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6e8g

CryoEM reconstruction of IST1-CHMP1B copolymer filament bound to ssDNA at 2.9 Angstrom resolution

Method: ELECTRON MICROSCOPY Dmax: 250.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

IST1 homolog

Homo sapiens

UniProt P53990

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count Chain A； UniProt 1–366 Chain BA； UniProt 1–366 Chain BB； UniProt 1–366 Chain C； UniProt 1–366 Chain DA； UniProt 1–366 Chain DB； UniProt 1–366 Chain E； UniProt 1–366 Chain FA； UniProt 1–366 Chain FB； UniProt 1–366 Chain G； UniProt 1–366 Chain HA； UniProt 1–366 Chain HB； UniProt 1–366 Chain I； UniProt 1–366 Chain JA； UniProt 1–366 Chain JB； UniProt 1–366 Chain K； UniProt 1–366 Chain LA； UniProt 1–366 Chain LB； UniProt 1–366 Chain M； UniProt 1–366 Chain NA； UniProt 1–366 Chain NB； UniProt 1–366 Chain O； UniProt 1–366 Chain PA； UniProt 1–366 Chain PB； UniProt 1–366 Chain Q； UniProt 1–366 Chain RA； UniProt 1–366 Chain RB； UniProt 1–366 Chain S； UniProt 1–366 Chain TA； UniProt 1–366 Chain TB； UniProt 1–366 Chain V； UniProt 1–366 Chain VA； UniProt 1–366 Chain X； UniProt 1–366 Chain XA； UniProt 1–366 Chain Z； UniProt 1–366 Chain ZA； UniProt 1–366 Not recorded Charged multivesicular body protein 1b × 36 （Q7LBR1） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；0 mm offset with 10 sec wait time and 2-4 sec blot Resolution 2.90 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 6E8G Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3FRR Structure of human IST1(NTD) - (residues 1-189)(P21) Deposited 2009-01-08 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 1–189（189 aa） Fragment：UNP residues 1-189
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；296 K；35% pentaethritol propexylate 180mM KCl 50 mM HEPES, pH 7.6 7% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 296K
Resolution 1.80 Å R-free 0.247
3FRS Structure of human IST1(NTD) (residues 1-189)(p43212) Deposited 2009-01-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 5–189（185 aa） Fragment：UNP residues 1-189
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；296 K；10mM Tris-HCL, pH 8.0, 350mM NaCl, 1mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 296K
Resolution 2.61 Å R-free 0.298
3JC1 Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer Deposited 2015-11-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 68 PDB declaration: 68-meric
Chain Aa 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ac 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ae 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ag 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ai 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ak 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Am 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ao 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Aq 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain As 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Au 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Aw 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ay 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ba 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bc 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Be 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bg 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bi 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bk 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bm 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bo 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bq 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bs 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bu 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Bw 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain By 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ca 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Cc 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ce 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Cg 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ci 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Ck 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Cm 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Chain Co 6–187（182 aa） Fragment：N-terminal domain (UNP residues 6-187)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 25 mM Tris, pH 8.0, 25 mM sodium chloride；pH 8；25 mM Tris, pH 8.0, 25 mM sodium chloride
cryo-EM vitrification conditions Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset)；Cryogen ETHANE；Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset), and plunged into liquid ethane (VITROBOT MARK III).
Resolution 4.00 Å
4U7E The crystal structure of the complex of LIP5 NTD and IST1 MIM Deposited 2014-07-30 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 341–364（24 aa） Fragment：UNP residues 341-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；30% (w/v) PEG5000MME, 0.1 M ammonium sulfate , 0.1 M MES
Resolution 1.60 Å R-free 0.201
4U7I Structure of the complex of Spartin MIT and IST1 MIM Deposited 2014-07-30 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 B 341–364（24 aa） Fragment：UNP residues 341-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；277 K；2.9 M Na-malonate
Resolution 1.79 Å R-free 0.220
4U7Y Structure of the complex of VPS4B MIT and IST1 MIM Deposited 2014-07-31 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 B 341–364（24 aa） Fragment：UNP residues 341-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；299 K；2.58 M Na-malonate
Resolution 2.50 Å R-free 0.271
4WZX ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins Deposited 2014-11-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 342–364（23 aa） Fragment：MIT-interacting motif (UNP residues 342-364)
Not recorded CO COBALT (II) ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；50mM MES pH 6.5, 5mM Cobalt chloride, 800mM ammonium sulfate
Resolution 1.39 Å R-free 0.180
6TZ4 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (right-handed) Deposited 2019-08-10 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric
Chain 01 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain AA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain AB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain B 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain CA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain CB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain D 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain EA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain EB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain F 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain GA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain GB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain H 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain IA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain IB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain J 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain KA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain KB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain L 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain MA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain MB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain N 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain OA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain OB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain P 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain QA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain QB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain R 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain SA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain SB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain T 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain UA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain W 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain WA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain Y 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain YA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.20 Å
6TZ5 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed) Deposited 2019-08-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 68 PDB declaration: 68-meric
Chain A 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain BA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain BB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain C 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain DA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain DB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain E 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain FA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain FB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain G 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain HA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain HB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain I 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain JA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain JB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain K 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain LA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain LB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain M 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain NA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain NB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain O 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain PA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain PB 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain Q 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain RA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain S 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain TA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain V 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain VA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain X 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain XA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain Z 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain ZA 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.10 Å
6TZA CryoEM reconstruction of ESCRT-III filament composed of IST1 NTD R16E K27E double mutant Deposited 2019-08-11 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric
Chain A 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain B 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain C 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain D 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain E 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain F 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain G 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain H 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain I 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain J 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain K 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain L 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain M 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Chain N 1–189（189 aa） Fragment：N-terminal domain (UNP residues 1-189)
Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E Mutation：R16E K27E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane.
Resolution 7.20 Å
7S7J Structure of Human SPASTIN-IST1 complex. Deposited 2021-09-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 342–364（23 aa） Fragment：UNP residues 342-364
Not recorded PG4 TETRAETHYLENE GLYCOL × 1 CA CALCIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；278 K；40% v/v PEG 300, 100 mM Sodium cacodylate / Hydrochloric acid pH=6.5, 200 mM Calcium Acetate
Resolution 1.15 Å R-free 0.157
8UC6 Calpain-7:IST1 Complex Deposited 2023-09-25 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 G 335–379（45 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；294 K；Both proteins were purified and concentrated to 20 mg/ml in buffer containing 25 mM Tris, pH 7.2, 150 mM NaCl, 1 mM TCEP, 0.5 mM EDTA. The proteins were mixed in a 1:2 molar ratio (CAPN7:IST1). Crystals grew at 21 C (294 K) in Rigaku Wizard Cryo condition D5 (25% (v/v) 1,2-Porpanediol, 100 mM Sodium phosphate dibasic/Citric acid pH 4.2, 5% (w/v) PEG 3000, 10% (v/v) Glycerol. Crystals were transferred briefly to crystallization buffer supplemented with 25% added glycerol prior to plunging in liquid nitrogen
Resolution 2.70 Å R-free 0.285
8UC6 Calpain-7:IST1 Complex Deposited 2023-09-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 335–379（45 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；294 K；Both proteins were purified and concentrated to 20 mg/ml in buffer containing 25 mM Tris, pH 7.2, 150 mM NaCl, 1 mM TCEP, 0.5 mM EDTA. The proteins were mixed in a 1:2 molar ratio (CAPN7:IST1). Crystals grew at 21 C (294 K) in Rigaku Wizard Cryo condition D5 (25% (v/v) 1,2-Porpanediol, 100 mM Sodium phosphate dibasic/Citric acid pH 4.2, 5% (w/v) PEG 3000, 10% (v/v) Glycerol. Crystals were transferred briefly to crystallization buffer supplemented with 25% added glycerol prior to plunging in liquid nitrogen
Resolution 2.70 Å R-free 0.285
8V2Q CHMP1B/IST1 ssRNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 182 PDB declaration: 182-meric
Chain B 1–364（364 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.95 Å
8V2R CryoEM of ssDNA bound CHMP1B/IST1 copolymer assembly Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain B 1–364（364 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
8V2S CHMP1B/IST1 dsDNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain B 1–364（364 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.72 Å

