1x02

Solution structure of stereo array isotope labeled (SAIL) calmodulin

Method: SOLUTION NMR Dmax: 67.6 Å Quality: EXCELLENT

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 1–148 Not recorded CA CALCIUM ION × 4 SOLUTION NMR NMR measurement conditions:pH 6.5;310 K;Pressure AMBIENT NMR sample composition:0.7mM SAIL calmodulin, 5mM MES-d13, 10mM bis-Tris-d19, 5mM CaCl2, 0.1mM NaN3 | 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 1–148; UniProt 1–148

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 1x02

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1x02
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1x02
Deposition date deposition_date2005-03-11
Structure title titleSolution structure of stereo array isotope labeled (SAIL) calmodulin
Keywords keywordsSAIL, stereo array isotope labeling, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier21.38
Radius of gyration Rg (electron density) rg_electron20.93
Forward intensity I(0) i01788920000.00
Molecular weight molecular_weight336510.0 kDa
Excluded volume excluded_volume411320 ų
Envelope volume envelope_volume81066 ų
Hydration-shell volume shell_volume28077 ų
Envelope diameter envelope_diameter72.6
Shell Rg shell_rg31.16
Envelope Rg envelope_rg23.87
Shape Rg shape_rg20.95
Total Rg total_rg21.08
Total atoms total_atoms45280
Residues n_residues2960
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 dmax67.6
Rg (real space) rg_real21.38
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.7890e+09
I(0) uncertainty (real space) i0_real_error2.2000e+07
Rg (reciprocal space) rg_reciprocal21.39
I(0) (reciprocal space) i0_reciprocal1789000000.0000
Solution quality estimate total_estimate0.9042
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.752
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha803500.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1x02a_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id1x02A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1x02A02
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)