1a1v

HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA

Method: X-RAY DIFFRACTION D_max: 71.4 Å Quality: EXCELLENT

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

PROTEIN (NS3 PROTEIN)

Hepatitis C virus (isolate H)

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–DNA Monomer Protein × 1 DNA 1 PDB declaration: dimeric（2） Consistent with all polymer counts	Chain A； UniProt 1193–1657	Fragment：HELICASE DOMAIN Mutation：;N-TERMINAL MET, K221Q, A277G, S301L, S332P, S410A, G530E, R582W, AND A 10 RESIDUE (GSGSHHHHHH) HISTIDINE TAG ATTACHED TO THE C-TERMINUS ; Non-standard monomer：Yes (specific site not provided by mmCIF)	;DNA (5'-D(UPUPUPUPUPUPUPU)-3') ; × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0	Resolution 2.20 Å R-free 0.287

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 1A1V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A1R HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX Deposited 1997-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1026–1205（180 aa） Fragment：PROTEASE DOMAIN Chain C 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN	Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.	Resolution 2.50 Å R-free 0.261
1A1R HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX Deposited 1997-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1026–1205（180 aa） Fragment：PROTEASE DOMAIN Chain D 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN	Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.	Resolution 2.50 Å R-free 0.261
1A1R HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX Deposited 1997-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1026–1205（180 aa） Fragment：PROTEASE DOMAIN Chain B 1026–1205（180 aa） Fragment：PROTEASE DOMAIN Chain C 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN Chain D 1677–1695（19 aa） Fragment：ACTIVATION DOMAIN	Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(ASMTGGQQMG) AT N-TERMINUS, INS(GSHHHHHH) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS Mutation：INS(KK) AT N-TERMINUS, C22S, INS(KK) AT C-TERMINUS	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.	Resolution 2.50 Å R-free 0.261
1CWX SOLUTION STRUCTURE OF THE HEPATITIS C VIRUS N-TERMINAL CAPSID PROTEIN 2-45 [C-HCV(2-45)] Deposited 1999-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–45（44 aa） Fragment：N-TERMINAL FRAGMENT	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.9；293 K；Ionic strength (raw mmCIF value) 0.1M NACL；Pressure AMBIENT NMR sample composition 40% D2-TRIFLUOROETHANOL;0.01M SODIUM PHOSPHATE;0.1M NACL	Resolution not provided
1HEI STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN Deposited 1997-03-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1206–1656（451 aa） Chain B 1206–1656（451 aa）	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；50MM CA ACETATE, 20MM NACACODYLATE PH 6.5, 8% PEG5000	Resolution 2.10 Å R-free 0.320
1JR6 Solution Structure of an Engineered Arginine-rich Subdomain 2 of the Hepatitis C Virus NS3 RNA Helicase Deposited 2001-08-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1353–1507（155 aa） Fragment：arginine-rich subdomain 2	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 75 mM KiPO4；Pressure ambient NMR sample composition 0.6 mM, U-15N,13C; \| 75 mM PHOSPHATE BUFFER; 5 mM DTT, 90%H2O, 10%D2O, 0.015% NaN3 NMR sample composition 0.6 mM, U-15N,13C; \| 75 mM PHOSPHATE BUFFER; 5 mM DTT, 99%D2O, 0.015% NaN3 NMR sample composition 0.3 mM, U-15N \| 75 mM PHOSPHATE BUFFER; 5 mM DTT, 90%H2O, 10%D2O, 0.015% NaN3	Resolution not provided
1N1L CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X) Deposited 2002-10-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1026–1205（180 aa） Fragment：Protease domain	Mutation：A164T	ZN ZINC ION × 1 TRL {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；Inhibitor soaked into crystal generated according to Kim et al. (1996) Cell, 87, 343-355, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.220
1N1L CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X) Deposited 2002-10-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1026–1205（180 aa） Fragment：Protease domain	Mutation：A164T	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；Inhibitor soaked into crystal generated according to Kim et al. (1996) Cell, 87, 343-355, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.220
1N1L CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X) Deposited 2002-10-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1026–1205（180 aa） Fragment：Protease domain Chain B 1026–1205（180 aa） Fragment：Protease domain	Mutation：A164T Mutation：A164T	ZN ZINC ION × 2 TRL {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；Inhibitor soaked into crystal generated according to Kim et al. (1996) Cell, 87, 343-355, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.220
1ONB Solution structure of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase Deposited 2003-02-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1353–1507（155 aa） Fragment：Arginine-rich subdomain 2	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 75 mM KIPO4；Pressure ambient NMR sample composition 0.6 mM, U-15N,13C \| 90% H2O/10% D2O NMR sample composition 0.6 mM, U-15N,13C \| 99.9%D2O	Resolution not provided
1R7C NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure, Sample in 50% tfe) Deposited 2003-10-21	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 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 OF SWISS-PROT SEQUENCE P27958)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；293 K；Pressure ambient NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 \| H2O/TFEd2 50/50 (v/v)	Resolution not provided
