[English] 日本語
Yorodumi
- PDB-9iui: Crystal structure of PSD-95 GK domain in complex with GK_FingR -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9iui
TitleCrystal structure of PSD-95 GK domain in complex with GK_FingR
Components
  • Disks large homolog 4
  • FingR targeting PSD-95
KeywordsPROTEIN BINDING / Protein complex
Function / homology
Function and homology information


RHO GTPases activate CIT / positive regulation of AMPA glutamate receptor clustering / neuronal ion channel clustering / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / Neurexins and neuroligins / neuroligin family protein binding / regulation of grooming behavior / structural constituent of postsynaptic density / synaptic vesicle maturation ...RHO GTPases activate CIT / positive regulation of AMPA glutamate receptor clustering / neuronal ion channel clustering / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / Neurexins and neuroligins / neuroligin family protein binding / regulation of grooming behavior / structural constituent of postsynaptic density / synaptic vesicle maturation / positive regulation of neuron projection arborization / receptor localization to synapse / cellular response to potassium ion / vocalization behavior / cerebellar mossy fiber / LGI-ADAM interactions / neuron spine / AMPA glutamate receptor clustering / Trafficking of AMPA receptors / protein localization to synapse / dendritic branch / proximal dendrite / positive regulation of dendrite morphogenesis / Activation of Ca-permeable Kainate Receptor / dendritic spine morphogenesis / negative regulation of receptor internalization / juxtaparanode region of axon / frizzled binding / acetylcholine receptor binding / neuron projection terminus / dendritic spine organization / regulation of NMDA receptor activity / Synaptic adhesion-like molecules / RAF/MAP kinase cascade / positive regulation of synapse assembly / NMDA selective glutamate receptor signaling pathway / beta-2 adrenergic receptor binding / neurotransmitter receptor localization to postsynaptic specialization membrane / cortical cytoskeleton / locomotory exploration behavior / AMPA glutamate receptor complex / kinesin binding / neuromuscular process controlling balance / excitatory synapse / social behavior / positive regulation of excitatory postsynaptic potential / regulation of neuronal synaptic plasticity / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / D1 dopamine receptor binding / positive regulation of synaptic transmission / regulation of postsynaptic membrane neurotransmitter receptor levels / ionotropic glutamate receptor binding / dendrite cytoplasm / cell periphery / PDZ domain binding / synaptic membrane / establishment of protein localization / regulation of long-term neuronal synaptic plasticity / postsynaptic density membrane / cell-cell adhesion / cerebral cortex development / neuromuscular junction / kinase binding / cell junction / synaptic vesicle / nervous system development / cell-cell junction / positive regulation of cytosolic calcium ion concentration / protein-containing complex assembly / scaffold protein binding / protein phosphatase binding / chemical synaptic transmission / dendritic spine / postsynaptic membrane / postsynapse / neuron projection / postsynaptic density / signaling receptor binding / synapse / dendrite / protein-containing complex binding / protein kinase binding / glutamatergic synapse / endoplasmic reticulum / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site / Guanylate kinase-like signature. / Guanylate kinase-like domain profile. ...Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site / Guanylate kinase-like signature. / Guanylate kinase-like domain profile. / Guanylate kinase-like domain / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / PDZ domain / SH3 domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Disks large homolog 4
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
unclassified sequences (unknown)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.93 Å
AuthorsZhu, S. / Cai, Q. / Zhang, M.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: Crystal structure of PSD-95 GK domain in complex with GK_FingR
Authors: Zhu, S. / Cai, Q. / Zhang, M.
History
DepositionJul 21, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 23, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Disks large homolog 4
B: FingR targeting PSD-95
C: Disks large homolog 4
D: FingR targeting PSD-95
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,9778
Polymers64,4934
Non-polymers4854
Water4,306239
1
A: Disks large homolog 4
B: FingR targeting PSD-95


Theoretical massNumber of molelcules
Total (without water)32,2462
Polymers32,2462
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2250 Å2
ΔGint-8 kcal/mol
Surface area13970 Å2
MethodPISA
2
C: Disks large homolog 4
D: FingR targeting PSD-95
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7316
Polymers32,2462
Non-polymers4854
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3050 Å2
ΔGint-9 kcal/mol
Surface area13370 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.429, 74.987, 136.567
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

