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- PDB-9v7g: Phycobilisome Rx rod from Gloeobacter violaceus PCC 7421 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 9v7g
TitlePhycobilisome Rx rod from Gloeobacter violaceus PCC 7421
Components
  • Glr2806 protein
  • Phycocyanin alpha chain
  • Phycocyanin beta chain
KeywordsPHOTOSYNTHESIS / Phycobilisome
Function / homology
Function and homology information


phycobilisome / plasma membrane-derived thylakoid membrane / photosynthesis
Similarity search - Function
Phycobilisome linker domain / Phycobilisome linker domain superfamily / Phycobilisome Linker polypeptide / Phycobilisome (PBS) linker domain profile. / Phycobilisome, alpha/beta subunit / Phycobilisome, alpha/beta subunit superfamily / Phycobilisome protein / Globin-like superfamily
Similarity search - Domain/homology
PHYCOCYANOBILIN / Phycocyanin beta chain / Phycocyanin alpha chain / Glr2806 protein
Similarity search - Component
Biological speciesGloeobacter violaceus PCC 7421 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.72 Å
AuthorsBurtseva, A.D. / Baymukhametov, T.N. / Slonimskiy, Y.B. / Popov, V.O. / Sluchanko, N.N. / Boyko, K.M.
Funding support Russian Federation, 1items
OrganizationGrant numberCountry
Russian Science Foundation23-74-00062 Russian Federation
CitationJournal: To Be Published
Title: Structure and quenching of a bundle-shaped phycobilisome
Authors: Burtseva, A.D. / Slonimskiy, Y.B. / Baymukhametov, T.N. / Sinetova, M.A. / Maksimov, E.G. / Popov, V.O. / Boyko, K.M. / Sluchanko, N.N.
History
DepositionMay 28, 2025Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 24, 2025Provider: repository / Type: Initial release
Revision 1.0Sep 24, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Sep 24, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Sep 24, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Sep 24, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Sep 24, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
X: Glr2806 protein
A: Phycocyanin alpha chain
B: Phycocyanin beta chain
C: Phycocyanin alpha chain
D: Phycocyanin beta chain
E: Phycocyanin alpha chain
F: Phycocyanin beta chain
G: Phycocyanin alpha chain
H: Phycocyanin beta chain
I: Phycocyanin alpha chain
J: Phycocyanin beta chain
K: Phycocyanin alpha chain
L: Phycocyanin beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)309,09431
Polymers298,49713
Non-polymers10,59618
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11X
21X
32X
42X
53X
63X
74X
84X
95X
105X
116X
126X
137X
147X
158X
168X
179X
189X
1910X
2010X
2111X
2211X
2312X
2412X
2513X
2613X
2714X
2814X
2915X
3015X
3116X
3216X
3317X
3417X
3518X
3618X
3719X
3819X
3920X
4020X
4121X
4221X
4322X
4422X
4523X
4623X
4724X
4824X
4925X
5025X
5126X
5226X
5327X
5427X
5528X
5628X
5729X
5829X
5930X
6030X

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36
19Local NCS retraints between domains: 37 38
20Local NCS retraints between domains: 39 40
21Local NCS retraints between domains: 41 42
22Local NCS retraints between domains: 43 44
23Local NCS retraints between domains: 45 46
24Local NCS retraints between domains: 47 48
25Local NCS retraints between domains: 49 50
26Local NCS retraints between domains: 51 52
27Local NCS retraints between domains: 53 54
28Local NCS retraints between domains: 55 56
29Local NCS retraints between domains: 57 58
30Local NCS retraints between domains: 59 60

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Components

#1: Protein Glr2806 protein


Mass: 81544.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria) / References: UniProt: Q7NGT2
#2: Protein
Phycocyanin alpha chain


Mass: 17679.852 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria) / References: UniProt: Q7M7F7
#3: Protein
Phycocyanin beta chain


Mass: 18478.953 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Gloeobacter violaceus PCC 7421 (bacteria) / References: UniProt: Q7M7C7
#4: Chemical
ChemComp-CYC / PHYCOCYANOBILIN


