8cg3

Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 1)

Method: ELECTRON MICROSCOPY D_max: 71.6 Å Quality: EXCELLENT

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

TAR DNA-binding protein 43

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 homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 1–414 Chain B； UniProt 1–414 Chain C； UniProt 1–414 Chain D； UniProt 1–414 Chain U； UniProt 1–414	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.39 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 8CG3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WF0 Solution structure of RRM domain in TAR DNA-binding protein-43 Deposited 2004-05-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 193–267（75 aa） Fragment：RRM domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 0.8mM U-15, 13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2CQG Solution structure of the RNA binding domain of TAR DNA-binding protein-43 Deposited 2005-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 96–185（90 aa） Fragment：RNA recognition motif	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 0.86mM 13C/15N-PROTEIN; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3 \| 90% H2O/10% D2O	Resolution not provided
2N2C NMR Structure of TDP-43 prion-like hydrophobic helix in DPC Deposited 2015-05-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 307–349（43 aa） Fragment：UNP residues 307-349	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；313 K；Ionic strength (raw mmCIF value) 1；Pressure ambient NMR sample composition 300 uM [U-100% 15N] entity-1, 60 mM DPC-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2N3X Solution Structure of TDP-43 Amyloidogenic Core Region Deposited 2015-06-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 311–360（50 aa） Fragment：UNP residues 311-360	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 80；Pressure ambient NMR sample composition 600 uM [U-99% 13C; U-99% 15N] GB1-TDP(311 - 360)-1, 20 mM sodium phosphate-2, 50 mM sodium chloride-3, 8 v/v [U-99% 2H] D2O-4, 0.02 v/v sodium azide-5, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
2N4G Solution Structure of the G335D Mutant of TDP-43 Amyloidogenic Core Region Deposited 2015-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 311–360（50 aa） Fragment：UNP residues 311-360	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 80；Pressure ambient NMR sample composition 600 uM [U-99% 13C; U-99% 15N] GB1-TDP(311-360)-G335D-1, 20 mM sodium phosphate-2, 50 mM sodium chloride-3, 8 % [U-99% 2H] D2O-4, 0.02 w/v sodium azide-5, 92 % H2O-6, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
2N4H Solution Structure of the Q343R Mutant of TDP-43 Amyloidogenic Core Region Deposited 2015-06-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 311–360（50 aa） Fragment：UNP residues 311-360	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 80；Pressure ambient NMR sample composition 600 uM [U-99% 13C; U-99% 15N] GB1-TDP(311-360)-Q343R-1, 20 mM sodium phosphate-2, 50 mM sodium chloride-3, 0.02 w/v sodium azide-4, 8 % [U-99% 2H] D2O-5, 92 % H2O-6, 92% H2O/8% D2O \| 92% H2O/8% D2O	Resolution not provided
2N4P Solution structure of the n-terminal domain of tdp-43 Deposited 2015-06-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–77（77 aa） Fragment：N-terminal residues 1-77	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.8；298 K；Pressure ambient NMR sample composition 0.5-0.7 mM [U-13C; U-15N] NTD, TCEP, CD3COOD/ CD3COO-Na+, NaN3, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4BS2 NMR structure of human TDP-43 tandem RRMs in complex with UG-rich RNA Deposited 2013-06-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 102–269（168 aa） Fragment：RNA BINDING DOMAIN, RESIDUES 102-269	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 50 NMR sample composition 94%WATER/6%D2O	Resolution not provided
4IUF Crystal Structure of Human TDP-43 RRM1 Domain in Complex with a Single-stranded DNA Deposited 2013-01-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 103–179（77 aa） Fragment：RRM1 Domain (UNP residues 103-179)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.12M CH3COONH4, 0.05M Bis-Tris, 16% PEG 3350, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.75 Å R-free 0.259
