[English] 日本語
Yorodumi
- EMDB-25581: cryoEM reconstruction of the HIV gp140 in complex with the extrac... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-25581
TitlecryoEM reconstruction of the HIV gp140 in complex with the extracellular domains of CD4 and the adnectin domain of Combinectin. The gp140 and CD4 coordinates from entry 6EDU were rigid body fitted to the EM map along withe the crystal structure of CD4+adnectin
Map data
Sample
  • Complex: Ternary complex of the HIV-1 gp140 trimer in complex with the extracellular domains (domains 1-4) of CD4 and an adnectin domain of Combinectin
    • Protein or peptide: BG505 SOSIP.664 gp140
    • Protein or peptide: BG505 SOSIP.664 gp140
    • Protein or peptide: BG505 SOSIP.664 gp140
    • Protein or peptide: T-cell surface glycoprotein CD4
    • Protein or peptide: AdnectinMonobody
    • Protein or peptide: BG505 SOSIP.664 gp140
Function / homology
Function and homology information


helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / maintenance of protein location in cell / T cell selection / MHC class II protein binding / cellular response to granulocyte macrophage colony-stimulating factor stimulus / interleukin-15-mediated signaling pathway / positive regulation of monocyte differentiation / Nef Mediated CD4 Down-regulation ...helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / maintenance of protein location in cell / T cell selection / MHC class II protein binding / cellular response to granulocyte macrophage colony-stimulating factor stimulus / interleukin-15-mediated signaling pathway / positive regulation of monocyte differentiation / Nef Mediated CD4 Down-regulation / Alpha-defensins / positive regulation of kinase activity / regulation of T cell activation / T cell receptor complex / extracellular matrix structural constituent / Other interleukin signaling / enzyme-linked receptor protein signaling pathway / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / regulation of calcium ion transport / macrophage differentiation / Generation of second messenger molecules / T cell differentiation / PD-1 signaling / positive regulation of protein kinase activity / Binding and entry of HIV virion / coreceptor activity / positive regulation of calcium-mediated signaling / protein tyrosine kinase binding / positive regulation of interleukin-2 production / T cell activation / Vpu mediated degradation of CD4 / calcium-mediated signaling / clathrin-coated endocytic vesicle membrane / cell surface receptor protein tyrosine kinase signaling pathway / positive regulation of T cell activation / positive regulation of peptidyl-tyrosine phosphorylation / transmembrane signaling receptor activity / Cargo recognition for clathrin-mediated endocytosis / Downstream TCR signaling / virus receptor activity / MHC class II protein complex binding / Clathrin-mediated endocytosis / signaling receptor activity / positive regulation of canonical NF-kappaB signal transduction / defense response to Gram-negative bacterium / adaptive immune response / positive regulation of MAPK cascade / positive regulation of viral entry into host cell / cell surface receptor signaling pathway / positive regulation of ERK1 and ERK2 cascade / early endosome / cell adhesion / immune response / positive regulation of protein phosphorylation / membrane raft / external side of plasma membrane / endoplasmic reticulum lumen / lipid binding / endoplasmic reticulum membrane / protein kinase binding / positive regulation of DNA-templated transcription / enzyme binding / signal transduction / protein homodimerization activity / zinc ion binding / identical protein binding / plasma membrane
Similarity search - Function
CD4, extracellular / T cell CD4 receptor C-terminal region / CD4, extracellular / T cell CD4 receptor C terminal region / T-cell surface antigen CD4 / Immunoglobulin C2-set / Immunoglobulin C2-set domain / Immunoglobulin / Immunoglobulin domain / Immunoglobulin subtype 2 ...CD4, extracellular / T cell CD4 receptor C-terminal region / CD4, extracellular / T cell CD4 receptor C terminal region / T-cell surface antigen CD4 / Immunoglobulin C2-set / Immunoglobulin C2-set domain / Immunoglobulin / Immunoglobulin domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
T-cell surface glycoprotein CD4
Similarity search - Component
Biological speciesHIV-1 06TG.HT008 (virus) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.7 Å
AuthorsConcha NO / William SP / Wenzel DL
Funding support United States, 1 items
OrganizationGrant numberCountry
Other private United States
CitationJournal: J Mol Biol / Year: 2022
Title: Novel Bent Conformation of CD4 Induced by HIV-1 Inhibitor Indirectly Prevents Productive Viral Attachment.
Authors: David Wensel / Shawn Williams / David P Dixon / Paris Ward / Patti McCormick / Nestor Concha / Eugene Stewart / Xuan Hong / Charles Mazzucco / Shreya Pal / Bo Ding / Christoph Fellinger / Mark Krystal /
Abstract: GSK3732394 is a multi-specific biologic inhibitor of HIV entry currently under clinical evaluation. A key component of this molecule is an adnectin (6940_B01) that binds to CD4 and inhibits ...GSK3732394 is a multi-specific biologic inhibitor of HIV entry currently under clinical evaluation. A key component of this molecule is an adnectin (6940_B01) that binds to CD4 and inhibits downstream actions of gp160. Studies were performed to determine the binding site of the adnectin on CD4 and to understand the mechanism of inhibition. Using hydrogen-deuterium exchange with mass spectrometry (HDX), CD4 peptides showed differential rates of deuteration (either enhanced or slowed) in the presence of the adnectin that mapped predominantly to the interface of domains 2 and 3 (D2-D3). In addition, an X-ray crystal structure of an ibalizumab Fab/CD4(D1-D4)/adnectin complex revealed an extensive interface between the adnectin and residues on CD4 domains D2-D4 that stabilize a novel T-shaped CD4 conformation. A cryo-EM map of the gp140/CD4/GSK3732394 complex clearly shows the bent conformation for CD4 while bound to gp140. Mutagenic analyses on CD4 confirmed that amino acid F202 forms a key interaction with the adnectin. In addition, amino acid L151 was shown to be a critical indirect determinant of the specificity for binding to the human CD4 protein over related primate CD4 molecules, as it appears to modulate CD4's flexibility to adopt the adnectin-bound conformation. The significant conformational change of CD4 upon adnectin binding brings the D1 domain of CD4 in proximity to the host cell membrane surface, thereby re-orienting the gp120 binding site in a direction that is inaccessible to incoming virus due to a steric clash between gp160 trimers on the virus surface and the target cell membrane.
History
DepositionNov 30, 2021-
Header (metadata) releaseJan 12, 2022-
Map releaseJan 12, 2022-
UpdateJan 12, 2022-
Current statusJan 12, 2022Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 4.42
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 4.42
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7t0o
  • Surface level: 4.42
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_25581.png

