1n59

Crystal structure of the Murine class I Major Histocompatibility Complex of H-2KB, B2-Microglobulin, and A 9-Residue immunodominant peptide epitope gp33 derived from LCMV

Method: X-RAY DIFFRACTION Dmax: 99.9 Å Quality: EXCELLENT

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

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 22–297 Fragment:Extracellular fragment Beta-2-microglobulin × 1 (P01887) nonameric peptide, gp33 derived from lymphocytic choriomeningitis virus × 1 (Q9QDK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG8000, magnesium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.95 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 22–297 Fragment:Extracellular fragment Beta-2-microglobulin × 1 (P01887) nonameric peptide, gp33 derived from lymphocytic choriomeningitis virus × 1 (Q9QDK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG8000, magnesium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.95 Å R-free 0.287

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 139 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA1B_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 22–297 Author chain C; PDBConstruct 1–276; UniProt 22–297

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, K-B alpha chain × 1 (P01901) nonameric peptide, gp33 derived from lymphocytic choriomeningitis virus × 1 (Q9QDK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG8000, magnesium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.95 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 21–119 Not recorded H-2 class I histocompatibility antigen, K-B alpha chain × 1 (P01901) nonameric peptide, gp33 derived from lymphocytic choriomeningitis virus × 1 (Q9QDK7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG8000, magnesium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.95 Å R-free 0.287

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 D; PDBConstruct 1–99; UniProt 21–119

nonameric peptide, gp33 derived from lymphocytic choriomeningitis virus

OrganismNot specified

UniProt Q9QDK7

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 P; UniProt 33–40 Mutation:C9M H-2 class I histocompatibility antigen, K-B alpha chain × 1 (P01901) Beta-2-microglobulin × 1 (P01887) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG8000, magnesium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.95 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Q; UniProt 33–40 Mutation:C9M H-2 class I histocompatibility antigen, K-B alpha chain × 1 (P01901) Beta-2-microglobulin × 1 (P01887) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;PEG8000, magnesium acetate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.95 Å R-free 0.287

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9QDK7_9VIRU
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–9; UniProt 33–40 Author chain Q; PDBConstruct 1–9; UniProt 33–40

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 1n59

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1n59
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1n59
Deposition date deposition_date2002-11-05
Structure title titleCrystal structure of the Murine class I Major Histocompatibility Complex of H-2KB, B2-Microglobulin, and A 9-Residue immunodominant peptide epitope gp33 derived from LCMV
Keywords keywordsMurine MHC, viral escape, LCMV, immunodominant epitope, 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_guinier32.20
Radius of gyration Rg (electron density) rg_electron31.41
Forward intensity I(0) i0128620000.00
Molecular weight molecular_weight88756.0 kDa
Excluded volume excluded_volume110260 ų
Envelope volume envelope_volume141500 ų
Hydration-shell volume shell_volume37056 ų
Envelope diameter envelope_diameter101.4
Shell Rg shell_rg38.94
Envelope Rg envelope_rg31.09
Shape Rg shape_rg31.39
Total Rg total_rg32.12
Total atoms total_atoms6260
Residues n_residues766
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 dmax99.9
Rg (real space) rg_real32.10
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.2860e+08
I(0) uncertainty (real space) i0_real_error1.8860e+06
Rg (reciprocal space) rg_reciprocal32.14
I(0) (reciprocal space) i0_reciprocal128600000.0000
Solution quality estimate total_estimate0.9077
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.177
Kurtosis Kurtosis kurtosis-0.635
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16900000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1n59a1
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_idd1n59a2
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_idd1n59b_
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_idd1n59c1
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_idd1n59c2
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_idd1n59d_
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)

CATH v4.4 (6 domains)

Domain ID domain_id1n59A01
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_id1n59A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1n59B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1n59C01
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_id1n59C02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1n59D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)