Mass: 588.694 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: C33H40N4O6 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY
Has protein modificationY

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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: Bundle-shaped phycobilisome / Type: COMPLEX / Entity ID: #1-#3 / Source: NATURAL
Source (natural)Organism: Gloeobacter violaceus PCC 7421 (bacteria)
Buffer solutionpH: 7
Buffer componentConc.: 50 mM / Name: Tris(hydroxymethyl)aminomethane hydrochloride / Formula: Tris-HCl
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS / Details: Preliminary grid screening was performed manually.
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 85000 X / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm / Cs: 0.01 mm / C2 aperture diameter: 100 µm / Alignment procedure: ZEMLIN TABLEAU
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 3.9 sec. / Electron dose: 66 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)
EM imaging opticsEnergyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV
Spherical aberration corrector: Microscope was modified with a Cs corrector (CEOS GmbH, Germany).
Image scansWidth: 5760 / Height: 4092

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Processing

EM software
IDNameVersionCategory
2SerialEM4.04image acquisition
4Warp1.0.9CTF correction
11cryoSPARC4.7final Euler assignment
13cryoSPARC4.73D reconstruction
CTF correctionType: NONE
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.72 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 746972 / Symmetry type: POINT
RefinementResolution: 2.72→2.72 Å / Cor.coef. Fo:Fc: 0.931 / WRfactor Rwork: 0.302 / SU B: 14.328 / SU ML: 0.272 / Average fsc free: 0 / Average fsc overall: 0.8222 / Average fsc work: 0.8222 / ESU R: 0.408
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rwork0.3017 147013 -
all0.302 --
Rfree--0 %
obs--100 %
Solvent computationSolvent model: NONE
Displacement parametersBiso mean: 41.041 Å2
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0090.01217919
ELECTRON MICROSCOPYr_bond_other_d0.0010.01616992
ELECTRON MICROSCOPYr_angle_refined_deg1.5811.81424384
ELECTRON MICROSCOPYr_angle_other_deg0.6611.74938864
ELECTRON MICROSCOPYr_dihedral_angle_1_deg4.84452194
ELECTRON MICROSCOPYr_dihedral_angle_2_deg17.1398.568454
ELECTRON MICROSCOPYr_dihedral_angle_3_deg17.008102856
ELECTRON MICROSCOPYr_dihedral_angle_6_deg15.18810777
ELECTRON MICROSCOPYr_chiral_restr0.0970.22699
ELECTRON MICROSCOPYr_gen_planes_refined0.0080.0222219
ELECTRON MICROSCOPYr_gen_planes_other0.0040.024145
ELECTRON MICROSCOPYr_nbd_refined0.2190.24555
ELECTRON MICROSCOPYr_symmetry_nbd_other0.2110.215915
ELECTRON MICROSCOPYr_nbtor_refined0.1870.29267
ELECTRON MICROSCOPYr_symmetry_nbtor_other0.0770.210801
ELECTRON MICROSCOPYr_xyhbond_nbd_refined0.1670.2252
ELECTRON MICROSCOPYr_symmetry_xyhbond_nbd_other0.0610.21
ELECTRON MICROSCOPYr_mcbond_it2.1643.9448815
ELECTRON MICROSCOPYr_mcbond_other2.1643.9448815
ELECTRON MICROSCOPYr_mcangle_it3.3917.07810996
ELECTRON MICROSCOPYr_mcangle_other3.3917.07810997
ELECTRON MICROSCOPYr_scbond_it2.5024.2679104
ELECTRON MICROSCOPYr_scbond_other2.5024.2679103
ELECTRON MICROSCOPYr_scangle_it4.2837.67513388
ELECTRON MICROSCOPYr_scangle_other4.2837.67513389
ELECTRON MICROSCOPYr_lrange_it5.67136.2921006
ELECTRON MICROSCOPYr_lrange_other5.67136.28921007
ELECTRON MICROSCOPYr_ncsr_local_group_10.0840.055389
ELECTRON MICROSCOPYr_ncsr_local_group_20.0960.055387
ELECTRON MICROSCOPYr_ncsr_local_group_30.0870.055463
ELECTRON MICROSCOPYr_ncsr_local_group_40.0910.055420
ELECTRON MICROSCOPYr_ncsr_local_group_50.0810.055477
ELECTRON MICROSCOPYr_ncsr_local_group_60.0890.055706
ELECTRON MICROSCOPYr_ncsr_local_group_70.1110.055621
ELECTRON MICROSCOPYr_ncsr_local_group_80.1090.055711
ELECTRON MICROSCOPYr_ncsr_local_group_90.1010.055712
ELECTRON MICROSCOPYr_ncsr_local_group_100.10.055651
ELECTRON MICROSCOPYr_ncsr_local_group_110.0890.055386