Downloads & links

-
Map

FileDownload / File: emd_25581.map.gz / Format: CCP4 / Size: 1.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 2.4624 Å
Density
Contour LevelBy EMDB: 4.42 / Movie #1: 4.42
Minimum - Maximum-5.1388183 - 28.004534
Average (Standard dev.)0.624528 (±2.529406)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin384125
Dimensions935099
Spacing999350
CellA: 243.7776 Å / B: 229.00319 Å / C: 123.119995 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.4624040404042.46239784946242.4624
M x/y/z999350
origin x/y/z0.0000.0000.000
length x/y/z243.778229.003123.120
α/β/γ90.00090.00090.000
start NX/NY/NZ253841
NX/NY/NZ999350
MAP C/R/S321
start NC/NR/NS413825
NC/NR/NS509399
D min/max/mean-5.13928.0050.625

-
Supplemental data

-
Mask #1

Fileemd_25581_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : Ternary complex of the HIV-1 gp140 trimer in complex with the ext...

EntireName: Ternary complex of the HIV-1 gp140 trimer in complex with the extracellular domains (domains 1-4) of CD4 and an adnectin domain of Combinectin
Components
  • Complex: Ternary complex of the HIV-1 gp140 trimer in complex with the extracellular domains (domains 1-4) of CD4 and an adnectin domain of Combinectin
    • Protein or peptide: BG505 SOSIP.664 gp140
    • Protein or peptide: BG505 SOSIP.664 gp140
    • Protein or peptide: BG505 SOSIP.664 gp140
    • Protein or peptide: T-cell surface glycoprotein CD4
    • Protein or peptide: AdnectinMonobody
    • Protein or peptide: BG505 SOSIP.664 gp140

-
Supramolecule #1: Ternary complex of the HIV-1 gp140 trimer in complex with the ext...

