8tbp

HLA-DRB1*15:01 in complex with smith antigen

Method: X-RAY DIFFRACTION Dmax: 83.7 Å Quality: EXCELLENT

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 HLA class II histocompatibility antigen, DRB1 beta chain × 1 (P01911) Small nuclear ribonucleoprotein-associated protein N peptide × 1 (P63162) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2M Disodium Malon 20% w/v PEG 3350 Resolution 3.13 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 26–207 Not recorded HLA class II histocompatibility antigen, DRB1 beta chain × 1 (P01911) Small nuclear ribonucleoprotein-associated protein N peptide × 1 (P63162) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2M Disodium Malon 20% w/v PEG 3350 Resolution 3.13 Å R-free 0.253

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 218 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 1–182; UniProt 26–207 Author chain C; PDBConstruct 1–182; UniProt 26–207

HLA class II histocompatibility antigen, DRB1 beta chain

Homo sapiens

UniProt P01911

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 B; UniProt 30–219 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Small nuclear ribonucleoprotein-associated protein N peptide × 1 (P63162) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2M Disodium Malon 20% w/v PEG 3350 Resolution 3.13 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 30–219 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) Small nuclear ribonucleoprotein-associated protein N peptide × 1 (P63162) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2M Disodium Malon 20% w/v PEG 3350 Resolution 3.13 Å R-free 0.253

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–190; UniProt 30–219 Author chain D; PDBConstruct 1–190; UniProt 30–219

Small nuclear ribonucleoprotein-associated protein N peptide

Homo sapiens

UniProt P63162

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 E; UniProt 65–79 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) HLA class II histocompatibility antigen, DRB1 beta chain × 1 (P01911) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2M Disodium Malon 20% w/v PEG 3350 Resolution 3.13 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 65–79 Not recorded HLA class II histocompatibility antigen, DR alpha chain × 1 (P01903) HLA class II histocompatibility antigen, DRB1 beta chain × 1 (P01911) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.2M Disodium Malon 20% w/v PEG 3350 Resolution 3.13 Å R-free 0.253

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name RSMN_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–15; UniProt 65–79 Author chain F; PDBConstruct 1–15; UniProt 65–79

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 8tbp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tbp
Deposition date deposition_date2023-06-29
Structure title titleHLA-DRB1*15:01 in complex with smith antigen
Keywords keywordsHuman Leukocyte Antigen, HLA, Major Histocompatibility Complex, MHC, 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_guinier28.88
Radius of gyration Rg (electron density) rg_electron27.69
Forward intensity I(0) i0125860000.00
Molecular weight molecular_weight88370.0 kDa
Excluded volume excluded_volume110500 ų
Envelope volume envelope_volume139030 ų
Hydration-shell volume shell_volume40492 ų
Envelope diameter envelope_diameter89.0
Shell Rg shell_rg36.23
Envelope Rg envelope_rg27.36
Shape Rg shape_rg27.68
Total Rg total_rg28.62
Total atoms total_atoms6280
Residues n_residues762
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 dmax83.7
Rg (real space) rg_real28.69
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.2590e+08
I(0) uncertainty (real space) i0_real_error1.7390e+06
Rg (reciprocal space) rg_reciprocal28.77
I(0) (reciprocal space) i0_reciprocal125900000.0000
Solution quality estimate total_estimate0.9101
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.055
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15740000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)