7lfm

MODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, TRICLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 97.0 Å Quality: EXCELLENT

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

Histocompatibility 2, M region locus 3

Mus musculus

UniProt Q31093

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 25–301 Mutation:G299 deletion Beta-2-microglobulin × 1 (P01887) Heptapeptide from NADH-ubiquinone oxidoreductase chain 1 × 1 (P03888) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;283 K;0.1 M Hepes, 20% (w/v) PEG 4000, 30% (v/v) ethylene glycol Resolution 1.60 Å R-free 0.217
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 25–301 Mutation:G299 deletion Beta-2-microglobulin × 1 (P01887) Heptapeptide from NADH-ubiquinone oxidoreductase chain 1 × 1 (P03888) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;283 K;0.1 M Hepes, 20% (w/v) PEG 4000, 30% (v/v) ethylene glycol Resolution 1.60 Å R-free 0.217

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.

5 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q31093_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 25–301 Author chain D; PDBConstruct 1–276; UniProt 25–301

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 Histocompatibility 2, M region locus 3 × 1 (Q31093) Heptapeptide from NADH-ubiquinone oxidoreductase chain 1 × 1 (P03888) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;283 K;0.1 M Hepes, 20% (w/v) PEG 4000, 30% (v/v) ethylene glycol Resolution 1.60 Å R-free 0.217
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 21–119 Not recorded Histocompatibility 2, M region locus 3 × 1 (Q31093) Heptapeptide from NADH-ubiquinone oxidoreductase chain 1 × 1 (P03888) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;283 K;0.1 M Hepes, 20% (w/v) PEG 4000, 30% (v/v) ethylene glycol Resolution 1.60 Å R-free 0.217

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

Heptapeptide from NADH-ubiquinone oxidoreductase chain 1

OrganismNot specified

UniProt P03888

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 1–7 Fragment:First seven amino-terminal residues Mutation:I6V Non-standard monomer:Yes (specific site not provided by mmCIF) Histocompatibility 2, M region locus 3 × 1 (Q31093) Beta-2-microglobulin × 1 (P01887) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;283 K;0.1 M Hepes, 20% (w/v) PEG 4000, 30% (v/v) ethylene glycol Resolution 1.60 Å R-free 0.217
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–7 Fragment:First seven amino-terminal residues Mutation:I6V Non-standard monomer:Yes (specific site not provided by mmCIF) Histocompatibility 2, M region locus 3 × 1 (Q31093) Beta-2-microglobulin × 1 (P01887) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;283 K;0.1 M Hepes, 20% (w/v) PEG 4000, 30% (v/v) ethylene glycol Resolution 1.60 Å R-free 0.217

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.

50 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU1M_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–7; UniProt 1–7 Author chain F; PDBConstruct 1–7; UniProt 1–7

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 7lfm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lfm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7lfm
Deposition date deposition_date2021-01-17
Structure title titleMODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, TRICLINIC CELL, REFINED AT 1.60 ANGSTROMS RESOLUTION
Keywords keywordsHISTOCOMPATIBILITY ANTIGEN/PEPTIDE, HISTOCOMPATIBILITY ANTIGEN-PEPTIDE 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_guinier31.05
Radius of gyration Rg (electron density) rg_electron30.14
Forward intensity I(0) i0128545000.00
Molecular weight molecular_weight88406.0 kDa
Excluded volume excluded_volume110020 ų
Envelope volume envelope_volume143310 ų
Hydration-shell volume shell_volume39090 ų
Envelope diameter envelope_diameter100.5
Shell Rg shell_rg37.65
Envelope Rg envelope_rg29.84
Shape Rg shape_rg30.11
Total Rg total_rg30.91
Total atoms total_atoms12227
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 dmax97.0
Rg (real space) rg_real30.92
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real1.2850e+08
I(0) uncertainty (real space) i0_real_error1.8140e+06
Rg (reciprocal space) rg_reciprocal30.98
I(0) (reciprocal space) i0_reciprocal128600000.0000
Solution quality estimate total_estimate0.9068
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.0
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.520
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha17910000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (3)

9. Files and Curves (10)