1cm1

MOTIONS OF CALMODULIN-SINGLE-CONFORMER REFINEMENT

Method: X-RAY DIFFRACTION Dmax: 53.5 Å Quality: GOOD

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

CALMODULIN

Bos taurus

UniProt P02593

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 A; UniProt 1–148 Not recorded CALMODULIN-DEPENDENT PROTEIN KINASE II-ALPHA × 1 (P11275) CA CALCIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:vapor diffusion - hanging drop - microseeding;pH 5.2;DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding Resolution 2.00 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–148 Not recorded CALMODULIN-DEPENDENT PROTEIN KINASE II-ALPHA × 2 (P11275) CA CALCIUM ION × 10 X-RAY DIFFRACTION X-ray crystallization conditions:vapor diffusion - hanging drop - microseeding;pH 5.2;DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding Resolution 2.00 Å R-free 0.302

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.

10 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–148; UniProt 1–148

CALMODULIN-DEPENDENT PROTEIN KINASE II-ALPHA

Bos taurus

UniProt P11275

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 B; UniProt 290–314 Fragment:CALMODULIN BINDING DOMAIN, RESIDUES 290 - 314 CALMODULIN × 1 (P02593) CA CALCIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:vapor diffusion - hanging drop - microseeding;pH 5.2;DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding Resolution 2.00 Å R-free 0.302
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 290–314 Fragment:CALMODULIN BINDING DOMAIN, RESIDUES 290 - 314 CALMODULIN × 2 (P02593) CA CALCIUM ION × 10 X-RAY DIFFRACTION X-ray crystallization conditions:vapor diffusion - hanging drop - microseeding;pH 5.2;DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding Resolution 2.00 Å R-free 0.302

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCC2A_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 290–314

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 1cm1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cm1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cm1
Deposition date deposition_date1997-09-23
Structure title titleMOTIONS OF CALMODULIN-SINGLE-CONFORMER REFINEMENT
Keywords keywordsCOMPLEX (CALCIUM-BINDING-TRANSFERASE), EF-HAND CALCIUM-BINDING PROTEIN, COMPLEX (CALCIUM-BINDING-TRANSFERASE) complex; COMPLEX (CALCIUM-BINDING/TRANSFERASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.07
Radius of gyration Rg (electron density) rg_electron15.66
Forward intensity I(0) i06898960.00
Molecular weight molecular_weight18198.0 kDa
Excluded volume excluded_volume22330 ų
Envelope volume envelope_volume26053 ų
Hydration-shell volume shell_volume14253 ų
Envelope diameter envelope_diameter52.8
Shell Rg shell_rg21.17
Envelope Rg envelope_rg15.71
Shape Rg shape_rg15.67
Total Rg total_rg16.60
Total atoms total_atoms1263
Residues n_residues161
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 dmax53.5
Rg (real space) rg_real16.98
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real6.8990e+06
I(0) uncertainty (real space) i0_real_error8.1560e+04
Rg (reciprocal space) rg_reciprocal16.99
I(0) (reciprocal space) i0_reciprocal6899000.0000
Solution quality estimate total_estimate0.8230
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.394
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha901300.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cm1a_
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_id1cm1A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (3)

9. Files and Curves (10)