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- PDB-9dhk: RMI1-RMI2 bound to cyclic peptide L3 -

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Basic information

Entry
Database: PDB / ID: 9dhk
TitleRMI1-RMI2 bound to cyclic peptide L3
Components
  • (RecQ-mediated genome instability protein ...) x 5
  • L3 peptide
KeywordsNUCLEAR PROTEIN / DNA damage repair / complex / cyclic peptide / competitive inhibitor
Function / homology
Function and homology information


regulation of sister chromatid segregation / RecQ family helicase-topoisomerase III complex / reduction of food intake in response to dietary excess / resolution of DNA recombination intermediates / maintenance of rDNA / resolution of meiotic recombination intermediates / Impaired BRCA2 binding to PALB2 / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function ...regulation of sister chromatid segregation / RecQ family helicase-topoisomerase III complex / reduction of food intake in response to dietary excess / resolution of DNA recombination intermediates / maintenance of rDNA / resolution of meiotic recombination intermediates / Impaired BRCA2 binding to PALB2 / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / Presynaptic phase of homologous DNA pairing and strand exchange / negative regulation of double-strand break repair via homologous recombination / response to glucose / double-strand break repair via homologous recombination / G2/M DNA damage checkpoint / multicellular organism growth / HDR through Homologous Recombination (HRR) / glucose homeostasis / Processing of DNA double-strand break ends / Regulation of TP53 Activity through Phosphorylation / DNA replication / nuclear speck / nuclear body / DNA repair / nucleotide binding / DNA binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
RecQ-mediated genome instability protein 2 / RecQ-mediated genome instability protein 2 / RecQ-mediated genome instability protein 1, C-terminal OB-fold domain / RecQ-mediated genome instability protein 1, N-terminal helical domain superfamily / : / Recq-mediated genome instability protein 1, C-terminal OB-fold / RMI1, N-terminal helical domain / DUF1767 / RecQ mediated genome instability protein 1, N-terminal / RecQ mediated genome instability protein, N-terminal OB-fold superfamily ...RecQ-mediated genome instability protein 2 / RecQ-mediated genome instability protein 2 / RecQ-mediated genome instability protein 1, C-terminal OB-fold domain / RecQ-mediated genome instability protein 1, N-terminal helical domain superfamily / : / Recq-mediated genome instability protein 1, C-terminal OB-fold / RMI1, N-terminal helical domain / DUF1767 / RecQ mediated genome instability protein 1, N-terminal / RecQ mediated genome instability protein, N-terminal OB-fold superfamily / RMI1, N-terminal OB-fold domain / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
RecQ-mediated genome instability protein 2 / RecQ-mediated genome instability protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsBythell-Douglas, R. / Lau, Y. / Alcock, L.J. / Patel, K. / Gao, T. / Deshpande, C.
Funding support Australia, 2items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP2003250 Australia
National Health and Medical Research Council (NHMRC, Australia)MRF2007488 Australia
CitationJournal: J.Med.Chem. / Year: 2025
Title: Potent Cyclic Peptide Inhibitors Disrupt the FANCM-RMI Interaction.
Authors: Alcock, L.J. / Gao, T. / Bythell-Douglas, R. / Gao, J. / Krishna Sudhakar, H. / Huang, T. / Young, R. / Vu, Q.N. / Deshpande, C. / Wilkinson-White, L.E. / Passioura, T. / Pickett, H.A. / Deans, A.J. / Lau, Y.H.
History
DepositionSep 3, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 2, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RecQ-mediated genome instability protein 1
B: RecQ-mediated genome instability protein 2
D: RecQ-mediated genome instability protein 1
E: RecQ-mediated genome instability protein 2
G: RecQ-mediated genome instability protein 1
H: RecQ-mediated genome instability protein 2
J: RecQ-mediated genome instability protein 1
K: RecQ-mediated genome instability protein 2
C: L3 peptide
F: L3 peptide
I: L3 peptide
L: L3 peptide


Theoretical massNumber of molelcules
Total (without water)135,95512
Polymers135,95512
Non-polymers00
Water5,206289
1
A: RecQ-mediated genome instability protein 1
B: RecQ-mediated genome instability protein 2
C: L3 peptide


Theoretical massNumber of molelcules
Total (without water)34,6223
Polymers34,6223
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5230 Å2
ΔGint-34 kcal/mol
Surface area13500 Å2
MethodPISA
2
D: RecQ-mediated genome instability protein 1
E: RecQ-mediated genome instability protein 2
F: L3 peptide


