — 9g7t

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

Inverted formin-2

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 967–991	Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.5；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition：1 mM DAD, 63 % v/v H2O, 7 % v/v [U-2H] D2O, 30 % v/v [U-99% 2H] TFE, 0.1 mM DSS, trifluoroethanol/water \| trifluoroethanol/water NMR sample composition：0.5 mM DAD, 70 % v/v [U-2H] D2O, 30 % v/v [U-99% 2H] TFE, 0.1 mM DSS, trifluoroethanol/water \| trifluoroethanol/water	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 9G7T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8RV2 Structure of the formin INF2 bound to the barbed end of F-actin. Deposited 2024-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 469–1240（772 aa） Chain F 469–1240（772 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1；12 mM HEPES pH 7.1, 100 mM KCl, 2.1 mM MgCl2, 1 mM EGTA, 1 mM TCEP, 0.2 mM ATP cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 3.41 Å
9AZ4 INF2 at the Barbed End of F-Actin Deposited 2024-03-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain G 551–987（437 aa） Chain H 551–987（437 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.37 Å
9AZP INF2 at the Barbed End of F-Actin with Incoming Profilin-Actin Deposited 2024-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain G 1–1249（1249 aa） Chain H 1–1249（1249 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.79 Å
9AZQ INF2 at the Barbed End of F-Actin with Incoming Actin Deposited 2024-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain G 551–610（60 aa） Chain H 625–947（323 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.82 Å
9B03 INF2 in the Middle of F-Actin (Up state) Deposited 2024-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain G 551–987（437 aa） Chain H 551–987（437 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
9B0K INF2 in the Middle of F-Actin (Down state) Deposited 2024-03-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain G 551–987（437 aa） Chain H 551–987（437 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å
9FJN Solution NMR structure of a peptide encompassing residues 2-19 of the human formin INF2 Deposited 2024-05-31	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–19（18 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 1 mM INF2(2-19), 7 % v/v [U-2H] D2O, 63 % v/v H2O, 30 % v/v [U-98% 2H] TFE, 0.1 mM DSS, trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
9FJW Solution NMR structure of a peptide encompassing residues 2-36 of the human formin INF2 Deposited 2024-05-31	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–36（35 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 1 mM INF2(2-36), 7 % v/v [U-2H] D2O, 63 % v/v H2O, 30 % v/v [U-98% 2H] TFE, 0.1 mM DSS, trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
9RWF Solution NMR structure of a peptide encompassing residues 967-991 of the human formin INF2 Deposited 2025-07-09	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 967–991（25 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 0.5 mM DAD, 0.1 mM DSS, 10 % v/v [U-2H] D2O, 90 % H2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM DAD, 0.1 mM DSS, 100 % [U-2H] D2O, 100% D2O \| 100% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	INF2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–26； UniProt 967–991

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	9g7t
Deposition date deposition_date	2024-07-22
Structure title title	Solution NMR structure of a peptide encompassing residues 967-991 of the human formin INF2
Keywords keywords	formins, actin, microtubules, inherited disease, CELL ADHESION; CELL ADHESION
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	12.09 Å
Radius of gyration Rg (electron density) rg_electron	12.13 Å
Forward intensity I(0) i0	45295900.00
Molecular weight molecular_weight	56826.0 kDa
Excluded volume excluded_volume	71835 Å³
Envelope volume envelope_volume	9105 Å³
Hydration-shell volume shell_volume	6679 Å³
Envelope diameter envelope_diameter	49.2 Å
Shell Rg shell_rg	17.25 Å
Envelope Rg envelope_rg	14.32 Å
Shape Rg shape_rg	12.11 Å
Total Rg total_rg	12.41 Å
Total atoms total_atoms	8260
Residues n_residues	500
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	46.6 Å
Rg (real space) rg_real	12.51 Å
Rg uncertainty (real space) rg_real_error	0.54 Å
I(0) (real space) i0_real	4.5300e+07
I(0) uncertainty (real space) i0_real_error	5.4110e+05
Rg (reciprocal space) rg_reciprocal	12.48 Å
I(0) (reciprocal space) i0_reciprocal	45300000.0000
Solution quality estimate total_estimate	0.6362
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	6.5 Å
Skewness Skewness skewness	0.632
Kurtosis Kurtosis kurtosis	-0.469
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3859.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.094; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.003; Smooth: 0.981

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Description description	Inverted formin-2
Molecular weight formula_weight	2886.4 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	8260

fit	/app/data/saxs_computation/g7/9g7t/9g7t.fit
pddf	/app/data/pr_computation/g7/9g7t/9g7t.pr.out
profile	/app/data/saxs_computation/g7/9g7t/9g7t.dat

Solution NMR structure of a peptide encompassing residues 967-991 of the human formin INF2

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

Inverted formin-2

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)