1f71

REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN

Method: SOLUTION NMR Dmax: 37.8 Å Quality: GOOD

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

CALMODULIN

Xenopus laevis

UniProt P62155

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 83–149 Fragment:C-TERMINAL DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 100mM KCl;Pressure ambient NMR sample composition:1 mM Calmodulin U-15N,13C; 5 mM Hepes buffer, 100 mM KCl | 90% H2O/10% D2O NMR sample composition:1 mM Calmodulin U-15N,13C; 5 mM Hepes buffer, 100 mM KCl; 21 mg/ml filamentous phage pf1 | 90% H2O/10% D2O 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 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–67; UniProt 83–149

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 1f71

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f71
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f71
Deposition date deposition_date2000-06-24
Structure title titleREFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN
Keywords keywordsCalcium binding, EF hand, four-helix bundle, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.01
Radius of gyration Rg (electron density) rg_electron11.38
Forward intensity I(0) i097888000.00
Molecular weight molecular_weight76844.0 kDa
Excluded volume excluded_volume93694 ų
Envelope volume envelope_volume15303 ų
Hydration-shell volume shell_volume10521 ų
Envelope diameter envelope_diameter38.7
Shell Rg shell_rg18.19
Envelope Rg envelope_rg12.66
Shape Rg shape_rg11.38
Total Rg total_rg11.64
Total atoms total_atoms10380
Residues n_residues670
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 dmax37.8
Rg (real space) rg_real11.92
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real9.7890e+07
I(0) uncertainty (real space) i0_real_error1.1100e+06
Rg (reciprocal space) rg_reciprocal11.92
I(0) (reciprocal space) i0_reciprocal97890000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.3
Skewness Skewness skewness0.028
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha154100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.946

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_idd1f71a_
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_id1f71A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)