Theoretical massNumber of molelcules
Total (without water)33,5733
Polymers33,5733
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5010 Å2
ΔGint-36 kcal/mol
Surface area13670 Å2
MethodPISA
3
G: RecQ-mediated genome instability protein 1
H: RecQ-mediated genome instability protein 2
I: L3 peptide


Theoretical massNumber of molelcules
Total (without water)33,1383
Polymers33,1383
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5030 Å2
ΔGint-38 kcal/mol
Surface area14000 Å2
MethodPISA
4
J: RecQ-mediated genome instability protein 1
K: RecQ-mediated genome instability protein 2
L: L3 peptide


Theoretical massNumber of molelcules
Total (without water)34,6223
Polymers34,6223
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5360 Å2
ΔGint-38 kcal/mol
Surface area13510 Å2
MethodPISA
Unit cell
Length a, b, c (Å)189.150, 50.622, 181.221
Angle α, β, γ (deg.)90.000, 118.047, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
32A
42A
53A
63A
74A
84A
95A
105A
116A
126A
137A
147A
158A
168A
179A
189A
1910A
2010A
2111A
2211A
2312A
2412A
2513A
2613A
2714A
2814A
2915A
3015A
3116A
3216A
3317A
3417A
3518A
3618A

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

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Components

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RecQ-mediated genome instability protein ... , 5 types, 8 molecules ADJBKEGH

#1: Protein RecQ-mediated genome instability protein 1 / BLM-associated protein of 75 kDa / BLAP75 / FAAP75


Mass: 16944.818 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RMI1, C9orf76 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H9A7
#2: Protein RecQ-mediated genome instability protein 2 / hRMI2 / BLM-associated protein of 18 kDa / BLAP18


Mass: 15886.305 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RMI2, C16orf75 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96E14
#3: Protein RecQ-mediated genome instability protein 2 / hRMI2 / BLM-associated protein of 18 kDa / BLAP18


Mass: 14837.186 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RMI2, C16orf75 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96E14
#4: Protein RecQ-mediated genome instability protein 1 / BLM-associated protein of 75 kDa / BLAP75 / FAAP75


Mass: 16140.933 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RMI1, C9orf76 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H9A7
#5: Protein RecQ-mediated genome instability protein 2 / hRMI2 / BLM-associated protein of 18 kDa / BLAP18


Mass: 15205.658 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RMI2, C16orf75 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96E14

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Protein/peptide / Non-polymers , 2 types, 293 molecules CFIL

#6: Protein/peptide
L3 peptide


Mass: 1791.145 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 289 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 2.77 Å3/Da / Density % sol: 55.54 %
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: 1.8 M sodium phosphate monobasic monohydrate / potassium phosphate dibasic pH 5.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 2, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.35→48.272 Å / Num. obs: 63378 / % possible obs: 99.2 % / Redundancy: 3.5 % / CC1/2: 0.983 / Net I/σ(I): 5.6
Reflection shellResolution: 2.35→2.41 Å / Mean I/σ(I) obs: 1.1 / Num. unique obs: 4427 / CC1/2: 0.406

