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- PDB-3oxq: Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex -

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Basic information

Entry
Database: PDB / ID: 3oxq
TitleCrystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex
Components
  • Calmodulin
  • Voltage-dependent L-type calcium channel subunit alpha-1C
KeywordsMETAL BINDING PROTEIN/TRANSPORT PROTEIN / EF hand IQ domain / calcium sensing / calcium binding / Ion channel / METAL BINDING PROTEIN-TRANSPORT PROTEIN complex
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 / high voltage-gated calcium channel activity ...: / 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 / high voltage-gated calcium channel activity / cardiac conduction / : / 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 / regulation of synaptic vesicle endocytosis / cell communication by electrical coupling involved in cardiac conduction / Calmodulin induced events / Reduction of cytosolic Ca++ levels / voltage-gated calcium channel complex / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / positive regulation of cyclic-nucleotide phosphodiesterase activity / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / regulation of synaptic vesicle exocytosis / CLEC7A (Dectin-1) induces NFAT activation / regulation of cardiac muscle cell action potential / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / Activation of RAC1 downstream of NMDARs / response to corticosterone / nitric-oxide synthase binding / 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 / 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 phosphoprotein phosphatase activity / Ion transport by P-type ATPases / Long-term potentiation / Uptake and function of anthrax toxins / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / adenylate cyclase binding / catalytic complex / DARPP-32 events / detection of calcium ion / regulation of cardiac muscle contraction / calcium ion import across plasma membrane / negative regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / voltage-gated calcium channel activity / RHO GTPases activate IQGAPs / 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 / eNOS activation / Activation of AMPK downstream of NMDARs / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / positive regulation of protein dephosphorylation / Ion homeostasis / regulation of calcium-mediated signaling / regulation of ryanodine-sensitive calcium-release channel activity / titin binding / positive regulation of protein autophosphorylation / voltage-gated potassium channel complex / sperm midpiece / calcium channel complex / response to amphetamine / activation of adenylate cyclase activity / 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 / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsKim, E.Y. / Rumpf, C.H. / Van Petegem, F. / Arant, R. / Findeisen, F. / Cooley, E.S. / Isacoff, E.Y. / Minor, D.L.
CitationJournal: Embo J. / Year: 2010
Title: Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.
Authors: Kim, E.Y. / Rumpf, C.H. / Van Petegem, F. / Arant, R.J. / Findeisen, F. / Cooley, E.S. / Isacoff, E.Y. / Minor, D.L.
History
DepositionSep 21, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 3, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / 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_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_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)86,23520
Polymers85,6746
Non-polymers56114
Water1,74797
1
A: Calmodulin
D: Calmodulin
E: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,11710
Polymers42,8373
Non-polymers2817
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4230 Å2
ΔGint-117 kcal/mol
Surface area20290 Å2
MethodPISA
2
B: Calmodulin
C: Calmodulin
F: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,11710
Polymers42,8373
Non-polymers2817
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4560 Å2
ΔGint-116 kcal/mol
Surface area20070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)39.716, 132.050, 158.222
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12A
22C
13B
23D
14E
24F
15E
25F

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LEULEUMETMET2AA4 - 765 - 77
21LEULEUMETMET2CC4 - 765 - 77
12GLUGLUMETMET2AA84 - 14585 - 146
22GLUGLUMETMET2CC84 - 14585 - 146
13LEULEUMETMET2BB4 - 765 - 77
23LEULEUMETMET2DD4 - 765 - 77
14GLYGLYARGARG3EE1560 - 15951 - 36
24GLYGLYARGARG3FF1560 - 15951 - 36
15THRTHRLYSLYS2EE1614 - 163355 - 74
25THRTHRLYSLYS2FF1614 - 163355 - 74

NCS ensembles :
ID
1
2
3
4
5

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Components

#1: Protein
Calmodulin / CaM


Mass: 16852.545 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, Calmodulin (CaM), CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII
Plasmid: pEGST / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-Rosetta / 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: 9131.688 Da / Num. of mol.: 2 / Fragment: preIQ/IQ domain (unp residues 1609-1685)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: CACH2, CACN2, CACNA1C, CACNL1A1, calcium channel CaV1.2, CCHL1A1
Plasmid: HMT-pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-Rosetta / 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


Mass: 18.015 Da / Num. of mol.: 97 / 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: 2.42 Å3/Da / Density % sol: 49.2 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: 0.2 M Li2SO4, 24.5% PEG3350, 0.1 M Bis-Tris pH5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 18, 2008
RadiationMonochromator: Double flat crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11587 Å / Relative weight: 1
ReflectionResolution: 2.55→30 Å / Num. all: 28142 / Num. obs: 27890 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 51.7 Å2 / Rsym value: 0.085 / Net I/σ(I): 16.2
Reflection shellResolution: 2.55→2.59 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 2.7 / Num. unique all: 1379 / Rsym value: 0.477 / % possible all: 97.3

