1ntl

Model of mouse Crry-Ig determined by solution scattering, curve fitting and homology modelling

Method: SOLUTION SCATTERING Dmax: 257.8 Å Quality: GOOD

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

Complement component receptor 1-like protein,Ig gamma-1 chain C region secreted form

Mus musculus

UniProt P01868

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 98–324 Chain B; UniProt 98–324 Fragment:Q64735 residues 83-401,P01868 residues 98-324 No other associated polymer SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution 30.00 Å

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.

15 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHG1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 325–551; UniProt 98–324 Author chain B; PDBConstruct 325–551; UniProt 98–324

Complement component receptor 1-like protein,Ig gamma-1 chain C region secreted form

Mus musculus

UniProt Q64735

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 83–401 Chain B; UniProt 83–401 Fragment:Q64735 residues 83-401,P01868 residues 98-324 No other associated polymer SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution 30.00 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name CR1L_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–319; UniProt 83–401 Author chain B; PDBConstruct 1–319; UniProt 83–401

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 1ntl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ntl
Deposition date deposition_date2003-01-30
Structure title titleModel of mouse Crry-Ig determined by solution scattering, curve fitting and homology modelling
Keywords keywordsIMMUNOLOGY, COMPLEMENT, GLYCOPROTEIN, SCR, CCP, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodSOLUTION SCATTERING

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

Radius of gyration Rg (Guinier) rg_guinier76.06
Radius of gyration Rg (electron density) rg_electron76.66
Forward intensity I(0) i0896568000.00
Molecular weight molecular_weight247020.0 kDa
Excluded volume excluded_volume298720 ų
Envelope volume envelope_volume450250 ų
Hydration-shell volume shell_volume57894 ų
Envelope diameter envelope_diameter278.3
Shell Rg shell_rg61.63
Envelope Rg envelope_rg70.70
Shape Rg shape_rg76.71
Total Rg total_rg76.39
Total atoms total_atoms
Residues n_residues
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 dmax257.8
Rg (real space) rg_real76.27
Rg uncertainty (real space) rg_real_error2.42
I(0) (real space) i0_real8.9580e+08
I(0) uncertainty (real space) i0_real_error1.8930e+07
Rg (reciprocal space) rg_reciprocal74.56
I(0) (reciprocal space) i0_reciprocal893100000.0000
Solution quality estimate total_estimate0.8386
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary98.2
Skewness Skewness skewness0.468
Kurtosis Kurtosis kurtosis0.008
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0088
Highest regularization parameter α highest_alpha54960000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.785; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.542

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)