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IST1_HUMAN
Isoform P53990-4
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–366； UniProt 1–366 Author chain BA； PDBConstruct 1–366； UniProt 1–366 Author chain BB； PDBConstruct 1–366； UniProt 1–366 Author chain C； PDBConstruct 1–366； UniProt 1–366 Author chain DA； PDBConstruct 1–366； UniProt 1–366 Author chain DB； PDBConstruct 1–366； UniProt 1–366 Author chain E； PDBConstruct 1–366； UniProt 1–366 Author chain FA； PDBConstruct 1–366； UniProt 1–366 Author chain FB； PDBConstruct 1–366； UniProt 1–366 Author chain G； PDBConstruct 1–366； UniProt 1–366 Author chain HA； PDBConstruct 1–366； UniProt 1–366 Author chain HB； PDBConstruct 1–366； UniProt 1–366 Author chain I； PDBConstruct 1–366； UniProt 1–366 Author chain JA； PDBConstruct 1–366； UniProt 1–366 Author chain JB； PDBConstruct 1–366； UniProt 1–366 Author chain K； PDBConstruct 1–366； UniProt 1–366 Author chain LA； PDBConstruct 1–366； UniProt 1–366 Author chain LB； PDBConstruct 1–366； UniProt 1–366 Author chain M； PDBConstruct 1–366； UniProt 1–366 Author chain NA； PDBConstruct 1–366； UniProt 1–366 Author chain NB； PDBConstruct 1–366； UniProt 1–366 Author chain O； PDBConstruct 1–366； UniProt 1–366 Author chain PA； PDBConstruct 1–366； UniProt 1–366 Author chain PB； PDBConstruct 1–366； UniProt 1–366 Author chain Q； PDBConstruct 1–366； UniProt 1–366 Author chain RA； PDBConstruct 1–366； UniProt 1–366 Author chain RB； PDBConstruct 1–366； UniProt 1–366 Author chain S； PDBConstruct 1–366； UniProt 1–366 Author chain TA； PDBConstruct 1–366； UniProt 1–366 Author chain TB； PDBConstruct 1–366； UniProt 1–366 Author chain V； PDBConstruct 1–366； UniProt 1–366 Author chain VA； PDBConstruct 1–366； UniProt 1–366 Author chain X； PDBConstruct 1–366； UniProt 1–366 Author chain XA； PDBConstruct 1–366； UniProt 1–366 Author chain Z； PDBConstruct 1–366； UniProt 1–366 Author chain ZA； PDBConstruct 1–366； UniProt 1–366

