1vdi

Solution structure of actin-binding domain of troponin in Ca2+-free state

Method: SOLUTION NMR Dmax: 58.0 Å Quality: REASONABLE

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

Troponin I, fast skeletal muscle

Gallus gallus

UniProt P68246

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 131–182 Fragment:residues 131-182 No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNI2_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–52; UniProt 131–182

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 1vdi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1vdi
Deposition date deposition_date2004-03-22
Structure title titleSolution structure of actin-binding domain of troponin in Ca2+-free state
Keywords keywordstroponin, actin, tropomyosin, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.90
Radius of gyration Rg (electron density) rg_electron14.08
Forward intensity I(0) i0240105000.00
Molecular weight molecular_weight122200.0 kDa
Excluded volume excluded_volume150340 ų
Envelope volume envelope_volume27813 ų
Hydration-shell volume shell_volume13332 ų
Envelope diameter envelope_diameter62.5
Shell Rg shell_rg23.68
Envelope Rg envelope_rg19.45
Shape Rg shape_rg14.04
Total Rg total_rg14.54
Total atoms total_atoms15320
Residues n_residues1040
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 dmax58.0
Rg (real space) rg_real14.19
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real2.4010e+08
I(0) uncertainty (real space) i0_real_error2.9310e+06
Rg (reciprocal space) rg_reciprocal14.17
I(0) (reciprocal space) i0_reciprocal240100000.0000
Solution quality estimate total_estimate0.7026
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.2
Skewness Skewness skewness0.761
Kurtosis Kurtosis kurtosis0.338
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha110900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.364; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.062; Smooth: 0.975

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_idd1vdia1
Class classj — Peptides
Fold Fold foldj.22 — Troponin I fragments
Superfamily Superfamily superfamilyj.22.1 — Troponin I fragments
Family Family familyj.22.1.1 — Troponin I fragments

CATH v4.4 (1 domains)

Domain ID domain_id1vdiA00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily180

8. Citations (1)

9. Files and Curves (10)