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- PDB-3g43: Crystal structure of the calmodulin-bound Cav1.2 C-terminal regul... -

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Basic information

Entry
Database: PDB / ID: 3g43
TitleCrystal structure of the calmodulin-bound Cav1.2 C-terminal regulatory domain dimer
Components
  • Calmodulin
  • Voltage-dependent L-type calcium channel subunit alpha-1C
KeywordsMETAL BINDING PROTEIN / calmodulin-bound / coiled coil / calcium channel / Acetylation / Calcium / Methylation / Phosphoprotein / Polymorphism / Ubl conjugation / Alternative splicing / Brugada syndrome / Calcium transport / Disease mutation / Glycoprotein / Ion transport / Ionic channel / Membrane / Transmembrane / Transport / Voltage-gated channel
Function / homology
Function and homology information


: / voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / immune system development / membrane depolarization during atrial cardiac muscle cell action potential / Phase 2 - plateau phase / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during AV node cell action potential / positive regulation of adenylate cyclase activity / cardiac conduction ...: / voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / immune system development / membrane depolarization during atrial cardiac muscle cell action potential / Phase 2 - plateau phase / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during AV node cell action potential / positive regulation of adenylate cyclase activity / cardiac conduction / high voltage-gated calcium channel activity / : / L-type voltage-gated calcium channel complex / establishment of protein localization to mitochondrial membrane / membrane depolarization during cardiac muscle cell action potential / type 3 metabotropic glutamate receptor binding / regulation of ventricular cardiac muscle cell action potential / cardiac muscle cell action potential involved in contraction / camera-type eye development / NCAM1 interactions / embryonic forelimb morphogenesis / CaM pathway / Cam-PDE 1 activation / calcium ion transport into cytosol / Sodium/Calcium exchangers / cell communication by electrical coupling involved in cardiac conduction / Calmodulin induced events / Reduction of cytosolic Ca++ levels / regulation of synaptic vesicle endocytosis / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / voltage-gated calcium channel complex / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / regulation of synaptic vesicle exocytosis / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / Activation of RAC1 downstream of NMDARs / mitochondrion-endoplasmic reticulum membrane tethering / CLEC7A (Dectin-1) induces NFAT activation / regulation of cardiac muscle cell action potential / autophagosome membrane docking / response to corticosterone / positive regulation of ryanodine-sensitive calcium-release channel activity / regulation of cell communication by electrical coupling involved in cardiac conduction / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of peptidyl-threonine phosphorylation / Synthesis of IP3 and IP4 in the cytosol / Unblocking of NMDA receptors, glutamate binding and activation / nitric-oxide synthase binding / Phase 0 - rapid depolarisation / alpha-actinin binding / protein phosphatase activator activity / regulation of heart rate by cardiac conduction / RHO GTPases activate PAKs / positive regulation of cyclic-nucleotide phosphodiesterase activity / positive regulation of phosphoprotein phosphatase activity / Ion transport by P-type ATPases / Long-term potentiation / calcium ion import across plasma membrane / Uptake and function of anthrax toxins / adenylate cyclase binding / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / catalytic complex / DARPP-32 events / detection of calcium ion / negative regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / voltage-gated calcium channel activity / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction / calcium channel inhibitor activity / cellular response to interferon-beta / positive regulation of DNA binding / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Protein methylation / phosphatidylinositol 3-kinase binding / enzyme regulator activity / eNOS activation / Activation of AMPK downstream of NMDARs / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / regulation of calcium-mediated signaling / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / positive regulation of protein dephosphorylation / voltage-gated potassium channel complex / Ion homeostasis / regulation of ryanodine-sensitive calcium-release channel activity / titin binding / positive regulation of protein autophosphorylation / sperm midpiece / calcium channel complex / activation of adenylate cyclase activity / response to amphetamine / substantia nigra development / adenylate cyclase activator activity
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2180 / Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2180 / Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain / Voltage-dependent L-type calcium channel, IQ-associated / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Voltage-dependent channel domain superfamily / EF-hand domain pair / Helix non-globular / EF-hand, calcium binding motif / Special / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / Ion transport domain / Ion transport protein / EF-hand domain pair
Similarity search - Domain/homology
Calmodulin-1 / Calmodulin-3 / Voltage-dependent L-type calcium channel subunit alpha-1C
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.1 Å
AuthorsFallon, J.L. / Quiocho, F.A.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 2009
Title: Crystal structure of dimeric cardiac L-type calcium channel regulatory domains bridged by Ca2+{middle dot}calmodulins.
Authors: Fallon, J.L. / Baker, M.R. / Xiong, L. / Loy, R.E. / Yang, G. / Dirksen, R.T. / Hamilton, S.L. / Quiocho, F.A.
#1: Journal: Structure / Year: 2005
Title: Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.
Authors: Fallon, J.L. / Halling, D.B. / Hamilton, S.L. / Quiocho, F.A.
History
DepositionFeb 3, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 3, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software
Revision 1.3Feb 21, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Calmodulin
B: Calmodulin
C: Calmodulin
D: Calmodulin
E: Voltage-dependent L-type calcium channel subunit alpha-1C
F: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)86,16020
Polymers85,5996
Non-polymers56114
Water9,332518
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12630 Å2
ΔGint-97.3 kcal/mol
Surface area29060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)39.790, 113.980, 182.130
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
DetailsBIOLOGICAL UNIT IS THE SAME AS AN ASYMMETRIC UNIT.

