[English] 日本語
Yorodumi
- PDB-4c6t: Crystal structure of the RPS4 and RRS1 TIR domain heterodimer -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4c6t
TitleCrystal structure of the RPS4 and RRS1 TIR domain heterodimer
Components
  • DISEASE RESISTANCE PROTEIN RPS4
  • PROBABLE WRKY TRANSCRIPTION FACTOR 52
KeywordsIMMUNE SYSTEM / PLANT TIR DOMAIN / SIGNAL TRANSDUCTION
Function / homology
Function and homology information


plant-type hypersensitive response / innate immune response-activating signaling pathway / NAD+ nucleosidase activity / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NADP+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / endomembrane system / ADP binding / defense response / sequence-specific DNA binding ...plant-type hypersensitive response / innate immune response-activating signaling pathway / NAD+ nucleosidase activity / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NADP+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / endomembrane system / ADP binding / defense response / sequence-specific DNA binding / defense response to bacterium / DNA-binding transcription factor activity / signal transduction / ATP binding / membrane / identical protein binding / nucleus / cytoplasm
Similarity search - Function
WRKY domain / WRKY domain superfamily / WRKY DNA -binding domain / WRKY domain profile. / DNA binding domain / Leucine-rich repeat 3 / Leucine Rich Repeat / C-JID domain / C-JID domain / Toll/interleukin-1 receptor homology (TIR) domain ...WRKY domain / WRKY domain superfamily / WRKY DNA -binding domain / WRKY domain profile. / DNA binding domain / Leucine-rich repeat 3 / Leucine Rich Repeat / C-JID domain / C-JID domain / Toll/interleukin-1 receptor homology (TIR) domain / Disease resistance protein, plants / Apoptotic protease-activating factors, helical domain / NB-ARC / NB-ARC domain / TIR domain / Toll - interleukin 1 - resistance / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Leucine-rich repeat domain superfamily / Winged helix DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
MALONIC ACID / Disease resistance protein RRS1 / Disease resistance protein RRS1 / Disease resistance protein RPS4
Similarity search - Component
Biological speciesARABIDOPSIS THALIANA (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å
AuthorsWilliams, S.J. / Sohn, K.H. / Wan, L. / Bernoux, M. / Ma, Y. / Segonzac, C. / Ve, T. / Sarris, P. / Ericsson, D.J. / Saucet, S.B. ...Williams, S.J. / Sohn, K.H. / Wan, L. / Bernoux, M. / Ma, Y. / Segonzac, C. / Ve, T. / Sarris, P. / Ericsson, D.J. / Saucet, S.B. / Zhang, X. / Parker, J. / Dodds, P.N. / Jones, J.D.G. / Kobe, B.
CitationJournal: Science / Year: 2014
Title: Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor.
Authors: Williams, S.J. / Sohn, K.H. / Wan, L. / Bernoux, M. / Sarris, P.F. / Segonzac, C. / Ve, T. / Ma, Y. / Saucet, S.B. / Ericsson, D.J. / Casey, L.W. / Lonhienne, T. / Winzor, D.J. / Zhang, X. / ...Authors: Williams, S.J. / Sohn, K.H. / Wan, L. / Bernoux, M. / Sarris, P.F. / Segonzac, C. / Ve, T. / Ma, Y. / Saucet, S.B. / Ericsson, D.J. / Casey, L.W. / Lonhienne, T. / Winzor, D.J. / Zhang, X. / Coerdt, A. / Parker, J.E. / Dodds, P.N. / Kobe, B. / Jones, J.D.G.
History
DepositionSep 19, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 28, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 22, 2015Group: Non-polymer description
Revision 1.2May 1, 2024Group: Data collection / Database references ...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 / 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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: PROBABLE WRKY TRANSCRIPTION FACTOR 52
B: DISEASE RESISTANCE PROTEIN RPS4
C: PROBABLE WRKY TRANSCRIPTION FACTOR 52
D: DISEASE RESISTANCE PROTEIN RPS4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,0836
Polymers73,8754
Non-polymers2082
Water0
1
A: PROBABLE WRKY TRANSCRIPTION FACTOR 52
B: DISEASE RESISTANCE PROTEIN RPS4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,0413
Polymers36,9372
Non-polymers1041
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1750 Å2
ΔGint-2.9 kcal/mol
Surface area18740 Å2
MethodPQS
2
C: PROBABLE WRKY TRANSCRIPTION FACTOR 52
D: DISEASE RESISTANCE PROTEIN RPS4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,0413
Polymers36,9372
Non-polymers1041
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1570 Å2
ΔGint-4.7 kcal/mol
Surface area19100 Å2
MethodPQS
Unit cell
Length a, b, c (Å)93.359, 93.359, 416.648
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
22
/ NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(-1, 0.008283, -0.005174), (0.008178, 0.4207, 0.9072), (-0.005337, -0.9072, -0.4207)32.68, -23.87, 36.98
2given(-0.999, -0.03112, 0.03064), (-0.04158, 0.4633, -0.8852), (0.01335, -0.8857, -0.4641)30.6, -20.21, -36.4

