4o00

Crystal structure of the Titin A-band domain A3

Method: X-RAY DIFFRACTION Dmax: 64.5 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 14217–14319 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;291 K;0.1M SPG buffer, 0.01M Tris-HCl, 31% PEG1500, 50mM NaCl, 1mM DTT, pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.85 Å R-free 0.208
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 14217–14319 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;291 K;0.1M SPG buffer, 0.01M Tris-HCl, 31% PEG1500, 50mM NaCl, 1mM DTT, pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.85 Å R-free 0.208

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 2–104; UniProt 14217–14319 Author chain B; PDBConstruct 2–104; UniProt 14217–14319

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 4o00

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4o00
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4o00
Deposition date deposition_date2013-12-13
Structure title titleCrystal structure of the Titin A-band domain A3
Keywords keywordsbeta barrel, fibronectin-3 domain, myosin-binding, 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_guinier19.26
Radius of gyration Rg (electron density) rg_electron18.37
Forward intensity I(0) i09515530.00
Molecular weight molecular_weight22665.0 kDa
Excluded volume excluded_volume28276 ų
Envelope volume envelope_volume33201 ų
Hydration-shell volume shell_volume15649 ų
Envelope diameter envelope_diameter63.2
Shell Rg shell_rg23.71
Envelope Rg envelope_rg18.58
Shape Rg shape_rg18.37
Total Rg total_rg19.20
Total atoms total_atoms3165
Residues n_residues206
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 dmax64.5
Rg (real space) rg_real19.22
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real9.5160e+06
I(0) uncertainty (real space) i0_real_error1.2550e+05
Rg (reciprocal space) rg_reciprocal19.23
I(0) (reciprocal space) i0_reciprocal9516000.0000
Solution quality estimate total_estimate0.8908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.228
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1829000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4o00a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.0 — automated matches
Domain ID domain_idd4o00a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4o00b1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.0 — automated matches
Domain ID domain_idd4o00b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4o00A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4o00B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)