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- PDB-3ae7: Crystal structure of porcine heart mitochondrial complex II bound... -

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Basic information

Entry
Database: PDB / ID: 3ae7
TitleCrystal structure of porcine heart mitochondrial complex II bound with 2-Iodo-N-(3-isopropoxy-phenyl)-benzamide
Components
  • (Succinate dehydrogenase [ubiquinone] ...) x 3
  • Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / respiratory complex II / inhibitors / Electron transport / Iron / Iron-sulfur / Metal-binding / Mitochondrion / Mitochondrion inner membrane / Oxidoreductase / Transit peptide / Transport / Tricarboxylic acid cycle / Heme / Transmembrane / FAD-binding protein / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
Function / homology
Function and homology information


Maturation of TCA enzymes and regulation of TCA cycle / Citric acid cycle (TCA cycle) / Oxidoreductases; Acting on the CH-OH group of donors; With a quinone or similar compound as acceptor / respiratory chain complex II (succinate dehydrogenase) / : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase (quinone) activity / succinate dehydrogenase / 3 iron, 4 sulfur cluster binding / ubiquinone binding ...Maturation of TCA enzymes and regulation of TCA cycle / Citric acid cycle (TCA cycle) / Oxidoreductases; Acting on the CH-OH group of donors; With a quinone or similar compound as acceptor / respiratory chain complex II (succinate dehydrogenase) / : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase (quinone) activity / succinate dehydrogenase / 3 iron, 4 sulfur cluster binding / ubiquinone binding / tricarboxylic acid cycle / aerobic respiration / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / electron transfer activity / heme binding / metal ion binding
Similarity search - Function
Single helix bin / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, CybS / CybS, succinate dehydrogenase cytochrome B small subunit / succinate dehydrogenase protein domain / Succinate dehydrogenase, cytochrome b subunit, conserved site / Succinate dehydrogenase cytochrome b subunit signature 1. / Succinate dehydrogenase cytochrome b subunit signature 2. / Succinate dehydrogenase, cytochrome b556 subunit / Succinate dehydrogenase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, transmembrane subunit ...Single helix bin / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, CybS / CybS, succinate dehydrogenase cytochrome B small subunit / succinate dehydrogenase protein domain / Succinate dehydrogenase, cytochrome b subunit, conserved site / Succinate dehydrogenase cytochrome b subunit signature 1. / Succinate dehydrogenase cytochrome b subunit signature 2. / Succinate dehydrogenase, cytochrome b556 subunit / Succinate dehydrogenase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, transmembrane subunit / Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit / Succinate dehydrogenase/Fumarate reductase transmembrane subunit / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain / Alpha-helical ferredoxin / Fumarate Reductase Iron-sulfur Protein; Chain B, domain 2 / Fumarate reductase/succinate dehydrogenase, transmembrane subunit / : / Succinate dehydrogenase/fumarate reductase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, FAD-binding site / Fumarate reductase / succinate dehydrogenase FAD-binding site. / FAD-dependent oxidoreductase SdhA/FrdA/AprA / 3 helical TM bundles of succinate and fumarate reductases / 4Fe-4S dicluster domain / Flavocytochrome C3; Chain A, domain 1 / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain / Succinate dehydrogenase/fumarate reductase iron-sulphur protein / Succinate dehydogenase/fumarate reductase N-terminal / 2Fe-2S iron-sulfur cluster binding domain / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal / Fumarate reductase flavoprotein C-term / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily / FAD-dependent oxidoreductase 2, FAD binding domain / Alpha-helical ferredoxin / FAD binding domain / Rhinovirus 14, subunit 4 / 2Fe-2S ferredoxin, iron-sulphur binding site / 2Fe-2S ferredoxin-type iron-sulfur binding region signature. / Beta-grasp domain / Beta-grasp domain superfamily / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / 3-Layer(bba) Sandwich / Ubiquitin-like (UB roll) / FAD/NAD(P)-binding domain superfamily / Few Secondary Structures / Irregular / Roll / Alpha-Beta Complex / Up-down Bundle / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
2-iodo-N-[3-(1-methylethoxy)phenyl]benzamide / FE3-S4 CLUSTER / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / IRON/SULFUR CLUSTER / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial / Succinate dehydrogenase cytochrome b560 subunit, mitochondrial / Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial / Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.62 Å
AuthorsHarada, S. / Sasaki, T. / Shindo, M. / Kido, Y. / Inaoka, D.K. / Omori, J. / Osanai, A. / Sakamoto, K. / Mao, J. / Matsuoka, S. ...Harada, S. / Sasaki, T. / Shindo, M. / Kido, Y. / Inaoka, D.K. / Omori, J. / Osanai, A. / Sakamoto, K. / Mao, J. / Matsuoka, S. / Inoue, M. / Honma, T. / Tanaka, A. / Kita, K.
CitationJournal: Int J Mol Sci / Year: 2015
Title: Structural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria
Authors: Inaoka, D.K. / Shiba, T. / Sato, D. / Balogun, E.O. / Sasaki, T. / Nagahama, M. / Oda, M. / Matsuoka, S. / Ohmori, J. / Honma, T. / Inoue, M. / Kita, K. / Harada, S.
History
DepositionFeb 4, 2010Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 9, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 5, 2015Group: Database references
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software
Revision 1.4Nov 1, 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_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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.pdbx_leaving_atom_flag / _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_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
B: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
C: Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
D: Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)125,92510
Polymers123,3184
Non-polymers2,6076
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13010 Å2
ΔGint-55 kcal/mol
Surface area42540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.175, 83.988, 293.691
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Succinate dehydrogenase [ubiquinone] ... , 3 types, 3 molecules ABD

