SAXSdb — 8uy3

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

Protein fem-1 homolog B

Mus musculus

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–377	Fragment：residues 1-377	Folliculin-interacting protein 1 × 1 （Q68FD7） Mitochondrial import receptor subunit TOM20 homolog × 1 （Q15388） ZN ZINC ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–377	Fragment：residues 1-377	Folliculin-interacting protein 1 × 1 （Q68FD7） ZN ZINC ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 1–377	Fragment：residues 1-377	Folliculin-interacting protein 1 × 1 （Q68FD7） Mitochondrial import receptor subunit TOM20 homolog × 1 （Q15388） ZN ZINC ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 1–377	Fragment：residues 1-377	Folliculin-interacting protein 1 × 1 （Q68FD7） Mitochondrial import receptor subunit TOM20 homolog × 1 （Q15388） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264

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 8UY3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7ROY The structure of the Fem1B:FNIP1 complex Deposited 2021-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–377（377 aa） Chain D 1–377（377 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；FEM1B-FNIP1 complex (20 mg/mL) was mixed in a 1:1 ratio with the reservoir solution containing 6% isopropanol, 150 mM NaCl, and 100 mM HEPES-NaOH pH 7.5	Resolution 2.90 Å R-free 0.230
7ROY The structure of the Fem1B:FNIP1 complex Deposited 2021-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–377（377 aa） Chain C 1–377（377 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；FEM1B-FNIP1 complex (20 mg/mL) was mixed in a 1:1 ratio with the reservoir solution containing 6% isopropanol, 150 mM NaCl, and 100 mM HEPES-NaOH pH 7.5	Resolution 2.90 Å R-free 0.230

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FEM1B_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–381； UniProt 1–377 Author chain B； PDBConstruct 5–381； UniProt 1–377 Author chain C； PDBConstruct 5–381； UniProt 1–377 Author chain D； PDBConstruct 5–381； UniProt 1–377

Folliculin-interacting protein 1

Mus musculus

UniProt Q68FD7

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain E； UniProt 590–619	Fragment：residues 590-619	Protein fem-1 homolog B × 1 （Q9Z2G0） Mitochondrial import receptor subunit TOM20 homolog × 1 （Q15388） ZN ZINC ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 590–619	Fragment：residues 590-619	Protein fem-1 homolog B × 1 （Q9Z2G0） ZN ZINC ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain H； UniProt 590–619	Fragment：residues 590-619	Protein fem-1 homolog B × 1 （Q9Z2G0） Mitochondrial import receptor subunit TOM20 homolog × 1 （Q15388） ZN ZINC ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain I； UniProt 590–619	Fragment：residues 590-619	Protein fem-1 homolog B × 1 （Q9Z2G0） Mitochondrial import receptor subunit TOM20 homolog × 1 （Q15388） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264

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 8UY3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7ROY The structure of the Fem1B:FNIP1 complex Deposited 2021-08-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 590–619（30 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；FEM1B-FNIP1 complex (20 mg/mL) was mixed in a 1:1 ratio with the reservoir solution containing 6% isopropanol, 150 mM NaCl, and 100 mM HEPES-NaOH pH 7.5	Resolution 2.90 Å R-free 0.230
7ROY The structure of the Fem1B:FNIP1 complex Deposited 2021-08-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 590–619（30 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；FEM1B-FNIP1 complex (20 mg/mL) was mixed in a 1:1 ratio with the reservoir solution containing 6% isopropanol, 150 mM NaCl, and 100 mM HEPES-NaOH pH 7.5	Resolution 2.90 Å R-free 0.230

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FNIP1_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 2–31； UniProt 590–619 Author chain F； PDBConstruct 2–31； UniProt 590–619 Author chain H； PDBConstruct 2–31； UniProt 590–619 Author chain I； PDBConstruct 2–31； UniProt 590–619

Mitochondrial import receptor subunit TOM20 homolog

Homo sapiens

UniProt Q15388

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain J； UniProt 62–127	Fragment：residues 62-127	Protein fem-1 homolog B × 1 （Q9Z2G0） Folliculin-interacting protein 1 × 1 （Q68FD7） ZN ZINC ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain K； UniProt 62–127	Fragment：residues 62-127	Protein fem-1 homolog B × 1 （Q9Z2G0） Folliculin-interacting protein 1 × 1 （Q68FD7） ZN ZINC ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain M； UniProt 62–127	Fragment：residues 62-127	Protein fem-1 homolog B × 1 （Q9Z2G0） Folliculin-interacting protein 1 × 1 （Q68FD7） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；10 mg/mL protein complex in 50 mM HEPES pH 7.5, 500 mM NaCl, 1 mM TCEP were mixed in a 2:1 ratio with the reservoir solution containing 30% PEG 3350, 0.2M Ammonium Citrate pH 7	Resolution 3.20 Å R-free 0.264

