5whp

Crystal structure of the segment, NFGTFS, from the A315T familial variant of the low complexity domain of TDP-43, residues 312-317

Method: X-RAY DIFFRACTION D_max: 25.3 Å Quality: GOOD

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

Segment of TAR DNA-binding protein 43

OrganismNot specified

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 312–317	Fragment：UNP residues 312-317 Mutation：A315T	No other associated polymer	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

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 5WHP	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 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 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 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 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 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 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 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 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 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 method 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 method 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 method 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 mutation/modification Different oligomeric state 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
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 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 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 mutation/modification 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 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 experimental method Different experimental conditions 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 experimental method Different experimental conditions 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 experimental method Different experimental conditions 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 experimental method Different experimental conditions 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 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 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 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 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 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 oligomeric state Different experimental method 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 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 experimental method Different experimental conditions 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 mutation/modification Different oligomeric state Different experimental method 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
8CG3 Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 1) Deposited 2023-02-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions 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 2.39 Å
8CGG Structure of TDP-43 amyloid filament from type A FTLD-TDP (variant 2) Deposited 2023-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions 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 construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions 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 experimental method Different experimental conditions 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 experimental method Different experimental conditions 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 experimental method Different experimental conditions 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 method 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 mutation/modification Different oligomeric state Different experimental method Different experimental conditions 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 1–6； UniProt 312–317

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	5whp
Deposition date deposition_date	2017-07-17
Structure title title	Crystal structure of the segment, NFGTFS, from the A315T familial variant of the low complexity domain of TDP-43, residues 312-317
Keywords keywords	Amyloid, LARKS, TDP-43, PROTEIN FIBRIL; PROTEIN FIBRIL
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	6.92 Å
Radius of gyration Rg (electron density) rg_electron	5.63 Å
Forward intensity I(0) i0	23750.80
Molecular weight molecular_weight	671.7 kDa
Excluded volume excluded_volume	831 Å³
Envelope volume envelope_volume	937 Å³
Hydration-shell volume shell_volume	1916 Å³
Envelope diameter envelope_diameter	20.2 Å
Shell Rg shell_rg	9.04 Å
Envelope Rg envelope_rg	6.02 Å
Shape Rg shape_rg	5.64 Å
Total Rg total_rg	7.50 Å
Total atoms total_atoms	48
Residues n_residues	6
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	25.3 Å
Rg (real space) rg_real	6.96 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	2.3750e+04
I(0) uncertainty (real space) i0_real_error	2.4340e+02
Rg (reciprocal space) rg_reciprocal	6.96 Å
I(0) (reciprocal space) i0_reciprocal	23750.0000
Solution quality estimate total_estimate	0.8356
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	24.4 Å
Skewness Skewness skewness	0.445
Kurtosis Kurtosis kurtosis	-0.038
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1579.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.687; Smooth: 0.798

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	15.330 Å
Unit-cell length b length_b	4.840 Å
Unit-cell length c length_c	23.570 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.91 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.000 Å
Low-resolution limit resolution_low	15.220 Å
R factor r_factor	0.0873
R_work r_work	0.0866
R_free r_free	0.0929

Description description	Segment of TAR DNA-binding protein 43
Molecular weight formula_weight	671.7 kDa
Mutation mutation	A315T
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	51

Crystal structure of the segment, NFGTFS, from the A315T familial variant of the low complexity domain of TDP-43, residues 312-317

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

Segment of 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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	3

fit	/app/data/saxs_computation/wh/5whp/5whp.fit
pddf	/app/data/pr_computation/wh/5whp/5whp.pr.out
profile	/app/data/saxs_computation/wh/5whp/5whp.dat