Charged multivesicular body protein 1b

Homo sapiens

UniProt Q7LBR1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count Chain AA； UniProt 1–199 Chain AB； UniProt 1–199 Chain B； UniProt 1–199 Chain CA； UniProt 1–199 Chain CB； UniProt 1–199 Chain D； UniProt 1–199 Chain EA； UniProt 1–199 Chain EB； UniProt 1–199 Chain F； UniProt 1–199 Chain GA； UniProt 1–199 Chain GB； UniProt 1–199 Chain H； UniProt 1–199 Chain IA； UniProt 1–199 Chain IB； UniProt 1–199 Chain J； UniProt 1–199 Chain KA； UniProt 1–199 Chain KB； UniProt 1–199 Chain L； UniProt 1–199 Chain MA； UniProt 1–199 Chain MB； UniProt 1–199 Chain N； UniProt 1–199 Chain OA； UniProt 1–199 Chain OB； UniProt 1–199 Chain P； UniProt 1–199 Chain QA； UniProt 1–199 Chain QB； UniProt 1–199 Chain R； UniProt 1–199 Chain SA； UniProt 1–199 Chain SB； UniProt 1–199 Chain T； UniProt 1–199 Chain UA； UniProt 1–199 Chain UB； UniProt 1–199 Chain W； UniProt 1–199 Chain WA； UniProt 1–199 Chain Y； UniProt 1–199 Chain YA； UniProt 1–199 Mutation：K37E IST1 homolog × 36 （P53990） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；0 mm offset with 10 sec wait time and 2-4 sec blot Resolution 2.90 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 6E8G Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3JC1 Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer Deposited 2015-11-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 68 PDB declaration: 68-meric
Chain Ab 4–163（160 aa） Fragment：UNP residues 4-163
Chain Ad 4–163（160 aa） Fragment：UNP residues 4-163
Chain Af 4–163（160 aa） Fragment：UNP residues 4-163
Chain Ah 4–163（160 aa） Fragment：UNP residues 4-163
Chain Aj 4–163（160 aa） Fragment：UNP residues 4-163
Chain Al 4–163（160 aa） Fragment：UNP residues 4-163
Chain An 4–163（160 aa） Fragment：UNP residues 4-163
Chain Ap 4–163（160 aa） Fragment：UNP residues 4-163
Chain Ar 4–163（160 aa） Fragment：UNP residues 4-163
Chain At 4–163（160 aa） Fragment：UNP residues 4-163
Chain Av 4–163（160 aa） Fragment：UNP residues 4-163
Chain Ax 4–163（160 aa） Fragment：UNP residues 4-163
Chain Az 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bb 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bd 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bf 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bh 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bj 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bl 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bn 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bp 4–163（160 aa） Fragment：UNP residues 4-163
Chain Br 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bt 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bv 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bx 4–163（160 aa） Fragment：UNP residues 4-163
Chain Bz 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cb 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cd 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cf 4–163（160 aa） Fragment：UNP residues 4-163
Chain Ch 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cj 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cl 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cn 4–163（160 aa） Fragment：UNP residues 4-163
Chain Cp 4–163（160 aa） Fragment：UNP residues 4-163
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 25 mM Tris, pH 8.0, 25 mM sodium chloride；pH 8；25 mM Tris, pH 8.0, 25 mM sodium chloride
cryo-EM vitrification conditions Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset)；Cryogen ETHANE；Deposited 3.5 uL sample, blotted 3-6 seconds (0 mm offset), and plunged into liquid ethane (VITROBOT MARK III).
Resolution 4.00 Å
4TXQ Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM Deposited 2014-07-04 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 C 176–199（24 aa） Fragment：UNP residues 176-199
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277.15 K；Protein mixture was added in 1:1 ratio with a solution of 16% MPD, 0.1 M Tris and equilibrated against a mother liquid of 8% MPD, 0.1 M Tris
Resolution 2.21 Å R-free 0.227
4TXQ Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM Deposited 2014-07-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 176–199（24 aa） Fragment：UNP residues 176-199