4Y00 Crystal Structure of Human TDP-43 RRM1 Domain with D169G Mutation in Complex with an Unmodified Single-stranded DNA Deposited 2015-02-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 101–191（91 aa） Fragment：UNP residues 101-191	Mutation：D169G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.05 M CH3COONH4, pH 5.0, 15% v/v Jeffamine ED-2001, pH 7.0	Resolution 3.00 Å R-free 0.295
4Y00 Crystal Structure of Human TDP-43 RRM1 Domain with D169G Mutation in Complex with an Unmodified Single-stranded DNA Deposited 2015-02-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain B 101–191（91 aa） Fragment：UNP residues 101-191	Mutation：D169G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.05 M CH3COONH4, pH 5.0, 15% v/v Jeffamine ED-2001, pH 7.0	Resolution 3.00 Å R-free 0.295
4Y00 Crystal Structure of Human TDP-43 RRM1 Domain with D169G Mutation in Complex with an Unmodified Single-stranded DNA Deposited 2015-02-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain C 101–191（91 aa） Fragment：UNP residues 101-191	Mutation：D169G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.05 M CH3COONH4, pH 5.0, 15% v/v Jeffamine ED-2001, pH 7.0	Resolution 3.00 Å R-free 0.295
4Y00 Crystal Structure of Human TDP-43 RRM1 Domain with D169G Mutation in Complex with an Unmodified Single-stranded DNA Deposited 2015-02-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain D 101–191（91 aa） Fragment：UNP residues 101-191	Mutation：D169G	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.05 M CH3COONH4, pH 5.0, 15% v/v Jeffamine ED-2001, pH 7.0	Resolution 3.00 Å R-free 0.295
4Y0F Crystal Structure of Human TDP-43 RRM1 Domain in Complex with an Unmodified Single-stranded DNA Deposited 2015-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 101–191（91 aa） Fragment：UNP residues 101-191	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.12M ammonium acetate, 0.08M BIS-TRIS, pH 5.5, 20% PEG 3350	Resolution 2.65 Å R-free 0.288
4Y0F Crystal Structure of Human TDP-43 RRM1 Domain in Complex with an Unmodified Single-stranded DNA Deposited 2015-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain B 101–191（91 aa） Fragment：UNP residues 101-191	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.12M ammonium acetate, 0.08M BIS-TRIS, pH 5.5, 20% PEG 3350	Resolution 2.65 Å R-free 0.288
5MRG Solution structure of TDP-43 (residues 1-102) Deposited 2016-12-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–102（102 aa） Fragment：N-terminal domain, UNP residues 1-102	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.9；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 0.35 mM 13C15N TDP-43(1-102), 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
5W50 Crystal structure of the segment, LIIKGI, from the RRM2 of TDP-43, residues 248-253 Deposited 2017-06-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 248–253（6 aa） Fragment：RRM2 peptide (UNP residues 248-253) Chain B 248–253（6 aa） Fragment：RRM2 peptide (UNP residues 248-253)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；298 K；100 mM CHES, pH 9.5, 20% PEG8000, 10 mM lithium hydroxide	Resolution 1.40 Å R-free 0.207
5W52 MicroED structure of the segment, DLIIKGISVHI, from the RRM2 of TDP-43, residues 247-257 Deposited 2017-06-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257)	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 8.5 cryo-EM vitrification conditions Cryogen ETHANE X-ray crystallization conditions BATCH；pH 8.5；310 K；50 mM CHES, pH 8.5	Resolution 1.40 Å R-free 0.306
5W7V CryoEM structure of the segment, DLIIKGISVHI, assembled into a triple-helical fibril Deposited 2017-06-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 270 PDB declaration: 270-meric	Chain 0 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 1 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 2 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 3 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 4 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 5 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 6 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 7 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 8 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
