5r8t - Revision history

OCA at 11:37, 21 February 2024

OCA — Wed, 21 Feb 2024 11:37:48 GMT

←Older revision		Revision as of 11:37, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='5r8t' size='340' side='right'caption='[[5r8t]], [[Resolution\|resolution]] 1.27Å' scene=''>		<StructureSection load='5r8t' size='340' side='right'caption='[[5r8t]], [[Resolution\|resolution]] 1.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5r8t]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Wcpv Wcpv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5R8T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5R8T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5r8t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5R8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5R8T FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.27Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~rep, 1a-1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=2697049 WCPV])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5r8t OCA], [~~http~~://pdbe.org/5r8t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5r8t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5r8t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5r8t ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5r8t OCA], [https://pdbe.org/5r8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5r8t RCSB], [https://www.ebi.ac.uk/pdbsum/5r8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5r8t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/R1AB_SARS2 R1AB_SARS2]] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.[UniProtKB:P0C6X7] Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.[UniProtKB:P0C6X7] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.[UniProtKB:P0C6X7] Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7]<ref>PMID:32198291</ref> Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7] Responsible for replication and transcription of the viral RNA genome.[UniProtKB:P0C6X7] Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[UniProtKB:P0C6X7] Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.[UniProtKB:P0C6X7] Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[UniProtKB:P0C6X7] Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[UniProtKB:P0C6X7]	+	[https://www.uniprot.org/uniprot/R1AB_SARS2 R1AB_SARS2] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.[UniProtKB:P0C6X7] Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.[UniProtKB:P0C6X7] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.[UniProtKB:P0C6X7] Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7]<ref>PMID:32198291</ref> Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7] Responsible for replication and transcription of the viral RNA genome.[UniProtKB:P0C6X7] Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[UniProtKB:P0C6X7] Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.[UniProtKB:P0C6X7] Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[UniProtKB:P0C6X7] Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[UniProtKB:P0C6X7]
		+
		+	==See Also==
		+	*[[Virus protease 3D structures\|Virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 15:		Line 18:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Wcpv~~]]	+	[[Category: Severe acute respiratory syndrome coronavirus 2]]
-	[[Category: Aimon, A]]	+	[[Category: Aimon A]]
-	[[Category: Brandao-Neto, J]]	+	[[Category: Brandao-Neto J]]
-	[[Category: Carbery, A]]	+	[[Category: Carbery A]]
-	~~[[Category: Delft, F von~~]]	+	[[Category: Douangamath A]]
-	[[Category: Douangamath, A]]	+	[[Category: Dunnett L]]
-	[[Category: Dunnett, L]]	+	[[Category: Fearon D]]
-	[[Category: Fearon, D]]	+	[[Category: Gehrtz P]]
-	[[Category: Gehrtz, P]]	+	[[Category: Krojer T]]
-	[[Category: Krojer, T]]	+	[[Category: London N]]
-	[[Category: London, N]]	+	[[Category: Lukacik P]]
-	[[Category: Lukacik, P]]	+	[[Category: Owen CD]]
-	[[Category: Owen~~, C D~~]]	+	[[Category: Powell AJ]]
-	[[Category: Powell~~, A J~~]]	+	[[Category: Resnick E]]
-	[[Category: Resnick, E]]	+	[[Category: Skyner R]]
-	[[Category: Skyner, R]]	+	[[Category: Snee M]]
-	[[Category: Snee, M]]	+	[[Category: Strain-Damerell CM]]
-	[[Category: Strain-Damerell~~, C M~~]]	+	[[Category: Walsh MA]]
-	[[Category: Walsh~~, M A~~]]	+	[[Category: Wild C]]
-	[[Category: Wild, C]]	+	[[Category: Von Delft F]]
-	[[Category: ~~Hydrolase]]~~	+
-	~~[[Category: Pandda]]~~	+
-	~~[[Category: Sgc - diamond i04-1 fragment screening]]~~	+
-	~~[[Category: Xchemexplorer~~]]	+