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 8UY3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4APO AIP TPR domain in complex with human Tomm20 peptide Deposited 2012-04-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 140–145（6 aa） Fragment：RESIDUES 140-145	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions PEG 3350, AMMONIUM SULFATE, BIS-TRIS PH 5.5	Resolution 1.90 Å R-free 0.234
4APO AIP TPR domain in complex with human Tomm20 peptide Deposited 2012-04-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 140–145（6 aa） Fragment：RESIDUES 140-145	Not recorded	12P DODECAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions PEG 3350, AMMONIUM SULFATE, BIS-TRIS PH 5.5	Resolution 1.90 Å R-free 0.234
7VC9 Tom20 subunits Deposited 2021-09-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain M 1–145（145 aa） Chain N 1–145（145 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 13.00 Å
8XVA Human TOM complex with whole Tom20 Deposited 2024-01-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: 11-meric	Chain K 1–145（145 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.92 Å
9EIH Import stalled PINK1 TOM complex Deposited 2024-11-26	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 × 26 PDB declaration: 26-meric	Chain C 1–145（145 aa） Chain D 1–145（145 aa）	Not recorded	PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 17	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9EII Import stalled PINK1 TOM complex, symmetry expanded Deposited 2024-11-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: 13-meric	Chain D 1–145（145 aa）	Not recorded	PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blot force 10 for 2 s.	Resolution 2.75 Å
9EIJ Import stalled PINK1 TOM complex, extended TOM20 helix class Deposited 2024-11-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: 15-meric	Chain D 1–145（145 aa）	Not recorded	PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 9	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blot force 10 for 2 s.	Resolution 3.30 Å
9J79 Cryo-EM structure of CRL2-FEM1B bound with TOM20(tetramer) Deposited 2024-08-18	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 × 19 PDB declaration: 19-meric	Chain B 25–145（121 aa） Chain C 25–145（121 aa） Chain G 25–145（121 aa） Chain S 25–145（121 aa）	Not recorded	ZN ZINC ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.08 Å
9J7A local refinement of FEM1B bound with TOM20 (dimer) Deposited 2024-08-18	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 B 25–145（121 aa） Chain C 25–145（121 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.13 Å
9J7B local refinement of FEM1B bound with TOM20(tetramer) Deposited 2024-08-18	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 × 11 PDB declaration: 11-meric	Chain B 25–145（121 aa） Chain C 25–145（121 aa） Chain G 25–145（121 aa） Chain Q 25–145（121 aa） Chain S 25–145（121 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.12 Å
9JCE local refinement of FEM1B bound with TOM20 Deposited 2024-08-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 25–145（121 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.59 Å

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

View Construct and Data Evidence

UniProt name	TOM20_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain J； PDBConstruct 1–66； UniProt 62–127 Author chain K； PDBConstruct 1–66； UniProt 62–127 Author chain M； PDBConstruct 1–66； UniProt 62–127

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	8uy3
Deposition date deposition_date	2023-11-12
最后修订 last_revision	2025-03-19
Structure title title	Fem1B with FNIP1 and Tom20 fragment
Keywords keywords	Fem1B FNP1 ubiquitin, proteasome, reductive stress response, TOM complex electron transport chain mitochondria, PROTEIN BINDING; PROTEIN BINDING
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	40.29 Å
Radius of gyration Rg (electron density) rg_electron	40.03 Å
Forward intensity I(0) i0	591793000.00
Molecular weight molecular_weight	195830.0 kDa
Excluded volume excluded_volume	244000 Å³
Envelope volume envelope_volume	331940 Å³
Hydration-shell volume shell_volume	67996 Å³
Envelope diameter envelope_diameter	139.9 Å
Shell Rg shell_rg	46.70 Å
Envelope Rg envelope_rg	39.16 Å
Shape Rg shape_rg	40.04 Å
Total Rg total_rg	40.36 Å
Total atoms total_atoms	13732
Residues n_residues	1749
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	130.0 Å
Rg (real space) rg_real	40.15 Å
Rg uncertainty (real space) rg_real_error	0.93 Å
I(0) (real space) i0_real	5.9180e+08
I(0) uncertainty (real space) i0_real_error	8.5000e+06
Rg (reciprocal space) rg_reciprocal	40.29 Å
I(0) (reciprocal space) i0_reciprocal	591900000.0000
Solution quality estimate total_estimate	0.8874
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	50.0 Å
Skewness Skewness skewness	0.202
Kurtosis Kurtosis kurtosis	-0.362
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	48850000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.879

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Protein fem-1 homolog B
Molecular weight formula_weight	42362.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,B,D
Atom count atom_count	13741

SGSSMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLSHADCDRRSRIEALELLGASFANDRENYDIMKTYHYLYLAMLERFQDGDNILEKEVLPPIHAYGNRTECRNPQELEAIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYADNMEFEQCIKLWLHALHLRQKG

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Folliculin-interacting protein 1
Molecular weight formula_weight	3505.0 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,H,I

GRNKSSLLFKESEETRTPNCNCKYCSHPVLG

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Mitochondrial import receptor subunit TOM20 homolog
Molecular weight formula_weight	7364.4 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,K,M

DAEAVQKFFLEEIQLGEELLAQGEYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQMLLTKLP

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 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 non-polymer

Description description	4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
Molecular weight formula_weight	238.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

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8. Citations (1)

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Unit-cell length a length_a	183.715 Å
Unit-cell length b length_b	183.715 Å
Unit-cell length c length_c	183.715 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	48

Space group space_group	P 21 3
Space-group number int_tables_number	198
Crystal system crystal_system	cubic

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	45.930 Å
R factor r_factor	0.2404
R_work r_work	0.2391
R_free r_free	0.2644

fit	/app/data/saxs_computation/uy/8uy3/8uy3.fit
pddf	/app/data/pr_computation/uy/8uy3/8uy3.pr.out
profile	/app/data/saxs_computation/uy/8uy3/8uy3.dat

Fem1B with FNIP1 and Tom20 fragment

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

Protein fem-1 homolog B

State in the Current Structure

Other States of the Same Protein in the Database

Folliculin-interacting protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Mitochondrial import receptor subunit TOM20 homolog

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

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)