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- PDB-7o0w: Cryo-EM structure of the RC-dLH complex (model_1b) from Gemmatimo... -

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Basic information

Entry
Database: PDB / ID: 7o0w
TitleCryo-EM structure of the RC-dLH complex (model_1b) from Gemmatimonas phototrophica at 2.47 A
Components
  • (LHC domain-containing ...) x 2
  • LHh-alpha
  • Light-harvesting protein B:885 subunit beta
  • MULTIHEME_CYTC domain-containing protein
  • PRCH domain-containing protein
  • Photosynthetic reaction center L subunit
  • RC-Hc
  • RC-M
  • RC-S
  • RC-U
KeywordsMEMBRANE PROTEIN / Photosynthesis / reaction centre light harvesting complex / RC-dLH / RC-LH1 / carotenoid / quinone / bacteriochlorophyll a / Gemmatimonas phototrophica
Function / homology
Function and homology information


organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / chlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / electron transfer activity / iron ion binding / heme binding ...organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / chlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / electron transfer activity / iron ion binding / heme binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, beta domain superfamily / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain ...Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, beta domain superfamily / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta subunit / Photosynthetic reaction centre, H subunit, N-terminal / Photosynthetic reaction centre, H subunit, N-terminal domain superfamily / Photosynthetic reaction centre, H-chain N-terminal region / Photosynthetic reaction centre, L subunit / Multiheme cytochrome superfamily / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature.
Similarity search - Domain/homology
Chem-0V9 / BACTERIOCHLOROPHYLL A / BACTERIOPHEOPHYTIN A / Chem-CD4 / SPIRILLOXANTHIN / : / HEME C / MENAQUINONE 8 / 2-acetamido-2-deoxy-alpha-D-glucopyranose / Chem-PGW ...Chem-0V9 / BACTERIOCHLOROPHYLL A / BACTERIOPHEOPHYTIN A / Chem-CD4 / SPIRILLOXANTHIN / : / HEME C / MENAQUINONE 8 / 2-acetamido-2-deoxy-alpha-D-glucopyranose / Chem-PGW / Chem-UYH / Chem-V75 / Chem-V7B / Chem-V7N / Reaction center protein L chain / Uncharacterized protein / Antenna complex alpha/beta subunit domain-containing protein / Light-harvesting protein B:885 subunit beta / Photosynthetic reaction centre H subunit N-terminal domain-containing protein / DUF2742 domain-containing protein
Similarity search - Component
Biological speciesGemmatimonas phototrophica (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.47 Å
AuthorsQian, P. / Koblizek, M.
Funding support Czech Republic, United Kingdom, European Union, 7items
OrganizationGrant numberCountry
Czech Science Foundation19-28778X,19-28323X Czech Republic
Biotechnology and Biological Sciences Research Council (BBSRC)BB/M000265/1 United Kingdom
European Research Council (ERC)854126European Union
European Regional Development FundCZ.02.1.01/0.0/0.0/15_003/0000441 Czech Republic
Wellcome TrustWellcome Trust United Kingdom
Medical Research Council (MRC, United Kingdom)MC UP 120117 United Kingdom
Royal SocietyUF160039 United Kingdom
CitationJournal: Sci Adv / Year: 2022
Title: 2.4-Å structure of the double-ring photosystem.
Authors: Pu Qian / Alastair T Gardiner / Ivana Šímová / Katerina Naydenova / Tristan I Croll / Philip J Jackson / Nupur / Miroslav Kloz / Petra Čubáková / Marek Kuzma / Yonghui Zeng / Pablo ...Authors: Pu Qian / Alastair T Gardiner / Ivana Šímová / Katerina Naydenova / Tristan I Croll / Philip J Jackson / Nupur / Miroslav Kloz / Petra Čubáková / Marek Kuzma / Yonghui Zeng / Pablo Castro-Hartmann / Bart van Knippenberg / Kenneth N Goldie / David Kaftan / Pavel Hrouzek / Jan Hájek / Jon Agirre / C Alistair Siebert / David Bína / Kasim Sader / Henning Stahlberg / Roman Sobotka / Christopher J Russo / Tomáš Polívka / C Neil Hunter / Michal Koblížek /
Abstract: Phototrophic Gemmatimonadetes evolved the ability to use solar energy following horizontal transfer of photosynthesis-related genes from an ancient phototrophic proteobacterium. The electron cryo- ...Phototrophic Gemmatimonadetes evolved the ability to use solar energy following horizontal transfer of photosynthesis-related genes from an ancient phototrophic proteobacterium. The electron cryo-microscopy structure of the photosystem at 2.4 Å reveals a unique, double-ring complex. Two unique membrane-extrinsic polypeptides, RC-S and RC-U, hold the central type 2 reaction center (RC) within an inner 16-subunit light-harvesting 1 (LH1) ring, which is encircled by an outer 24-subunit antenna ring (LHh) that adds light-gathering capacity. Femtosecond kinetics reveal the flow of energy within the RC-dLH complex, from the outer LHh ring to LH1 and then to the RC. This structural and functional study shows that has independently evolved its own compact, robust, and highly effective architecture for harvesting and trapping solar energy.
History
DepositionMar 27, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 2, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 16, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

