8eqs

Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc

Method: ELECTRON MICROSCOPY D_max: 81.9 Å Quality: GOOD

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

ORF3a protein

Severe acute respiratory syndrome coronavirus

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–274 Chain B； UniProt 1–274	Not recorded	Apolipoprotein A-I × 2 （P02647） PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.10 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	AP3A_SARS
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–274； UniProt 1–274 Author chain B； PDBConstruct 1–274； UniProt 1–274

Apolipoprotein A-I

Homo sapiens

UniProt P02647

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 79–267 Chain D； UniProt 79–267	Not recorded	ORF3a protein × 2 （P59632） PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.10 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8EQS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AV1 CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I Deposited 1997-09-23	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 × 4 PDB declaration: tetrameric	Chain A 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN Chain B 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN Chain C 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN Chain D 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN	Mutation：N-TERMINAL MET, DEL(1-43) Mutation：N-TERMINAL MET, DEL(1-43) Mutation：N-TERMINAL MET, DEL(1-43) Mutation：N-TERMINAL MET, DEL(1-43)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；277 K；PROTEIN WAS CRYSTALLIZED FROM 1.2 M NA CITRATE, 100 MM HEPES, PH 7.5 AT 4 DEGREES CELSIUS. CRYSTALS WERE STABILIZED IN 1.4 M NA CITRATE, 100 MM HEPES, PH 7.5., temperature 277K	Resolution 4.00 Å R-free 0.428
1GW3 THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE Deposited 1997-06-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 166–211（46 aa） Fragment：RESIDUES 142 - 187	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.9；310 K	Resolution not provided
1GW4 THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE Deposited 1997-06-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 166–211（46 aa） Fragment：RESIDUES 142 - 187	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.9；323 K	Resolution not provided
1ODP PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.6, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40 Deposited 1996-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 190–209（20 aa） Fragment：RESIDUES 166 - 185	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；310 K	Resolution not provided
1ODQ PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40 Deposited 1996-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 190–209（20 aa） Fragment：RESIDUES 166 - 185	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.7；310 K	Resolution not provided
1ODR PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.0, 37 DEGREES CELSIUS AND PEPTIDE:DPC MOLE RATIO OF 1:40 Deposited 1996-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 190–209（20 aa） Fragment：RESIDUES 166 - 185	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；310 K	Resolution not provided
2MSC NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc Deposited 2014-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient NMR sample composition 20 mM TRIS-1, 100 mM sodium chloride-2, 2 mM TCEP-3, 5 mM MgCl2-4, 0.6 mM U-15N, Ile C-delta-13C K-Ras-5, 0.6 mM membrane scaffold protein-6, 0.6 mM GUANOSINE-5'-DIPHOSPHATE-7, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-8, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-9, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-10, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 20 mM TRIS-11, 100 mM sodium chloride-12, 2 mM TCEP-13, 5 mM Magnesium-14, 0.6 mM U-15N, Ile C-delta-13C K-Ras-15, 0.6 mM membrane scaffold protein-16, 0.6 mM GUANOSINE-5'-DIPHOSPHATE-17, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-18, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-19, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-20, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-21, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MSD NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc Deposited 2014-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 68–265（198 aa） Fragment：UNP RESIDUES 68-265 Chain C 68–265（198 aa） Fragment：UNP RESIDUES 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-1, 0.6 mM membrane scaffold protein-2, 20 mM TRIS-3, 100 mM sodium chloride-4, 2 mM TCEP-5, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-6, 5 mM Magnesium-7, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-8, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-9, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-10, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-11, 0.6 mM membrane scaffold protein-12, 20 mM TRIS-13, 100 mM sodium chloride-14, 5 mM Magnesium-15, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-16, 2 mM TCEP-17, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-18, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-19, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-20, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-21, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MSE NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc Deposited 2014-07-29	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-1, 0.6 mM membrane scaffold protein-2, 0.7 mM A-RafRBD-3, 100 mM sodium chloride-4, 5 mM Magnesium-5, 20 mM TRIS-6, 2 mM TCEP-7, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-8, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-9, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-10, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-11, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.7 mM K-Ras-12, 0.7 mM membrane scaffold protein-13, 0.6 mM U-15N, Ile C-delta-13C A-RafRBD-14, 5 mM Magnesium-15, 20 mM TRIS-16, 