6cs1

SARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, two S1 CTDs in an upwards conformation

Method: ELECTRON MICROSCOPY Dmax: 173.6 Å Quality: REASONABLE

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

Spike glycoprotein,Fibritin

Enterobacteria phage T4

UniProt D9IEJ2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 3 其他Polymer 21 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 457–484 Chain B; UniProt 457–484 Chain C; UniProt 457–484 Mutation:K968P, V969P 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D9IEJ2_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1179–1206; UniProt 457–484 Author chain B; PDBConstruct 1179–1206; UniProt 457–484 Author chain C; PDBConstruct 1179–1206; UniProt 457–484

Spike glycoprotein,Fibritin

Enterobacteria phage T4

UniProt P59594

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 3 其他Polymer 21 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–1190 Chain B; UniProt 14–1190 Chain C; UniProt 14–1190 Mutation:K968P, V969P 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.60 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.

76 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_CVHSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1177; UniProt 14–1190 Author chain B; PDBConstruct 1–1177; UniProt 14–1190 Author chain C; PDBConstruct 1–1177; UniProt 14–1190

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 6cs1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6cs1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6cs1
Deposition date deposition_date2018-03-19
Structure title titleSARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, two S1 CTDs in an upwards conformation
Keywords keywordsmembrane fusion, glycoprotein, receptor binding, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.02
Radius of gyration Rg (electron density) rg_electron52.79
Forward intensity I(0) i01921750000.00
Molecular weight molecular_weight369390.0 kDa
Excluded volume excluded_volume462990 ų
Envelope volume envelope_volume689040 ų
Hydration-shell volume shell_volume108350 ų
Envelope diameter envelope_diameter181.3
Shell Rg shell_rg56.53
Envelope Rg envelope_rg51.61
Shape Rg shape_rg52.83
Total Rg total_rg52.74
Total atoms total_atoms25995
Residues n_residues3202
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 dmax173.6
Rg (real space) rg_real52.88
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real1.9220e+09
I(0) uncertainty (real space) i0_real_error3.4510e+07
Rg (reciprocal space) rg_reciprocal53.12
I(0) (reciprocal space) i0_reciprocal1922000000.0000
Solution quality estimate total_estimate0.6523
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.6
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha178300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 0.007; Positv: 1.000; Valcen: 0.969; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)