1zac

N-DOMAIN OF TROPONIN C FROM CHICKEN SKELETAL MUSCLE, NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 41.4 Å Quality: GOOD

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

TROPONIN-C

Gallus gallus

UniProt P02588

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 1–90 Fragment:N-DOMAIN, RESIDUES 1-90 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.7;277 K;Ionic strength (raw mmCIF value) 50mM KCL;Pressure 1 NMR sample composition:WATER 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.

22 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNC2_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–90; UniProt 1–90

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 1zac

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1zac
Deposition date deposition_date1998-04-07
Structure title titleN-DOMAIN OF TROPONIN C FROM CHICKEN SKELETAL MUSCLE, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywordsCALCIUM-BINDING, EF-HAND, MUSCLE PROTEIN, LOW-TEMPERATURE; CALCIUM-BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.55
Radius of gyration Rg (electron density) rg_electron11.87
Forward intensity I(0) i02370600.00
Molecular weight molecular_weight9961.0 kDa
Excluded volume excluded_volume12188 ų
Envelope volume envelope_volume13768 ų
Hydration-shell volume shell_volume9823 ų
Envelope diameter envelope_diameter40.8
Shell Rg shell_rg17.66
Envelope Rg envelope_rg12.35
Shape Rg shape_rg11.87
Total Rg total_rg13.25
Total atoms total_atoms1347
Residues n_residues90
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 dmax41.4
Rg (real space) rg_real13.44
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real2.3710e+06
I(0) uncertainty (real space) i0_real_error2.2600e+04
Rg (reciprocal space) rg_reciprocal13.45
I(0) (reciprocal space) i0_reciprocal2371000.0000
Solution quality estimate total_estimate0.8136
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.9
Skewness Skewness skewness0.048
Kurtosis Kurtosis kurtosis-0.354
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha503100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

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_idd1zaca_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like

CATH v4.4 (1 domains)

Domain ID domain_id1zacA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (2)

9. Files and Curves (10)