SAXSdb — 1hf9

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

ATPASE INHIBITOR (MITOCHONDRIAL)

BOS TAURUS

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 69–109 Chain B； UniProt 69–109	Fragment：C-TERMINAL DOMAIN (44-84)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.5；300 K；Pressure 1	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 1HF9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GMJ The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase Deposited 2001-09-14	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 26–109（84 aa） Chain B 26–109（84 aa）	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；296 K；CRYSTALS WERE GROWN BY EQUILIBRATING A IF1-H49K SOLUTION, AT 6 MG/ML IN BUFFER 10 MM TRIS-HCL PH 8.0, RESERVOIR CONTAINING 0.8 M MONO-SODIUM DIHYDROGEN PHOSPHAT AGAINST A 0.8 M MONO-POTASSIUM DIHYDROGEN PHOSPHATE AND 0.1 M HEPES-NA BUFFER PH 8, AT 23C, IN SITTING-DROP VAPOR-DIFFUSION TRAYS.	Resolution 2.20 Å R-free 0.280
1GMJ The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase Deposited 2001-09-14	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 26–109（84 aa） Chain D 26–109（84 aa）	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；296 K；CRYSTALS WERE GROWN BY EQUILIBRATING A IF1-H49K SOLUTION, AT 6 MG/ML IN BUFFER 10 MM TRIS-HCL PH 8.0, RESERVOIR CONTAINING 0.8 M MONO-SODIUM DIHYDROGEN PHOSPHAT AGAINST A 0.8 M MONO-POTASSIUM DIHYDROGEN PHOSPHATE AND 0.1 M HEPES-NA BUFFER PH 8, AT 23C, IN SITTING-DROP VAPOR-DIFFUSION TRAYS.	Resolution 2.20 Å R-free 0.280
1OHH BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1 Deposited 2003-05-27	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 H 26–109（84 aa）	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.6；PROTEIN 20MG/ML IN 100MM PIPES-NAOH PH6.6, 40MM MGSO4, 0.04% NA AZIDE, 10% GLYCEROL, 0.002% PMSF. DROPS EQUAL VOLUME OF PROTEIN AND 10MM AMP-PNP, 300MM NACL, 16% PEG 4000, 5MM SPERMIDINE. BATCH METHOD., pH 6.60	Resolution 2.80 Å R-free 0.280
2V7Q The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1. Deposited 2007-07-31	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 × 10 PDB declaration: decameric	Chain J 26–85（60 aa） Fragment：RESIDUES 26-85	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.2；pH 8.2	Resolution 2.10 Å R-free 0.245
4TSF The Pathway of Binding of the Intrinsically Disordered Mitochondrial Inhibitor Protein to F1-ATPase Deposited 2014-06-18	Different construct 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 H 26–85（60 aa） Fragment：UNP residues 26-85 Chain I 26–85（60 aa） Fragment：UNP residues 26-85	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 8.2；295 K；Tris-HCl, PEG 4000, magnesium chloride, EDTA, NaCl, spermidine	Resolution 3.20 Å R-free 0.272
4TT3 The Pathway of Binding of the Intrinsically Disordered Mitochondrial Inhibitor Protein to F1-ATPase Deposited 2014-06-19	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 H 26–85（60 aa） Fragment：UNP residues 36-85 Chain I 26–85（60 aa） Fragment：UNP residues 36-85 Chain J 26–85（60 aa） Fragment：UNP residues 36-85	Mutation：K39A Mutation：K39A Mutation：K39A	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 GOL GLYCEROL × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 8.2；295 K；PEG 4000, Tris-HCl, magnesium chloride, EDTA, ATP, NaCl, spermidine	Resolution 3.21 Å R-free 0.283
4Z1M Bovine F1-ATPase inhibited by three copies of the inhibitor protein IF1 crystallised in the presence of thiophosphate. Deposited 2015-03-27	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 H 26–85（60 aa） Chain I 26–85（60 aa） Chain J 26–85（60 aa）	Mutation：K39A Mutation：K39A Mutation：K39A	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 GOL GLYCEROL × 2 CL CHLORIDE ION × 11 ADP ADENOSINE-5'-DIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；295 K；Tris.HCl, MgCl2, EDTA, sodium monothiophosphate, ATP NaCl, spermidine, PEG 4000	Resolution 3.30 Å R-free 0.275
6YY0 bovine ATP synthase F1-peripheral stalk domain, state 1 Deposited 2020-05-04	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 × 14 PDB declaration: tetradecameric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting.	Resolution 3.23 Å
6Z1R bovine ATP synthase F1-peripheral stalk domain, state 2 Deposited 2020-05-14	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 × 21 PDB declaration: 21-meric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting.	Resolution 3.29 Å
6Z1U bovine ATP synthase F1c8-peripheral stalk domain, state 3 Deposited 2020-05-14	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 × 21 PDB declaration: 21-meric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting.	Resolution 3.47 Å
6ZPO bovine ATP synthase monomer state 1 (combined) Deposited 2020-07-09	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 × 29 PDB declaration: 29-meric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting.	Resolution 4.00 Å
6ZQM bovine ATP synthase monomer state 2 (combined) Deposited 2020-07-10	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 × 29 PDB declaration: 29-meric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting.	Resolution 3.29 Å
6ZQN bovine ATP synthase monomer state 3 (combined) Deposited 2020-07-10	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 × 29 PDB declaration: 29-meric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 CDL CARDIOLIPIN × 3 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting.	Resolution 4.00 Å
7AJB bovine ATP synthase dimer state1:state1 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.20 Å
7AJC bovine ATP synthase dimer state1:state2 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 11.90 Å
7AJD bovine ATP synthase dimer state1:state3 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.00 Å
7AJE bovine ATP synthase dimer state2:state1 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.40 Å
7AJF bovine ATP synthase dimer state2:state2 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–109（84 aa） Chain J 26–109（84 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.45 Å
7AJG bovine ATP synthase dimer state2:state3 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 10.70 Å
7AJH bovine ATP synthase dimer state3:state1 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.70 Å
7AJI bovine ATP synthase dimer state3:state2 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 11.40 Å
7AJJ bovine ATP synthase dimer state3:state3 Deposited 2020-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain AJ 26–85（60 aa） Chain J 26–85（60 aa）	Not recorded	CDL CARDIOLIPIN × 6 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 13.10 Å
9W2R Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1) Deposited 2025-07-28	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 × 29 PDB declaration: 29-meric	Chain J 26–85（60 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9W2S Cryo-EM structure of FoF1-ATPase monomer state 3 on the bovine heart submitochondrial particles (FoF1-2) Deposited 2025-07-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric	Chain J 26–85（60 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IATP_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–41； UniProt 69–109 Author chain B； PDBConstruct 1–41； UniProt 69–109