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Components

#1: Protein
Calmodulin / / CaM


Mass: 16721.350 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII
Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62158, UniProt: P0DP23*PLUS
#2: Protein Voltage-dependent L-type calcium channel subunit alpha-1C / Voltage-gated calcium channel subunit alpha Cav1.2 / Calcium channel / L type / alpha-1 polypeptide ...Voltage-gated calcium channel subunit alpha Cav1.2 / Calcium channel / L type / alpha-1 polypeptide / isoform 1 / cardiac muscle


Mass: 9356.910 Da / Num. of mol.: 2 / Fragment: C-terminal fragment: UNP residues 1609-1682
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CACNA1C, CACH2, CACN2, CACNL1A1, CCHL1A1 / Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q13936
#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 518 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.41 Å3/Da / Density % sol: 49.01 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 20% PEG 6000, 1.0 M LiCl, 3% w/v MPD, 100 mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONAPS 19-ID10.95372
SYNCHROTRONCAMD GCPCC20.9510, 0.9500, 0.9450
Detector
TypeIDDetectorDate
ADSC QUANTUM 3151CCDMar 20, 2007
MAR CCD 165 mm2CCDDec 14, 2006
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SAGITALLY FOCUSED Si(111)SINGLE WAVELENGTHMx-ray1
2Si(111) CHANNELMADMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.953721
20.9511
30.951
40.9451
ReflectionRedundancy: 4.7 % / Av σ(I) over netI: 26.02 / Number: 185304 / Rmerge(I) obs: 0.062 / Χ2: 0.69 / D res high: 2.7 Å / D res low: 50 Å / Num. obs: 39795 / % possible obs: 88.1
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
5.815090.710.0240.5664.8
4.625.8192.710.0420.6654.7
4.034.6291.310.0450.7494.7
3.664.0390.810.0640.8584.7
3.43.6690.310.080.7334.7
3.23.491.310.10.6534.7
3.043.288.610.1410.6024.7
2.913.048810.1890.6094.7
2.82.918710.2630.5954.6
2.72.870.410.4030.9174
ReflectionResolution: 2.1→20 Å / Num. all: 49459 / Num. obs: 49200 / % possible obs: 99.8 % / Observed criterion σ(I): 1 / Redundancy: 5.9 % / Rmerge(I) obs: 0.041 / Χ2: 1.001 / Net I/σ(I): 39.6
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.278 / Mean I/σ(I) obs: 5.3 / Num. unique all: 4799 / Χ2: 0.767 / % possible all: 99.9

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Phasing

PhasingMethod: MAD
Phasing MADD res high: 2.79 Å / D res low: 19.81 Å / FOM : 0.52 / FOM acentric: 0.518 / FOM centric: 0.553 / Reflection: 35562
Phasing MAD set