-
Protein , 2 types, 4 molecules ACBD

#1: Protein Disks large homolog 4 / Postsynaptic density protein 95 / PSD-95 / Synapse-associated protein 90 / SAP-90 / SAP90


Mass: 21690.418 Da / Num. of mol.: 2 / Fragment: GK domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Dlg4, Dlgh4, Psd95 / Production host: Escherichia coli (E. coli) / References: UniProt: P31016
#2: Protein FingR targeting PSD-95


Mass: 10555.861 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) unclassified sequences (unknown) / Production host: Escherichia coli (E. coli)

-
Non-polymers , 4 types, 243 molecules

#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 239 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestN
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.64 Å3/Da / Density % sol: 53.36 %
Crystal growTemperature: 289 K / Method: vapor diffusion / pH: 5 / Details: 0.1M Sodium Citrate pH 5.0, 20% PEG 20000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9793 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 17, 2021
RadiationMonochromator: LN2-cooled DCM with Si(111) crystals / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 1.93→50 Å / Num. obs: 51565 / % possible obs: 98.7 % / Observed criterion σ(I): -3 / Redundancy: 13.1 % / CC1/2: 0.999 / Rmerge(I) obs: 0.138 / Rrim(I) all: 0.144 / Net I/σ(I): 12.82
Reflection shell
Resolution (Å)Rmerge(I) obsNum. unique obsCC1/2Rrim(I) allDiffraction-ID
1.93-2.042.40277760.6962.5051
2.04-2.191.53878310.8721.5981
2.19-2.360.91872710.9510.9551
2.36-2.580.51967680.9860.541
2.58-2.890.28361160.9950.2941
2.89-3.330.12754320.9990.1321
3.33-4.080.06645880.9990.0691
4.08-5.750.043365610.0451
5.75-500.035212710.0361

