7lit

Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G

Method: ELECTRON MICROSCOPY D_max: 81.9 Å Quality: GOOD

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

Maritimacin

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

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 × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain A； UniProt 1–265	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–265	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
3	Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 1–265	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
4	Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 1–265	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
5	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–265	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 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 7LIT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3DKT Crystal structure of Thermotoga maritima encapsulin Deposited 2008-06-26	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 × 120 PDB declaration: 120-meric	Chain A 1–265（265 aa） Chain B 1–265（265 aa） Chain C 1–265（265 aa） Chain D 1–265（265 aa） Chain E 1–265（265 aa） Chain F 1–265（265 aa） Chain G 1–265（265 aa） Chain H 1–265（265 aa） Chain I 1–265（265 aa） Chain J 1–265（265 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.1；292 K；0.1M citrate, 21.5% MPD (v/v), 0.25M ammonium acetate, pH5.1, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 3.10 Å R-free 0.239
6WKV Cryo-EM structure of engineered variant of the Encapsulin from Thermotoga maritima (TmE) Deposited 2020-04-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain 0 1–265（265 aa） Chain 1 1–265（265 aa） Chain 2 1–265（265 aa） Chain 3 1–265（265 aa） Chain 4 1–265（265 aa） Chain 5 1–265（265 aa） Chain 6 1–265（265 aa） Chain 7 1–265（265 aa） Chain 8 1–265（265 aa） Chain 9 1–265（265 aa） Chain A 1–265（265 aa） Chain B 1–265（265 aa） Chain C 1–265（265 aa） Chain D 1–265（265 aa） Chain E 1–265（265 aa） Chain F 1–265（265 aa） Chain G 1–265（265 aa） Chain H 1–265（265 aa） Chain I 1–265（265 aa） Chain J 1–265（265 aa） Chain K 1–265（265 aa） Chain L 1–265（265 aa） Chain M 1–265（265 aa） Chain N 1–265（265 aa） Chain O 1–265（265 aa） Chain P 1–265（265 aa） Chain Q 1–265（265 aa） Chain R 1–265（265 aa） Chain S 1–265（265 aa） Chain T 1–265（265 aa） Chain U 1–265（265 aa） Chain V 1–265（265 aa） Chain W 1–265（265 aa） Chain X 1–265（265 aa） Chain Y 1–265（265 aa） Chain Z 1–265（265 aa） Chain a 1–265（265 aa） Chain b 1–265（265 aa） Chain c 1–265（265 aa） Chain d 1–265（265 aa） Chain e 1–265（265 aa） Chain f 1–265（265 aa） Chain g 1–265（265 aa） Chain h 1–265（265 aa） Chain i 1–265（265 aa） Chain j 1–265（265 aa） Chain k 1–265（265 aa） Chain l 1–265（265 aa） Chain m 1–265（265 aa） Chain n 1–265（265 aa） Chain o 1–265（265 aa） Chain p 1–265（265 aa） Chain q 1–265（265 aa） Chain r 1–265（265 aa） Chain s 1–265（265 aa） Chain t 1–265（265 aa） Chain u 1–265（265 aa） Chain v 1–265（265 aa） Chain w 1–265（265 aa） Chain x 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different mutation/modification Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different mutation/modification Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different mutation/modification Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different mutation/modification Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
9Y8P Cryo-EM structure of Thermotoga maritima encapsulin shell Deposited 2025-09-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa） Chain AA 1–265（265 aa） Chain AB 1–265（265 aa） Chain B 1–265（265 aa） Chain BA 1–265（265 aa） Chain BB 1–265（265 aa） Chain C 1–265（265 aa） Chain CA 1–265（265 aa） Chain CB 1–265（265 aa） Chain D 1–265（265 aa） Chain DA 1–265（265 aa） Chain DB 1–265（265 aa） Chain E 1–265（265 aa） Chain EA 1–265（265 aa） Chain EB 1–265（265 aa） Chain F 1–265（265 aa） Chain FA 1–265（265 aa） Chain FB 1–265（265 aa） Chain G 1–265（265 aa） Chain GA 1–265（265 aa） Chain GB 1–265（265 aa） Chain H 1–265（265 aa） Chain HA 1–265（265 aa） Chain HB 1–265（265 aa） Chain I 1–265（265 aa） Chain IA 1–265（265 aa） Chain J 1–265（265 aa） Chain JA 1–265（265 aa） Chain K 1–265（265 aa） Chain KA 1–265（265 aa） Chain L 1–265（265 aa） Chain LA 1–265（265 aa） Chain M 1–265（265 aa） Chain MA 1–265（265 aa） Chain N 1–265（265 aa） Chain NA 1–265（265 aa） Chain O 1–265（265 aa） Chain OA 1–265（265 aa） Chain P 1–265（265 aa） Chain PA 1–265（265 aa） Chain Q 1–265（265 aa） Chain QA 1–265（265 aa） Chain R 1–265（265 aa） Chain RA 1–265（265 aa） Chain S 1–265（265 aa） Chain SA 1–265（265 aa） Chain T 1–265（265 aa） Chain TA 1–265（265 aa） Chain U 1–265（265 aa） Chain UA 1–265（265 aa） Chain V 1–265（265 aa） Chain VA 1–265（265 aa） Chain W 1–265（265 aa） Chain WA 1–265（265 aa） Chain X 1–265（265 aa） Chain XA 1–265（265 aa） Chain Y 1–265（265 aa） Chain YA 1–265（265 aa） Chain Z 1–265（265 aa） Chain ZA 1–265（265 aa）	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

12 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MARIT_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–258； UniProt 1–265

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	7lit
Deposition date deposition_date	2021-01-27
Structure title title	Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G
Keywords keywords	Encapsulin, Nanocompartment, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
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	24.34 Å
Radius of gyration Rg (electron density) rg_electron	23.48 Å
Forward intensity I(0) i0	14851700.00
Molecular weight molecular_weight	29914.0 kDa
Excluded volume excluded_volume	37839 Å³
Envelope volume envelope_volume	48563 Å³
Hydration-shell volume shell_volume	18879 Å³
Envelope diameter envelope_diameter	87.3 Å
Shell Rg shell_rg	28.28 Å
Envelope Rg envelope_rg	23.93 Å
Shape Rg shape_rg	23.47 Å
Total Rg total_rg	24.19 Å
Total atoms total_atoms	2114
Residues n_residues	258
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	81.9 Å
Rg (real space) rg_real	24.45 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	1.4850e+07
I(0) uncertainty (real space) i0_real_error	2.0720e+05
Rg (reciprocal space) rg_reciprocal	24.43 Å
I(0) (reciprocal space) i0_reciprocal	14850000.0000
Solution quality estimate total_estimate	0.8579
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.1 Å
Skewness Skewness skewness	0.383
Kurtosis Kurtosis kurtosis	-0.496
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3173000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.797; Smooth: 0.884

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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	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	2.53 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	90905

Description description	Maritimacin
Molecular weight formula_weight	29603.8 kDa
EC 编号 ec_number	3.4.-.-
Mutation mutation	K182G, L190G, Del(182-189)
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2114

Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G

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

Maritimacin

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
NCBI Class编号 ncbi_taxonomy_id	243274
宿主生物 host_organism	Escherichia coli BL21(DE3)

Description description	RIBOFLAVIN
Molecular weight formula_weight	376.4 kDa
Source method src_method	syn
Copy count entity_count	1

fit	/app/data/saxs_computation/li/7lit/7lit.fit
pddf	/app/data/pr_computation/li/7lit/7lit.pr.out
profile	/app/data/saxs_computation/li/7lit/7lit.dat