bundle of His cell to Purkinje myocyte communication / regulation of cardiac conduction / regulation of cardiac muscle contraction / regulation of heart rate / non-specific serine/threonine protein kinase / protein kinase activity / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding ...bundle of His cell to Purkinje myocyte communication / regulation of cardiac conduction / regulation of cardiac muscle contraction / regulation of heart rate / non-specific serine/threonine protein kinase / protein kinase activity / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / metal ion binding / nucleus / cytoplasm Similarity search - Function
Ankyrin repeats (many copies) / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site ...Ankyrin repeats (many copies) / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily Similarity search - Domain/homology
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.54 Å / Relative weight: 1
Reflection
Resolution: 3.06→50 Å / Num. obs: 30089 / % possible obs: 99.1 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.099 / Χ2: 2.233 / Net I/av σ(I): 20.486 / Net I/σ(I): 11 / Num. measured all: 103684
Reflection shell
Diffraction-ID: 1 / Rejects: 0
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Num. unique all
Χ2
% possible all
3.06-3.2
3.5
0.779
1467
1.75
99.9
3.2-3.26
3.5
0.574
1548
1.549
100
3.26-3.33
3.6
0.548
1475
1.728
99.9
3.33-3.39
3.5
0.395
1542
1.79
100
3.39-3.47
3.6
0.36
1491
1.803
99.8
3.47-3.55
3.6
0.273
1511
1.881
99.8
3.55-3.64
3.6
0.214
1498
1.977
99.7
3.64-3.73
3.5
0.191
1526
2.057
99.8
3.73-3.84
3.6
0.166
1476
2.185
99.9
3.84-3.97
3.5
0.141
1532
2.134
99.7
3.97-4.11
3.5
0.123
1500
2.334
99.6
4.11-4.27
3.4
0.098
1512
2.435
99.5
4.27-4.47
3.4
0.089
1501
2.692
98.5
4.47-4.7
3.3
0.079
1489
2.721
99.1
4.7-5
3.3
0.075
1501
2.545
98.9
5-5.38
3.4
0.073
1511
2.574
99.2
5.38-5.93
3.4
0.07
1525
2.469
99.3
5.93-6.78
3.4
0.065
1517
2.515
99.3
6.78-8.54
3.2
0.047
1510
2.741
98.7
8.54-50
2.8
0.039
1457
3.368
92.2
-
Processing
Software
Name
Version
Classification
REFMAC
5.8.0073
refinement
SCALEPACK
datascaling
PDB_EXTRACT
3.15
dataextraction
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.07→20 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.92 / SU B: 39.507 / SU ML: 0.327 / Cross valid method: THROUGHOUT / ESU R Free: 0.426 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.251
1512
5 %
RANDOM
Rwork
0.209
-
-
-
obs
0.211
28481
95.8 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK