7lik

Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R

Method: ELECTRON MICROSCOPY Dmax: 92.9 Å Quality: GOOD

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

Maritimacin

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

UniProt Q9WZP2

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: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
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–265 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
3 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–265 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
4 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–265 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
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–265 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

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.

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 1–265; 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

SAXS profile for 7lik

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lik
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7lik
Deposition date deposition_date2021-01-27
Structure title titleThermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R
Keywords keywordsEncapsulin, Nanocompartment, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.70
Radius of gyration Rg (electron density) rg_electron24.81
Forward intensity I(0) i015880900.00
Molecular weight molecular_weight30844.0 kDa
Excluded volume excluded_volume39027 ų
Envelope volume envelope_volume54055 ų
Hydration-shell volume shell_volume19945 ų
Envelope diameter envelope_diameter90.4
Shell Rg shell_rg29.35
Envelope Rg envelope_rg25.21
Shape Rg shape_rg24.80
Total Rg total_rg25.46
Total atoms total_atoms2180
Residues n_residues265
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax92.9
Rg (real space) rg_real25.79
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real1.5880e+07
I(0) uncertainty (real space) i0_real_error2.8900e+05
Rg (reciprocal space) rg_reciprocal25.77
I(0) (reciprocal space) i0_reciprocal15880000.0000
Solution quality estimate total_estimate0.7530
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.536
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3748000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.681; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.748; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)