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  • Deposited structure unit
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Assembly

Deposited unit
AA: LHh-alpha
AB: LHh-alpha
AC: LHh-alpha
AD: LHh-alpha
AE: LHh-alpha
AF: LHh-alpha
AG: LHh-alpha
AH: LHh-alpha
AI: LHh-alpha
AJ: LHh-alpha
AK: LHh-alpha
AL: LHh-alpha
AM: LHh-alpha
AN: LHh-alpha
AO: LHh-alpha
AP: LHh-alpha
AQ: LHh-alpha
AR: LHh-alpha
AS: LHh-alpha
AT: LHh-alpha
AU: LHh-alpha
AV: LHh-alpha
AW: LHh-alpha
AX: LHh-alpha
BA: Light-harvesting protein B:885 subunit beta
BB: Light-harvesting protein B:885 subunit beta
BC: Light-harvesting protein B:885 subunit beta
BD: Light-harvesting protein B:885 subunit beta
BE: Light-harvesting protein B:885 subunit beta
BF: Light-harvesting protein B:885 subunit beta
BG: Light-harvesting protein B:885 subunit beta
BH: Light-harvesting protein B:885 subunit beta
BI: Light-harvesting protein B:885 subunit beta
BJ: Light-harvesting protein B:885 subunit beta
BK: Light-harvesting protein B:885 subunit beta
BL: Light-harvesting protein B:885 subunit beta
BM: Light-harvesting protein B:885 subunit beta
BN: Light-harvesting protein B:885 subunit beta
BO: Light-harvesting protein B:885 subunit beta
BP: Light-harvesting protein B:885 subunit beta
BQ: Light-harvesting protein B:885 subunit beta
BR: Light-harvesting protein B:885 subunit beta
BS: Light-harvesting protein B:885 subunit beta
BT: Light-harvesting protein B:885 subunit beta
BU: Light-harvesting protein B:885 subunit beta
BV: Light-harvesting protein B:885 subunit beta
BW: Light-harvesting protein B:885 subunit beta
BX: Light-harvesting protein B:885 subunit beta
C: MULTIHEME_CYTC domain-containing protein
C1: RC-S
C2: RC-U
H1: PRCH domain-containing protein
H2: RC-Hc
L: Photosynthetic reaction center L subunit
M: RC-M
aa: LHC domain-containing protein
ab: LHC domain-containing protein
ac: LHC domain-containing protein
ad: LHC domain-containing protein
ae: LHC domain-containing protein
af: LHC domain-containing protein
ag: LHC domain-containing protein
ah: LHC domain-containing protein
ai: LHC domain-containing protein
aj: LHC domain-containing protein
ak: LHC domain-containing protein
al: LHC domain-containing protein
am: LHC domain-containing protein
an: LHC domain-containing protein
ao: LHC domain-containing protein
ap: LHC domain-containing protein
ba: Light-harvesting protein B:885 subunit beta
bb: Light-harvesting protein B:885 subunit beta
bc: Light-harvesting protein B:885 subunit beta
bd: Light-harvesting protein B:885 subunit beta
be: Light-harvesting protein B:885 subunit beta
bf: Light-harvesting protein B:885 subunit beta
bg: Light-harvesting protein B:885 subunit beta
bh: Light-harvesting protein B:885 subunit beta
bi: Light-harvesting protein B:885 subunit beta
bj: Light-harvesting protein B:885 subunit beta
bk: Light-harvesting protein B:885 subunit beta
bl: Light-harvesting protein B:885 subunit beta
bm: Light-harvesting protein B:885 subunit beta
bn: Light-harvesting protein B:885 subunit beta
bo: Light-harvesting protein B:885 subunit beta
bp: Light-harvesting protein B:885 subunit beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)864,025405
Polymers645,20787
Non-polymers218,818318
Water7,314406
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: microscopy, gel filtration chromatography shows a single peak. Individual components of the complex were confirmed by Mass.
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 8 types, 31 molecules AAABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAVAWAXCC1C2H1H2LM