5W7V CryoEM structure of the segment, DLIIKGISVHI, assembled into a triple-helical fibril Deposited 2017-06-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric	Chain 0 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 1 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 2 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 3 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 4 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 5 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 6 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 7 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 8 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
5W7V CryoEM structure of the segment, DLIIKGISVHI, assembled into a triple-helical fibril Deposited 2017-06-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 9 PDB declaration: nonameric	Chain 0 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 1 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 2 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 3 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 4 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 5 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 6 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 7 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257) Chain 8 247–257（11 aa） Fragment：RRM2 peptide (UNP residues 247-257)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
5WHN Crystal structure of the segment, NFGAFS, from the low complexity domain of TDP-43, residues 312-317 Deposited 2017-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric	Chain A 312–317（6 aa） Fragment：UNP residues 312-317	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；100mM phosphate/citrate 4.2, 40% ethanol, 5% PEG 1000	Resolution 1.10 Å R-free 0.160
5WHP Crystal structure of the segment, NFGTFS, from the A315T familial variant of the low complexity domain of TDP-43, residues 312-317 Deposited 2017-07-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 312–317（6 aa） Fragment：UNP residues 312-317	Mutation：A315T	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；100mM sodium acetate 4.6, 200mM ammonium acetate, 30% PEG 4000	Resolution 1.00 Å R-free 0.093
5WIA Crystal structure of the segment, GNNSYS, from the low complexity domain of TDP-43, residues 370-375 Deposited 2017-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 370–375（6 aa） Fragment：UNP residues 370-375	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；100mM bis tris propane 8.5, 200mM sodium nitrate, 20% PEG 3350	Resolution 1.00 Å R-free 0.181
5WIQ Crystal structure of the segment, GFNGGFG, from the low complexity domain of TDP-43, residues 396-402 Deposited 2017-07-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 396–402（7 aa） Fragment：UNP residues 396-402 Chain B 396–402（7 aa） Fragment：UNP residues 396-402	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；298 K；100mM sodium acetate pH 4.5, 800mM sodium phosphate monobasic, 1200mM potassium phosphate dibasic	Resolution 1.25 Å R-free 0.168
5WKB MicroED structure of the segment, NFGEFS, from the A315E familial variant of the low complexity domain of TDP-43, residues 312-317 Deposited 2017-07-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 312–317（6 aa） Fragment：UNP residues 312-317	Mutation：A315E	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.5；1x PBS, pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE X-ray crystallization conditions Batch；pH 7.5；298 K；1x PBS, pH 7.5	Resolution 1.00 Å R-free 0.270
5WKD Crystal structure of the segment, GNNQGSN, from the low complexity domain of TDP-43, residues 300-306 Deposited 2017-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 300–306（7 aa） Fragment：UNP residues 300-306	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM Bis-Tris propane, pH 7.5, 200 mM sodium sulfate, 20% PEG3350	Resolution 1.80 Å R-free 0.195
5X4F Solution Structure of the N-terminal Domain of TDP-43 Deposited 2017-02-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–77（77 aa） Fragment：UNP residues 1-77	Mutation：C39S/C50S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.08；Pressure 1 NMR sample composition 1 mM U-99% 13C; U-99% 15N TDP(1-77)-GB1-C39/C50S, 20 mM sodium phosphate, 50 mM sodium chloride, 0.05 v/v sodium azide, 90 % H2O, 10 % D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6B1G Solution structure of TDP-43 N-terminal domain dimer. Deposited 2017-09-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–80（80 aa） Fragment：NTD domain Chain B 1–80（80 aa） Fragment：NTD domain	Mutation：S48E Mutation：Y4R	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure 1 NMR sample composition 0.7 mM [U-99% 13C; U-99% 15N] TDP-43 NTD S48E, 2.0 mM TDP-43 NTD Y4R, 20 mM HEPES, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.7 mM [U-99% 13C; U-99% 15N] TDP-43 NTD Y4R, 2 mM TDP-43 NTD S48E, 20 mM HEPES, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6CFH SWGMMGMLASQ segment from the low complexity domain of TDP-43 Deposited 2018-02-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 333–343（11 aa） Fragment：SWGMMGMLASQ segment Chain B 333–343（11 aa） Fragment：SWGMMGMLASQ segment	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE X-ray crystallization conditions Batch；pH 7.5；303 K；phosphate buffered saline, shaken for 80 hours	Resolution 1.50 Å R-free 0.313
