1df3

SOLUTION STRUCTURE OF A RECOMBINANT MOUSE MAJOR URINARY PROTEIN

Method: SOLUTION NMR Dmax: 59.0 Å Quality: GOOD

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

MAJOR URINARY PROTEIN

Mus musculus

UniProt P11589

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–180 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.2;308 K;Ionic strength (raw mmCIF value) 10mM PHOSPHATE;Pressure AMBIENT NMR sample composition:UNIFORMLY 15N- AND 13C/15N-LABELLED RECOMBINANT MUP FROM MOUSE; 10MM PHOSPHATE BUFFER Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name MUP2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–162; UniProt 19–180

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 1df3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1df3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1df3
Deposition date deposition_date1999-11-17
Structure title titleSOLUTION STRUCTURE OF A RECOMBINANT MOUSE MAJOR URINARY PROTEIN
Keywords keywords;LIPOCALIN, CARRIER PROTEIN, PHEROMONE, 8-STRANDED BETA-BARREL, BINDING POCKET, DISULFIDE BRIDGE (64-157), SIGNALING PROTEIN, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.24
Radius of gyration Rg (electron density) rg_electron15.37
Forward intensity I(0) i0529359000.00
Molecular weight molecular_weight186970.0 kDa
Excluded volume excluded_volume230990 ų
Envelope volume envelope_volume41188 ų
Hydration-shell volume shell_volume19159 ų
Envelope diameter envelope_diameter63.0
Shell Rg shell_rg24.49
Envelope Rg envelope_rg18.14
Shape Rg shape_rg15.35
Total Rg total_rg15.70
Total atoms total_atoms26010
Residues n_residues1620
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 dmax59.0
Rg (real space) rg_real16.11
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real5.2940e+08
I(0) uncertainty (real space) i0_real_error6.9900e+06
Rg (reciprocal space) rg_reciprocal16.12
I(0) (reciprocal space) i0_reciprocal529400000.0000
Solution quality estimate total_estimate0.8229
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.5
Skewness Skewness skewness0.111
Kurtosis Kurtosis kurtosis-0.226
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1057000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.565; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1df3a_
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.1 — Retinol binding protein-like

CATH v4.4 (1 domains)

Domain ID domain_id1df3A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain

8. Citations (3)

9. Files and Curves (10)