[English] 日本語
Yorodumi
- PDB-3j3v: Atomic model of the immature 50S subunit from Bacillus subtilis (... -

+
Open data


ID or keywords:

Loading...

no data

-
Basic information

Entry
Database: PDB / ID: 3j3v
TitleAtomic model of the immature 50S subunit from Bacillus subtilis (state I-a)
Components
  • (50S ribosomal protein ...) x 22
  • (ribosome RNA ...) x 2
KeywordsRIBOSOME / Ribosome biogenesis / ribosome assembly / RNA folding / YlqF
Function / homology
Function and homology information


positive regulation of rRNA processing / nucleoid / maturation of LSU-rRNA / ribosome assembly / cytoplasmic translation / rRNA processing / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / large ribosomal subunit / ribosomal large subunit assembly ...positive regulation of rRNA processing / nucleoid / maturation of LSU-rRNA / ribosome assembly / cytoplasmic translation / rRNA processing / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / large ribosomal subunit / ribosomal large subunit assembly / 5S rRNA binding / regulation of translation / transferase activity / tRNA binding / negative regulation of translation / ribosome / rRNA binding / structural constituent of ribosome / translation / mRNA binding / response to antibiotic / RNA binding / DNA binding / cytosol
Ribosomal protein L13, conserved site / Ribosomal protein L5, N-terminal / Ribosomal protein L1, conserved site / Ribosomal protein L1-like / Ribosomal protein L1/ribosomal biogenesis protein / Ribosomal protein L21-like / Ribosomal protein L15 / Ribosomal protein L5, C-terminal / Ribosomal protein L20, C-terminal / Ribosomal protein L2 signature. ...Ribosomal protein L13, conserved site / Ribosomal protein L5, N-terminal / Ribosomal protein L1, conserved site / Ribosomal protein L1-like / Ribosomal protein L1/ribosomal biogenesis protein / Ribosomal protein L21-like / Ribosomal protein L15 / Ribosomal protein L5, C-terminal / Ribosomal protein L20, C-terminal / Ribosomal protein L2 signature. / Ribosomal protein L29/L35 superfamily / L21-like superfamily / Ribosomal L18e/L15P superfamily / Ribosomal protein L17 superfamily / Ribosomal protein L22/L17 superfamily / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L4 domain superfamily / Ribosomal protein L5 domain superfamily / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11, N-terminal / Ribosomal protein L6, bacterial-type / Ribosomal protein L3, conserved site / Ribosomal protein L3, bacterial/organelle-type / Ribosomal protein L14P, conserved site / Ribosomal protein L6, alpha-beta domain / Ribosomal protein L11, C-terminal / Ribosomal protein L11, conserved site / Ribosomal protein L2, conserved site / Ribosomal protein L5, conserved site / Ribosomal protein L5, bacterial-type / Ribosomal protein L34, conserved site / Ribosomal protein L18e/L15P / Ribosomal Proteins L2, RNA binding domain / Ribosomal protein L2, C-terminal / Ribosomal protein L6, alpha-beta domain superfamily / Ribosomal protein L14 superfamily / Ribosomal protein L21, conserved site / Ribosomal protein L19 / Ribosomal protein L1p/L10e family / Ribosomal proteins 50S-L15, 50S-L18e, 60S-L27A / Ribosomal prokaryotic L21 protein / Ribosomal L29 protein / Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast / Ribosomal protein L17 / Ribosomal L32p protein family / Ribosomal protein L4/L1 family / Ribosomal protein L11, N-terminal domain / Ribosomal Proteins L2, C-terminal domain / Ribosomal proteins 50S L24/mitochondrial 39S L24 / Ribosomal protein L14 signature. / Ribosomal protein L23 signature. / Ribosomal protein L5 signature. / ribosomal L5P family C-terminus / Ribosomal protein L13 / Ribosomal protein L13 superfamily / Ribosomal protein L23 / Ribosomal protein L30, ferredoxin-like fold domain superfamily / Ribosomal protein L19 superfamily / Ribosomal Protein L26/L24, KOW domain / Ribosomal Proteins L2, RNA binding domain / Ribosomal protein L22p/L17e / Ribosomal protein L14p/L23e / Ribosomal protein L5 / Ribosomal protein L34 / Ribosomal protein L3 / Ribosomal protein L11, RNA binding domain / Ribosomal protein L30p/L7e / Ribosomal protein L6 / Ribosomal protein L20 / KOW motif / Ribosomal