#1: Protein ...
LHh-alpha


Mass: 6061.153 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria)
#3: Protein MULTIHEME_CYTC domain-containing protein


Mass: 38457.609 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BHR6
#4: Protein RC-S


Mass: 21079.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria)
#5: Protein RC-U


Mass: 13656.403 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BK87
#6: Protein PRCH domain-containing protein


Mass: 7854.894 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BJ28
#7: Protein RC-Hc


Mass: 20022.566 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria)
#8: Protein Photosynthetic reaction center L subunit / Reaction center protein L chain


Mass: 30581.662 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BHR2
#9: Protein RC-M


Mass: 41154.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria)

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Protein/peptide , 1 types, 40 molecules BABBBCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBWBXbabbbcbdbebf...

#2: Protein/peptide ...
Light-harvesting protein B:885 subunit beta


Mass: 5084.809 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BHS8

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LHC domain-containing ... , 2 types, 16 molecules aaabacadaeafagahaiajakalamanaoap

#10: Protein LHC domain-containing protein


Mass: 7695.042 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BHS7
#11: Protein
LHC domain-containing protein


Mass: 7723.052 Da / Num. of mol.: 15 / Source method: isolated from a natural source / Source: (natural) Gemmatimonas phototrophica (bacteria) / References: UniProt: A0A143BHS7

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Sugars , 3 types, 127 molecules

#12: Polysaccharide alpha-L-rhamnopyranose-(1-4)-alpha-D-mannopyranose


Type: oligosaccharide / Mass: 326.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LRhapa1-4DManpa1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a1122h-1a_1-5][a2211m-1a_1-5]/1-2/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(3+1)][a-D-Manp]{[(4+1)][a-L-Rhap]{}}}LINUCSPDB-CARE
#14: Sugar...
ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 123 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM
#19: Sugar ChemComp-NDG / 2-acetamido-2-deoxy-alpha-D-glucopyranose / N-acetyl-alpha-D-glucosamine / 2-acetamido-2-deoxy-alpha-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE / N-Acetylglucosamine


Type: D-saccharide, alpha linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-glucopyranosamineCOMMON NAMEGMML 1.0
a-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 14 types, 597 molecules

#13: Chemical...
ChemComp-BCL / BACTERIOCHLOROPHYLL A / Bacteriochlorophyll


Mass: 911.504 Da / Num. of mol.: 108 / Source method: obtained synthetically / Formula: C55H74MgN4O6 / Feature type: SUBJECT OF INVESTIGATION
#15: Chemical...
ChemComp-V7N / (2~{E},4~{E},6~{E},10~{E},12~{E},14~{E},16~{E},18~{E},20~{E},22~{Z},24~{E},26~{E},28~{E})-23-methanoyl-31-methoxy-2,6,10,14,19,27,31-heptamethyl-dotriaconta-2,4,6,10,12,14,16,18,20,22,24,26,28-tridecaenoic acid


Mass: 610.865 Da / Num. of mol.: 40 / Source method: obtained synthetically / Formula: C41H54O4 / Feature type: SUBJECT OF INVESTIGATION
#16: Chemical
ChemComp-0V9 / (19R,22S)-25-amino-22-hydroxy-22-oxido-16-oxo-17,21,23-trioxa-22lambda~5~-phosphapentacosan-19-yl (9Z)-hexadec-9-enoate


Mass: 689.943 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: C37H72NO8P / Feature type: SUBJECT OF INVESTIGATION
#17: Chemical
ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#18: Chemical ChemComp-V75 / (2~{S},3~{S},4~{S},5~{S})-4,5-diacetyloxy-3-oxidanyl-oxane-2-carboxylic acid


