8cmb

Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Spike peptide S486-505

Method: X-RAY DIFFRACTION Dmax: 86.7 Å Quality: GOOD

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

HLA class II histocompatibility antigen, DR alpha chain

Homo sapiens

UniProt P01903

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–207 Not recorded Human leukocyte antigen DR beta chain allotype DR1 (DRB1*0101) × 1 ;Spike protein S2' ; × 1 (P0DTC2) EDO 1,2-ETHANEDIOL × 10 DHL 2-AMINO-ETHANETHIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;291 K;0.1 M MES pH 6.0, 20 % PEG1500 Resolution 1.84 Å R-free 0.231

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.

139 other PDB entries and 219 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–183; UniProt 26–207

;Spike protein S2' ;

OrganismNot specified

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 486–505 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Human leukocyte antigen DR beta chain allotype DR1 (DRB1*0101) × 1 EDO 1,2-ETHANEDIOL × 10 DHL 2-AMINO-ETHANETHIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;291 K;0.1 M MES pH 6.0, 20 % PEG1500 Resolution 1.84 Å R-free 0.231

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 486–505

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 8cmb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8cmb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8cmb
Deposition date deposition_date2023-02-19
Structure title titleHuman Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Spike peptide S486-505
Keywords keywords;HLA-II, HLA-DR, HLA-DR1, human leukocyte antigen, major histocompatibility complex, major histocompatibility complex class 2, SARS-CoV-2, coronavirus, COVID-19, Spike, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.94
Radius of gyration Rg (electron density) rg_electron23.95
Forward intensity I(0) i035283400.00
Molecular weight molecular_weight45726.0 kDa
Excluded volume excluded_volume57108 ų
Envelope volume envelope_volume68990 ų
Hydration-shell volume shell_volume24297 ų
Envelope diameter envelope_diameter85.9
Shell Rg shell_rg30.62
Envelope Rg envelope_rg24.31
Shape Rg shape_rg23.93
Total Rg total_rg24.82
Total atoms total_atoms3227
Residues n_residues388
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 dmax86.7
Rg (real space) rg_real24.96
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real3.5280e+07
I(0) uncertainty (real space) i0_real_error5.2890e+05
Rg (reciprocal space) rg_reciprocal24.96
I(0) (reciprocal space) i0_reciprocal35280000.0000
Solution quality estimate total_estimate0.7922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.362
Kurtosis Kurtosis kurtosis-0.360
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8069000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.891; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)