-
Processing

Software
NameVersionClassification
PHENIX(1.20.1_4487: ???)refinement
XDSdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.93→49.72 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 38.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2782 2566 5 %
Rwork0.2387 --
obs0.2406 51363 98.3 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.93→49.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4370 0 32 239 4641
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0054529
X-RAY DIFFRACTIONf_angle_d0.7666124
X-RAY DIFFRACTIONf_dihedral_angle_d6.362630
X-RAY DIFFRACTIONf_chiral_restr0.058667
X-RAY DIFFRACTIONf_plane_restr0.006791
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.93-1.960.51931200.47942274X-RAY DIFFRACTION84
1.96-20.44851390.44792618X-RAY DIFFRACTION96
2-2.050.43951420.42422700X-RAY DIFFRACTION100
2.05-2.10.42041420.38662695X-RAY DIFFRACTION100
2.1-2.150.40231440.35722726X-RAY DIFFRACTION100
2.15-2.210.31331430.32542723X-RAY DIFFRACTION100
2.21-2.270.35331430.30542721X-RAY DIFFRACTION100
2.27-2.340.35311400.28662668X-RAY DIFFRACTION98
2.34-2.430.29831430.27282716X-RAY DIFFRACTION100
2.43-2.530.34191450.26632731X-RAY DIFFRACTION99
2.53-2.640.28581430.27432722X-RAY DIFFRACTION99
2.64-2.780.30111440.26522763X-RAY DIFFRACTION99
2.78-2.950.33861400.25152685X-RAY DIFFRACTION99
2.95-3.180.26231460.24262773X-RAY DIFFRACTION100
3.18-3.50.26821450.22482776X-RAY DIFFRACTION100
3.5-4.010.24261450.19832758X-RAY DIFFRACTION99
4.01-5.050.22421480.16772833X-RAY DIFFRACTION100
5.05-49.720.20451540.18232915X-RAY DIFFRACTION98
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)
11.42281.2931-0.07011.6857-0.17520.79180.0133-0.23290.237-0.0492-0.15560.3046-0.2217-0.19450.09460.3730.0756-0.02910.5236-0.0130.3927-10.57617.1546-13.7661
23.2139-0.2811-0.08672.22970.13913.6395-0.2103-0.1451-0.17750.41620.07860.29960.3222-0.49810.18470.3285-0.0320.05520.5793-0.0110.4023-22.4556-9.6355-5.63
32.10830.65-0.32242.937-0.35063.043-0.3389-0.0483-0.0005-0.17950.07020.41760.3536-0.48570.34570.4023-0.08720.02750.53920.02020.4431-15.2949-8.4296-12.622
41.90680.47780.20133.5943-0.53754.1549-0.42090.1307-0.3368-0.32190.068-0.59210.394-0.1930.29670.38710.01160.1050.42370.03660.4705-8.7487-1.5808-17.8974
52.38850.2773-0.49341.01470.30274.1681-0.067-0.17960.0670.0215-0.0015-0.1379-0.23150.32310.07820.3103-0.0278-0.00660.38770.04440.32593.71017.2414-12.2029
61.858-0.4098-0.94533.041-0.77016.1487-0.5652-0.78310.56840.1011-0.04660.0941-1.082-0.074-0.01360.842-0.2307-0.14031.2454-0.18670.6123-8.273811.429316.2639
71.1050.3889-1.28691.2046-0.67632.69690.3659-1.121-0.2970.05360.4130.1634-0.7726-0.385-0.38240.46580.01370.05421.26050.05490.4613-14.92585.372521.5816
81.57250.12210.90880.42350.9122.1130.6731-0.2330.4508-0.0787-0.06230.0663-0.9066-0.3608-0.41780.55480.0380.00740.5598-0.10780.4729-12.177711.96921.2717
92.7517-0.75182.00052.9683-0.07464.85660.2317-1.3342-0.3239-0.2514-0.1278-0.25560.43590.1507-0.05370.3467-0.05180.03310.74580.03140.3963-12.4543-0.23177.5025
103.4696-0.7224-0.88340.2857-0.08281.3577-0.1808-0.2083-1.4580.7112-0.19880.4430.6110.2241-0.01680.95090.128-0.13761.11590.40620.9108-4.1705-9.463117.4536
111.97840.37270.01511.28650.44594.00490.2841-0.4199-0.19110.0464-0.45740.1099-0.11-0.27850.06670.4162-0.02340.08630.69630.03420.4082-17.08782.670910.0116
120.6426-0.48070.3681.51660.11310.4890.1738-1.1094-0.1670.111-0.2044-0.2790.28210.4395-0.00420.346-0.0928-0.05621.16450.13250.4699-8.9678-0.330315.829
134.57181.18162.98651.01330.51512.6334-0.0396-0.0175-0.5216-0.09180.3736-0.4844-0.17570.7359-0.22720.3614-0.01490.02990.6974-0.02180.3518-8.09020.7858-2.7691
141.3188-0.80340.79213.164-0.69815.4522-0.032-0.5692-0.04341.3345-0.5193-0.631-0.0258-0.0292-0.06560.2903-0.5638-0.33091.98720.03340.348-5.19214.861120.984