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277.15 K；Protein mixture was added in 1:1 ratio with a solution of 16% MPD, 0.1 M Tris and equilibrated against a mother liquid of 8% MPD, 0.1 M Tris
Resolution 2.21 Å R-free 0.227
4TXR Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM and CHMP5 MIM Deposited 2014-07-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 176–199（24 aa） Fragment：UNP residues 176-199
Not recorded ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277.15 K；19% PEG 4000, 0.025 M sodium acetate
Resolution 1.00 Å R-free 0.180
6TZ4 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (right-handed) Deposited 2019-08-10 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 72 PDB declaration: 72-meric
Chain 02 1–199（199 aa）
Chain A 1–199（199 aa）
Chain BA 1–199（199 aa）
Chain BB 1–199（199 aa）
Chain C 1–199（199 aa）
Chain DA 1–199（199 aa）
Chain DB 1–199（199 aa）
Chain E 1–199（199 aa）
Chain FA 1–199（199 aa）
Chain FB 1–199（199 aa）
Chain G 1–199（199 aa）
Chain HA 1–199（199 aa）
Chain HB 1–199（199 aa）
Chain I 1–199（199 aa）
Chain JA 1–199（199 aa）
Chain JB 1–199（199 aa）
Chain K 1–199（199 aa）
Chain LA 1–199（199 aa）
Chain LB 1–199（199 aa）
Chain M 1–199（199 aa）
Chain NA 1–199（199 aa）
Chain NB 1–199（199 aa）
Chain O 1–199（199 aa）
Chain PA 1–199（199 aa）
Chain PB 1–199（199 aa）
Chain Q 1–199（199 aa）
Chain RA 1–199（199 aa）
Chain RB 1–199（199 aa）
Chain S 1–199（199 aa）
Chain TA 1–199（199 aa）
Chain V 1–199（199 aa）
Chain VA 1–199（199 aa）
Chain X 1–199（199 aa）
Chain XA 1–199（199 aa）
Chain Z 1–199（199 aa）
Chain ZA 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.20 Å
6TZ5 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed) Deposited 2019-08-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 68 PDB declaration: 68-meric
Chain AA 1–199（199 aa）
Chain AB 1–199（199 aa）
Chain B 1–199（199 aa）
Chain CA 1–199（199 aa）
Chain CB 1–199（199 aa）
Chain D 1–199（199 aa）
Chain EA 1–199（199 aa）
Chain EB 1–199（199 aa）
Chain F 1–199（199 aa）
Chain GA 1–199（199 aa）
Chain GB 1–199（199 aa）
Chain H 1–199（199 aa）
Chain IA 1–199（199 aa）
Chain IB 1–199（199 aa）
Chain J 1–199（199 aa）
Chain KA 1–199（199 aa）
Chain KB 1–199（199 aa）
Chain L 1–199（199 aa）
Chain MA 1–199（199 aa）
Chain MB 1–199（199 aa）
Chain N 1–199（199 aa）
Chain OA 1–199（199 aa）
Chain OB 1–199（199 aa）
Chain P 1–199（199 aa）
Chain QA 1–199（199 aa）
Chain QB 1–199（199 aa）
Chain R 1–199（199 aa）
Chain SA 1–199（199 aa）
Chain T 1–199（199 aa）
Chain UA 1–199（199 aa）
Chain W 1–199（199 aa）
Chain WA 1–199（199 aa）
Chain Y 1–199（199 aa）
Chain YA 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 3.10 Å
6TZ9 CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only Deposited 2019-08-11 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 26 PDB declaration: 26-meric
Chain A 1–199（199 aa）
Chain AA 1–199（199 aa）
Chain B 1–199（199 aa）
Chain C 1–199（199 aa）
Chain D 1–199（199 aa）
Chain E 1–199（199 aa）
Chain F 1–199（199 aa）
Chain G 1–199（199 aa）
Chain H 1–199（199 aa）
Chain I 1–199（199 aa）
Chain J 1–199（199 aa）
Chain K 1–199（199 aa）
Chain L 1–199（199 aa）
Chain M 1–199（199 aa）
Chain N 1–199（199 aa）
Chain O 1–199（199 aa）
Chain P 1–199（199 aa）
Chain Q 1–199（199 aa）
Chain R 1–199（199 aa）
Chain S 1–199（199 aa）
Chain T 1–199（199 aa）
Chain V 1–199（199 aa）
Chain W 1–199（199 aa）
Chain X 1–199（199 aa）
Chain Y 1–199（199 aa）
Chain Z 1–199（199 aa）
Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E Mutation：K37E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted with Whatman No. 1 filter paper for 4-8 seconds with a 0 mm offset at 19C and 100 percent humidity before plunging into liquid ethane
Resolution 6.20 Å
8V2Q CHMP1B/IST1 ssRNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 182 PDB declaration: 182-meric
Chain A 1–199（199 aa）
Mutation：M136V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.95 Å
8V2R CryoEM of ssDNA bound CHMP1B/IST1 copolymer assembly Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain A 1–199（199 aa）
Mutation：M136V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
8V2S CHMP1B/IST1 dsDNA bound copolymer Deposited 2023-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain A 1–199（199 aa）
Mutation：M136V No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.72 Å

