[English] 日本語
Yorodumi
- PDB-1e7p: QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1e7p
TitleQUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Components(Fumarate reductase ...) x 3
KeywordsOXIDOREDUCTASE / SUCCINATE DEHYDROGENASE / RESPIRATORY CHAIN / CITRIC ACID CYCLE / FLAVOPROTEIN / IRON- SULPHUR PROTEIN IRON- SULPHUR PROTEIN / DIHAEM CYTOCHROME B
Function / homology
Function and homology information


succinate dehydrogenase (quinone) activity / succinate dehydrogenase / anaerobic respiration / 3 iron, 4 sulfur cluster binding / tricarboxylic acid cycle / respiratory electron transport chain / electron transport chain / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding ...succinate dehydrogenase (quinone) activity / succinate dehydrogenase / anaerobic respiration / 3 iron, 4 sulfur cluster binding / tricarboxylic acid cycle / respiratory electron transport chain / electron transport chain / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / metal ion binding / plasma membrane
Similarity search - Function
Ubiquitin-like (UB roll) - #820 / Fumarate reductase type B, transmembrane subunit / 4Fe-4S dicluster domain / Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit / Succinate dehydrogenase/Fumarate reductase transmembrane subunit / Fumarate reductase/succinate dehydrogenase, 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 ...Ubiquitin-like (UB roll) - #820 / Fumarate reductase type B, transmembrane subunit / 4Fe-4S dicluster domain / Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit / Succinate dehydrogenase/Fumarate reductase transmembrane subunit / Fumarate reductase/succinate dehydrogenase, 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 / 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 / Flavocytochrome C3; Chain A, domain 1 / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily / FAD-dependent oxidoreductase 2, FAD binding domain / FAD binding domain / Alpha-helical ferredoxin / 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 / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / Ubiquitin-like (UB roll) / Roll / Alpha-Beta Complex / Up-down Bundle / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
FE3-S4 CLUSTER / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / MALONIC ACID / IRON/SULFUR CLUSTER / Fumarate reductase flavoprotein subunit / Fumarate reductase cytochrome b subunit / Fumarate reductase iron-sulfur subunit
Similarity search - Component
Biological speciesWolinella succinogenes (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsLancaster, C.R.D. / Kroeger, A.
Citation
Journal: Eur.J.Biochem. / Year: 2001
Title: A Third Crystal Form of Wolinella Succinogenes Quinol:Fumarate Reductase Reveals Domain Closure at the Site of Fumarate Reduction
Authors: Lancaster, C.R.D. / Gross, R. / Simon, J.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2000
Title: Essential Role of Glu-C66 for Menaquinol Oxidation Indicates Transmembrane Electrochemical Potential Generation by Wolinella Succinogenes Fumarate Reductase
Authors: Lancaster, C.R.D. / Gross, R. / Haas, A. / Ritter, M. / Maentele, W. / Simon, J. / Kroeger, A.
#2: Journal: Nature / Year: 1999
Title: Structure of Fumarate Reductase from Wolinella Succinogenes at 2.2 Angstroms Resolution
Authors: Lancaster, C.R.D. / Kroeger, A. / Auer, M. / Michel, H.
History
DepositionSep 1, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 9, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 17, 2013Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Other / Refinement description / Structure summary / Version format compliance
Revision 1.2Apr 22, 2015Group: Non-polymer description
Revision 2.0Nov 21, 2018Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Source and taxonomy / Structure summary
Category: atom_site / entity ...atom_site / entity / entity_src_gen / entity_src_nat / pdbx_unobs_or_zero_occ_atoms / struct_ref
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity.pdbx_mutation / _entity.src_method / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code
Revision 2.1Dec 13, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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.conn_type_id / _struct_conn.id / _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 2.2Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Fumarate reductase flavoprotein subunit
B: Fumarate reductase iron-sulfur subunit
C: Fumarate reductase cytochrome b subunit
D: Fumarate reductase flavoprotein subunit
E: Fumarate reductase iron-sulfur subunit
F: Fumarate reductase cytochrome b subunit
G: Fumarate reductase flavoprotein subunit
H: Fumarate reductase iron-sulfur subunit
I: Fumarate reductase cytochrome b subunit
J: Fumarate reductase flavoprotein subunit
K: Fumarate reductase iron-sulfur subunit
L: Fumarate reductase cytochrome b subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)533,04048
Polymers519,12212
Non-polymers13,91836
Water00
1
A: Fumarate reductase flavoprotein subunit
B: Fumarate reductase iron-sulfur subunit
C: Fumarate reductase cytochrome b subunit
D: Fumarate reductase flavoprotein subunit
E: Fumarate reductase iron-sulfur subunit
F: Fumarate reductase cytochrome b subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)266,52024
Polymers259,5616
Non-polymers6,95918
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38830 Å2
ΔGint-362.5 kcal/mol
Surface area76100 Å2
MethodPISA
2
G: Fumarate reductase flavoprotein subunit
H: Fumarate reductase iron-sulfur subunit
I: Fumarate reductase cytochrome b subunit
J: Fumarate reductase flavoprotein subunit
K: Fumarate reductase iron-sulfur subunit
L: Fumarate reductase cytochrome b subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)266,52024
Polymers259,5616
Non-polymers6,95918
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38830 Å2
ΔGint-359.8 kcal/mol
Surface area76090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)81.074, 290.240, 153.614
Angle α, β, γ (deg.)90.00, 95.73, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.57768, -0.54733, -0.60557), (-0.5435, -0.2956, 0.78564), (-0.60901, 0.78297, -0.12672)-0.16689, -6.8204, 6.04004
2given(-0.42759, 0.00845, -0.90393), (-0.00563, -0.99996, -0.00669), (-0.90396, 0.00223, 0.42762)44.39704, 58.59339, 83.8085
3given(0.79356, -0.47221, 0.38377), (0.55227, 0.29417, -0.78004), (0.25545, 0.83095, 0.49423)39.00774, 65.35092, 86.57045