1R7D NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Ensemble of 51 structures, sample in 50% tfe) Deposited 2003-10-21	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 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 of Swiss-Prot sequence P27958)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；293 K；Pressure ambient NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 \| H2O/TFEd2 50/50 (v/v)	Resolution not provided
1R7E NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure. Sample in 100mM SDS). Deposited 2003-10-21	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 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 OF SWISS-PROT SEQUENCE P27958)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；313 K；Pressure ambient NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 \| 100mM SDS in H2O/D2O 95/5 (v/v)	Resolution not provided
1R7F NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Ensemble of 43 structures. Sample in 100mM SDS) Deposited 2003-10-21	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 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 of Swiss-Prot sequence P27958)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；313 K；Pressure ambient NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 \| 100mM SDS in H2O/D2O 95/5 (v/v)	Resolution not provided
1R7G NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure, Sample in 100mM DPC) Deposited 2003-10-21	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 1973–2003（31 aa） Fragment：Nonstructural protein NS5A (P56)(residues 1973-2003 OF SWISS-PROT SEQUENCE P27958)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；313 K；Pressure ambient NMR sample composition 1.2mM NS5A[1-31], 10mM DTTd10 \| 100mM DPC in H2O/D2O 95/5 (v/v)	Resolution not provided
1RGQ M9A HCV Protease complex with pentapeptide keto-amide inhibitor Deposited 2003-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1026–1206（181 aa） Fragment：RESIDUES 1027-1207 Chain B 1026–1206（181 aa） Fragment：RESIDUES 1027-1207	Not recorded	ZN ZINC ION × 2 AKP N-(PYRAZIN-2-YLCARBONYL)LEUCYLISOLEUCYL-N~1~-{1-[2-({1-CARBOXY-2-[4-(PHOSPHONOOXY)PHENYL]ETHYL}AMINO)-1,1-DIHYDROXY-2-OXOETHYL]BUT-3-ENYL}-3-CYCLOHEXYLALANINAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.2M N/KPO4, 2.0M NaCl, 10mM MES, 15% glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.312
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 902–1025（124 aa） Fragment：protease domain of NS2 Chain B 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	BOG octyl beta-D-glucopyranoside × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.28 Å R-free 0.268
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 902–1025（124 aa） Fragment：protease domain of NS2 Chain D 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	BOG octyl beta-D-glucopyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.28 Å R-free 0.268
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 902–1025（124 aa） Fragment：protease domain of NS2 Chain F 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	BOG octyl beta-D-glucopyranoside × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.28 Å R-free 0.268
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 902–1025（124 aa） Fragment：protease domain of NS2 Chain H 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	BOG octyl beta-D-glucopyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.28 Å R-free 0.268
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 902–1025（124 aa） Fragment：protease domain of NS2 Chain J 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	BOG octyl beta-D-glucopyranoside × 2 DMU DECYL-BETA-D-MALTOPYRANOSIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.28 Å R-free 0.268
2HD0 Structure of the catalytic domain of hepatitis C virus NS2 Deposited 2006-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain K 902–1025（124 aa） Fragment：protease domain of NS2 Chain L 902–1025（124 aa） Fragment：protease domain of NS2	Not recorded	BOG octyl beta-D-glucopyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris pH 8.5 0.8 M Ammonium Acetate 0.25 M Lithium Chloride 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.28 Å R-free 0.268
2JXF The solution structure of HCV NS4B(40-69) Deposited 2007-11-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1751–1780（30 aa） Fragment：Non-structural protein 4B, UNP residues 1751-1780	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1mM NS4B(40-69); 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O \| 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O	Resolution not provided
2KDR Solution structure of HCV NS4B(227-254) Deposited 2009-01-15	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 X 1938–1965（28 aa） Fragment：UNP residues 1938-1965	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) none；Pressure ambient NMR sample composition 2mM protein-1, 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O \| 50% v/v Trifluoro Ethanol D2OH; 50% v/v H2O	Resolution not provided
2N1P Structure of the C-terminal membrane domain of HCV NS5B protein Deposited 2015-04-15	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 2982–3011（30 aa） Fragment：C-terminal domain (UNP residues 2982-3011)	Mutation：C14S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions 298 K；Pressure ambient NMR sample composition 1.4 mM protein, 1 M [U-2H] SDS, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2O8M Crystal structure of the S139A mutant of Hepatitis C Virus NS3/4A protease Deposited 2006-12-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1677–1695（19 aa） Chain D 1677–1695（19 aa）	Not recorded	ZN ZINC ION × 2 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1.25 to 1.5M NaCl, 0.1 M MES, .1M Na/K PO4, 5mM beta-mercaptoethanol, pH 5.6-6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.228