-
Components

#1: Protein PROBABLE WRKY TRANSCRIPTION FACTOR 52 / DISEASE RESISTANCE PROTEIN RRS1 / DISEASE RESISTANCE PROTEIN SLH1 / PROTEIN SENSITIVE TO LOW ...DISEASE RESISTANCE PROTEIN RRS1 / DISEASE RESISTANCE PROTEIN SLH1 / PROTEIN SENSITIVE TO LOW HUMIDITY 1 / RESISTANCE TO RALSTONI A SOLANACEARUM 1 PROTEIN / WRKY DNA-BINDING PROTEIN 52


Mass: 17250.496 Da / Num. of mol.: 2
Fragment: TOLL/INTERLEUKIN-1 RECEPTOR DOMAIN, RESIDUES 6-153
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PMCSG7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q9FH83, UniProt: P0DKH5*PLUS
#2: Protein DISEASE RESISTANCE PROTEIN RPS4 /


Mass: 19686.801 Da / Num. of mol.: 2
Fragment: TOLL/INTERLEUKIN-1 RECEPTOR DOMAIN, RESIDUES 11-178
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PMCSG7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q9XGM3
#3: Chemical ChemComp-MLA / MALONIC ACID / DICARBOXYLIC ACID C3 / PROPANEDIOLIC ACID / METHANEDICARBOXYLIC ACID / Malonic acid


Mass: 104.061 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H4O4

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.57 Å3/Da / Density % sol: 65.58 % / Description: NONE
Crystal growpH: 6 / Details: 1.8 M SODIUM MALONATE PH 6.0

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9539
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Aug 29, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9539 Å / Relative weight: 1
ReflectionResolution: 2.65→29.84 Å / Num. obs: 32619 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 23 % / Biso Wilson estimate: 73.73 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 27.5
Reflection shellResolution: 2.65→2.78 Å / Redundancy: 24 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 2 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: RPS4 TIR AND RRS1 TIR