ELECTRON MICROSCOPYr_ncsr_local_group_120.0790.055451
ELECTRON MICROSCOPYr_ncsr_local_group_130.0880.055424
ELECTRON MICROSCOPYr_ncsr_local_group_140.0840.055399
ELECTRON MICROSCOPYr_ncsr_local_group_150.1020.055629
ELECTRON MICROSCOPYr_ncsr_local_group_160.1020.055668
ELECTRON MICROSCOPYr_ncsr_local_group_170.0980.055654
ELECTRON MICROSCOPYr_ncsr_local_group_180.0960.055619
ELECTRON MICROSCOPYr_ncsr_local_group_190.0770.055442
ELECTRON MICROSCOPYr_ncsr_local_group_200.0830.055393
ELECTRON MICROSCOPYr_ncsr_local_group_210.0880.055417
ELECTRON MICROSCOPYr_ncsr_local_group_220.1120.055658
ELECTRON MICROSCOPYr_ncsr_local_group_230.1030.055662
ELECTRON MICROSCOPYr_ncsr_local_group_240.0990.055613
ELECTRON MICROSCOPYr_ncsr_local_group_250.0750.055461
ELECTRON MICROSCOPYr_ncsr_local_group_260.0820.055465
ELECTRON MICROSCOPYr_ncsr_local_group_270.1080.055710
ELECTRON MICROSCOPYr_ncsr_local_group_280.1020.055655
ELECTRON MICROSCOPYr_ncsr_local_group_290.0870.055436
ELECTRON MICROSCOPYr_ncsr_local_group_300.0880.055691
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11XELECTRON MICROSCOPYLocal ncs0.083980.05009
12XELECTRON MICROSCOPYLocal ncs0.083980.05009
23XELECTRON MICROSCOPYLocal ncs0.095880.05008
24XELECTRON MICROSCOPYLocal ncs0.095880.05008
35XELECTRON MICROSCOPYLocal ncs0.086990.05009
36XELECTRON MICROSCOPYLocal ncs0.086990.05009
47XELECTRON MICROSCOPYLocal ncs0.091410.05009
48XELECTRON MICROSCOPYLocal ncs0.091410.05009
59XELECTRON MICROSCOPYLocal ncs0.080740.05009
510XELECTRON MICROSCOPYLocal ncs0.080740.05009
611XELECTRON MICROSCOPYLocal ncs0.088930.05008
612XELECTRON MICROSCOPYLocal ncs0.088930.05008
713XELECTRON MICROSCOPYLocal ncs0.110980.05008
714XELECTRON MICROSCOPYLocal ncs0.110980.05008
815XELECTRON MICROSCOPYLocal ncs0.108540.05008
816XELECTRON MICROSCOPYLocal ncs0.108540.05008
917XELECTRON MICROSCOPYLocal ncs0.100780.05009
918XELECTRON MICROSCOPYLocal ncs0.100780.05009
1019XELECTRON MICROSCOPYLocal ncs0.100330.05008
1020XELECTRON MICROSCOPYLocal ncs0.100330.05008
1121XELECTRON MICROSCOPYLocal ncs0.08890.05008
1122XELECTRON MICROSCOPYLocal ncs0.08890.05008
1223XELECTRON MICROSCOPYLocal ncs0.079420.05009
1224XELECTRON MICROSCOPYLocal ncs0.079420.05009
1325XELECTRON MICROSCOPYLocal ncs0.087550.05009
1326XELECTRON MICROSCOPYLocal ncs0.087550.05009
1427XELECTRON MICROSCOPYLocal ncs0.084310.05009
1428XELECTRON MICROSCOPYLocal ncs0.084310.05009
1529XELECTRON MICROSCOPYLocal ncs0.102380.05008
1530XELECTRON MICROSCOPYLocal ncs0.102380.05008
1631XELECTRON MICROSCOPYLocal ncs0.101690.05008
1632XELECTRON MICROSCOPYLocal ncs0.101690.05008
1733XELECTRON MICROSCOPYLocal ncs0.097850.05008
1734XELECTRON MICROSCOPYLocal ncs0.097850.05008
1835XELECTRON MICROSCOPYLocal ncs0.095680.05008
1836XELECTRON MICROSCOPYLocal ncs0.095680.05008
1937XELECTRON MICROSCOPYLocal ncs0.077120.05009
1938XELECTRON MICROSCOPYLocal ncs0.077120.05009
2039XELECTRON MICROSCOPYLocal ncs0.083230.05008
2040XELECTRON MICROSCOPYLocal ncs0.083230.05008
2141XELECTRON MICROSCOPYLocal ncs0.087740.05009
2142XELECTRON MICROSCOPYLocal ncs0.087740.05009
2243XELECTRON MICROSCOPYLocal ncs0.11240.05008
2244XELECTRON MICROSCOPYLocal ncs0.11240.05008
2345XELECTRON MICROSCOPYLocal ncs0.102580.05008
2346XELECTRON MICROSCOPYLocal ncs0.102580.05008
2447XELECTRON MICROSCOPYLocal ncs0.099320.05008
2448XELECTRON MICROSCOPYLocal ncs0.099320.05008
2549XELECTRON MICROSCOPYLocal ncs0.075150.05009
2550XELECTRON MICROSCOPYLocal ncs0.075150.05009
2651XELECTRON MICROSCOPYLocal ncs0.08240.05009
2652XELECTRON MICROSCOPYLocal ncs0.08240.05009
2753XELECTRON MICROSCOPYLocal ncs0.108370.05008
2754XELECTRON MICROSCOPYLocal ncs0.108370.05008
2855XELECTRON MICROSCOPYLocal ncs0.101910.05008
2856XELECTRON MICROSCOPYLocal ncs0.101910.05008
2957XELECTRON MICROSCOPYLocal ncs0.086840.05009
2958XELECTRON MICROSCOPYLocal ncs0.086840.05009
3059XELECTRON MICROSCOPYLocal ncs0.087990.05009
3060XELECTRON MICROSCOPYLocal ncs0.087990.05009
LS refinement shell

