1pqz

MURINE CYTOMEGALOVIRUS IMMUNOMODULATORY PROTEIN M144

Method: X-RAY DIFFRACTION Dmax: 76.3 Å Quality: GOOD

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

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–119 Fragment:Mature Beta-2-Microglobulin MCMV M144 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.8;293 K;16% PEG 8k 100mM cacodylate pH 5.8, .02% Ethyl Acetate, 150mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 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 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

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 1pqz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pqz
Deposition date deposition_date2003-06-19
Structure title titleMURINE CYTOMEGALOVIRUS IMMUNOMODULATORY PROTEIN M144
Keywords keywords;Virus, immune evasion, MCMV, MHC, IG domain, Structural Genomics, PSI, Protein Structure Initiative, Midwest Center for Structural Genomics, MCSG, Viral protein-Immune system COMPLEX ;; Viral protein/Immune system
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.30
Radius of gyration Rg (electron density) rg_electron22.30
Forward intensity I(0) i027062400.00
Molecular weight molecular_weight38130.0 kDa
Excluded volume excluded_volume47047 ų
Envelope volume envelope_volume59105 ų
Hydration-shell volume shell_volume22414 ų
Envelope diameter envelope_diameter77.6
Shell Rg shell_rg28.81
Envelope Rg envelope_rg22.57
Shape Rg shape_rg22.26
Total Rg total_rg23.22
Total atoms total_atoms2681
Residues n_residues337
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 dmax76.3
Rg (real space) rg_real23.29
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.7060e+07
I(0) uncertainty (real space) i0_real_error3.5620e+05
Rg (reciprocal space) rg_reciprocal23.29
I(0) (reciprocal space) i0_reciprocal27060000.0000
Solution quality estimate total_estimate0.8961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha7255000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1pqza1
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_idd1pqza2
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_idd1pqzb_
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 (3 domains)

Domain ID domain_id1pqzA01
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_id1pqzA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1pqzB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)