#1: Protein Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial / Flavoprotein subunit of complex II / Fp


Mass: 68313.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: Q0QF01, succinate dehydrogenase
#2: Protein Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial / Iron-sulfur subunit of complex II / Ip


Mass: 28764.217 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: Q007T0, succinate dehydrogenase
#4: Protein Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial / Succinate-ubiquinone oxidoreductase cytochrome b small subunit / CybS / Succinate-ubiquinone ...Succinate-ubiquinone oxidoreductase cytochrome b small subunit / CybS / Succinate-ubiquinone reductase membrane anchor subunit / QPs3 / CII-4 / Succinate dehydrogenase complex subunit D


Mass: 10936.758 Da / Num. of mol.: 1 / Fragment: residues 57-159 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: A5GZW8

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Protein , 1 types, 1 molecules C

#3: Protein Succinate dehydrogenase cytochrome b560 subunit, mitochondrial / Succinate-ubiquinone oxidoreductase cytochrome B large subunit / CYBL


Mass: 15304.081 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: D0VWV4

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Non-polymers , 6 types, 6 molecules

#5: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#6: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2
#7: Chemical ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe4S4
#8: Chemical ChemComp-F3S / FE3-S4 CLUSTER


Mass: 295.795 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe3S4
#9: Chemical ChemComp-12J / 2-iodo-N-[3-(1-methylethoxy)phenyl]benzamide / 2-Iodo-N-(3-isopropoxyphenyl)benzamide


Mass: 381.208 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H16INO2
#10: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4

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Details

Compound detailsTHESE COMPLEX FORMS MITOCHONDRIAL RESPIRATORY COMPLEX II.
Has protein modificationY
Sequence detailsTHE SEQUENCE OF CHAIN D IS REFERRED IN REF 2 IN A5GZW8, UNIPROT.

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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: 3.56 Å3/Da / Density % sol: 65.44 % / Mosaicity: 0.76 °
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 25mM HEPES-NAOH, 6% PEG 4000, 200mM Sucrose, 100mM NaCl, 10mM CaCl2, 0.5mM EDTA, 3% 1,6-haxanediol, 0.5% n-decyl-beta-D-maltoside, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 0.98 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Nov 7, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 3.6→50 Å / Num. obs: 20323 / % possible obs: 97 % / Redundancy: 6.1 % / Rmerge(I) obs: 0.149 / Χ2: 1.64 / Net I/σ(I): 16.143
Reflection shellResolution: 3.6→3.66 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.553 / Mean I/σ(I) obs: 2.22 / Num. unique all: 809 / Χ2: 1.262 / % possible all: 77.8

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation4 Å48.13 Å
Translation4 Å48.13 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1ZOY

