8ovu

Human titin immunoglobulin-like 21 domain

Method: X-RAY DIFFRACTION Dmax: 69.5 Å Quality: GOOD

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

Titin

Homo sapiens

UniProt Q8WZ42

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 3500–3598 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.06 M divalent ions (CaCl2, MgCl2), 0.1 M sodium HEPES, pH 7.5, 50% v/v Polyethylene glycol monomethyl ether (PEGMME) 550, PEG 20K from Morpheus HT-96 screening plate (Molecular Dimensions) Resolution 1.95 Å R-free 0.239
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3500–3598 Not recorded MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.06 M divalent ions (CaCl2, MgCl2), 0.1 M sodium HEPES, pH 7.5, 50% v/v Polyethylene glycol monomethyl ether (PEGMME) 550, PEG 20K from Morpheus HT-96 screening plate (Molecular Dimensions) Resolution 1.95 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.

54 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TITIN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–99; UniProt 3500–3598 Author chain B; PDBConstruct 1–99; UniProt 3500–3598

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 8ovu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ovu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ovu
Deposition date deposition_date2023-04-26
Structure title titleHuman titin immunoglobulin-like 21 domain
Keywords keywordsTitin, Muscle, Immunoglobulin-like, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.31
Radius of gyration Rg (electron density) rg_electron18.45
Forward intensity I(0) i07921220.00
Molecular weight molecular_weight21499.0 kDa
Excluded volume excluded_volume27237 ų
Envelope volume envelope_volume32578 ų
Hydration-shell volume shell_volume15587 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg23.74
Envelope Rg envelope_rg18.79
Shape Rg shape_rg18.43
Total Rg total_rg19.40
Total atoms total_atoms3009
Residues n_residues198
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 dmax69.5
Rg (real space) rg_real19.35
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.9210e+06
I(0) uncertainty (real space) i0_real_error1.0080e+05
Rg (reciprocal space) rg_reciprocal19.34
I(0) (reciprocal space) i0_reciprocal7921000.0000
Solution quality estimate total_estimate0.7728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.427
Kurtosis Kurtosis kurtosis-0.053
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1522000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.729; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.854; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)