-
Components

-
Fumarate reductase ... , 3 types, 12 molecules ADGJBEHKCFIL

#1: Protein
Fumarate reductase flavoprotein subunit


Mass: 72825.055 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: 8-ALPHA-[-N-EPSILON-HISTIDYL] COVALENT BOND BETWEEN FLAVIN ADENINE DINUCLEOTIDE (FAD) AND HIS 43
Source: (gene. exp.) Wolinella succinogenes (bacteria) / Gene: frdA, WS0831 / Production host: Wolinella succinogenes (bacteria) / References: UniProt: P17412, fumarate reductase (quinol)
#2: Protein
Fumarate reductase iron-sulfur subunit


Mass: 27197.453 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Wolinella succinogenes (bacteria) / Gene: frdB, WS0830 / Production host: Wolinella succinogenes (bacteria) / References: UniProt: P17596, succinate dehydrogenase
#3: Protein
Fumarate reductase cytochrome b subunit


Mass: 29758.070 Da / Num. of mol.: 4 / Mutation: E66Q
Source method: isolated from a genetically manipulated source
Details: HAEM AXIAL LIGANDS - HIS 44, HIS 93, HIS 143 HIS 182
Source: (gene. exp.) Wolinella succinogenes (bacteria)
Strain: ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W
Gene: frdC, WS0832 / Variant: FRDC-E66Q / Production host: Wolinella succinogenes (bacteria) / References: UniProt: P17413

-
Sugars , 1 types, 4 molecules

#11: Sugar
ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM

-
Non-polymers , 7 types, 32 molecules

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


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#5: Chemical
ChemComp-MLA / MALONIC ACID / DICARBOXYLIC ACID C3 / PROPANEDIOLIC ACID / METHANEDICARBOXYLIC ACID


Mass: 104.061 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H4O4
#6: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#7: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe2S2
#8: Chemical
ChemComp-F3S / FE3-S4 CLUSTER


Mass: 295.795 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe3S4
#9: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe4S4
#10: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C34H32FeN4O4

-
Details

Compound detailsCHAINS: C, F, I, L CONTAIN ENGINEERED MUTATION E66Q
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.46 Å3/Da / Density % sol: 64 %
Crystal growpH: 6 / Details: pH 6.00
Crystal grow
*PLUS
pH: 6.4 / Method: vapor diffusion
Details: used microseeding, Lancaster, C.R.D., (1999) Nature, 402, 377.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formulaDetails
11 mM1dropK3Fe(CN)6
20.05 %dodecyl-beta-D-maltoside1drop
30.20 %decylmaltoside1drop
42.4 %benzamidine1drop
55 %PEG33501drop
675 mM1dropNaCl
75 %DME1drop
81 mMDMN1drop
91 mMmalonate1drop
1010 mMHEPES1drop
1110 mMcitrate1droppH6.4
129.5 mg/mlprotein1drop
13150 mM1reservoirNaCl
1410 %PEG33501reservoir
1520 mMcitrate1reservoirpH5.6

-
Data collection

DiffractionMean temperature: 275 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.958
DetectorType: MARRESEARCH / Detector: CCD / Date: Jul 9, 2000 / Details: MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.958 Å / Relative weight: 1
ReflectionResolution: 3.1→30 Å / Num. obs: 102882 / % possible obs: 80.8 % / Observed criterion σ(I): -1 / Redundancy: 2.7 % / Biso Wilson estimate: 65.4 Å2 / Rsym value: 0.06 / Net I/σ(I): 11.9
Reflection shellResolution: 3.1→3.29 Å / Redundancy: 1.97 % / Mean I/σ(I) obs: 2 / Rsym value: 0.26 / % possible all: 61.7

-
Processing

Software
NameVersionClassification
CNS1refinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1QLA

1qla
PDB Unreleased entry


Resolution: 3.1→30 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 10000000 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: N(OBS)/N(PAR) = 1.57
RfactorNum. reflection% reflectionSelection details
Rfree0.291 750 0.7 %750 THIN SHELLS
Rwork0.283 ---
obs0.283 102882 80.8 %-
Solvent computationBsol: 48.4 Å2 / ksol: 0.31 e/Å3
Displacement parametersBiso mean: 84.8 Å2
Refine analyzeLuzzati coordinate error obs: 0.66 Å
Refinement stepCycle: LAST / Resolution: 3.1→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms36276 0 804 0 37080
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.012
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.6
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d22.5
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d1.73
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it0.9981.5
X-RAY DIFFRACTIONc_mcangle_it1.1162
X-RAY DIFFRACTIONc_scbond_it1.7952
X-RAY DIFFRACTIONc_scangle_it1.8762.5
LS refinement shellResolution: 3.1→3.29 Å / Rfactor Rfree error: 0.049 / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.454 95 0.7 %
Rwork0.477 12962 -
obs--61.7 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION3ION.PARAMION.TOP
X-RAY DIFFRACTION4PARHEM.ROYTOPHEM.ROY
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg22.5
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.73
LS refinement shell
*PLUS
Rfactor obs: 0.477

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

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

Read more