1zoy


Resolution: 3.62→48.13 Å / Cor.coef. Fo:Fc: 0.906 / Cor.coef. Fo:Fc free: 0.86 / WRfactor Rfree: 0.272 / WRfactor Rwork: 0.226 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.786 / SU B: 81.032 / SU ML: 0.587 / SU R Cruickshank DPI: 0.637 / SU Rfree: 0.765 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.765 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.305 1046 5.2 %RANDOM
Rwork0.256 ---
obs0.259 20118 96.02 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 142.68 Å2 / Biso mean: 145.11 Å2 / Biso min: 20 Å2
Baniso -1Baniso -2Baniso -3
1-0.42 Å20 Å20 Å2
2--0.62 Å20 Å2
3----1.04 Å2
Refinement stepCycle: LAST / Resolution: 3.62→48.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8480 0 135 0 8615
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.0228821
X-RAY DIFFRACTIONr_angle_refined_deg0.8441.98811970
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.87251088
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.18923.413375
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.857151469
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.0431559
X-RAY DIFFRACTIONr_chiral_restr0.0520.21304
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0216644
X-RAY DIFFRACTIONr_mcbond_it0.0871.55410
X-RAY DIFFRACTIONr_mcangle_it0.15628675
X-RAY DIFFRACTIONr_scbond_it0.06933411
X-RAY DIFFRACTIONr_scangle_it0.124.53278
LS refinement shellResolution: 3.616→3.71 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.361 68 -
Rwork0.38 1077 -
all-1145 -
obs-1145 75.98 %
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)
12.5878-0.3418-0.07841.29360.73053.9478-0.04760.2716-0.04280.04490.0739-0.053-0.23720.1387-0.02630.55360.06860.02940.5629-0.00390.882619.852-17.893-17.41
21.83952.06740.41714.40011.06414.2835-0.11820.22050.11-0.7414-0.01240.2082-0.649-0.58110.13060.41530.1360.02340.6593-0.02510.89813.541-16.139-20.167
31.9738-0.86790.9552.06430.2038-1.3816-0.12620.23490.571-0.62270.0372-0.1259-0.672-0.18590.0891.52980.12490.09680.44330.14951.123818.4768.762-24.995
40.43960.34340.34143.952.05260.52030.0868-0.04380.2152-0.0788-0.01670.069-0.2231-0.0421-0.07010.62490.11740.07830.6276-0.03770.954812.314-13.951-11.352
52.7096-0.2472-0.18894.3838-0.18752.1424-0.17050.3868-0.02340.24610.14840.6902-0.1944-0.96960.02210.36550.19640.08241.0153-0.06490.7026-7.177-15.311-20.629
61.57790.5307-0.43750.98660.03053.83720.1232-0.29230.44660.2976-0.22350.2948-0.8342-0.69320.10030.6680.23520.06880.5442-0.07050.9253.649-6.354-5.015
71.4018-0.43630.33362.7166-1.20145.0539-0.04760.85340.4551-0.1777-0.01950.0538-0.3757-0.94940.06710.54760.1847-0.02021.04730.07150.80522.013-11.898-46.191
82.77630.5262-2.3423-0.21020.83524.5813-0.04670.13290.03670.06850.0397-0.22110.27410.34950.0070.74690.0034-0.00380.47440.05850.986628.773-24.098-39.96
94.3714-3.37052.345613.5938-1.07064.81470.14280.1136-0.2584-0.712-0.49240.00040.366-0.37520.34970.6141-0.04220.15820.7872-0.15570.797811.139-30.991-47.277
105.11981.36694.233-4.88-5.21463.6552-0.8696-0.5933-0.3434-1.2228-0.05021.3902-0.85370.28850.91982.05020.03070.01710.12940.11021.065228.935-26.886-71.41
110.17432.3772-2.803-3.4725-0.46836.7318-0.28270.49910.0395-0.15570.08010.3104-0.42-0.25640.20261.5560.07370.01151.0771-0.17150.962134.024-29.357-93.475
121.8447-1.9245-6.67345.24793.188410.67850.1123-0.04950.1961-0.5745-0.1417-0.5142-0.6253-0.47050.02940.8575-0.03170.15120.42690.00750.896734.462-17.429-66.609
1310.56243.9017-15.0953.69793.371630.8921-0.5181-0.2884-0.7357-0.1893-0.3277-0.55591.79-0.33860.84581.61250.19490.33390.13320.13751.092534.026-10.875-71.775
145.4905-0.6657-1.27043.66190.2924.41070.0339-0.4669-0.4653-0.5571-0.1697-0.22850.0020.45460.13580.80860.01130.18250.3792-0.03880.904539.542-31.912-65.459
154.34580.07312.19321.611-2.57061.77550.63880.28650.09520.1437-0.7737-0.065-0.72910.3810.13491.815-0.02180.46840.5588-0.19890.997638.771-37.102-78.572
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 191
2X-RAY DIFFRACTION2A192 - 261
3X-RAY DIFFRACTION3A262 - 354
4X-RAY DIFFRACTION4A355 - 429
5X-RAY DIFFRACTION5A430 - 511
6X-RAY DIFFRACTION6A512 - 622
7X-RAY DIFFRACTION7B9 - 106
8X-RAY DIFFRACTION8B107 - 247
9X-RAY DIFFRACTION9C6 - 35
10X-RAY DIFFRACTION10C36 - 63
11X-RAY DIFFRACTION11C64 - 89
12X-RAY DIFFRACTION12C90 - 120
13X-RAY DIFFRACTION13C121 - 143
14X-RAY DIFFRACTION14D35 - 96
15X-RAY DIFFRACTION15D97 - 136

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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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