Mass: 262.213 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H14O8 / Feature type: SUBJECT OF INVESTIGATION
#20: Chemical ChemComp-PGW / (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate / 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-(1-glycerol)] / PHOSPHATIDYLGLYCEROL / Phosphatidylglycerol


Mass: 749.007 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C40H77O10P / Comment: phospholipid*YM
#21: Chemical
ChemComp-CD4 / (2R,5R,11R,14R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-2,14-bis(tetradecanoyloxy)-4,6,10,12,16-pentaoxa-5,11-diphosphatriacont-1-yl tetradecanoate / tetramyristoyl-cardiolipin


Mass: 1241.633 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C65H126O17P2
#22: Chemical ChemComp-BPH / BACTERIOPHEOPHYTIN A / Pheophytin


Mass: 889.215 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C55H76N4O6 / Feature type: SUBJECT OF INVESTIGATION
#23: Chemical ChemComp-MQ8 / MENAQUINONE 8 / 2-METHYL-3-(3,7,11,15,19,23,27,31-OCTAMETHYL-DOTRIACONTA-2,6,10,14,18,22,26,30-OCTAENYL)-[1,4]NAPTHOQUINONE / Vitamin K2


Mass: 717.116 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C51H72O2
#24: Chemical ChemComp-FE / FE (III) ION / Iron


Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe
#25: Chemical ChemComp-CRT / SPIRILLOXANTHIN / RHODOVIOLASCIN


Mass: 596.925 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C42H60O2
#26: Chemical ChemComp-V7B / [(2~{S})-3-[(2~{R},3~{R},4~{R},5~{S},6~{R})-6-(hydroxymethyl)-5-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,4-bis(oxidanyl)oxan-2-yl]oxy-2-(12-methyltridecanoyloxy)propyl] 12-methyltridecanoate


Mass: 837.086 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C43H80O15 / Feature type: SUBJECT OF INVESTIGATION
#27: Chemical ChemComp-UYH / [(2~{S})-3-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-2-octadecanoyloxy-propyl] octadecanoate


Mass: 787.158 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C45H86O10 / Feature type: SUBJECT OF INVESTIGATION
#28: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 406 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: RC-dLH model_1b / Type: COMPLEX
Details: Reaction centre light harvesting complex (model_1b) from Gemmatimonas phototrophic AP64
Entity ID: #1-#11 / Source: NATURAL
Molecular weightValue: 0.800 MDa / Experimental value: NO
Source (natural)Organism: Gemmatimonas phototrophica (bacteria) / Strain: AP64
Buffer solutionpH: 8
Details: The final purified complex is in 20mM Tris.Cl, 0.025 DDM, PH 8.0 buffer.
Buffer component
IDConc.NameBuffer-ID
120 mMTris.Cl1
20.02 %DDM1
SpecimenConc.: 6.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: The protein complex was isolated from photosynthetic membrane using detergent beta-DDM. After purification, concentrated protein sample solution was stored in LN before using.
Specimen supportGrid material: GOLD / Grid type: Homemade
VitrificationInstrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K / Details: Talmon type

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 120000 X / Nominal defocus max: -2400 nm / Nominal defocus min: -800 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 1.2 sec. / Electron dose: 24.8 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 19865
Details: All movies were recorded from a HexAuFoil grid with a special EPU version, which can recognise 300 nm holes on the grid.

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Processing

Software
NameVersionClassification
phenix.real_space_refinedev_4014refinement
PHENIXdev_4014refinement
EM software
IDNameVersionCategory
5Cootmodel fitting
6UCSF Chimeramodel fitting
14RELION3.1classification
15RELION3.13D reconstruction
9CTFFIND4CTF correction
12EMAN2initial Euler assignment
13EMAN2final Euler assignment
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1517482
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.47 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 100616 / Algorithm: BACK PROJECTION / Symmetry type: POINT
Atomic model buildingB value: 30 / Protocol: FLEXIBLE FIT / Space: REAL / Details: ISOLDE incorporated in ChimeraX was used.
Atomic model building
IDPDB-ID 3D fitting-ID
11LGH

1lgh

1
25Y5S

5y5s

1
36ET5

6et5

1
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 52.41 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00558460
ELECTRON MICROSCOPYf_angle_d1.09880415
ELECTRON MICROSCOPYf_chiral_restr0.05018226
ELECTRON MICROSCOPYf_plane_restr0.01199068
ELECTRON MICROSCOPYf_dihedral_angle_d16.695719941

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