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHM1B_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain AA； PDBConstruct 1–199； UniProt 1–199 Author chain AB； PDBConstruct 1–199； UniProt 1–199 Author chain B； PDBConstruct 1–199； UniProt 1–199 Author chain CA； PDBConstruct 1–199； UniProt 1–199 Author chain CB； PDBConstruct 1–199； UniProt 1–199 Author chain D； PDBConstruct 1–199； UniProt 1–199 Author chain EA； PDBConstruct 1–199； UniProt 1–199 Author chain EB； PDBConstruct 1–199； UniProt 1–199 Author chain F； PDBConstruct 1–199； UniProt 1–199 Author chain GA； PDBConstruct 1–199； UniProt 1–199 Author chain GB； PDBConstruct 1–199； UniProt 1–199 Author chain H； PDBConstruct 1–199； UniProt 1–199 Author chain IA； PDBConstruct 1–199； UniProt 1–199 Author chain IB； PDBConstruct 1–199； UniProt 1–199 Author chain J； PDBConstruct 1–199； UniProt 1–199 Author chain KA； PDBConstruct 1–199； UniProt 1–199 Author chain KB； PDBConstruct 1–199； UniProt 1–199 Author chain L； PDBConstruct 1–199； UniProt 1–199 Author chain MA； PDBConstruct 1–199； UniProt 1–199 Author chain MB； PDBConstruct 1–199； UniProt 1–199 Author chain N； PDBConstruct 1–199； UniProt 1–199 Author chain OA； PDBConstruct 1–199； UniProt 1–199 Author chain OB； PDBConstruct 1–199； UniProt 1–199 Author chain P； PDBConstruct 1–199； UniProt 1–199 Author chain QA； PDBConstruct 1–199； UniProt 1–199 Author chain QB； PDBConstruct 1–199； UniProt 1–199 Author chain R； PDBConstruct 1–199； UniProt 1–199 Author chain SA； PDBConstruct 1–199； UniProt 1–199 Author chain SB； PDBConstruct 1–199； UniProt 1–199 Author chain T； PDBConstruct 1–199； UniProt 1–199 Author chain UA； PDBConstruct 1–199； UniProt 1–199 Author chain UB； PDBConstruct 1–199； UniProt 1–199 Author chain W； PDBConstruct 1–199； UniProt 1–199 Author chain WA； PDBConstruct 1–199； UniProt 1–199 Author chain Y； PDBConstruct 1–199； UniProt 1–199 Author chain YA； PDBConstruct 1–199； UniProt 1–199