protein L22/L17, conserved site / Ribosomal protein L19, conserved site / Ribosomal protein L22 signature. / Ribosomal protein L34 / Ribosomal protein L4/L1e / Ribosomal protein L29, conserved site / Ribosomal protein L19 / Ribosomal protein L29/L35 / Ribosomal protein L21 / Ribosomal protein L15, conserved site / Ribosomal protein L22/L17 / Ribosomal protein L23/L25, conserved site / Ribosomal protein L11/L12 / Ribosomal protein L6 / Ribosomal protein L3 / Ribosomal protein L17 / Ribosomal protein L14P / Ribosomal protein L2 / Ribosomal protein L3 signature. / Ribosomal protein L15 signature. / Ribosomal protein L6 signature 1. / Ribosomal protein L29 signature. / Ribosomal protein L30 signature. / Ribosomal protein L13 signature. / Ribosomal protein L34 signature. / Ribosomal protein L20 signature. / Ribosomal protein L19 signature. / Ribosomal protein L24 signature. / Ribosomal protein L17 signature. / Ribosomal protein L21 signature.
50S ribosomal protein L2 / 50S ribosomal protein L1 / 50S ribosomal protein L11 / 50S ribosomal protein L13 / 50S ribosomal protein L20 / 50S ribosomal protein L18 / 50S ribosomal protein L6 / 50S ribosomal protein L23 / 50S ribosomal protein L4 / 50S ribosomal protein L3 ...50S ribosomal protein L2 / 50S ribosomal protein L1 / 50S ribosomal protein L11 / 50S ribosomal protein L13 / 50S ribosomal protein L20 / 50S ribosomal protein L18 / 50S ribosomal protein L6 / 50S ribosomal protein L23 / 50S ribosomal protein L4 / 50S ribosomal protein L3 / 50S ribosomal protein L29 / 50S ribosomal protein L22 / 50S ribosomal protein L21 / 50S ribosomal protein L17 / 50S ribosomal protein L30 / 50S ribosomal protein L15 / 50S ribosomal protein L5 / 50S ribosomal protein L14 / 50S ribosomal protein L24 / 50S ribosomal protein L34 / 50S ribosomal protein L32 / 50S ribosomal protein L19 / gb:al009126.3:
Biological speciesBacillus subtilis (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 13.3 Å
AuthorsLi, N. / Guo, Q. / Zhang, Y. / Yuan, Y. / Ma, C. / Lei, J. / Gao, N.
CitationJournal: Nucleic Acids Res. / Year: 2013
Title: Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.
Authors: Ningning Li / Yuling Chen / Qiang Guo / Yixiao Zhang / Yi Yuan / Chengying Ma / Haiteng Deng / Jianlin Lei / Ning Gao /
Abstract: Ribosome assembly is a process fundamental for all cellular activities. The efficiency and accuracy of the subunit assembly are tightly regulated and closely monitored. In the present work, we ...Ribosome assembly is a process fundamental for all cellular activities. The efficiency and accuracy of the subunit assembly are tightly regulated and closely monitored. In the present work, we characterized, both compositionally and structurally, a set of in vivo 50S subunit precursors (45S), isolated from a mutant bacterial strain. Our qualitative mass spectrometry data indicate that L28, L16, L33, L36 and L35 are dramatically underrepresented in the 45S particles. This protein spectrum shows interesting similarity to many qualitatively analyzed 50S precursors from different genetic background, indicating the presence of global rate-limiting steps in the late-stage assembly of 50S subunit. Our structural data reveal two major intermediate states for the 45S particles. Consistently, both states severally lack those proteins, but they also differ in the stability of the functional centers of the 50S subunit, demonstrating that they are translationally inactive. Detailed analysis indicates that the orientation of H38 accounts for the global conformational differences in these intermediate structures, and suggests that the reorientation of H38 to its native position is rate-limiting during the late-stage assembly. Especially, H38 plays an essential role in stabilizing the central protuberance, through the interaction with the 5S rRNA, and the correctly orientated H38 is likely a prerequisite for further maturation of the 50S subunit.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Apr 28, 2013 / Release: Jun 12, 2013
RevisionDateData content typeGroupProviderType
1.0Jun 12, 2013Structure modelrepositoryInitial release
1.1Aug 28, 2013Structure modelDatabase references