OCA at 06:12, 6 May 2020

OCA — Wed, 06 May 2020 06:12:02 GMT

←Older revision		Revision as of 06:12, 6 May 2020
Line 3:		Line 3:
	<StructureSection load='5r8t' size='340' side='right'caption='[[5r8t]], [[Resolution\|resolution]] 1.27Å' scene=''>		<StructureSection load='5r8t' size='340' side='right'caption='[[5r8t]], [[Resolution\|resolution]] 1.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5r8t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5R8T OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5R8T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5r8t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Wcpv Wcpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5R8T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5R8T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5r8t OCA], [http://pdbe.org/5r8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5r8t RCSB], [http://www.ebi.ac.uk/pdbsum/5r8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5r8t ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">rep, 1a-1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 WCPV])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5r8t OCA], [http://pdbe.org/5r8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5r8t RCSB], [http://www.ebi.ac.uk/pdbsum/5r8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5r8t ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/R1AB_SARS2 R1AB_SARS2]] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.[UniProtKB:P0C6X7] Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.[UniProtKB:P0C6X7] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.[UniProtKB:P0C6X7] Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7]<ref>PMID:32198291</ref> Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7] Responsible for replication and transcription of the viral RNA genome.[UniProtKB:P0C6X7] Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[UniProtKB:P0C6X7] Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.[UniProtKB:P0C6X7] Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[UniProtKB:P0C6X7] Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[UniProtKB:P0C6X7]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Wcpv]]
	[[Category: Aimon, A]]		[[Category: Aimon, A]]
	[[Category: Brandao-Neto, J]]		[[Category: Brandao-Neto, J]]

OCA at 09:04, 1 April 2020

OCA — Wed, 01 Apr 2020 09:04:32 GMT

←Older revision		Revision as of 09:04, 1 April 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5r8t is ~~ON HOLD~~	+	==PanDDA analysis group deposition of ground-state model of SARS-CoV-2 main protease screened against DSI poised (Enamine), Fraglites and Peplites (Newcastle university), Mini Frags (Astex), York 3D (York university), electrophile cysteine covalent (Weizman institute) fragment libraries==
-		+	<StructureSection load='5r8t' size='340' side='right'caption='[[5r8t]], [[Resolution\|resolution]] 1.27Å' scene=''>
-	~~Authors~~: ~~Fearon, D~~.~~, Powell, A~~.J.~~, Douangamath, A~~., ~~Owen, C~~.D.~~, Wild, C~~., ~~Krojer, T~~., ~~Lukacik, P~~., ~~Strain-Damerell, C~~.M., ~~Walsh, M~~.A., ~~von~~ Delft, F.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5r8t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5R8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5R8T FirstGlance]. <br>
-	~~Description~~: ~~PanDDA analysis group deposition of ground-state model (cluster 2) of COVID-19 main protease screened against the DSI poised fragment library~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5r8t OCA], [http://pdbe.org/5r8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5r8t RCSB], [http://www.ebi.ac.uk/pdbsum/5r8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5r8t ProSAT]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Aimon, A]]
		+	[[Category: Brandao-Neto, J]]
		+	[[Category: Carbery, A]]
		+	[[Category: Delft, F von]]
		+	[[Category: Douangamath, A]]
		+	[[Category: Dunnett, L]]
		+	[[Category: Fearon, D]]
		+	[[Category: Gehrtz, P]]
		+	[[Category: Krojer, T]]
		+	[[Category: London, N]]
	[[Category: Lukacik, P]]		[[Category: Lukacik, P]]
-	[[Category: ~~Strain-Damerell~~, C.M]]	+	[[Category: Owen, C D]]
-	[[Category: ~~Fearon~~, D]]	+	[[Category: Powell, A J]]
-	[[Category: ~~Walsh~~, M.A]]	+	[[Category: Resnick, E]]
-	[[Category: ~~Von Delft~~, F]]	+	[[Category: Skyner, R]]
		+	[[Category: Snee, M]]
		+	[[Category: Strain-Damerell, C M]]
		+	[[Category: Walsh, M A]]
	[[Category: Wild, C]]		[[Category: Wild, C]]
-	[[Category: ~~Powell, A.J~~]]	+	[[Category: Hydrolase]]
-	[[Category: ~~Douangamath, A~~]]	+	[[Category: Pandda]]
-	[[Category: ~~Krojer, T~~]]	+	[[Category: Sgc - diamond i04-1 fragment screening]]
-	[[Category: ~~Owen, C.D~~]]	+	[[Category: Xchemexplorer]]

OCA: Protected "5r8t" [edit=sysop:move=sysop]

OCA — Wed, 11 Mar 2020 05:50:02 GMT

Protected "5r8t" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:50, 11 March 2020

OCA: New page: '''Unreleased structure''' The entry 5r8t is ON HOLD Authors: Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A...

OCA — Wed, 11 Mar 2020 05:50:01 GMT

New page: '''Unreleased structure''' The entry 5r8t is ON HOLD Authors: Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A...

New page

'''Unreleased structure'''

The entry 5r8t is ON HOLD

Authors: Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.

Description: PanDDA analysis group deposition of ground-state model (cluster 2) of COVID-19 main protease screened against the DSI poised fragment library
[[Category: Unreleased Structures]]
[[Category: Lukacik, P]]
[[Category: Strain-Damerell, C.M]]
[[Category: Fearon, D]]
[[Category: Walsh, M.A]]
[[Category: Von Delft, F]]
[[Category: Wild, C]]
[[Category: Powell, A.J]]
[[Category: Douangamath, A]]
[[Category: Krojer, T]]
[[Category: Owen, C.D]]