8hsm

CRYSTAL STRUCTURE OF BAT MHC CLASS I MYLU-B-67

Method: X-RAY DIFFRACTION Dmax: 75.6 Å Quality: EXCELLENT

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

Ig-like domain-containing protein

Myotis lucifugus

UniProt G1PNR4

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 22–301 Not recorded Beta-2-microglobulin × 1 (L5K3Y9) PHE-PRO-GLN-SER-ALA-PRO-HIS-GLY-VAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;300 K;0.2M Sodium fluoride,20%w/v Polyethylene glycol 3350, Resolution 2.20 Å R-free 0.258

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G1PNR4_MYOLU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–280; UniProt 22–301

Beta-2-microglobulin

Pteropus alecto

UniProt L5K3Y9

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 187–278 Not recorded Ig-like domain-containing protein × 1 (G1PNR4) PHE-PRO-GLN-SER-ALA-PRO-HIS-GLY-VAL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;300 K;0.2M Sodium fluoride,20%w/v Polyethylene glycol 3350, Resolution 2.20 Å R-free 0.258

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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L5K3Y9_PTEAL
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–95; UniProt 187–278

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 8hsm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8hsm
Deposition date deposition_date2022-12-20
Structure title titleCRYSTAL STRUCTURE OF BAT MHC CLASS I MYLU-B-67
Keywords keywordsMHC, IMMUNOLIGY, IMMUNE SYSTEM TRANSFERASE 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_guinier24.20
Radius of gyration Rg (electron density) rg_electron23.09
Forward intensity I(0) i035259800.00
Molecular weight molecular_weight44410.0 kDa
Excluded volume excluded_volume54891 ų
Envelope volume envelope_volume67891 ų
Hydration-shell volume shell_volume24642 ų
Envelope diameter envelope_diameter76.0
Shell Rg shell_rg29.91
Envelope Rg envelope_rg23.19
Shape Rg shape_rg23.06
Total Rg total_rg23.98
Total atoms total_atoms3141
Residues n_residues387
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 dmax75.6
Rg (real space) rg_real24.13
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real3.5260e+07
I(0) uncertainty (real space) i0_real_error4.8090e+05
Rg (reciprocal space) rg_reciprocal24.15
I(0) (reciprocal space) i0_reciprocal35260000.0000
Solution quality estimate total_estimate0.9049
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8269000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)