-
Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
  • Download
  • Superimposition on EM map
  • EMDB-5642
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
0: 50S ribosomal protein L32
2: 50S ribosomal protein L34
5: 50S ribosomal protein L1
6: 50S ribosomal protein L11
A: ribosome RNA 23S
B: ribosome RNA 5S
C: 50S ribosomal protein L2
D: 50S ribosomal protein L3
E: 50S ribosomal protein L4
F: 50S ribosomal protein L5
G: 50S ribosomal protein L6
J: 50S ribosomal protein L13
K: 50S ribosomal protein L14
L: 50S ribosomal protein L15
N: 50S ribosomal protein L17
O: 50S ribosomal protein L18
P: 50S ribosomal protein L19
Q: 50S ribosomal protein L20
R: 50S ribosomal protein L21
S: 50S ribosomal protein L22
T: 50S ribosomal protein L23
U: 50S ribosomal protein L24
X: 50S ribosomal protein L29
Y: 50S ribosomal protein L30


Theoretical massNumber of molelcules
Total (without water)1,314,09624
Polymers1,314,09624
Non-polymers00
Water0
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

-
Components

+
50S ribosomal protein ... , 22 types, 22 molecules 0256CDEFGJKLNOPQRSTUXY

#1: Protein/peptide 50S ribosomal protein L32 /


Mass: 6745.073 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: O34687
#2: Protein/peptide 50S ribosomal protein L34 /


Mass: 5271.332 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P05647
#3: Protein/peptide 50S ribosomal protein L1 / / BL1


Mass: 25026.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: Q06797
#4: Protein/peptide 50S ribosomal protein L11 / / BL11


Mass: 14951.442 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: Q06796
#7: Protein/peptide 50S ribosomal protein L2 / / BL2


Mass: 30335.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P42919
#8: Protein/peptide 50S ribosomal protein L3 / / BL3


Mass: 22723.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P42920
#9: Protein/peptide 50S ribosomal protein L4 /


Mass: 22424.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P42921
#10: Protein/peptide 50S ribosomal protein L5 / / BL6


Mass: 20177.564 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P12877
#11: Protein/peptide 50S ribosomal protein L6 / / BL10


Mass: 19543.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P46898
#12: Protein/peptide 50S ribosomal protein L13 /


Mass: 16407.104 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P70974
#13: Protein/peptide 50S ribosomal protein L14 /


Mass: 13175.288 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P12875
#14: Protein/peptide 50S ribosomal protein L15 /


Mass: 15410.694 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P19946
#15: Protein/peptide 50S ribosomal protein L17 / / BL15 / BL21


Mass: 13774.806 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P20277
#16: Protein/peptide 50S ribosomal protein L18 / / BL16


Mass: 12993.829 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P46899
#17: Protein/peptide 50S ribosomal protein L19 /


Mass: 13416.853 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: O31742
#18: Protein/peptide 50S ribosomal protein L20 /


Mass: 13669.189 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P55873
#19: Protein/peptide 50S ribosomal protein L21 / / BL20


Mass: 11296.081 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P26908
#20: Protein/peptide 50S ribosomal protein L22 /


Mass: 12481.608 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P42060
#21: Protein/peptide 50S ribosomal protein L23 /


Mass: 10978.813 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P42924
#22: Protein/peptide 50S ribosomal protein L24 / / 12 kDa DNA-binding protein / BL23 / HPB12


Mass: 11166.120 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P0CI78
#23: Protein/peptide 50S ribosomal protein L29 /


Mass: 7728.029 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P12873
#24: Protein/peptide 50S ribosomal protein L30 / / BL27


Mass: 6650.795 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: UniProt: P19947

-
Ribosome RNA ... , 2 types, 2 molecules AB

#5: RNA chain ribosome RNA 23S


Mass: 949324.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: GenBank: AL009126.3
#6: RNA chain ribosome RNA 5S


Mass: 38423.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bacillus subtilis (bacteria) / Strain: 168 / References: GenBank: AL009126.3

-
Experimental details

-
Experiment

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

-
Sample preparation

ComponentName: Immature 50S subunit from YlqF-deficient Bacillus subtilis strain
Type: RIBOSOME
Buffer solutionName: 100mM NH4Cl, 20mM Tris-HCl, 10mM MgOAc2, 1mM TCEP. / pH: 7.5 / Details: 100mM NH4Cl, 20mM Tris-HCl, 10mM MgOAc2, 1mM TCEP.
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Method: Blot for 20 seconds before plunging

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS / Date: Dec 6, 2011
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 59000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / Camera length: 0 mm
Specimen holderModel: FEI TITAN KRIOS AUTOGRID HOLDER / Tilt angle max: 0 ° / Tilt angle min: 0 °
Image recordingElectron dose: 20 e/Å2 / Film or detector model: FEI EAGLE (4k x 4k)
Radiation wavelengthRelative weight: 1