Highest resolution: 2.79 Å / Lowest resolution: 19.81 Å

IDR cullisR cullis acentricR cullis centricR krautR kraut acentricR kraut centricFOM FOM acentricFOM centricLocLoc acentricLoc centricPower (kW)Power acentricPower centric
f_w10.8280.8270.8570.040.040.0320.0960.0830.27212.12112.19611.170.3370.3330.401
f_w1_FRIED0.5630.5530.8640.0410.0420.0350.3430.3490.26112.10912.16711.4042.2312.2022.647
f_w20.8010.8040.7590.0360.0370.030.1840.1690.39811.98312.0611.010.7040.6940.853
f_w2_FRIED0.590.5820.7620.0390.0390.0320.3420.3380.39711.93511.99911.1532.0221.9932.43
f_w3_FRIED0.5810.5639.5130.0390.0410.0130.3120.336012.10312.16611.3582.0632.0342.468
Phasing MAD set shell
IDResolution (Å)R cullisR cullis acentricR cullis centricR krautR kraut acentricR kraut centricFOM FOM acentricFOM centricLocLoc acentricLoc centricPower (kW)Power acentricPower centric
f_w15.54-19.810.8840.8950.820.0150.0150.0160.210.1740.4567.7857.7927.8330.7940.7940.794
f_w14.42-5.540.8380.8430.7870.0220.0210.0250.1550.1390.3438.7638.7668.7910.5910.5920.58
f_w13.86-4.420.8980.9030.8430.0230.0230.0240.1170.1040.2959.8989.9019.9270.450.450.459
f_w13.51-3.860.850.8510.8230.0350.0350.0360.0810.0740.20112.00912.01112.0310.3310.3330.313
f_w13.26-3.510.8570.8570.8580.0470.0470.0460.0620.0570.15813.15113.15413.1910.2690.2690.26
f_w13.07-3.260.8030.8010.8410.0680.0690.0620.0510.0460.13313.89613.89713.9090.2260.2260.241
f_w12.92-3.070.7860.7820.9010.0970.0980.0840.0380.0350.09815.33515.33715.3540.1840.1840.192
f_w12.79-2.920.8180.8130.9510.1360.1380.1110.0270.0250.07317.92817.93318.0010.1470.1470.148
f_w1_FRIED5.54-19.810.3220.3030.9660.0190.0190.0210.5130.5250.4359.0139.0229.0694.7024.6974.736
f_w1_FRIED4.42-5.540.3980.3860.8210.0260.0260.0270.4620.4740.3269.1799.1829.2033.7293.743.595
f_w1_FRIED3.86-4.420.5020.490.8550.0270.0270.0270.4190.4290.28510.14610.14910.1752.8222.8162.896
f_w1_FRIED3.51-3.860.6010.5920.8490.0390.0390.0350.3550.3640.20412.37612.37812.3982.0342.0361.998
f_w1_FRIED3.26-3.510.6490.6430.8210.0490.0490.0470.3140.3220.15912.6212.62312.6581.761.7641.692
f_w1_FRIED3.07-3.260.6870.6810.8260.0660.0660.0640.2510.2590.1213.57613.57713.5891.4431.441.496
f_w1_FRIED2.92-3.070.7220.7160.8830.0870.0870.0840.2010.2060.08914.94814.94914.9661.181.1791.196
f_w1_FRIED2.79-2.920.7330.7280.8780.1190.1190.1110.1630.1670.07316.4716.47416.5370.9910.9891.03
f_w25.54-19.810.660.6760.5780.0140.0130.0150.380.3450.6247.6437.6517.6921.7381.7351.76
f_w24.42-5.540.7460.7530.6730.0190.0190.0220.2850.2670.4998.4038.4058.431.2881.2911.253
f_w23.86-4.420.7790.7870.6910.0210.0210.0210.2370.2210.4549.1669.1689.1931.0010.9981.038
f_w23.51-3.860.7970.80.7530.0340.0340.0360.1620.1530.32212.24312.24512.2650.660.6620.637
f_w23.26-3.510.850.850.8550.0430.0430.0440.1230.1170.23512.93812.94112.9760.5510.5520.526
f_w23.07-3.260.8090.8090.8060.0630.0630.0580.1010.0950.20614.08814.08914.1020.4480.4470.467
f_w22.92-3.070.7920.790.8280.0890.0890.0790.0780.0730.16815.16615.16715.1840.3720.3720.376
f_w22.79-2.920.8480.8450.9250.1280.1280.1110.0580.0540.12718.17918.18418.2510.2870.2870.295
f_w2_FRIED5.54-19.810.3410.3240.6520.0170.0170.0190.5250.5150.6068.6048.6128.6584.4294.4244.46
f_w2_FRIED4.42-5.540.4170.4060.690.0230.0230.0250.4680.4660.4968.6188.628.6453.5753.5813.503
f_w2_FRIED3.86-4.420.5170.5070.750.0240.0250.0230.420.4180.4479.4969.4999.5242.7172.7082.838
f_w2_FRIED3.51-3.860.6150.6090.7490.0380.0380.0360.3510.3520.3312.20412.20512.2251.8561.8581.832
f_w2_FRIED3.26-3.510.6490.6430.8180.0460.0460.0440.3010.3040.25112.37912.38112.4151.6161.6181.573
f_w2_FRIED3.07-3.260.7040.70.7830.0640.0640.060.2480.2490.22513.71913.7213.7331.2831.281.333
f_w2_FRIED2.92-3.070.7190.7150.8080.0850.0850.080.1980.1990.17514.78914.7914.8061.0711.071.081
f_w2_FRIED2.79-2.920.7680.7630.8860.1180.1180.110.1540.1560.13317.42117.42617.4910.8450.8430.877
f_w3_FRIED5.54-19.810.3150.294100.0170.0180.0120.4560.52508.4388.4468.494.8334.8264.881
f_w3_FRIED4.42-5.540.4130.396100.0240.0250.0130.4340.47209.0719.0749.0943.5323.5413.427
f_w3_FRIED3.86-4.420.5010.4836.1630.0250.0260.010.3880.41709.6759.6779.7022.7282.7212.825
f_w3_FRIED3.51-3.860.5990.5817.3370.0350.0370.0120.3370.359011.85111.85311.8711.931.9321.888
f_w3_FRIED3.26-3.510.6750.6568.0340.0450.0470.0150.2850.302013.08913.09213.1251.5361.5381.517
f_w3_FRIED3.07-3.260.7030.6839.1770.0650.0680.0170.2240.237014.0314.03114.0431.2591.2571.296
f_w3_FRIED2.92-3.070.7360.718100.0830.0860.0190.1780.187014.80314.80414.8191.0671.0671.064
f_w3_FRIED2.79-2.920.770.749100.1190.1240.0240.1340.142017.53317.53717.5970.8390.8370.868
Phasing MAD shell
Resolution (Å)FOM FOM acentricFOM centricReflection
5.54-19.810.77340.77710.75814594
4.42-5.540.69380.6950.6854601
3.86-4.420.62250.62350.61374656
3.51-3.860.53250.53270.53154512
3.26-3.510.46530.46830.4164526
3.07-3.260.40160.40330.3724456
2.92-3.070.33420.33580.3014413
2.79-2.920.28110.28290.24653804