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0109refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2BE6

2be6


Resolution: 2.55→30 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.911 / SU B: 24.109 / SU ML: 0.266 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.327 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.28815 1400 5 %RANDOM
Rwork0.24071 ---
obs0.24315 26433 98.66 %-
all-28238 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 61.488 Å2
Baniso -1Baniso -2Baniso -3
1--1.16 Å20 Å20 Å2
2--2.81 Å20 Å2
3----1.65 Å2
Refinement stepCycle: LAST / Resolution: 2.55→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4923 0 14 97 5034
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0224971
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.461.9556704
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.7035656
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.96125.776232
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.57615800
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.81524
X-RAY DIFFRACTIONr_chiral_restr0.1020.2779
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.023770
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.08933302
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it3.33145170
X-RAY DIFFRACTIONr_scbond_it2.47431669
X-RAY DIFFRACTIONr_scangle_it3.91841534
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A292TIGHT POSITIONAL0.040.05
1A258MEDIUM POSITIONAL0.050.5
1A292TIGHT THERMAL0.190.5
1A258MEDIUM THERMAL0.232
2A248TIGHT POSITIONAL0.030.05
2A220MEDIUM POSITIONAL0.050.5
2A248TIGHT THERMAL0.140.5
2A220MEDIUM THERMAL0.142
3B292TIGHT POSITIONAL0.030.05
3B247MEDIUM POSITIONAL0.10.5
3B292TIGHT THERMAL0.140.5
3B247MEDIUM THERMAL0.172
4E144TIGHT POSITIONAL0.040.05
4E128LOOSE POSITIONAL0.045
4E144TIGHT THERMAL0.170.5
4E128LOOSE THERMAL0.1310
5E80TIGHT POSITIONAL0.030.05
5E87MEDIUM POSITIONAL0.110.5
5E80TIGHT THERMAL0.220.5
5E87MEDIUM THERMAL0.422
LS refinement shellResolution: 2.547→2.613 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.355 102 -
Rwork0.308 1759 -
obs--91.23 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.3018-0.51260.68420.96320.13333.1553-0.01090.02040.1856-0.0053-0.01720.0131-0.1509-0.07420.02820.01280.00760.00340.02720.01920.031131.563-25.4426.124
25.97241.7497-0.54154.8817-0.84243.7437-0.03560.0570.3427-0.168-0.05960.21070.0532-0.11640.09530.0083-0.0039-0.01820.01930.02850.106415.392-8.6573.26
31.1205-0.1768-1.62632.71851.45453.2998-0.0278-0.1417-0.03340.0372-0.0069-0.03820.0185-0.01430.03470.0130.0235-0.00720.1258-0.00060.0079-20.548-36.282-52.594
41.30640.53981.2590.94190.34762.6592-0.0454-0.00450.08350.04650.0191-0.0398-0.06650.02940.02640.0269-0.01060.00110.0099-0.01190.0275-28.571-25.466-85.108
55.2986-0.57130.69285.17391.40642.9827-0.0372-0.07040.27250.218-0.0788-0.1327-0.02260.01120.11610.0122-0.0032-0.01270.0078-0.00950.0414-12.116-8.734-82.722
62.19580.9809-1.80073.4047-2.32814.1551-0.11430.05540.0451-0.0510.03850.0206-0.13040.00640.07580.0359-0.0246-0.01860.10530.01520.010123.171-36.311-26.654
79.18062.9726.73331.92712.60425.1826-0.3072-0.09330.2727-0.01180.09070.0532-0.24-0.06190.21660.08720.026-0.04450.1031-0.02740.0273-5.769-22.112-39.095
84.428-2.9296-2.0283.2336-0.83064.5988-0.0907-0.2911-0.00380.030.10110.04470.08740.3-0.01040.013-0.013-0.0210.07770.02780.162922.772-16.06310.167
99.4924-4.70665.32133.1675-3.43614.1650.04580.29790.0667-0.0977-0.00970.0835-0.01310.0384-0.03610.0438-0.0079-0.01950.05350.01790.02126.949-21.642-40.877
108.53351.4313-3.02510.4049-0.53431.0770.1058-0.01310.1460.0144-0.0627-0.0252-0.03730.0138-0.04310.0048-0.00070.00480.040.00130.0334-19.483-15.923-89.493
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A4 - 77
2X-RAY DIFFRACTION2A85 - 145
3X-RAY DIFFRACTION3B4 - 76
4X-RAY DIFFRACTION4C4 - 77
5X-RAY DIFFRACTION5C85 - 145
6X-RAY DIFFRACTION6D4 - 76
7X-RAY DIFFRACTION7E1560 - 1598
8X-RAY DIFFRACTION8E1614 - 1631
9X-RAY DIFFRACTION9F1560 - 1600
10X-RAY DIFFRACTION10F1614 - 1633

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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