SupramoleculeName: Ternary complex of the HIV-1 gp140 trimer in complex with the extracellular domains (domains 1-4) of CD4 and an adnectin domain of Combinectin
type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all
Details: the gp140 trimer at 0.67 mg/ml was mixed with soluble CD4 first, and then with Combinection in a 1.25:1 ratio. The sample was incubated overnight at 4 degC. The sample was concentrated to ...Details: the gp140 trimer at 0.67 mg/ml was mixed with soluble CD4 first, and then with Combinection in a 1.25:1 ratio. The sample was incubated overnight at 4 degC. The sample was concentrated to 35ul before injecting into a Phenomenex 4.6 x 300 mm 3um bead 500Angstroms pore Yara SEC column equilibrated with 20mM Hepes pH7.5, 200 mM KCl, 5mM MgCl2. The complexes were eluted with a flow rate of 0.2 ml/min and fractions collected every 20 seconds into a Thermo-Fisher UV transparent 96-well plates. The absorbance at 280nm was measured for each fraction using a Spectramax plate scanner. The high-molecular weight complex appeared to be comprised of gp140:CD4:Combinectin in a 1:1:1 ratio. The sample used for cryo-EM studies was the single peak fraction of gp140/CD4/Combinectin (0.076 mg/ml)

-
Macromolecule #1: BG505 SOSIP.664 gp140

MacromoleculeName: BG505 SOSIP.664 gp140 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: HIV-1 06TG.HT008 (virus)
Molecular weightTheoretical: 72.830398 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: AENLWVTVYY GVPVWKDAET TLFCASDAKA YETEKHNVWA THACVPTDPN PQEIHLENVT EEFNMWKNNM VEQMHTDIIS LWDQSLKPC VKLTPLCVTL NCTNVTNNIT DDMRGELKNC SFNMTTELRD KKQKVYSLFY RLDVVQINEN QGNRSNNSNK E YRLINCNT ...String:
AENLWVTVYY GVPVWKDAET TLFCASDAKA YETEKHNVWA THACVPTDPN PQEIHLENVT EEFNMWKNNM VEQMHTDIIS LWDQSLKPC VKLTPLCVTL NCTNVTNNIT DDMRGELKNC SFNMTTELRD KKQKVYSLFY RLDVVQINEN QGNRSNNSNK E YRLINCNT SAITQACPKV SFEPIPIHYC APAGFAILKC KDKKFNGTGP CPSVSTVQCT HGIKPVVSTQ LLLNGSLAEE EV MIRSENI TNNAKNILVQ FNTPVQINCT RPNNNTRKSI RIGPGQAFYA TGDIIGDIRQ AHCNVSKATW NETLGKVVKQ LRK HFGNNT IIRFANSSGG DLEVTTHSFN CGGEFFYCNT SGLFNSTWIS NTSVQGSNST GSNDSITLPC RIKQIINMWQ RIGQ AMYAP PIQGVIRCVS NITGLILTRD GGSTNSTTET FRPGGGDMRD NWRSELYKYK VVKIEPLGVA PTRCKRRVVG RRRRR RAVG IGAVFLGFLG AAGSTMGAAS MTLTVQARNL LSGIVQQQSN LLRAPEAQQH LLKLTVWGIK QLQARVLAVE RYLRDQ QLL GIWGCSGKLI CCTNVPWNSS WSNRNLSEIW DNMTWLQWDK EISNYTQIIY GLLEESQNQQ EKNEQDLLAL DGSGSGG SG HHHHHHHH

-
Macromolecule #2: BG505 SOSIP.664 gp140

MacromoleculeName: BG505 SOSIP.664 gp140 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: HIV-1 06TG.HT008 (virus)
Molecular weightTheoretical: 3.337105 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)

-
Macromolecule #3: BG505 SOSIP.664 gp140

MacromoleculeName: BG505 SOSIP.664 gp140 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: HIV-1 06TG.HT008 (virus)
Molecular weightTheoretical: 3.252 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