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing
CNS1.2refinement
PDB_EXTRACT3.006data extraction
HKL-3000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MAD / Resolution: 2.1→19.93 Å / Rfactor Rfree error: 0.005 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.832 / Data cutoff high absF: 26268948 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflectionSelection details
Rfree0.269 3191 7.1 %RANDOM
Rwork0.22 ---
all0.253 49200 --
obs0.22 47974 97.3 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 54.198 Å2 / ksol: 0.35 e/Å3
Displacement parametersBiso max: 92.54 Å2 / Biso mean: 46.363 Å2 / Biso min: 17.78 Å2
Baniso -1Baniso -2Baniso -3
1-2.4 Å20 Å20 Å2
2--2.69 Å20 Å2
3----5.09 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.32 Å0.25 Å
Luzzati d res low-5 Å
Luzzati sigma a0.15 Å0.11 Å
Refinement stepCycle: LAST / Resolution: 2.1→19.93 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4997 0 14 518 5529
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.005
X-RAY DIFFRACTIONc_angle_deg1
X-RAY DIFFRACTIONc_dihedral_angle_d18
X-RAY DIFFRACTIONc_improper_angle_d0.63
X-RAY DIFFRACTIONc_mcbond_it1.671.5
X-RAY DIFFRACTIONc_mcangle_it2.72
X-RAY DIFFRACTIONc_scbond_it2.382
X-RAY DIFFRACTIONc_scangle_it3.612.5
LS refinement shellResolution: 2.1→2.23 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.265 421 6.8 %
Rwork0.215 5730 -
all-6151 -
obs--76 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2water_rep.paramwater.top
X-RAY DIFFRACTION3ion.paramion.top

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