5e8p

The structure of the TEIPP associated altered peptide ligand Trh4-p5NLE in complex with H-2D(b)

Method: X-RAY DIFFRACTION Dmax: 101.1 Å Quality: EXCELLENT

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

H-2 class I histocompatibility antigen, D-B alpha chain

Mus musculus

UniProt P01899

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 (P01887) Ceramide synthase 5 × 1 (Q9D6K9) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl Resolution 2.00 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 25–300 Not recorded Beta-2-microglobulin × 1 (P01887) Ceramide synthase 5 × 1 (Q9D6K9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl Resolution 2.00 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.

93 other PDB entries and 201 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA11_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 25–300 Author chain D; PDBConstruct 1–276; UniProt 25–300

Beta-2-microglobulin

Mus musculus

UniProt P01887

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 H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Ceramide synthase 5 × 1 (Q9D6K9) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl Resolution 2.00 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 21–119 Not recorded H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Ceramide synthase 5 × 1 (Q9D6K9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl Resolution 2.00 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.

290 other PDB entries and 482 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 21–119 Author chain E; PDBConstruct 1–99; UniProt 21–119

Ceramide synthase 5

OrganismNot specified

UniProt Q9D6K9

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 379–387 Fragment:UNP residues 379-387 Non-standard monomer:Yes (specific site not provided by mmCIF) H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Beta-2-microglobulin × 1 (P01887) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl Resolution 2.00 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 379–387 Fragment:UNP residues 379-387 Non-standard monomer:Yes (specific site not provided by mmCIF) H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Beta-2-microglobulin × 1 (P01887) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;1.6 M ammonium sulphate, 0.1 M Tris-HCl, 0.5 M NaCl Resolution 2.00 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.

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

View Construct and Data Evidence
UniProt name CERS5_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 379–387 Author chain F; PDBConstruct 1–9; UniProt 379–387

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 5e8p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5e8p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5e8p
Deposition date deposition_date2015-10-14
Structure title titleThe structure of the TEIPP associated altered peptide ligand Trh4-p5NLE in complex with H-2D(b)
Keywords keywordsCancer, Neo-epitope, TAP-deficiency, TEIPP, MHC-I, Sulfur-pi interactions, Non-classical peptide binding, 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_guinier32.12
Radius of gyration Rg (electron density) rg_electron31.28
Forward intensity I(0) i0129537000.00
Molecular weight molecular_weight88338.0 kDa
Excluded volume excluded_volume109420 ų
Envelope volume envelope_volume143640 ų
Hydration-shell volume shell_volume37953 ų
Envelope diameter envelope_diameter108.3
Shell Rg shell_rg38.82
Envelope Rg envelope_rg30.81
Shape Rg shape_rg31.26
Total Rg total_rg31.99
Total atoms total_atoms6225
Residues n_residues757
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 dmax101.1
Rg (real space) rg_real31.98
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.2950e+08
I(0) uncertainty (real space) i0_real_error1.9710e+06
Rg (reciprocal space) rg_reciprocal32.04
I(0) (reciprocal space) i0_reciprocal129500000.0000
Solution quality estimate total_estimate0.9085
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.3
Skewness Skewness skewness0.142
Kurtosis Kurtosis kurtosis-0.573
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha15030000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id5e8pA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id5e8pA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5e8pB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5e8pD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id5e8pD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5e8pE00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)