7zsd

cryo-EM structure of omicron spike in complex with de novo designed binder, local

Method: ELECTRON MICROSCOPY Dmax: 78.7 Å Quality: REASONABLE

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

Spike glycoprotein

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain M; UniProt 332–527 Not recorded de novo designed binder × 1 (Q9VKJ9) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 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.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain M; PDBConstruct 1–196; UniProt 332–527

de novo designed binder

Drosophila melanogaster

UniProt Q9VKJ9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 359–423 Not recorded Spike glycoprotein × 1 (P0DTC2) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C2D1_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 7–71; UniProt 359–423

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 7zsd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zsd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zsd
Deposition date deposition_date2022-05-06
Structure title titlecryo-EM structure of omicron spike in complex with de novo designed binder, local
Keywords keywordsSARS-COV2, de novo, design binder, spike, RBD, receptor binding domain, ANTIVIRAL PROTEIN; ANTIVIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier21.92
Radius of gyration Rg (electron density) rg_electron21.36
Forward intensity I(0) i015508100.00
Molecular weight molecular_weight29989.0 kDa
Excluded volume excluded_volume37686 ų
Envelope volume envelope_volume46268 ų
Hydration-shell volume shell_volume19177 ų
Envelope diameter envelope_diameter76.7
Shell Rg shell_rg27.00
Envelope Rg envelope_rg21.65
Shape Rg shape_rg21.29
Total Rg total_rg22.40
Total atoms total_atoms2120
Residues n_residues261
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 dmax78.7
Rg (real space) rg_real22.07
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.5510e+07
I(0) uncertainty (real space) i0_real_error2.1080e+05
Rg (reciprocal space) rg_reciprocal22.04
I(0) (reciprocal space) i0_reciprocal15510000.0000
Solution quality estimate total_estimate0.6570
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.551
Kurtosis Kurtosis kurtosis-0.030
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3465000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.667; Stabil: 1.000; Sysdev: 0.262; Positv: 1.000; Valcen: 0.787; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)