6xy3

2.0 Angstrom crystal structure of Ca/CaM N53I:RyR2 peptide complex

Method: X-RAY DIFFRACTION Dmax: 60.0 Å Quality: GOOD

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

Calmodulin-1

Homo sapiens

UniProt P0DP23

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain AAA; UniProt 1–149 Not recorded RyR2 peptide × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Sodium acetate trihydrate pH 4.5, 10% w/v Polyethylene glycol 10,000 Resolution 2.00 Å R-free 0.260

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.

213 other PDB entries and 279 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 1–149; UniProt 1–149

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 6xy3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xy3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xy3
Deposition date deposition_date2020-01-29
Structure title title2.0 Angstrom crystal structure of Ca/CaM N53I:RyR2 peptide complex
Keywords keywordscalcium-binding protein, cardiac muscle contraction, RyR2, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.06
Radius of gyration Rg (electron density) rg_electron17.04
Forward intensity I(0) i06723190.00
Molecular weight molecular_weight18382.0 kDa
Excluded volume excluded_volume22703 ų
Envelope volume envelope_volume26335 ų
Hydration-shell volume shell_volume13617 ų
Envelope diameter envelope_diameter58.6
Shell Rg shell_rg22.09
Envelope Rg envelope_rg17.08
Shape Rg shape_rg17.03
Total Rg total_rg17.90
Total atoms total_atoms2505
Residues n_residues165
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 dmax60.0
Rg (real space) rg_real18.07
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real6.7230e+06
I(0) uncertainty (real space) i0_real_error8.4710e+04
Rg (reciprocal space) rg_reciprocal18.07
I(0) (reciprocal space) i0_reciprocal6723000.0000
Solution quality estimate total_estimate0.8820
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1034000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)