100 mM sodium chloride-17, 2 mM TCEP-18, 0.7 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-19, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-20, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-21, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-22, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-23, 0.7 mM A-RafRBD-24, 0.6 mM membrane scaffold protein-25, 20 mM TRIS-26, 100 mM sodium chloride-27, 5 mM Magnesium-28, 2 mM TCEP-29, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-30, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-31, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-32, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-33, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-34, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.7 mM K-Ras-35, 0.6 mM U-15N, Ile C-delta-13C A-RafRBD-36, 0.7 mM membrane scaffold protein-37, 20 mM TRIS-38, 100 mM sodium chloride-39, 5 mM Magnesium-40, 2 mM TCEP-41, 0.7 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-42, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-43, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-44, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-45, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-46, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N5E The 3D solution structure of discoidal high-density lipoprotein particles Deposited 2015-07-15	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 A 79–267（189 aa） Chain B 79–267（189 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；316 K；Ionic strength (raw mmCIF value) 100；Pressure ambient NMR sample composition 0.5-1.0 mM [U-99% 13C; U-99% 15N] H2O, 1 mM stereospecific Methyl-labeling H2O, 1 mM selective unlabeling H2O, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3K2S Solution structure of double super helix model Deposited 2009-09-30	Different construct 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 A 25–267（243 aa） Chain B 25–267（243 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 200 CLR CHOLESTEROL × 20	SOLUTION SCATTERING mmCIF provides none of the parsed conditions	Resolution not provided
3R2P 2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals the Assembly of HDL by Dimerization. Deposited 2011-03-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 25–208（184 aa） Fragment：N-terminal domain (UNP 25-208)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；298 K；0.15M potassium bromide, 30% PEG 2000 MME, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.280
4V6M Structure of the ribosome-SecYE complex in the membrane environment Deposited 2011-02-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 55 PDB declaration: 60-meric	Chain A0 68–267（200 aa） Chain A1 68–267（200 aa）	Not recorded	PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 101 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 32	ELECTRON MICROSCOPY cryo-EM buffer 20 mM Hepes (pH 7.2), 100 mM KOAc, 10 mM Mg(OAc)2, 1 mM DTT, 250 microg/ml chloramphenicol；pH 7.2；20 mM Hepes (pH 7.2), 100 mM KOAc, 10 mM Mg(OAc)2, 1 mM DTT, 250 microg/ml chloramphenicol cryo-EM vitrification conditions Cryogen ETHANE；liquid ethane was used as a cryogen	Resolution 7.10 Å
6CC9 NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Deposited 2018-02-06	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 A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 EWS (2R,4S)-4-[(5-bromo-1H-indole-3-carbonyl)amino]-2-[(4-chlorophenyl)methyl]piperidin-1-ium × 1	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 100 mM NaCl；Pressure ambient NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 1 mM Cmpd2, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM [U-15N] GTPase KRas isoform b, 1 mM Cmpd2, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6CCH NMR data-driven model of GTPase KRas-GMPPNP tethered to a nanodisc (E3 state) Deposited 2018-02-07	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 A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 105；Pressure 1 NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 0.4 mM PE-DTPA-Gd, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6CCX NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Deposited 2018-02-07	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 A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 EWS (2R,4S)-4-[(5-bromo-1H-indole-3-carbonyl)amino]-2-[(4-chlorophenyl)methyl]piperidin-1-ium × 1	SOLUTION NMR NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 105；Pressure 1 NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 0.4 mM PE-DTPA-Gd, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6CLZ MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs Deposited 2018-03-02	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 B 79–267（189 aa） Fragment：residues 79-267 Chain C 79–267（189 aa） Fragment：residues 79-267	Not recorded	PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 218 NA SODIUM ION × 1 CL CHLORIDE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.2；303 K；Ionic strength (raw mmCIF value) 300；Pressure 1 NMR sample composition 20 mM Tris-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs Deposited 2018-03-02	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 B 79–267（189 aa） Fragment：residues 79-267 Chain C 79–267（189 aa） Fragment：residues 79-267	Not recorded	PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 218 NA SODIUM ION × 1 CL CHLORIDE ION × 1	SOLUTION NMR NMR measurement conditions pH 7.2；303 K；Ionic strength (raw mmCIF value) 300；Pressure 1 NMR sample composition 20 mM Tri-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
