3ws3

Crystal Structure of H-2D in complex with an insulin derived peptide

Method: X-RAY DIFFRACTION Dmax: 102.5 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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–298 Fragment:EXTRACELLULAR DOMAIN Beta-2-microglobulin × 1 (P01887) Insulin derived 9-mer peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;0.2M Ammonium Sulfate, 25% PEG 3350, 0.1M HEPES, 30% Ethylene Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.33 Å R-free 0.294
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 26–298 Fragment:EXTRACELLULAR DOMAIN Beta-2-microglobulin × 1 (P01887) Insulin derived 9-mer peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;0.2M Ammonium Sulfate, 25% PEG 3350, 0.1M HEPES, 30% Ethylene Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.33 Å R-free 0.294

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 1–273; UniProt 26–298 Author chain C; PDBConstruct 1–273; UniProt 26–298

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) Insulin derived 9-mer peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;0.2M Ammonium Sulfate, 25% PEG 3350, 0.1M HEPES, 30% Ethylene Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.33 Å R-free 0.294
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, D-B alpha chain × 1 (P01899) Insulin derived 9-mer peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;0.2M Ammonium Sulfate, 25% PEG 3350, 0.1M HEPES, 30% Ethylene Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.33 Å R-free 0.294

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 2–100; UniProt 21–119 Author chain D; PDBConstruct 2–100; UniProt 21–119

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 3ws3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ws3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ws3
Deposition date deposition_date2014-02-28
Structure title titleCrystal Structure of H-2D in complex with an insulin derived peptide
Keywords keywords;Class I MHC, Major histocompatibility complex, insulin, H-2D, Structural Genomics, PSI-Biology, New York Structural Genomics Research Consortium, NYSGRC, 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_guinier32.42
Radius of gyration Rg (electron density) rg_electron31.59
Forward intensity I(0) i0128729000.00
Molecular weight molecular_weight88485.0 kDa
Excluded volume excluded_volume109730 ų
Envelope volume envelope_volume144120 ų
Hydration-shell volume shell_volume37756 ų
Envelope diameter envelope_diameter103.4
Shell Rg shell_rg39.06
Envelope Rg envelope_rg31.13
Shape Rg shape_rg31.56
Total Rg total_rg32.32
Total atoms total_atoms6241
Residues n_residues755
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 dmax102.5
Rg (real space) rg_real32.30
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.2870e+08
I(0) uncertainty (real space) i0_real_error1.8740e+06
Rg (reciprocal space) rg_reciprocal32.35
I(0) (reciprocal space) i0_reciprocal128700000.0000
Solution quality estimate total_estimate0.8360
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.8
Skewness Skewness skewness0.153
Kurtosis Kurtosis kurtosis-0.597
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14380000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3ws3A01
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_id3ws3A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3ws3B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3ws3C01
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_id3ws3C02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3ws3D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)