Resolution: 2.65→29.794 Å / SU ML: 0.36 / σ(F): 1.34 / Phase error: 21.13 / Stereochemistry target values: ML
Details: CRYSTALS OF THE RRS1 AND RPS4 TIR DOMAIN HETERODIMER WERE OBTAINED BY LINKING RRS1(6-153) AND RPS4(10-178) WITH A FIVE-RESIDUE (GSGGS) LINKER . A REGION ENCOMPASSING 11 RESIDUES INCLUDING ...Details: CRYSTALS OF THE RRS1 AND RPS4 TIR DOMAIN HETERODIMER WERE OBTAINED BY LINKING RRS1(6-153) AND RPS4(10-178) WITH A FIVE-RESIDUE (GSGGS) LINKER . A REGION ENCOMPASSING 11 RESIDUES INCLUDING THE LINKER COULD NOT BE MODELED DUE TO THE LACK OF INTERPRETABLE ELECTRON DENSITY. WE FAVOR THE INTERPRETATION THAT THE LINKED CHAIN OCCURS BETWEEN MOLECULES A-D, B-C. HOWEVER, AS IT IS NOT POSSIBLE TO MODEL THE LINKER REGION WITH CERTAINTY WE CANNOT EXPLICITLY DETERMINE WHICH MOLECULES ARE LINKED IN THE CRYSTAL. FOR THIS REASON, WE HAVE LABELLED THE RRS1 AND RPS4 TIR DOMAIN MOLECULES AS SEPARATE CHAINS IN THE COORDINATE FILE DEPOSITED. THE FUNCTIONALLY IMPORTANT HETERODIMERISATION INTERFACE BETWEEN RRS1 AND RPS4 TIR DOMAINS OCCURS BETWEEN PROTEIN CHAINS A-B AND C-D.
RfactorNum. reflection% reflection
Rfree0.2267 1997 6.1 %
Rwork0.1823 --
obs0.185 32498 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.65→29.794 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4952 0 14 0 4966
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0095044
X-RAY DIFFRACTIONf_angle_d1.1676790
X-RAY DIFFRACTIONf_dihedral_angle_d13.5491919
X-RAY DIFFRACTIONf_chiral_restr0.05769
X-RAY DIFFRACTIONf_plane_restr0.006869
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.65-2.71630.37711380.33862106X-RAY DIFFRACTION100
2.7163-2.78970.36181390.29832124X-RAY DIFFRACTION100
2.7897-2.87170.2861390.26052119X-RAY DIFFRACTION100
2.8717-2.96430.29361380.25472113X-RAY DIFFRACTION100
2.9643-3.07010.28161400.24032128X-RAY DIFFRACTION100
3.0701-3.19290.26831410.24542153X-RAY DIFFRACTION100
3.1929-3.33810.2471410.2112168X-RAY DIFFRACTION100
3.3381-3.51380.2371410.19462135X-RAY DIFFRACTION100
3.5138-3.73350.22421410.18252178X-RAY DIFFRACTION100
3.7335-4.02120.241420.17642156X-RAY DIFFRACTION100
4.0212-4.42470.20681440.15422204X-RAY DIFFRACTION100
4.4247-5.06220.18531450.15062217X-RAY DIFFRACTION100
5.0622-6.36760.21711480.17842260X-RAY DIFFRACTION100
6.3676-29.79620.20121600.15162440X-RAY DIFFRACTION100
Refinement TLS params.