6PTS NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state A) Deposited 2019-07-16	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1 NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 150；Pressure 1 NMR sample composition 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C KRAS, 0.2 mM U-12C, 14N, 1H RBD-CRD, 0.4 mM U-12C, 14N, 1H MSP, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 0.4 mM U-12C, 14N, 1H MSP, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM U-15N; Ile C-delta-13C, Met methyl-13C KRAS, 0.5 mM Leu C-delta-13C, Val C-gamma-13C, RBD-CRD, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-99% 15N]; [U-13C]; RBD, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.3 mM [U-99% 15N]; [U-13C]; CRD, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6PTW NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state B) Deposited 2019-07-16	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 68–265（198 aa） Fragment：UNP residues 68-265 Chain C 68–265（198 aa） Fragment：UNP residues 68-265	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1 NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 150；Pressure 1 NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N; U-2H] KRAS, 0.2 mM [U-12C; U-14N; U-1H] RBD-CRD, 0.4 mM [U-12C; U-14N; U-1H] MSP, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM [U-12C; U-14N; U-1H] KRAS, 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N; U-2H] RBD-CRD, 0.4 mM [U-12C; U-14N; U-1H] MSP, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N] RBD-CRD, 0.2 mM [U-12C; U-14N; U-1H] KRAS Q43C, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N] RBD-CRD, 0.2 mM [U-12C; U-14N; U-1H] KRAS N-term C, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-15N; Ile C-delta-13C; Met methyl-13C] KRAS, 0.5 mM [Leu C-delta-13C; Val C-gamma-13C] RBD-CRD, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-13C; U-15N] RBD, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-13C; U-15N] CRD, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6W4E NMR-driven structure of KRAS4B-GTP homodimer on a lipid bilayer nanodisc Deposited 2020-03-10	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 68–265（198 aa） Chain D 68–265（198 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6W4F NMR-driven structure of KRAS4B-GDP homodimer on a lipid bilayer nanodisc Deposited 2020-03-10	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 68–265（198 aa） Chain D 68–265（198 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
7KJR Cryo-EM structure of SARS-CoV-2 ORF3a Deposited 2020-10-26	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 79–267（189 aa） Fragment：UNP residues 79-267 Chain D 79–267（189 aa） Fragment：UNP residues 79-267	Not recorded	PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；1 blot force 5 second wait time 3 second blot time	Resolution 2.08 Å
7RSC NMR-driven structure of the KRAS4B-G12D "alpha-alpha" dimer on a lipid bilayer nanodisc Deposited 2021-08-11	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 68–265（198 aa） Chain E 68–265（198 aa）	Not recorded	GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2 7Q9 [(2~{R})-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] (~{Z})-octadec-9-enoate × 128 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 32	SOLUTION NMR NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
7RSE NMR-driven structure of the KRAS4B-G12D "alpha-beta" dimer on a lipid bilayer nanodisc Deposited 2021-08-11	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 68–265（198 aa） Chain E 68–265（198 aa）	Not recorded	GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2 7Q9 [(2~{R})-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] (~{Z})-octadec-9-enoate × 128 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 32	SOLUTION NMR NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8VXJ The crystal structure of human apolipoprotein A-I in complex with Fab 55201 Deposited 2024-02-04	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 × 3 PDB declaration: trimeric	Chain C 25–267（243 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；15% PEG 6000, 0.1 M trisodium citrate-citric acid, pH 5.5, 0.02% NaN3	Resolution 2.70 Å R-free 0.298
8VXJ The crystal structure of human apolipoprotein A-I in complex with Fab 55201 Deposited 2024-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 25–267（243 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；15% PEG 6000, 0.1 M trisodium citrate-citric acid, pH 5.5, 0.02% NaN3	Resolution 2.70 Å R-free 0.298
9MXZ Lecithin:Cholesterol Acyltransferase Bound to Apolipoprotein A-I dimer in HDL Deposited 2025-01-21	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 25–267（243 aa） Chain E 25–267（243 aa）	Not recorded	6PL (4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE × 158	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.80 Å
9PVY Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I L90P amyloidosis patient Deposited 2025-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 25–267（243 aa） Chain B 25–267（243 aa） Chain C 25–267（243 aa） Chain D 25–267（243 aa） Chain E 25–267（243 aa） Chain F 25–267（243 aa） Chain G 25–267（243 aa） Chain H 25–267（243 aa） Chain I 25–267（243 aa） Chain J 25–267（243 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；H2O containing 5 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.15 Å
9PVZ Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient Deposited 2025-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 25–267（243 aa） Chain B 25–267（243 aa） Chain C 25–267（243 aa） Chain D 25–267（243 aa） Chain E 25–267（243 aa） Chain F 25–267（243 aa） Chain G 25–267（243 aa） Chain H 25–267（243 aa） Chain I 25–267（243 aa） Chain J 25–267（243 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；H2O containing 5 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9PW3 Cryo-EM structure of renal amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient Deposited 2025-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 25–267（243 aa） Chain B 25–267（243 aa） Chain C 25–267（243 aa） Chain D 25–267（243 aa） Chain E 25–267（243 aa） Chain F 25–267（243 aa） Chain G 25–267（243 aa） Chain H 25–267（243 aa） Chain I 25–267（243 aa） Chain J 25–267（243 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；H2O containing 5 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.73 Å