2OBQ Discovery of the HCV NS3/4A Protease Inhibitor SCH503034. Key Steps in Structure-Based Optimization Deposited 2006-12-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1677–1695（19 aa） Chain D 1677–1695（19 aa）	Mutation：C22S Mutation：C22S	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；The protein (NS3 complexed with KK-NS4a(21-39)-KK peptide) was at 12-15 mg/ml in 15 mM MES, pH 6.5 1 M NaCl 20 mM b-mercaptoethanol. Hanging Drops were formed by mixing 4:l protein solution with 4:l {0.75-1.0 M NaCl, 0.1M Na/K phosphate 0.1 M Mes, pH 5.8-6.1 20 mM b-mercaptoethanol} The drop was equilibrated the drops over 1 ml {(1.25-1.50 M) NaCl - 0.1M Na/K phosphate 0.1 M Mes, pH 5.6-5.8, 20 mM b-mercaptoethanol} , VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.264
2XI2 HCV-H77 NS5B Apo Polymerase Deposited 2010-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990	Mutation：YES	SO4 SULFATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES 0.1M PH 6.5, AMMONIUM SULFATE 0.2M, PEG 5000 MONOMETHYL ETHER	Resolution 1.80 Å R-free 0.207
2XI2 HCV-H77 NS5B Apo Polymerase Deposited 2010-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990	Mutation：YES	SO4 SULFATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES 0.1M PH 6.5, AMMONIUM SULFATE 0.2M, PEG 5000 MONOMETHYL ETHER	Resolution 1.80 Å R-free 0.207
2XI2 HCV-H77 NS5B Apo Polymerase Deposited 2010-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990	Mutation：YES	SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES 0.1M PH 6.5, AMMONIUM SULFATE 0.2M, PEG 5000 MONOMETHYL ETHER	Resolution 1.80 Å R-free 0.207
2XI3 HCV-H77 NS5B Polymerase Complexed With GTP Deposited 2010-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990	Mutation：YES	GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES 50MM PH 6.5, AMMONIUM SULFATE 0.2M, AMMONIUM ACETATE 0.25M, PEG 1000 25%-30%	Resolution 1.70 Å R-free 0.198
2XI3 HCV-H77 NS5B Polymerase Complexed With GTP Deposited 2010-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2421–2990（570 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 2421-2990	Mutation：YES	GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；MES 50MM PH 6.5, AMMONIUM SULFATE 0.2M, AMMONIUM ACETATE 0.25M, PEG 1000 25%-30%	Resolution 1.70 Å R-free 0.198
4JZN Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-1 Deposited 2013-04-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM TRIS pH 8.0 19% PEG4000 170mM Lithium Sulfate 15% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.05 Å R-free 0.235
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.22 Å R-free 0.236
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.22 Å R-free 0.236
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.22 Å R-free 0.236
4JZO Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27 Deposited 2013-04-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 434–446（13 aa） Fragment：Residues 434-446 of HCV strain H77 polyprotein	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；23% PEG 3350 250mM Sodium Thiocyanate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.22 Å R-free 0.236
4MWF Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C Deposited 2013-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 412–459（48 aa） Chain D 486–645（160 aa）	Mutation：N448D, N576D Mutation：N448D, N576D	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；20% (w/v) PEG 4000, 10% (v/v) isopropanol, and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.65 Å R-free 0.270
4MWF Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C Deposited 2013-09-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 412–459（48 aa） Chain C 486–645（160 aa）	Mutation：N448D, N576D Mutation：N448D, N576D	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；20% (w/v) PEG 4000, 10% (v/v) isopropanol, and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.65 Å R-free 0.270
4Q0X Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2 Deposited 2014-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 421–446（26 aa） Fragment：epitope II (UNP residues 421-446)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1 M imidazole, 14% w/v PEG550 MME, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.90 Å R-free 0.285
5FGB Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.4 Deposited 2015-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 405–425（21 aa）	Not recorded	GOL GLYCEROL × 2 SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；100 mM sodium citrate pH 5.2 300 mM ammonium sulfate 100 mM potassium phosphate 1 M lithium chloride	Resolution 1.65 Å R-free 0.190
5FGB Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.4 Deposited 2015-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 405–425（21 aa）	Not recorded	GOL GLYCEROL × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；293 K；100 mM sodium citrate pH 5.2 300 mM ammonium sulfate 100 mM potassium phosphate 1 M lithium chloride	Resolution 1.65 Å R-free 0.190
5FGC Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.8 Deposited 2015-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 405–425（21 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；32% PEG 4000 100 mM Tris-HCl pH 8.5 800 mM lithium chloride Crystals obtained using heterologous microseeding.	Resolution 1.90 Å R-free 0.236

