6clz

MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs

Method: SOLUTION NMR D_max: 119.9 Å Quality: GOOD

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

Matrix metalloproteinase-14

Homo sapiens

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 316–511	Fragment：residues 316-511	Apolipoprotein A-I × 2 （P02647） 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

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 6CLZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BQQ CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX Deposited 1998-08-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 114–287（174 aa）	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.60	Resolution 2.75 Å R-free 0.248
1BUV CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX Deposited 1998-09-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 114–287（174 aa）	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.6	Resolution 2.75 Å R-free 0.248
2MQS Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and Development: Spin Labels to Structure Deposited 2014-06-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 316–511（196 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；310 K；Ionic strength (raw mmCIF value) 10；Pressure ambient NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 10 mM；Pressure ambient NMR sample composition 300 uM [U-13C; U-15N; U-2H] Hemopexin-like (HPX) of MT1-MMP, 10 mM Sodium acetate, 1 mM EDTA, 1 mM Sodium azide, 93% H2O/7% D2O \| 93% H2O/7% D2O NMR sample composition 0.85 mM THP, 10 mM Sodium acetate, 1 mM EDTA, 1 mM Sodium azide, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
3C7X Hemopexin-like domain of matrix metalloproteinase 14 Deposited 2008-02-08	Different construct 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 316–511（196 aa） Fragment：UNP residues 316-511	Not recorded	NA SODIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；289 K；2.1M malic acid, 0.1M HCl, 40% acetone, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.70 Å R-free 0.207
3C7X Hemopexin-like domain of matrix metalloproteinase 14 Deposited 2008-02-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 316–511（196 aa） Fragment：UNP residues 316-511	Not recorded	NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；289 K；2.1M malic acid, 0.1M HCl, 40% acetone, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.70 Å R-free 0.207
3C7X Hemopexin-like domain of matrix metalloproteinase 14 Deposited 2008-02-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 316–511（196 aa） Fragment：UNP residues 316-511	Not recorded	NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；289 K；2.1M malic acid, 0.1M HCl, 40% acetone, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 1.70 Å R-free 0.207
3MA2 Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1) Deposited 2010-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 112–292（181 aa） Fragment：Residues 112-292	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；100 mM Bis-Tris pH 5.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.05 Å R-free 0.247
3MA2 Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1) Deposited 2010-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 112–292（181 aa） Fragment：Residues 112-292	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；292 K；100 mM Bis-Tris pH 5.5, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.05 Å R-free 0.247
3X23 Radixin complex Deposited 2014-12-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 563–582（20 aa） Fragment：cytoplasmic tail, UNP residues 563-582	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；297 K；12% polyethylene glycol 4000, 100mM MOPS (pH 7.0), 100mM NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 297K	Resolution 2.40 Å R-free 0.237
4P3C MT1-MMP:Fab complex (Form I) Deposited 2014-03-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain M 215–227（13 aa）	Not recorded	CL CHLORIDE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 EDO 1,2-ETHANEDIOL × 12 ACT ACETATE ION × 6 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% PEG 3350, 0.2M MgCl.hexahydrate, 0.1M Hepes	Resolution 1.94 Å R-free 0.200
4P3D MT1-MMP:Fab complex (Form II) Deposited 2014-03-07	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 C 215–227（13 aa） Fragment：MT1-MMP V-B loop Chain M 215–227（13 aa） Fragment：MT1-MMP V-B loop	Not recorded	CL CHLORIDE ION × 2 GOL GLYCEROL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 EDO 1,2-ETHANEDIOL × 3 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% PEG 3350, 0.2M MgCl.hexahydrate, 0.1M Hepes	Resolution 1.95 Å R-free 0.210
4QXU Novel Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling Conformational antibody Deposited 2014-07-22	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 K 218–228（11 aa） Fragment：peptide (unp residues 218-228)	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；0.1M (NH4)2SO4, 0.01M MgCl2 0.05M MES, 16% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.30 Å R-free 0.293
5H0U Crystal structure of the catalytic domain of membrane type 1 matrix metalloproteinase Deposited 2016-10-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 116–285（170 aa）	Not recorded	CA CALCIUM ION × 2 ZN ZINC ION × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Ammonium nitrate, PEG3350	Resolution 2.24 Å R-free 0.254
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs Deposited 2018-03-02	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 316–511（196 aa） Fragment：residues 316-511	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

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MMP14_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–196； UniProt 316–511

