6uzm

HLA-B*15:02 complexed with a synthetic peptide

Method: X-RAY DIFFRACTION Dmax: 74.0 Å Quality: EXCELLENT

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

MHC class I antigen

Homo sapiens

UniProt F4NBQ8

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 25–300 Not recorded Beta-2-microglobulin × 1 (P61769) Synthetic peptide HIS-LEU-ALA-SER-SER-GLY-HIS-SER-LEU × 1 GOL GLYCEROL × 2 EDO 1,2-ETHANEDIOL × 1 ACT ACETATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;0.2 ammonium acetate, 0.M tri-sodium citrate dihydrate pH5.6, 30% w/v PEG4000 Resolution 1.80 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F4NBQ8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 25–300

Beta-2-microglobulin

Homo sapiens

UniProt P61769

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 21–119 Not recorded MHC class I antigen × 1 (F4NBQ8) Synthetic peptide HIS-LEU-ALA-SER-SER-GLY-HIS-SER-LEU × 1 GOL GLYCEROL × 2 EDO 1,2-ETHANEDIOL × 1 ACT ACETATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;0.2 ammonium acetate, 0.M tri-sodium citrate dihydrate pH5.6, 30% w/v PEG4000 Resolution 1.80 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.

1313 other PDB entries and 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–100; UniProt 21–119

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 6uzm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6uzm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6uzm
Deposition date deposition_date2019-11-15
Structure title titleHLA-B*15:02 complexed with a synthetic peptide
Keywords keywordsleukocyte antigen, HLA, HLA-B, MHC, major histocompatiblity complex, 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_guinier24.09
Radius of gyration Rg (electron density) rg_electron22.92
Forward intensity I(0) i036456800.00
Molecular weight molecular_weight44702.0 kDa
Excluded volume excluded_volume55085 ų
Envelope volume envelope_volume67138 ų
Hydration-shell volume shell_volume24562 ų
Envelope diameter envelope_diameter77.2
Shell Rg shell_rg29.64
Envelope Rg envelope_rg23.00
Shape Rg shape_rg22.91
Total Rg total_rg23.73
Total atoms total_atoms3157
Residues n_residues384
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 dmax74.0
Rg (real space) rg_real24.02
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real3.6460e+07
I(0) uncertainty (real space) i0_real_error4.7610e+05
Rg (reciprocal space) rg_reciprocal24.04
I(0) (reciprocal space) i0_reciprocal36460000.0000
Solution quality estimate total_estimate0.9137
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.7
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.495
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7877000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)