26 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLG_HCVH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 2–466； UniProt 1193–1657

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	1a1v
Deposition date deposition_date	1997-12-17
Structure title title	HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA
Keywords keywords	HEPATITIS C VIRUS, RNA HELICASE, NONSTRUCTURAL PROTEINS, SINGLE-STRANDED DNA, HYDROLASE-DNA COMPLEX; HYDROLASE/DNA
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	23.60 Å
Radius of gyration Rg (electron density) rg_electron	23.04 Å
Forward intensity I(0) i0	39426300.00
Molecular weight molecular_weight	47607.0 kDa
Excluded volume excluded_volume	59148 Å³
Envelope volume envelope_volume	69362 Å³
Hydration-shell volume shell_volume	25365 Å³
Envelope diameter envelope_diameter	73.6 Å
Shell Rg shell_rg	29.93 Å
Envelope Rg envelope_rg	23.00 Å
Shape Rg shape_rg	23.06 Å
Total Rg total_rg	23.75 Å
Total atoms total_atoms	4009
Residues n_residues	436
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	71.4 Å
Rg (real space) rg_real	23.51 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	3.9430e+07
I(0) uncertainty (real space) i0_real_error	5.1170e+05
Rg (reciprocal space) rg_reciprocal	23.53 Å
I(0) (reciprocal space) i0_reciprocal	39430000.0000
Solution quality estimate total_estimate	0.9134
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.6 Å
Skewness Skewness skewness	0.211
Kurtosis Kurtosis kurtosis	-0.563
Angular range angular_range	— – 0.3350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8763000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.971

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(UPUPUPUPUPUPUPU)-3') ;
Molecular weight formula_weight	2276.4 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	B
Atom count atom_count	4486

UUUUUUUU

Entity 2 Entity 2 polymer

Description description	PROTEIN (NS3 PROTEIN)
Molecular weight formula_weight	51362.3 kDa
Mutation mutation	;N-TERMINAL MET, K221Q, A277G, S301L, S332P, S410A, G530E, R582W, AND A 10 RESIDUE (GSGSHHHHHH) HISTIDINE TAG ATTACHED TO THE C-TERMINUS ;
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MVDFIPVENLETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTGSGSHHHHHH

来源 Source

来源生物 organism	Hepatitis C virus (isolate H)
NCBI Class编号 ncbi_taxonomy_id	11108
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	159

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1a1va1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.14 — RNA helicase

Domain ID domain_id	d1a1va2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.14 — RNA helicase

CATH v4.4 (3 domains)

Domain ID domain_id	1a1vA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1a1vA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1a1vA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	820 — RNA Helicase; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — RNA Helicase Chain A , domain 3

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8. Citations (1)

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Unit-cell length a length_a	73.100 Å
Unit-cell length b length_b	117.500 Å
Unit-cell length c length_c	63.400 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.2280
R_work r_work	0.2280
R_free r_free	0.2870

fit	/app/data/saxs_computation/a1/1a1v/1a1v.fit
pddf	/app/data/pr_computation/a1/1a1v/1a1v.pr.out
profile	/app/data/saxs_computation/a1/1a1v/1a1v.dat

HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA

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

PROTEIN (NS3 PROTEIN)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)