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	APOA1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 23–211； UniProt 79–267 Author chain D； PDBConstruct 23–211； UniProt 79–267

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8eqs
Deposition date deposition_date	2022-10-09
Structure title title	Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc
Keywords keywords	Membrane protein, SARS-CoV, SARS-CoV-2, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	24.35 Å
Radius of gyration Rg (electron density) rg_electron	23.80 Å
Forward intensity I(0) i0	39233000.00
Molecular weight molecular_weight	51702.0 kDa
Excluded volume excluded_volume	65946 Å³
Envelope volume envelope_volume	79955 Å³
Hydration-shell volume shell_volume	28125 Å³
Envelope diameter envelope_diameter	81.9 Å
Shell Rg shell_rg	30.88 Å
Envelope Rg envelope_rg	23.89 Å
Shape Rg shape_rg	23.81 Å
Total Rg total_rg	24.63 Å
Total atoms total_atoms	3654
Residues n_residues	438
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	81.9 Å
Rg (real space) rg_real	24.33 Å
Rg uncertainty (real space) rg_real_error	0.52 Å
I(0) (real space) i0_real	3.9230e+07
I(0) uncertainty (real space) i0_real_error	5.6690e+05
Rg (reciprocal space) rg_reciprocal	24.33 Å
I(0) (reciprocal space) i0_reciprocal	39230000.0000
Solution quality estimate total_estimate	0.8688
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	29.9 Å
Skewness Skewness skewness	0.395
Kurtosis Kurtosis kurtosis	-0.082
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6441000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.787; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.941

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	ORF3a protein
Molecular weight formula_weight	36268.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3654

MDLFMRFFTLGSITAQPVKIDNASPASTVHATATIPLQASLPFGWLVIGVAFLAVFQSATKIIALNKRWQLALYKGFQFICNLLLLFVTIYSHLLLVAAGMEAQFLYLYALIYFLQCINACRIIMRCWLCWKCKSKNPLLYDANYFVCWHTHNYDYCIPYNSVTDTIVVTEGDGISTPKLKEDYQIGGYSEDRHSGVKDYVVVHGYFTEVYYQLESTQITTDTGIENATFFIFNKLVKDPPNVQIHTIDGSSGVANPAMDPIYDEPTTTTSVPLGGRGLEVLFQGPGSGQLVGSGGLEGGGGWSHPQFEKGGGSGGGSGGGSWSHPQFEK

来源 Source

来源生物 organism	Severe acute respiratory syndrome coronavirus
通用名 common_name	SARS-CoV
NCBI Class编号 ncbi_taxonomy_id	2901879
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Apolipoprotein A-I
Molecular weight formula_weight	24704.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

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 3 Entity 3 non-polymer

Description description	1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
Molecular weight formula_weight	744.0 kDa
Source method src_method	syn
Copy count entity_count	2

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8. Citations (2)

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Resolution resolution	3.10 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	162607

fit	/app/data/saxs_computation/eq/8eqs/8eqs.fit
pddf	/app/data/pr_computation/eq/8eqs/8eqs.pr.out
profile	/app/data/saxs_computation/eq/8eqs/8eqs.dat

Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc

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

ORF3a protein

State in the Current Structure

Other States of the Same Protein in the Database

Apolipoprotein A-I

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)