9arv

CryoEM structure of AMETA-A3

Method: ELECTRON MICROSCOPY Dmax: 176.6 Å Quality: GOOD

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

Isoform 1 of Immunoglobulin heavy constant mu

Homo sapiens

UniProt P01871

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain A; UniProt 106–453 Chain B; UniProt 106–453 Chain C; UniProt 106–453 Chain D; UniProt 106–453 Chain E; UniProt 106–453 Chain L; UniProt 106–453 Chain M; UniProt 106–453 Chain N; UniProt 106–453 Chain O; UniProt 106–453 Chain P; UniProt 106–453 Not recorded Immunoglobulin J chain × 1 (P01591) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHM_HUMAN
Isoform P01871-1
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–375; UniProt 106–453 Author chain B; PDBConstruct 28–375; UniProt 106–453 Author chain C; PDBConstruct 28–375; UniProt 106–453 Author chain D; PDBConstruct 28–375; UniProt 106–453 Author chain E; PDBConstruct 28–375; UniProt 106–453 Author chain L; PDBConstruct 28–375; UniProt 106–453 Author chain M; PDBConstruct 28–375; UniProt 106–453 Author chain N; PDBConstruct 28–375; UniProt 106–453 Author chain O; PDBConstruct 28–375; UniProt 106–453 Author chain P; PDBConstruct 28–375; UniProt 106–453

Immunoglobulin J chain

Homo sapiens

UniProt P01591

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain J; UniProt 1–159 Not recorded Isoform 1 of Immunoglobulin heavy constant mu × 10 (P01871) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGJ_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain J; PDBConstruct 1–159; UniProt 1–159

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 9arv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9arv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9arv
Deposition date deposition_date2024-02-23
Structure title titleCryoEM structure of AMETA-A3
Keywords keywordsIgM, nanobody, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.91
Radius of gyration Rg (electron density) rg_electron56.89
Forward intensity I(0) i01017130000.00
Molecular weight molecular_weight263320.0 kDa
Excluded volume excluded_volume328320 ų
Envelope volume envelope_volume527960 ų
Hydration-shell volume shell_volume78887 ų
Envelope diameter envelope_diameter190.6
Shell Rg shell_rg55.43
Envelope Rg envelope_rg56.82
Shape Rg shape_rg56.91
Total Rg total_rg56.78
Total atoms total_atoms36630
Residues n_residues2376
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 dmax176.6
Rg (real space) rg_real57.06
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real1.0170e+09
I(0) uncertainty (real space) i0_real_error1.9600e+07
Rg (reciprocal space) rg_reciprocal56.75
I(0) (reciprocal space) i0_reciprocal1017000000.0000
Solution quality estimate total_estimate0.8397
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.8
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86020000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.018

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)