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	1hf9
Deposition date deposition_date	2000-11-30
Structure title title	C-Terminal Coiled-Coil Domain from Bovine IF1
Keywords keywords	ATPASE INHIBITOR, F1 ATPASE INHIBITOR, MITOCHONDRION, TRANSIT PEPTIDE; ATPASE INHIBITOR
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	18.29 Å
Radius of gyration Rg (electron density) rg_electron	18.49 Å
Forward intensity I(0) i0	1932430000.00
Molecular weight molecular_weight	348920.0 kDa
Excluded volume excluded_volume	428320 Å³
Envelope volume envelope_volume	37486 Å³
Hydration-shell volume shell_volume	15761 Å³
Envelope diameter envelope_diameter	75.3 Å
Shell Rg shell_rg	27.33 Å
Envelope Rg envelope_rg	22.80 Å
Shape Rg shape_rg	18.47 Å
Total Rg total_rg	18.65 Å
Total atoms total_atoms	49630
Residues n_residues	2870
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	72.0 Å
Rg (real space) rg_real	18.66 Å
Rg uncertainty (real space) rg_real_error	0.91 Å
I(0) (real space) i0_real	1.9320e+09
I(0) uncertainty (real space) i0_real_error	3.0180e+07
Rg (reciprocal space) rg_reciprocal	18.61 Å
I(0) (reciprocal space) i0_reciprocal	1932000000.0000
Solution quality estimate total_estimate	0.6893
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	13.6 Å
Skewness Skewness skewness	0.627
Kurtosis Kurtosis kurtosis	-0.384
Angular range angular_range	— – 0.4350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	195100.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.304; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.046; Smooth: 1.000

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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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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1hf9a_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.8 — F1 ATPase inhibitor, IF1, C-terminal domain
Family Family family	h.4.8.1 — F1 ATPase inhibitor, IF1, C-terminal domain

Domain ID domain_id	d1hf9b_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.8 — F1 ATPase inhibitor, IF1, C-terminal domain
Family Family family	h.4.8.1 — F1 ATPase inhibitor, IF1, C-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id	1hf9A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	500 — Single helix bin

Domain ID domain_id	1hf9B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	500 — Single helix bin

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	ATPASE INHIBITOR (MITOCHONDRIAL)
Molecular weight formula_weight	4999.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	49630

来源生物 organism	BOS TAURUS
通用名 common_name	COW
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	ESCHERICHIA COLI

C-Terminal Coiled-Coil Domain from Bovine IF1

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

ATPASE INHIBITOR (MITOCHONDRIAL)

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/hf/1hf9/1hf9.fit
pddf	/app/data/pr_computation/hf/1hf9/1hf9.pr.out
profile	/app/data/saxs_computation/hf/1hf9/1hf9.dat