-
Processing

EM software
IDNameCategory
1MDFFmodel fitting
2Modellermodel fitting
3modeRNAmodel fitting
4S2Smodel fitting
5Relion3D reconstruction
CTF correctionDetails: Each particle
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionMethod: Reference projections / Resolution: 13.3 Å / Resolution method: OTHER / Num. of particles: 21020
Details: (Single particle details: This is one of the classified groups with the software RELION) (Single particle--Applied symmetry: C1)
Symmetry type: POINT
Atomic model building
IDProtocolSpaceTarget criteriaDetails
1FLEXIBLE FITREALCross-correlationMETHOD--Flexible fitting REFINEMENT PROTOCOL--Atom models of the 23S and 5S rRNAs were built using the software S2S and modeRNA, with the crystal structures of the 50S subunits from E. coli (PDB ID- 2AW4) and Thermus thermophilus (PDB ID- 2J01) as template. Models of ribosomal proteins, L1, L3, L4, L6, L10, L13, L14, L15, L17, L19, L20, L21, L22, L23, L24, L27, L29, L30, L31, L32, L33, L34, L35 and L36 were downloaded from the SWISS-MODEL Repository. The others, including L2, L5, L11, L16, L18 and L28 were modeled using MODELLER with crystal structures of E. coli and T. thermophilus 50S subunits as templates.The combined atomic model of the B. subtilis 50S subunit was docked into a high resolution mature 50S density map and optimized using MDFF. This optimized model was docked into the EM density using Chimera and flexible fitted into the density using MDFF. DETAILS--Ref- Schuwirth, B.S., Borovinskaya, M.A., Hau, C.W., Zhang, W., Vila-Sanjurjo, A., Holton, J.M. and Cate, J.H. (2005) Structures of the bacterial ribosome at 3.5 A resolution. Science, 310, 827-834. Selmer, M., Dunham, C.M., Murphy, F.V.t., Weixlbaumer, A., Petry, S., Kelley, A.C., Weir, J.R. and Ramakrishnan, V. (2006) Structure of the 70S ribosome complexed with mRNA and tRNA. Science, 313, 1935-1942. Jossinet, F. and Westhof, E. (2005) Sequence to Structure (S2S)- display, manipulate and interconnect RNA data from sequence to structure. Bioinformatics, 21, 3320-3321. Rother, M., Rother, K., Puton, T. and Bujnicki, J.M. (2011) ModeRNA- a tool for comparative modeling of RNA 3D structure. Nucleic acids research, 39, 4007-4022. Kiefer, F., Arnold, K., Kunzli, M., Bordoli, L. and Schwede, T. (2009) The SWISS-MODEL Repository and associated resources. Nucleic acids research, 37, D387-392. Eswar, N., Webb, B., Marti-Renom, M.A., Madhusudhan, M.S., Eramian, D., Shen, M.Y., Pieper, U. and Sali, A. (2006) Comparative protein structure modeling using Modeller. Current protocols in bioinformatics / editoral board, Andreas D. Baxevanis ... [et al.], Chapter 5, Unit 5 6. Trabuco, L.G., Villa, E., Mitra, K., Frank, J. and Schulten, K. (2008) Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure, 16, 673-683. Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C. and Ferrin, T.E. (2004) UCSF Chimera--a visualization system for exploratory research and analysis. Journal of computational chemistry, 25, 1605-1612.
2
Atomic model building
IDPDB-ID3D fitting-ID
12J011
22AW42
Refinement stepCycle: LAST
ProteinNucleic acidLigandSolventTotal
Num. atoms21701 64456 0 0 86157

+
About Yorodumi

-
News

-
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. (see PDBe EMDB page)
  • 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 at PDBe / 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. See below links for details.
  • 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

+
Jun 16, 2017. Omokage search with filter

Omokage search with filter

  • Result of Omokage search can be filtered by keywords and the database types

Related info.: Omokage search

+
Sep 15, 2016. EM Navigator & Yorodumi renewed

EM Navigator & Yorodumi renewed

  • New versions of EM Navigator and Yorodumi started

Related info.: Changes in new EM Navigator and Yorodumi

+
Aug 31, 2016. New EM Navigator & Yorodumi

New EM Navigator & Yorodumi

  • In 15th Sep 2016, the development versions of EM Navigator and Yorodumi will replace the official versions.
  • Current version will continue as 'legacy version' for some time.

Related info.: Changes in new EM Navigator and Yorodumi / EM Navigator / Yorodumi

Read more

-
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.

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