6jiu

Structure of RyR2 (F/A/C/L-Ca2+/Ca2+CaM dataset)

Method: ELECTRON MICROSCOPY Dmax: 260.1 Å Quality: EXCELLENT

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

Peptidyl-prolyl cis-trans isomerase FKBP1B

Homo sapiens

UniProt P68106

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–108 Chain E; UniProt 1–108 Chain H; UniProt 1–108 Chain K; UniProt 1–108 Not recorded RyR2 × 4 Calmodulin-1 × 4 (P0DP23) ZN ZINC ION × 4 CA CALCIUM ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 CFF CAFFEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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.

117 other PDB entries and 119 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FKB1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–108; UniProt 1–108 Author chain E; PDBConstruct 1–108; UniProt 1–108 Author chain H; PDBConstruct 1–108; UniProt 1–108 Author chain K; PDBConstruct 1–108; UniProt 1–108

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–149 Chain F; UniProt 1–149 Chain I; UniProt 1–149 Chain L; UniProt 1–149 Not recorded RyR2 × 4 Peptidyl-prolyl cis-trans isomerase FKBP1B × 4 (P68106) ZN ZINC ION × 4 CA CALCIUM ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 CFF CAFFEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–149; UniProt 1–149 Author chain F; PDBConstruct 1–149; UniProt 1–149 Author chain I; PDBConstruct 1–149; UniProt 1–149 Author chain L; 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 6jiu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6jiu
Deposition date deposition_date2019-02-23
Structure title titleStructure of RyR2 (F/A/C/L-Ca2+/Ca2+CaM dataset)
Keywords keywordscryo-EM, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron100.40
Forward intensity I(0) i034935100000.00
Molecular weight molecular_weight1593700.0 kDa
Excluded volume excluded_volume1990100 ų
Envelope volume envelope_volume3950800 ų
Hydration-shell volume shell_volume321150 ų
Envelope diameter envelope_diameter373.4
Shell Rg shell_rg99.69
Envelope Rg envelope_rg98.59
Shape Rg shape_rg100.60
Total Rg total_rg100.00
Total atoms total_atoms112212
Residues n_residues14684
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 dmax260.1
Rg (real space) rg_real96.76
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real3.3420e+10
I(0) uncertainty (real space) i0_real_error6.1530e+08
Rg (reciprocal space) rg_reciprocal100.90
I(0) (reciprocal space) i0_reciprocal34930000000.0000
Solution quality estimate total_estimate0.9132
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary121.4
Skewness Skewness skewness0.122
Kurtosis Kurtosis kurtosis-0.656
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.7124
Highest regularization parameter α highest_alpha2996000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.997; Stabil: 0.974; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)