2ol3

crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule

Method: X-RAY DIFFRACTION Dmax: 113.1 Å Quality: GOOD

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

BM3.3 T-CELL RECEPTOR ALPHA-CHAIN

Mus musculus

UniProt Q5R1F1

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 23–116 Not recorded BM3.3 T-CELL RECEPTOR BETA-CHAIN × 1 (P04214) ALLOGENEIC H-2KBM8 MHC CLASS I MOLECULE × 1 (P01901) Beta-2-microglobulin × 1 (P01887) NATURALLY PROCESSED OCTAPEPTIDE PBM8 × 1 (Q91YE7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;12 % PEG 6000, 100 mM Hepes, pH 7.5, and 150 mM Magnesium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.90 Å R-free 0.284

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 Q5R1F1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–94; UniProt 23–116

BM3.3 T-CELL RECEPTOR BETA-CHAIN

Mus musculus

UniProt P04214

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 22–116 Not recorded BM3.3 T-CELL RECEPTOR ALPHA-CHAIN × 1 (Q5R1F1) ALLOGENEIC H-2KBM8 MHC CLASS I MOLECULE × 1 (P01901) Beta-2-microglobulin × 1 (P01887) NATURALLY PROCESSED OCTAPEPTIDE PBM8 × 1 (Q91YE7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;12 % PEG 6000, 100 mM Hepes, pH 7.5, and 150 mM Magnesium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.90 Å R-free 0.284

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TVB6_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–95; UniProt 22–116

ALLOGENEIC H-2KBM8 MHC CLASS I MOLECULE

Mus musculus

UniProt P01901

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 22–300 Fragment:EXTRACELLULAR DOMAINS (ALPHA1, ALPHA2, ALPHA3) BM3.3 T-CELL RECEPTOR ALPHA-CHAIN × 1 (Q5R1F1) BM3.3 T-CELL RECEPTOR BETA-CHAIN × 1 (P04214) Beta-2-microglobulin × 1 (P01887) NATURALLY PROCESSED OCTAPEPTIDE PBM8 × 1 (Q91YE7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;12 % PEG 6000, 100 mM Hepes, pH 7.5, and 150 mM Magnesium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.90 Å R-free 0.284

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.

83 other PDB entries and 140 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA1B_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–279; UniProt 22–300

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain L; UniProt 21–119 Not recorded BM3.3 T-CELL RECEPTOR ALPHA-CHAIN × 1 (Q5R1F1) BM3.3 T-CELL RECEPTOR BETA-CHAIN × 1 (P04214) ALLOGENEIC H-2KBM8 MHC CLASS I MOLECULE × 1 (P01901) NATURALLY PROCESSED OCTAPEPTIDE PBM8 × 1 (Q91YE7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;12 % PEG 6000, 100 mM Hepes, pH 7.5, and 150 mM Magnesium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.90 Å R-free 0.284

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 4
Chains and sequence ranges Author chain L; PDBConstruct 2–100; UniProt 21–119

NATURALLY PROCESSED OCTAPEPTIDE PBM8

OrganismNot specified

UniProt Q91YE7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain P; UniProt 484–491 Not recorded BM3.3 T-CELL RECEPTOR ALPHA-CHAIN × 1 (Q5R1F1) BM3.3 T-CELL RECEPTOR BETA-CHAIN × 1 (P04214) ALLOGENEIC H-2KBM8 MHC CLASS I MOLECULE × 1 (P01901) Beta-2-microglobulin × 1 (P01887) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;12 % PEG 6000, 100 mM Hepes, pH 7.5, and 150 mM Magnesium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.90 Å R-free 0.284

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 RBM5_MOUSE
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–8; UniProt 484–491

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 2ol3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ol3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ol3
Deposition date deposition_date2007-01-18
Structure title titlecrystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule
Keywords keywordsT CELL RECEPTOR, CLASS I MHC, H-2KBm8, TCR-PMHC 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_guinier31.08
Radius of gyration Rg (electron density) rg_electron31.23
Forward intensity I(0) i081798600.00
Molecular weight molecular_weight70911.0 kDa
Excluded volume excluded_volume88424 ų
Envelope volume envelope_volume112540 ų
Hydration-shell volume shell_volume32468 ų
Envelope diameter envelope_diameter120.9
Shell Rg shell_rg35.40
Envelope Rg envelope_rg31.65
Shape Rg shape_rg31.18
Total Rg total_rg31.76
Total atoms total_atoms4996
Residues n_residues613
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 dmax113.1
Rg (real space) rg_real31.42
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real8.1800e+07
I(0) uncertainty (real space) i0_real_error1.4290e+06
Rg (reciprocal space) rg_reciprocal31.28
I(0) (reciprocal space) i0_reciprocal81790000.0000
Solution quality estimate total_estimate0.8032
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.641
Kurtosis Kurtosis kurtosis-0.018
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11190000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.618; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.636; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2ol3a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2ol3b_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2ol3h1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd2ol3h2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain
Domain ID domain_idd2ol3l2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd2ol3l3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (5 domains)

Domain ID domain_id2ol3A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2ol3B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2ol3H01
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_id2ol3H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2ol3L00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)