-
Macromolecule #4: T-cell surface glycoprotein CD4

MacromoleculeName: T-cell surface glycoprotein CD4 / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.385449 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: KKVVLGKKGD TVELTCTASQ KKSIQFHWKN SNQIKILGNQ GSFLTKGPSK LNDRADSRRS LWDQGNFPLI IKNLKIEDSD TYICEVEDQ KEEVQLLVFG LTANSDTHLL QGQSLTLTLE SPPGSSPSVQ CRSPRGKNIQ GGKTLSVSQL ELQDSGTWTC T VLQNQKKV ...String:
KKVVLGKKGD TVELTCTASQ KKSIQFHWKN SNQIKILGNQ GSFLTKGPSK LNDRADSRRS LWDQGNFPLI IKNLKIEDSD TYICEVEDQ KEEVQLLVFG LTANSDTHLL QGQSLTLTLE SPPGSSPSVQ CRSPRGKNIQ GGKTLSVSQL ELQDSGTWTC T VLQNQKKV EFKIDIVVLA FQKASSIVYK KEGEQVEFSF PLAFTVEKLT GSGELWWQAE RASSSKSWIT FDLKNKEVSV KR VTQDPKL QMGKKLPLHL TLPQALPQYA GSGNLTLALE AKTGKLHQEV NLVVMRATQL QKNLTCEVWG PTSPKLMLSL KLE NKEAKV SKREKAVWVL NPEAGMWQCL LSDSGQVLLE SNIKVLPTHH HHHH

-
Macromolecule #5: Adnectin

MacromoleculeName: Adnectin / type: protein_or_peptide / ID: 5
Details: The native 10th fibronectin type III (10Fn3) domain from human fibronectin was used as the template for construction of novel libraries of Adnectin variants (Wenzel, D., et al. (2017) ...Details: The native 10th fibronectin type III (10Fn3) domain from human fibronectin was used as the template for construction of novel libraries of Adnectin variants (Wenzel, D., et al. (2017) Antimicrobial Agents and Chemotherapy, Vol 61(8), e00508-17, pp 1-19)
Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.959172 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GVSDVPRDLE VVAATPTSLL ISWDAPAVTV HSYHIQYWPL GSYQRYQVFS VPGSKSTATI SGLKPGVEYQ IRVYAETGGA DSDQSMGWI QIGYRTEGDK PSQHHHHHH

-
Macromolecule #6: BG505 SOSIP.664 gp140

MacromoleculeName: BG505 SOSIP.664 gp140 / type: protein_or_peptide / ID: 6 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: HIV-1 06TG.HT008 (virus)
Molecular weightTheoretical: 2.996685 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.08 mg/mL
BufferpH: 7.5
Component:
ConcentrationName
20.0 mMHEPES
200.0 mMKCl
5.0 mMMgCl
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 30.0 kPa
Details: glow discharged for 20 sec using a EasyGlo (20mA, 0.3 mBar)
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Detailsthe gp140/CD4/Combinectin (0.076 mg/ml), 3.5uL were applied to Quantifoil 1.2/1.3 Cu 400 mesh grids that had previously been glow discharged for 20 sec using a EasyGlo (20mA, 0.3 mBar). The grids were plunged into liquid ethane using a Vitrobot plunger (chamber set to 4 degC and 80% RH) immediately after blotting from 2.5 to 4 sec

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.4 µm / Nominal defocus min: 1.4000000000000001 µm
Specialist opticsPhase plate: OTHER / Spherical aberration corrector: Cs corrector
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Digitization - Sampling interval: 11.0 µm / Number real images: 1078 / Average exposure time: 75.7 sec. / Average electron dose: 1.022 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

CTF correctionSoftware - Name: CTFFIND
Startup modelType of model: OTHER / Details: initial model generated with cisTEM
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final 3D classificationNumber classes: 4 / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final reconstructionNumber classes used: 3 / Applied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 8.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 208485
FSC plot (resolution estimation)

-
Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT
Output model

PDB-7t0o:
cryoEM reconstruction of the HIV gp140 in complex with the extracellular domains of CD4 and the adnectin domain of Combinectin. The gp140 and CD4 coordinates from entry 6EDU were rigid body fitted to the EM map along withe the crystal structure of CD4+adnectin

+
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