6wkv

Cryo-EM structure of engineered variant of the Encapsulin from Thermotoga maritima (TmE)

Method: ELECTRON MICROSCOPY Dmax: 247.8 Å Quality: GOOD

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

Encapsulin

Thermotoga maritima

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 0; UniProt 1–265 Chain 1; UniProt 1–265 Chain 2; UniProt 1–265 Chain 3; UniProt 1–265 Chain 4; UniProt 1–265 Chain 5; UniProt 1–265 Chain 6; UniProt 1–265 Chain 7; UniProt 1–265 Chain 8; UniProt 1–265 Chain 9; UniProt 1–265 Chain A; UniProt 1–265 Chain B; UniProt 1–265 Chain C; UniProt 1–265 Chain D; UniProt 1–265 Chain E; UniProt 1–265 Chain F; UniProt 1–265 Chain G; UniProt 1–265 Chain H; UniProt 1–265 Chain I; UniProt 1–265 Chain J; UniProt 1–265 Chain K; UniProt 1–265 Chain L; UniProt 1–265 Chain M; UniProt 1–265 Chain N; UniProt 1–265 Chain O; UniProt 1–265 Chain P; UniProt 1–265 Chain Q; UniProt 1–265 Chain R; UniProt 1–265 Chain S; UniProt 1–265 Chain T; UniProt 1–265 Chain U; UniProt 1–265 Chain V; UniProt 1–265 Chain W; UniProt 1–265 Chain X; UniProt 1–265 Chain Y; UniProt 1–265 Chain Z; UniProt 1–265 Chain a; UniProt 1–265 Chain b; UniProt 1–265 Chain c; UniProt 1–265 Chain d; UniProt 1–265 Chain e; UniProt 1–265 Chain f; UniProt 1–265 Chain g; UniProt 1–265 Chain h; UniProt 1–265 Chain i; UniProt 1–265 Chain j; UniProt 1–265 Chain k; UniProt 1–265 Chain l; UniProt 1–265 Chain m; UniProt 1–265 Chain n; UniProt 1–265 Chain o; UniProt 1–265 Chain p; UniProt 1–265 Chain q; UniProt 1–265 Chain r; UniProt 1–265 Chain s; UniProt 1–265 Chain t; UniProt 1–265 Chain u; UniProt 1–265 Chain v; UniProt 1–265 Chain w; UniProt 1–265 Chain x; UniProt 1–265 Not recorded FMN FLAVIN MONONUCLEOTIDE × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 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 52 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 0; PDBConstruct 1–258; UniProt 1–265 Author chain 1; PDBConstruct 1–258; UniProt 1–265 Author chain 2; PDBConstruct 1–258; UniProt 1–265 Author chain 3; PDBConstruct 1–258; UniProt 1–265 Author chain 4; PDBConstruct 1–258; UniProt 1–265 Author chain 5; PDBConstruct 1–258; UniProt 1–265 Author chain 6; PDBConstruct 1–258; UniProt 1–265 Author chain 7; PDBConstruct 1–258; UniProt 1–265 Author chain 8; PDBConstruct 1–258; UniProt 1–265 Author chain 9; PDBConstruct 1–258; UniProt 1–265 Author chain A; PDBConstruct 1–258; UniProt 1–265 Author chain B; PDBConstruct 1–258; UniProt 1–265 Author chain C; PDBConstruct 1–258; UniProt 1–265 Author chain D; PDBConstruct 1–258; UniProt 1–265 Author chain E; PDBConstruct 1–258; UniProt 1–265 Author chain F; PDBConstruct 1–258; UniProt 1–265 Author chain G; PDBConstruct 1–258; UniProt 1–265 Author chain H; PDBConstruct 1–258; UniProt 1–265 Author chain I; PDBConstruct 1–258; UniProt 1–265 Author chain J; PDBConstruct 1–258; UniProt 1–265 Author chain K; PDBConstruct 1–258; UniProt 1–265 Author chain L; PDBConstruct 1–258; UniProt 1–265 Author chain M; PDBConstruct 1–258; UniProt 1–265 Author chain N; PDBConstruct 1–258; UniProt 1–265 Author chain O; PDBConstruct 1–258; UniProt 1–265 Author chain P; PDBConstruct 1–258; UniProt 1–265 Author chain Q; PDBConstruct 1–258; UniProt 1–265 Author chain R; PDBConstruct 1–258; UniProt 1–265 Author chain S; PDBConstruct 1–258; UniProt 1–265 Author chain T; PDBConstruct 1–258; UniProt 1–265 Author chain U; PDBConstruct 1–258; UniProt 1–265 Author chain V; PDBConstruct 1–258; UniProt 1–265 Author chain W; PDBConstruct 1–258; UniProt 1–265 Author chain X; PDBConstruct 1–258; UniProt 1–265 Author chain Y; PDBConstruct 1–258; UniProt 1–265 Author chain Z; PDBConstruct 1–258; UniProt 1–265 Author chain a; PDBConstruct 1–258; UniProt 1–265 Author chain b; PDBConstruct 1–258; UniProt 1–265 Author chain c; PDBConstruct 1–258; UniProt 1–265 Author chain d; PDBConstruct 1–258; UniProt 1–265 Author chain e; PDBConstruct 1–258; UniProt 1–265 Author chain f; PDBConstruct 1–258; UniProt 1–265 Author chain g; PDBConstruct 1–258; UniProt 1–265 Author chain h; PDBConstruct 1–258; UniProt 1–265 Author chain i; PDBConstruct 1–258; UniProt 1–265 Author chain j; PDBConstruct 1–258; UniProt 1–265 Author chain k; PDBConstruct 1–258; UniProt 1–265 Author chain l; PDBConstruct 1–258; UniProt 1–265 Author chain m; PDBConstruct 1–258; UniProt 1–265 Author chain n; PDBConstruct 1–258; UniProt 1–265 Author chain o; PDBConstruct 1–258; UniProt 1–265 Author chain p; PDBConstruct 1–258; UniProt 1–265 Author chain q; PDBConstruct 1–258; UniProt 1–265 Author chain r; PDBConstruct 1–258; UniProt 1–265 Author chain s; PDBConstruct 1–258; UniProt 1–265 Author chain t; PDBConstruct 1–258; UniProt 1–265 Author chain u; PDBConstruct 1–258; UniProt 1–265 Author chain v; PDBConstruct 1–258; UniProt 1–265 Author chain w; PDBConstruct 1–258; UniProt 1–265 Author chain x; 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