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

SAXS profile for 6e8g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6e8g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e8g
Deposition date deposition_date2018-07-29
Structure title titleCryoEM reconstruction of IST1-CHMP1B copolymer filament bound to ssDNA at 2.9 Angstrom resolution
Keywords keywordsESCRT-III, CHMP1B, IST1, ssDNA, DNA BINDING PROTEIN, PROTEIN FIBRIL; DNA BINDING PROTEIN, PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier97.98 Å
Radius of gyration Rg (electron density) rg_electron96.97 Å
Forward intensity I(0) i026396000000.00
Molecular weight molecular_weight1391000.0 kDa
Excluded volume excluded_volume1747000 ų
Envelope volume envelope_volume3485500 ų
Hydration-shell volume shell_volume289280 ų
Envelope diameter envelope_diameter258.3 Å
Shell Rg shell_rg111.70 Å
Envelope Rg envelope_rg87.67 Å
Shape Rg shape_rg97.05 Å
Total Rg total_rg96.76 Å
Total atoms total_atoms97272
Residues n_residues12276
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax250.2 Å
Rg (real space) rg_real96.98 Å
Rg uncertainty (real space) rg_real_error0.89 Å
I(0) (real space) i0_real2.6390e+10
I(0) uncertainty (real space) i0_real_error5.6510e+08
Rg (reciprocal space) rg_reciprocal100.90 Å
I(0) (reciprocal space) i0_reciprocal26660000000.0000
Solution quality estimate total_estimate0.8213
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary156.4 Å
Skewness Skewness skewness-0.254
Kurtosis Kurtosis kurtosis-0.897
Angular range angular_range— – 0.0800 Å−1
Current regularization parameter α current_alpha0.0046
Highest regularization parameter α highest_alpha2677000000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.000
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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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9. Files and Curves (10)