6N37 SegA-sym, conformation of TDP-43 low complexity domain segment A sym Deposited 2018-11-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 195–244（50 aa） Chain B 195–244（50 aa） Chain C 195–244（50 aa） Chain D 195–244（50 aa） Chain E 195–244（50 aa） Chain F 195–244（50 aa） Chain G 195–244（50 aa） Chain H 195–244（50 aa） Chain I 195–244（50 aa） Chain J 195–244（50 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6N3A SegA-long, conformation of TDP-43 low complexity domain segment A long Deposited 2018-11-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain A 195–244（50 aa） Chain B 195–244（50 aa） Chain C 195–244（50 aa） Chain D 195–244（50 aa） Chain E 195–244（50 aa） Chain F 195–244（50 aa） Chain G 195–244（50 aa） Chain H 195–244（50 aa） Chain I 195–244（50 aa） Chain J 195–244（50 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
6N3B SegA-asym, conformation of TDP-43 low complexity domain segment A asym Deposited 2018-11-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 195–244（50 aa） Chain B 195–244（50 aa） Chain C 195–244（50 aa） Chain D 195–244（50 aa） Chain E 195–244（50 aa） Chain F 195–244（50 aa） Chain G 195–244（50 aa） Chain H 195–244（50 aa） Chain I 195–244（50 aa） Chain J 195–244（50 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6N3C SegB, conformation of TDP-43 low complexity domain segment A Deposited 2018-11-14	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 170–215（46 aa） Chain B 170–215（46 aa） Chain C 170–215（46 aa） Chain D 170–215（46 aa） Chain E 170–215（46 aa） Chain F 170–215（46 aa） Chain G 170–215（46 aa） Chain H 170–215（46 aa） Chain I 170–215（46 aa） Chain J 170–215（46 aa） Chain K 170–215（46 aa） Chain L 170–215（46 aa） Chain M 170–215（46 aa） Chain N 170–215（46 aa） Chain O 170–215（46 aa） Chain P 170–215（46 aa） Chain Q 170–215（46 aa） Chain R 170–215（46 aa） Chain S 170–215（46 aa） Chain T 170–215（46 aa）	Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E Mutation：A315E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
6T4B CRYSTAL STRUCTURE OF HUMAN TDP-43 N-TERMINAL DOMAIN AT 2.55 A RESOLUTION Deposited 2019-10-13	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 1–80（80 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.2M Sodium bromide, 0.1M Bis-Tris propane 6.5, 20% PEG 3350	Resolution 2.55 Å R-free 0.263
6T4B CRYSTAL STRUCTURE OF HUMAN TDP-43 N-TERMINAL DOMAIN AT 2.55 A RESOLUTION Deposited 2019-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1–80（80 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.2M Sodium bromide, 0.1M Bis-Tris propane 6.5, 20% PEG 3350	Resolution 2.55 Å R-free 0.263
6T4B CRYSTAL STRUCTURE OF HUMAN TDP-43 N-TERMINAL DOMAIN AT 2.55 A RESOLUTION Deposited 2019-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 1–80（80 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.2M Sodium bromide, 0.1M Bis-Tris propane 6.5, 20% PEG 3350	Resolution 2.55 Å R-free 0.263
6T4B CRYSTAL STRUCTURE OF HUMAN TDP-43 N-TERMINAL DOMAIN AT 2.55 A RESOLUTION Deposited 2019-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 1–80（80 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.2M Sodium bromide, 0.1M Bis-Tris propane 6.5, 20% PEG 3350	Resolution 2.55 Å R-free 0.263
6T4B CRYSTAL STRUCTURE OF HUMAN TDP-43 N-TERMINAL DOMAIN AT 2.55 A RESOLUTION Deposited 2019-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain I 1–80（80 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.2M Sodium bromide, 0.1M Bis-Tris propane 6.5, 20% PEG 3350	Resolution 2.55 Å R-free 0.263