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Processing

Software
NameVersionClassification
REFMAC5.8.0403refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.35→48.272 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.912 / SU B: 21.714 / SU ML: 0.231 / Cross valid method: FREE R-VALUE / ESU R: 0.318 / ESU R Free: 0.235
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2467 3158 4.983 %
Rwork0.2035 60219 -
all0.206 --
obs-63377 99.047 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 40.057 Å2
Baniso -1Baniso -2Baniso -3
1--0.362 Å20 Å20.33 Å2
2---1.142 Å2-0 Å2
3---0.735 Å2
Refinement stepCycle: LAST / Resolution: 2.35→48.272 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9139 0 16 289 9444
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0129378
X-RAY DIFFRACTIONr_bond_other_d0.0010.0169217
X-RAY DIFFRACTIONr_angle_refined_deg1.9411.64412696
X-RAY DIFFRACTIONr_angle_other_deg0.6161.56921266
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4151167
X-RAY DIFFRACTIONr_dihedral_angle_2_deg15.841580
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.941101688
X-RAY DIFFRACTIONr_dihedral_angle_6_deg15.87510376
X-RAY DIFFRACTIONr_chiral_restr0.0790.21422
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0210859
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022057
X-RAY DIFFRACTIONr_nbd_refined0.2230.21635
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1960.28228
X-RAY DIFFRACTIONr_nbtor_refined0.1850.24475
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0880.25471
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1420.2265
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0060.21
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1570.224
X-RAY DIFFRACTIONr_nbd_other0.2130.2143
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1760.211
X-RAY DIFFRACTIONr_mcbond_it2.5152.1034701
X-RAY DIFFRACTIONr_mcbond_other2.5162.1034700
X-RAY DIFFRACTIONr_mcangle_it3.9513.765856
X-RAY DIFFRACTIONr_mcangle_other3.9513.765856
X-RAY DIFFRACTIONr_scbond_it4.0732.5584677
X-RAY DIFFRACTIONr_scbond_other4.0732.5594678
X-RAY DIFFRACTIONr_scangle_it6.3114.466837
X-RAY DIFFRACTIONr_scangle_other6.314.466838
X-RAY DIFFRACTIONr_lrange_it8.46125.77236854
X-RAY DIFFRACTIONr_lrange_other8.45925.74336772
X-RAY DIFFRACTIONr_ncsr_local_group_10.0840.054336
X-RAY DIFFRACTIONr_ncsr_local_group_20.0990.054307
X-RAY DIFFRACTIONr_ncsr_local_group_30.0820.054415
X-RAY DIFFRACTIONr_ncsr_local_group_40.140.053747
X-RAY DIFFRACTIONr_ncsr_local_group_50.1240.053746
X-RAY DIFFRACTIONr_ncsr_local_group_60.1060.053869
X-RAY DIFFRACTIONr_ncsr_local_group_70.0790.054455
X-RAY DIFFRACTIONr_ncsr_local_group_80.0850.054325
X-RAY DIFFRACTIONr_ncsr_local_group_90.1120.053818
X-RAY DIFFRACTIONr_ncsr_local_group_100.1290.053771
X-RAY DIFFRACTIONr_ncsr_local_group_110.0890.054259
X-RAY DIFFRACTIONr_ncsr_local_group_120.1220.053773
X-RAY DIFFRACTIONr_ncsr_local_group_130.0980.05401
X-RAY DIFFRACTIONr_ncsr_local_group_140.130.05390
X-RAY DIFFRACTIONr_ncsr_local_group_150.0510.05407
X-RAY DIFFRACTIONr_ncsr_local_group_160.1280.05393
X-RAY DIFFRACTIONr_ncsr_local_group_170.10.05401
X-RAY DIFFRACTIONr_ncsr_local_group_180.1220.05393
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.084270.05009
12AX-RAY DIFFRACTIONLocal ncs0.084270.05009
23AX-RAY DIFFRACTIONLocal ncs0.099040.05009
24AX-RAY DIFFRACTIONLocal ncs0.099040.05009
35AX-RAY DIFFRACTIONLocal ncs0.081740.05009
36AX-RAY DIFFRACTIONLocal ncs0.081740.05009
47AX-RAY DIFFRACTIONLocal ncs0.139560.05008
48AX-RAY DIFFRACTIONLocal ncs0.139560.05008
59AX-RAY DIFFRACTIONLocal ncs0.123760.05008
510AX-RAY DIFFRACTIONLocal ncs0.123760.05008
611AX-RAY DIFFRACTIONLocal ncs0.105970.05009
612AX-RAY DIFFRACTIONLocal ncs0.105970.05009
713AX-RAY DIFFRACTIONLocal ncs0.078770.05009
714AX-RAY DIFFRACTIONLocal ncs0.078770.05009
815AX-RAY DIFFRACTIONLocal ncs0.084640.05008
816AX-RAY DIFFRACTIONLocal ncs0.084640.05008
917AX-RAY DIFFRACTIONLocal ncs0.112210.05009
918AX-RAY DIFFRACTIONLocal ncs0.112210.05009