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

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
14.2148-1.4274-0.06191.55072.08676.1979-0.209-0.0124-0.22670.26850.0313-0.29980.40040.59410.22620.59110.0707-0.03910.44840.01530.42837.4941-42.864717.0116
23.8405-0.2682-0.41346.30881.0326.3364-0.0424-0.43050.40760.7979-0.2439-0.0407-0.09980.17050.26180.6868-0.0242-0.08380.4583-0.02490.49312.0859-37.79825.3959
32.18991.40630.5583.3903-1.47364.60650.0001-0.85870.11270.8078-0.45510.8080.6453-0.74070.4311.01530.00210.11540.7943-0.13150.6977-7.2061-39.740835.3646
43.04280.43690.65193.25460.90463.4626-0.34680.0510.5626-0.21210.03840.6195-0.4301-0.17160.290.75870.0985-0.12170.5506-0.03820.5647-3.1055-39.629310.2646
53.7293-0.44510.16836.44341.35426.2821-0.09180.58260.0863-0.9714-0.11990.6503-0.3384-0.50410.27110.80910.0022-0.07350.5119-0.01780.60230.0355-56.59990.5755
62.8888-0.99511.3472.51972.00513.6561-0.46940.7776-0.0057-0.927-0.2021.02830.0637-1.37450.59441.1653-0.1293-0.02190.9061-0.25821.1326-9.3566-67.4672-4.285
71.7293-0.07470.33644.7133-0.33781.6034-0.02610.1801-0.2679-0.2368-0.19680.66390.4532-0.28550.20950.8583-0.05790.02310.5124-0.04350.67061.2608-70.44983.5463
81.8635-0.47990.21715.83370.30121.0631-0.0055-0.2914-0.96850.68140.0214-0.77430.89130.28360.0780.99370.11340.07120.58980.09060.81649.1546-70.593610.3408
95.15030.1848-0.35494.25892.27833.7761-0.091-0.0644-0.13020.3844-0.1236-0.1533-0.11640.81880.2090.62480.01760.04120.4344-0.04730.533312.3077-57.08793.2695
109.14767.2137-0.39517.6199-2.55762.6349-1.12641.6017-1.595-2.80550.2361-1.1652-0.76621.01261.04421.3497-0.00640.30591.7597-0.25150.883413.3908-61.8431-9.0588
114.09971.0879-1.04184.24742.03113.5637-0.22860.1156-0.5422-0.18980.1844-0.3090.7297-0.69150.04830.7616-0.14670.2310.5002-0.08090.750225.603-57.5566-3.854
123.3321.20010.4234.24220.70653.0847-0.69140.162-0.5935-0.7950.43770.21960.7065-1.10250.16361.1024-0.23440.160.8191-0.16311.01520.8409-61.6421-8.7377
133.35372.1367-0.5644.88022.03752.95-0.26740.4345-1.1424-0.433-0.12330.48820.815-0.67740.240.9036-0.18080.11140.7122-0.24691.023927.1654-62.5738-14.84
142.4242-0.8798-0.29655.07760.84483.4089-0.28390.8455-1.0725-0.54240.2356-0.37610.52430.29380.04250.8509-0.16520.26130.5879-0.23840.992235.8482-61.9843-15.6496
152.50830.3669-0.72513.5091-0.11020.428-0.3230.6429-1.6023-0.50610.5753-0.90420.79010.3170.07621.3303-0.08140.33330.6877-0.31591.650639.5185-71.0807-17.3779
163.45171.66420.53863.70970.36884.3434-0.1130.0703-0.0910.2517-0.263-0.3742-0.6990.420.35530.6905-0.0830.11470.5938-0.08170.713435.3712-49.5114-5.4936
173.6709-0-1.74615.1810.21235.2599-0.0295-0.29890.48620.07930.0994-1.1717-0.62730.6003-0.07080.7186-0.0832-0.10140.61330.01790.81632.2084-48.100214.0025
180.13180.12620.29320.13370.28460.67650.659-0.2337-0.5471.3577-0.0252-0.54040.68531.7822-0.65021.0971-0.0129-0.41891.48790.2191.247344.701-50.584225.0431
193.1967-1.29690.60721.6838-1.90142.3726-0.5462-0.859-0.26611.27590.2388-0.4576-0.13710.90950.33971.06880.108-0.13061.08910.16060.947333.7417-55.53726.4255
204.4322-1.5662-2.36012.0054-1.36724.8041-0.2961-0.8251-0.59120.57080.2419-0.18870.48780.44570.02080.9493-0.0001-0.04940.79960.16910.793224.5192-59.481423.4037
216.73170.91390.89946.70391.43895.5588-0.0892-0.82360.51070.4311-0.25360.9262-0.34530.01690.24420.6657-0.01660.0550.67930.0170.738719.6721-47.759216.3729
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN B AND (RESID 13 THROUGH 41 )
2X-RAY DIFFRACTION2CHAIN B AND (RESID 42 THROUGH 119 )
3X-RAY DIFFRACTION3CHAIN B AND (RESID 120 THROUGH 148 )
4X-RAY DIFFRACTION4CHAIN B AND (RESID 149 THROUGH 178 )
5X-RAY DIFFRACTION5CHAIN A AND (RESID 8 THROUGH 42 )
6X-RAY DIFFRACTION6CHAIN A AND (RESID 43 THROUGH 59 )
7X-RAY DIFFRACTION7CHAIN A AND (RESID 60 THROUGH 106 )
8X-RAY DIFFRACTION8CHAIN A AND (RESID 107 THROUGH 130 )
9X-RAY DIFFRACTION9CHAIN A AND (RESID 131 THROUGH 144 )
10X-RAY DIFFRACTION10CHAIN A AND (RESID 145 THROUGH 148 )
11X-RAY DIFFRACTION11CHAIN D AND (RESID 16 THROUGH 41 )
12X-RAY DIFFRACTION12CHAIN D AND (RESID 42 THROUGH 57 )
13X-RAY DIFFRACTION13CHAIN D AND (RESID 58 THROUGH 82 )
14X-RAY DIFFRACTION14CHAIN D AND (RESID 83 THROUGH 119 )
15X-RAY DIFFRACTION15CHAIN D AND (RESID 120 THROUGH 148 )
16X-RAY DIFFRACTION16CHAIN D AND (RESID 149 THROUGH 178 )
17X-RAY DIFFRACTION17CHAIN C AND (RESID 8 THROUGH 42 )
18X-RAY DIFFRACTION18CHAIN C AND (RESID 43 THROUGH 53 )
19X-RAY DIFFRACTION19CHAIN C AND (RESID 54 THROUGH 88 )
20X-RAY DIFFRACTION20CHAIN C AND (RESID 89 THROUGH 130 )
21X-RAY DIFFRACTION21CHAIN C AND (RESID 131 THROUGH 150 )

+
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