7KWZ TDP-43 LCD amyloid fibrils Deposited 2020-12-02	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 151–298（148 aa） Chain B 151–298（148 aa） Chain C 151–298（148 aa） Chain D 151–298（148 aa） Chain E 151–298（148 aa）	Mutation：low complexity domain (UNP residues 151-298) Mutation：low complexity domain (UNP residues 151-298) Mutation：low complexity domain (UNP residues 151-298) Mutation：low complexity domain (UNP residues 151-298) Mutation：low complexity domain (UNP residues 151-298)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7N9H Structure of the mammalian importin a1 bound to the TDP-43 NLS Deposited 2021-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 79–102（24 aa） Fragment：Nuclear localization signal motif, residues 79-102	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；0.5M sodium citrate, 10 mM mercaptoethanol	Resolution 2.20 Å R-free 0.215
7PY2 Structure of pathological TDP-43 filaments from ALS with FTLD Deposited 2021-10-08	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–414（414 aa） Chain B 1–414（414 aa） Chain C 1–414（414 aa） Chain D 1–414（414 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.59 Å
7Q3U Cryo-EM structure of TDP43 core peptide amyloid fiber Deposited 2021-10-28	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 279–360（82 aa） Chain B 279–360（82 aa） Chain C 279–360（82 aa） Chain D 279–360（82 aa） Chain E 279–360（82 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8A6I Structure of the low complexity domain of TDP-43 (fragment 309-350) with methionine sulfoxide modifications Deposited 2022-06-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 309–350（42 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；288 K；Ionic strength (raw mmCIF value) 10；Pressure 1 NMR sample composition 500 uM [U-13C; U-15N] TDP-43 fragment 309-350, 20 mM HEPES, 10 mM potassium chloride, 5 mM MgCl2, 1 mM ATP, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8CGG Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 2) Deposited 2023-02-04	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–414（414 aa） Chain B 1–414（414 aa） Chain C 1–414（414 aa） Chain D 1–414（414 aa） Chain U 1–414（414 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å
8CGH Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 3) Deposited 2023-02-04	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–414（414 aa） Chain B 1–414（414 aa） Chain C 1–414（414 aa） Chain D 1–414（414 aa） Chain U 1–414（414 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.68 Å
8QX9 TDP-43 amyloid fibrils: Morphology-1a Deposited 2023-10-24	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: 12-meric	Chain A 1–414（414 aa） Chain B 1–414（414 aa） Chain C 1–414（414 aa） Chain D 1–414（414 aa） Chain E 1–414（414 aa） Chain F 1–414（414 aa） Chain G 1–414（414 aa） Chain H 1–414（414 aa） Chain I 1–414（414 aa） Chain J 1–414（414 aa） Chain K 1–414（414 aa） Chain L 1–414（414 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.76 Å
8QXA TDP-43 amyloid fibrils: Morphology-1b Deposited 2023-10-24	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: 12-meric	Chain A 1–414（414 aa） Chain B 1–414（414 aa） Chain C 1–414（414 aa） Chain D 1–414（414 aa） Chain E 1–414（414 aa） Chain F 1–414（414 aa） Chain G 1–414（414 aa） Chain H 1–414（414 aa） Chain I 1–414（414 aa） Chain J 1–414（414 aa） Chain K 1–414（414 aa） Chain L 1–414（414 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.05 Å
8QXB TDP-43 amyloid fibrils: Morphology-2 Deposited 2023-10-24	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric	Chain A 1–414（414 aa） Chain B 1–414（414 aa） Chain C 1–414（414 aa） Chain D 1–414（414 aa） Chain E 1–414（414 aa） Chain F 1–414（414 aa） Chain G 1–414（414 aa） Chain H 1–414（414 aa） Chain I 1–414（414 aa） Chain J 1–414（414 aa） Chain K 1–414（414 aa） Chain L 1–414（414 aa） Chain M 1–414（414 aa） Chain N 1–414（414 aa） Chain O 1–414（414 aa） Chain P 1–414（414 aa） Chain Q 1–414（414 aa） Chain R 1–414（414 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.86 Å
9FOF Structure of heteromeric amyloid filament of TDP-43 and AXNA11 from FTLD-TDP Type C (variant 2) Deposited 2024-06-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain A 282–345（64 aa） Chain C 282–345（64 aa） Chain E 282–345（64 aa） Chain G 282–345（64 aa） Chain I 282–345（64 aa） Chain q 282–345（64 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9FOR Structure of heteromeric amyloid filament of TDP-43 and AXNA11 from FTLD-TDP Type C (variant 1) Deposited 2024-06-12	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 284–345（62 aa） Chain C 284–345（62 aa） Chain E 284–345（62 aa） Chain G 284–345（62 aa） Chain o 284–345（62 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.75 Å