Refine-ID: ELECTRON MICROSCOPY / Num. reflection Rfree: _ / Total num. of bins used: 20 / % reflection obs: 100 %

Resolution (Å)Rfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc workWRfactor Rwork
2.82-2.8930.748108560.748108560.5490.748
2.893-2.9730.455105730.455105730.6450.455
2.973-3.0590.42103850.42103850.6960.42
3.059-3.1530.379100110.379100110.7510.379
3.153-3.2560.35696130.35696130.7960.356
3.256-3.370.32293970.32293970.8390.322
3.37-3.4970.30591350.30591350.8640.305
3.497-3.640.29386930.29386930.8790.293
3.64-3.8020.27783070.27783070.90.277
3.802-3.9870.27580410.27580410.910.275
3.987-4.2030.26675430.26675430.9210.266
4.203-4.4570.26772530.26772530.9250.267
4.457-4.7650.2667200.2667200.9250.26
4.765-5.1460.25762390.25762390.9190.257
5.146-5.6360.2858220.2858220.8990.28
5.636-6.30.34152730.34152730.8770.341
6.3-7.2720.33245720.33245720.8710.332
7.272-8.90.26839220.26839220.9060.268
8.9-12.5580.21629930.21629930.9480.216
12.558-132.3490.28716630.28716630.9750.287

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