151.1492-0.6547-0.79030.98540.00920.84320.16140.3264-0.20.00910.0160.10270.0607-0.47290.45520.37310.0489-0.03390.2518-0.04970.3791-6.2896-33.0614-33.6506
161.15950.58490.1240.5210.83772.0780.04330.17990.2326-0.1065-0.10120.1995-0.6104-0.656-0.0370.39370.06940.00430.2616-0.02530.4207-12.9967-28.9168-27.9955
173.3769-0.67340.11333.1206-0.07232.9158-0.4246-0.0350.14571.07360.06910.3729-0.2964-0.77390.35720.60160.02130.1220.73920.04460.587-25.0203-40.6343-17.3157
182.3451-0.69690.11333.0761-1.01711.73130.0213-0.0968-1.0277-0.17330.30050.83810.5379-0.3267-0.47790.6488-0.09710.00120.6043-0.04320.7901-20.9747-52.1098-25.4067
192.44340.76050.06713.5506-1.05812.9638-0.2562-0.3123-0.1147-0.34750.02510.20950.4251-0.95340.22120.4581-0.0898-0.00820.5332-0.08810.4896-15.924-45.7478-28.8878
201.30750.75510.13233.2259-0.53583.4918-0.3178-0.2415-0.3822-0.35620.1375-0.59120.2871-0.30170.21860.3720.04120.1050.36130.00320.5064-9.1266-38.9706-33.891
212.4936-0.608-0.99561.5012-0.24782.8459-0.2066-0.27140.02480.1360.1068-0.1186-0.09940.78380.17860.3573-0.0094-0.00040.48640.02590.35173.1448-29.7447-26.4921
222.4188-0.3767-0.38572.84420.24965.8278-0.4194-0.7227-0.13090.1409-0.11580.07260.59631.42990.66750.34290.11840.06260.57430.10820.41577.7652-37.8845-24.0126
232.17890.3568-0.07141.87021.17572.8899-0.0640.0340.27860.0722-0.1660.0447-0.55690.18470.25320.4736-0.0191-0.00560.43410.01010.34540.3396-24.3939-33.9268
241.80830.0151-0.07274.0989-1.02824.7299-0.1435-0.39990.2380.32870.3427-0.2371-0.85940.1368-0.18890.3899-0.02830.01610.9446-0.1430.4188-11.8392-29.31291.5176
252.92631.32050.73911.75890.71433.69230.0727-0.6704-0.3491-0.035-0.0858-0.2710.15590.13160.02630.26050.090.04270.50830.01890.3547-11.2891-36.9905-8.3007
262.390.1508-0.03331.66470.19351.72870.0628-0.9764-0.32910.22580.1769-0.025-0.1660.3251-0.23740.29230.0801-0.0030.60930.05760.355-11.6731-35.7547-1.5999
274.8451.02612.80791.16950.38452.80010.19650.0787-0.59560.0228-0.0577-0.19540.03570.4061-0.02980.36890.04210.01130.5704-0.00880.3902-8.3491-36.7496-18.9245
281.5821-0.1683-0.60662.4425-2.15424.2451-0.2271-1.5923-0.00620.8097-0.8368-0.83920.0586-0.02540.41070.5136-0.1801-0.14791.05410.02490.4729-4.8996-32.66644.6438
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 533 through 566 )
2X-RAY DIFFRACTION2chain 'A' and (resid 567 through 594 )
3X-RAY DIFFRACTION3chain 'A' and (resid 595 through 621 )
4X-RAY DIFFRACTION4chain 'A' and (resid 622 through 640 )
5X-RAY DIFFRACTION5chain 'A' and (resid 641 through 713 )
6X-RAY DIFFRACTION6chain 'B' and (resid 0 through 6 )
7X-RAY DIFFRACTION7chain 'B' and (resid 7 through 15 )
8X-RAY DIFFRACTION8chain 'B' and (resid 16 through 22 )
9X-RAY DIFFRACTION9chain 'B' and (resid 23 through 32 )
10X-RAY DIFFRACTION10chain 'B' and (resid 33 through 39 )
11X-RAY DIFFRACTION11chain 'B' and (resid 40 through 53 )
12X-RAY DIFFRACTION12chain 'B' and (resid 54 through 70 )
13X-RAY DIFFRACTION13chain 'B' and (resid 71 through 81 )
14X-RAY DIFFRACTION14chain 'B' and (resid 82 through 90 )
15X-RAY DIFFRACTION15chain 'C' and (resid 533 through 543 )
16X-RAY DIFFRACTION16chain 'C' and (resid 544 through 566 )
17X-RAY DIFFRACTION17chain 'C' and (resid 567 through 579 )
18X-RAY DIFFRACTION18chain 'C' and (resid 580 through 594 )
19X-RAY DIFFRACTION19chain 'C' and (resid 595 through 621 )
20X-RAY DIFFRACTION20chain 'C' and (resid 622 through 640 )
21X-RAY DIFFRACTION21chain 'C' and (resid 641 through 666 )
22X-RAY DIFFRACTION22chain 'C' and (resid 667 through 687 )
23X-RAY DIFFRACTION23chain 'C' and (resid 688 through 713 )
24X-RAY DIFFRACTION24chain 'D' and (resid 0 through 16 )
25X-RAY DIFFRACTION25chain 'D' and (resid 17 through 45 )
26X-RAY DIFFRACTION26chain 'D' and (resid 46 through 70 )
27X-RAY DIFFRACTION27chain 'D' and (resid 71 through 81 )
28X-RAY DIFFRACTION28chain 'D' and (resid 82 through 90 )

+
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