41 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TADBP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–414； UniProt 1–414 Author chain B； PDBConstruct 1–414； UniProt 1–414 Author chain C； PDBConstruct 1–414； UniProt 1–414 Author chain D； PDBConstruct 1–414； UniProt 1–414 Author chain U； PDBConstruct 1–414； UniProt 1–414

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	8cg3
Deposition date deposition_date	2023-02-03
Structure title title	Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 1)
Keywords keywords	;TDP-43, FTD, FTLD, amyloid, filaments, fibril, neurodegeneration, neurodegenerative disease, RBP, RNA-binding protein, LCD, low-complexity domain, frontotemporal dementia, frontotemporal lobar degeneration, pathological, RNA BINDING PROTEIN, PROTEIN FIBRIL ;; PROTEIN FIBRIL
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	23.31 Å
Radius of gyration Rg (electron density) rg_electron	22.53 Å
Forward intensity I(0) i0	44308000.00
Molecular weight molecular_weight	43728.0 kDa
Excluded volume excluded_volume	51409 Å³
Envelope volume envelope_volume	66298 Å³
Hydration-shell volume shell_volume	24683 Å³
Envelope diameter envelope_diameter	73.6 Å
Shell Rg shell_rg	29.22 Å
Envelope Rg envelope_rg	22.59 Å
Shape Rg shape_rg	22.54 Å
Total Rg total_rg	23.18 Å
Total atoms total_atoms	3040
Residues n_residues	445
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	71.6 Å
Rg (real space) rg_real	23.25 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	4.4310e+07
I(0) uncertainty (real space) i0_real_error	5.7930e+05
Rg (reciprocal space) rg_reciprocal	23.26 Å
I(0) (reciprocal space) i0_reciprocal	44310000.0000
Solution quality estimate total_estimate	0.9144
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.4 Å
Skewness Skewness skewness	0.210
Kurtosis Kurtosis kurtosis	-0.599
Angular range angular_range	— – 0.3400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12010000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.988

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

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

Resolution resolution	2.390 Å
Low-resolution limit resolution_low	86.000 Å
R factor r_factor	0.3913
R_work r_work	0.3913
R_free r_free	—

Resolution resolution	2.39 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	71963

Description description	TAR DNA-binding protein 43
Molecular weight formula_weight	44784.7 kDa
Source method src_method	man
Copy count entity_count	5

Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 1)

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

TAR DNA-binding protein 43

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Polymer type type	polypeptide(L)
Chain IDs strand_id	U,A,B,C,D
Atom count atom_count	3040

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	Homo sapiens

fit	/app/data/saxs_computation/cg/8cg3/8cg3.fit
pddf	/app/data/pr_computation/cg/8cg3/8cg3.pr.out
profile	/app/data/saxs_computation/cg/8cg3/8cg3.dat