7lfl

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

Method: X-RAY DIFFRACTION Dmax: 75.4 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 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 0.239

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 11 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

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 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 0.239

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 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 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 0.239

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 54 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

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 7lfl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7lfl
Deposition date deposition_date2021-01-17
Structure title titleMODEL OF MHC CLASS Ib H2-M3 WITH MOUSE ND1 N-TERMINAL HEPTAPEPTIDE, VAL MUTANT, MONOCLINIC 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_guinier24.32
Radius of gyration Rg (electron density) rg_electron23.30
Forward intensity I(0) i034197700.00
Molecular weight molecular_weight44229.0 kDa
Excluded volume excluded_volume55027 ų
Envelope volume envelope_volume68178 ų
Hydration-shell volume shell_volume24510 ų
Envelope diameter envelope_diameter78.9
Shell Rg shell_rg30.13
Envelope Rg envelope_rg23.42
Shape Rg shape_rg23.27
Total Rg total_rg24.20
Total atoms total_atoms6115
Residues n_residues378
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 dmax75.4
Rg (real space) rg_real24.26
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real3.4200e+07
I(0) uncertainty (real space) i0_real_error4.6760e+05
Rg (reciprocal space) rg_reciprocal24.28
I(0) (reciprocal space) i0_reciprocal34200000.0000
Solution quality estimate total_estimate0.9119
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7344000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (3)

9. Files and Curves (10)