1019AX-RAY DIFFRACTIONLocal ncs0.12880.05008
1020AX-RAY DIFFRACTIONLocal ncs0.12880.05008
1121AX-RAY DIFFRACTIONLocal ncs0.089360.05008
1122AX-RAY DIFFRACTIONLocal ncs0.089360.05008
1223AX-RAY DIFFRACTIONLocal ncs0.12210.05008
1224AX-RAY DIFFRACTIONLocal ncs0.12210.05008
1325AX-RAY DIFFRACTIONLocal ncs0.098450.05007
1326AX-RAY DIFFRACTIONLocal ncs0.098450.05007
1427AX-RAY DIFFRACTIONLocal ncs0.130440.05007
1428AX-RAY DIFFRACTIONLocal ncs0.130440.05007
1529AX-RAY DIFFRACTIONLocal ncs0.050690.05008
1530AX-RAY DIFFRACTIONLocal ncs0.050690.05008
1631AX-RAY DIFFRACTIONLocal ncs0.127880.05007
1632AX-RAY DIFFRACTIONLocal ncs0.127880.05007
1733AX-RAY DIFFRACTIONLocal ncs0.099690.05007
1734AX-RAY DIFFRACTIONLocal ncs0.099690.05007
1835AX-RAY DIFFRACTIONLocal ncs0.121910.05008
1836AX-RAY DIFFRACTIONLocal ncs0.121910.05008
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.35-2.4110.3582280.32543880.32747080.8980.91698.04590.324
2.411-2.4770.3382270.31642840.31745220.9160.92499.75670.315
2.477-2.5480.3182230.30441600.30544500.9190.93298.49440.3
2.548-2.6270.3192180.2940810.29243090.9310.94199.76790.286
2.627-2.7120.3092130.27239070.27441710.9350.94998.77730.263
2.712-2.8070.2571900.23838460.23940770.9560.96298.99440.226
2.807-2.9130.3052000.23536490.23938710.9360.96299.43170.22
2.913-3.0310.2611970.21835410.2237700.9510.96899.15120.201
3.031-3.1660.261760.20934470.21136510.9530.97299.23310.189
3.166-3.3190.2611830.20232090.20534100.9520.97599.47210.182
3.319-3.4980.2261680.18631110.18833040.9710.9899.24330.171
3.498-3.7090.2411590.19129480.19331320.9650.98199.20180.177
3.709-3.9630.2191310.16227800.16429420.9670.98598.94630.149
3.963-4.2790.1871280.1526210.15227690.9790.98799.27770.138
4.279-4.6830.1831240.12824030.13125400.980.9999.48820.119
4.683-5.230.1791060.14521750.14722960.9780.98799.34670.135
5.23-6.0270.224810.17419450.17620450.9760.98599.07090.16
6.027-7.3530.203970.17316510.17517640.980.98599.0930.158
7.353-10.280.183690.15813000.15913850.9820.98698.84480.152
10.28-48.2720.31400.2557730.2578410.8980.95496.67060.254
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.30450.77470.87681.42350.45321.91480.01380.0060.1218-0.02210.02370.3056-0.0555-0.2119-0.03740.06850.01740.09960.03210.0370.2297-15.60861.89581.6967
22.425-0.17130.17151.940.40842.48390.01250.41750.0522-0.3959-0.05430.2767-0.0677-0.16530.04190.16090.0036-0.0020.08780.01320.2055-13.6365-6.255761.6494
31.421-0.69110.58642.3945-1.25322.81040.0566-0.0266-0.0940.0833-0.0280.0056-0.0407-0.0474-0.02850.1991-0.02610.05530.0096-0.01280.0432-49.14430.857428.3844
42.3121-0.2763-0.33032.71170.30042.54980.0369-0.13150.26560.0822-0.00010.0514-0.2844-0.2292-0.03680.30720.00610.05660.0347-0.01560.0493-52.301221.966230.9168
52.87271.32070.27421.7390.03051.2975-0.09330.16270.0362-0.15340.0099-0.17370.01780.01940.08340.12040.01860.11490.02170.00520.219-66.7626-6.399463.5896
61.42710.0335-0.29592.41780.3151.84220.00360.2384-0.097-0.1197-0.0229-0.23980.1993-0.00420.01930.17940.01740.13440.0435-0.01670.2234-65.7368-27.334359.4473
72.91220.71540.67781.21770.16841.61520.0364-0.1384-0.06240.0767-0.0472-0.1620.08160.12940.01080.2270.02530.03440.02650.0120.0404-37.9168-7.265218.2441
81.73630.1537-0.10792.15460.27662.42010.07880.0756-0.0809-0.0154-0.0508-0.41730.01220.5419-0.0280.19260.01690.02780.14720.01470.1605-22.10710.68456.099
94.5928-0.39891.38781.358-1.52589.0083-0.07810.17940.1879-0.14140.0027-0.0124-0.52270.22540.07540.1672-0.01620.0130.07120.01180.211-2.57467.279467.4244
105.2677-3.23010.96765.04660.35911.7978-0.1072-0.29790.05020.43820.220.02350.1758-0.0063-0.11280.23920.01060.04250.15750.01480.0858-51.932310.872645.7024
115.1672-0.4112.36562.54821.3576.35920.23540.39150.122-0.69230.0663-0.624-0.0480.4101-0.30170.2208-0.02910.20510.1743-0.03420.4289-53.1468-16.387852.5569
1212.5087-0.2396-2.18851.71680.53153.4609-0.00630.3483-0.35340.00250.0482-0.05790.13990.0423-0.04190.20820.0021-0.01020.1029-0.00910.1251-32.7388-12.7475-0.2983
Refinement TLS groupSelection: ALL

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