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 79–267 Chain C； UniProt 79–267	Fragment：residues 79-267	Matrix metalloproteinase-14 × 1 （P50281） 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6CLZ	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 conditions	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 conditions	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 conditions	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 conditions	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 conditions	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 ligand/ion Different experimental conditions	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 ligand/ion Different experimental conditions	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 oligomeric state Different ligand/ion Different experimental conditions	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 construct Different oligomeric state Different ligand/ion Different experimental conditions	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	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 method 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 ligand/ion Different experimental conditions	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 ligand/ion Different experimental conditions	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 ligand/ion Different experimental conditions	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
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs Deposited 2018-03-02	Different experimental conditions	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 oligomeric state Different ligand/ion Different experimental conditions	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 oligomeric state Different ligand/ion Different experimental conditions	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 oligomeric state Different ligand/ion Different experimental conditions	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 oligomeric state Different ligand/ion Different experimental conditions	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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental conditions	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-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] (~{Z})-octadec-9-enoate × 128 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 32	SOLUTION NMR NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
7RSE NMR-driven structure of the KRAS4B-G12D "alpha-beta" dimer on a lipid bilayer nanodisc Deposited 2021-08-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 68–265（198 aa） Chain E 68–265（198 aa）	Not recorded	GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2 7Q9 [(2~{R})-3-[oxidanyl-[2-(trimethyl-$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
8EQS Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc Deposited 2022-10-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 79–267（189 aa） Chain D 79–267（189 aa）	Not recorded	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
8VXJ The crystal structure of human apolipoprotein A-I in complex with Fab 55201 Deposited 2024-02-04	Different construct Different mutation/modification 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 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 oligomeric state 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 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 method 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 method 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 method 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 B； PDBConstruct 1–211； UniProt 79–267 Author chain C； PDBConstruct 1–211； 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	6clz
Deposition date deposition_date	2018-03-02
Structure title title	MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs
Keywords keywords	MT1-MMP, MMP-14, Nanodisc, lipids, peripheral membrane protein, protease domain, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
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	46.39 Å
Radius of gyration Rg (electron density) rg_electron	39.81 Å
Forward intensity I(0) i0	45693400000.00
Molecular weight molecular_weight	3313600.0 kDa
Excluded volume excluded_volume	4783200 Å³
Envelope volume envelope_volume	497690 Å³
Hydration-shell volume shell_volume	93109 Å³
Envelope diameter envelope_diameter	127.1 Å
Shell Rg shell_rg	51.58 Å
Envelope Rg envelope_rg	41.17 Å
Shape Rg shape_rg	39.98 Å
Total Rg total_rg	38.59 Å
Total atoms total_atoms	538860
Residues n_residues	9270
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	119.9 Å
Rg (real space) rg_real	45.88 Å
Rg uncertainty (real space) rg_real_error	0.69 Å
I(0) (real space) i0_real	4.5690e+10
I(0) uncertainty (real space) i0_real_error	7.9670e+08
Rg (reciprocal space) rg_reciprocal	46.38 Å
I(0) (reciprocal space) i0_reciprocal	45720000000.0000
Solution quality estimate total_estimate	0.8287
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	70.5 Å
Skewness Skewness skewness	-0.333
Kurtosis Kurtosis kurtosis	-0.467
Angular range angular_range	— – 0.1700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7884000.0000
Real-space data points n_real_points	35
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Matrix metalloproteinase-14
Molecular weight formula_weight	23131.3 kDa
EC 编号 ec_number	3.4.24.80
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	538860

PNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSG

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 2 Entity 2 polymer

Description description	Apolipoprotein A-I
Molecular weight formula_weight	24912.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

STFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

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-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Molecular weight formula_weight	678.9 kDa
Source method src_method	syn
Copy count entity_count	218

Entity 4 Entity 4 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d6clza_
Class class	b — All beta proteins
Fold Fold fold	b.66 — 4-bladed beta-propeller
Superfamily Superfamily superfamily	b.66.1 — Hemopexin-like domain
Family Family family	b.66.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id	6clzA00
Class class	2 — Mainly Beta
Architecture architecture	110 — 4 Propeller
Topology topology	10 — Hemopexin
Homologous superfamily homologous superfamily	10 — Hemopexin-like domain

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8. Citations (1)

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fit	/app/data/saxs_computation/cl/6clz/6clz.fit
pddf	/app/data/pr_computation/cl/6clz/6clz.pr.out
profile	/app/data/saxs_computation/cl/6clz/6clz.dat

MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs

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

Matrix metalloproteinase-14

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

6. Entities and Polymers Entities & Polymers (5)

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

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)