5m02

Crystal structure of murine P14 TCR / H-2Db with PF, modified gp33 peptide from LCMV

Method: X-RAY DIFFRACTION Dmax: 131.1 Å Quality: GOOD

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 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 25–300 Not recorded Beta-2-microglobulin × 1 (P01887) Protein Trav14-1,T-cell receptor alpha chain C region × 1 (A0A0G2JF94,P01849) T-cell receptor beta chain V region C5,T-cell receptor beta-2 chain C region × 1 (P04213,P01851) LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND PF × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;19% PEG 6000, 0.1M Tris HCl pH 8.0 Resolution 1.75 Å R-free 0.214

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 202 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

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 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Protein Trav14-1,T-cell receptor alpha chain C region × 1 (A0A0G2JF94,P01849) T-cell receptor beta chain V region C5,T-cell receptor beta-2 chain C region × 1 (P04213,P01851) LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND PF × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;19% PEG 6000, 0.1M Tris HCl pH 8.0 Resolution 1.75 Å R-free 0.214

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 483 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 21–119; UniProt 21–119

Protein Trav14-1,T-cell receptor alpha chain C region

Mus musculus

UniProt A0A0G2JF94

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 22–120 Not recorded H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Beta-2-microglobulin × 1 (P01887) T-cell receptor beta chain V region C5,T-cell receptor beta-2 chain C region × 1 (P04213,P01851) LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND PF × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;19% PEG 6000, 0.1M Tris HCl pH 8.0 Resolution 1.75 Å R-free 0.214

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0G2JF94_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–99; UniProt 22–120

Protein Trav14-1,T-cell receptor alpha chain C region

Mus musculus

UniProt P01849

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 3–88 Not recorded H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Beta-2-microglobulin × 1 (P01887) T-cell receptor beta chain V region C5,T-cell receptor beta-2 chain C region × 1 (P04213,P01851) LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND PF × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;19% PEG 6000, 0.1M Tris HCl pH 8.0 Resolution 1.75 Å R-free 0.214

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCA_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 120–205; UniProt 3–88

T-cell receptor beta chain V region C5,T-cell receptor beta-2 chain C region

Mus musculus

UniProt P01851

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 1–127 Not recorded H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Beta-2-microglobulin × 1 (P01887) Protein Trav14-1,T-cell receptor alpha chain C region × 1 (A0A0G2JF94,P01849) LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND PF × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;19% PEG 6000, 0.1M Tris HCl pH 8.0 Resolution 1.75 Å R-free 0.214

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCB2_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 112–238; UniProt 1–127

T-cell receptor beta chain V region C5,T-cell receptor beta-2 chain C region

Mus musculus

UniProt P04213

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 11–102 Not recorded H-2 class I histocompatibility antigen, D-B alpha chain × 1 (P01899) Beta-2-microglobulin × 1 (P01887) Protein Trav14-1,T-cell receptor alpha chain C region × 1 (A0A0G2JF94,P01849) LCMV-DERIVED GP33 ALTERED PEPTIDE LIGAND PF × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;19% PEG 6000, 0.1M Tris HCl pH 8.0 Resolution 1.75 Å R-free 0.214

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 TVB5_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–92; UniProt 11–102

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 5m02

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5m02
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5m02
Deposition date deposition_date2016-10-03
Structure title titleCrystal structure of murine P14 TCR / H-2Db with PF, modified gp33 peptide from LCMV
Keywords keywordsMHC class I, TCR, H-2Db, gp33, LCMV, 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_guinier37.29
Radius of gyration Rg (electron density) rg_electron37.80
Forward intensity I(0) i0136427000.00
Molecular weight molecular_weight92469.0 kDa
Excluded volume excluded_volume114850 ų
Envelope volume envelope_volume154790 ų
Hydration-shell volume shell_volume37515 ų
Envelope diameter envelope_diameter137.8
Shell Rg shell_rg39.15
Envelope Rg envelope_rg38.27
Shape Rg shape_rg37.76
Total Rg total_rg38.02
Total atoms total_atoms6521
Residues n_residues809
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 dmax131.1
Rg (real space) rg_real37.92
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real1.3640e+08
I(0) uncertainty (real space) i0_real_error2.0520e+06
Rg (reciprocal space) rg_reciprocal37.53
I(0) (reciprocal space) i0_reciprocal136400000.0000
Solution quality estimate total_estimate0.7715
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.3
Skewness Skewness skewness0.681
Kurtosis Kurtosis kurtosis-0.126
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15900000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.622; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.702; Smooth: 0.458

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id5m02A01
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_id5m02A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5m02B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5m02G01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5m02H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5m02H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)