SAXS profile for 6wkv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6wkv
Deposition date deposition_date2020-04-17
Structure title titleCryo-EM structure of engineered variant of the Encapsulin from Thermotoga maritima (TmE)
Keywords keywordsProteolysis, Cytolysis, Defense Response to Bacterium, Extracellular Region, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron104.80
Forward intensity I(0) i041431000000.00
Molecular weight molecular_weight1791800.0 kDa
Excluded volume excluded_volume2263000 ų
Envelope volume envelope_volume6080500 ų
Hydration-shell volume shell_volume492690 ų
Envelope diameter envelope_diameter246.9
Shell Rg shell_rg116.20
Envelope Rg envelope_rg88.58
Shape Rg shape_rg104.80
Total Rg total_rg105.00
Total atoms total_atoms127740
Residues n_residues15420
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 dmax247.8
Rg (real space) rg_real105.30
Rg uncertainty (real space) rg_real_error0.18
I(0) (real space) i0_real4.1470e+10
I(0) uncertainty (real space) i0_real_error6.4810e+08
Rg (reciprocal space) rg_reciprocal114.90
I(0) (reciprocal space) i0_reciprocal42740000000.0000
Solution quality estimate total_estimate0.8580
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary181.7
Skewness Skewness skewness-0.484
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha1.2770
Highest regularization parameter α highest_alpha49940000000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 0.974; Sysdev: 1.000; Positv: 1.000; Valcen: 0.908; 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)