7k0g - Revision history

OCA at 15:15, 18 October 2023

OCA — Wed, 18 Oct 2023 15:15:38 GMT

←Older revision		Revision as of 15:15, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='7k0g' size='340' side='right'caption='[[7k0g]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='7k0g' size='340' side='right'caption='[[7k0g]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7k0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Hcov~~-~~sars Hcov~~-~~sars~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7k0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K0G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1S:(1R,2S)-2-({N-[(benzyloxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic+acid'>B1S</scene>, <scene name='pdbligand=K36:(1S,2S)-2-({N-[(BENZYLOXY)CARBONYL]-L-LEUCYL}AMINO)-1-HYDROXY-3-[(3S)-2-OXOPYRROLIDIN-3-YL]PROPANE-1-SULFONIC+ACID'>K36</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]] 1.85Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=694009 HCoV-SARS])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1S:(1R,2S)-2-({N-[(benzyloxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic+acid'>B1S</scene>, <scene name='pdbligand=K36:(1S,2S)-2-({N-[(BENZYLOXY)CARBONYL]-L-LEUCYL}AMINO)-1-HYDROXY-3-[(3S)-2-OXOPYRROLIDIN-3-YL]PROPANE-1-SULFONIC+ACID'>K36</scene></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=7k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k0g OCA], [https://pdbe.org/7k0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k0g RCSB], [https://www.ebi.ac.uk/pdbsum/7k0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k0g 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=7k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k0g OCA], [https://pdbe.org/7k0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k0g RCSB], [https://www.ebi.ac.uk/pdbsum/7k0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k0g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~R1A_CVHSA R1A_CVHSA]~~] The ~~papain~~-~~like proteinase (PL~~-~~PRO~~) ~~is responsible~~ for the cleavages located at the N-terminus of 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host ~~IRF~~-3.<ref>PMID:~~17024178~~</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> ~~The main proteinase 3CL~~-~~PRO is responsible~~ for ~~the majority of cleavages as it cleaves~~ the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]~~. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity)~~. Also ~~contains~~ an ADP-ribose-1''-phosphate (ADRP)~~-binding function~~.<ref>PMID:~~17024178~~</ref> <ref>PMID:~~17692280~~</ref> <ref>PMID:~~19369340~~</ref> ~~Nsp7-nsp8~~ hexadecamer may ~~possibly confer processivity to the polymerase, maybe~~ by ~~binding to dsRNA or by producing~~ primers ~~utilized by the latter~~.<ref>PMID:~~17024178~~</ref> <ref>PMID:~~17692280</ref> <ref>PMID:19369340~~</ref> ~~Nsp9 is~~ a ssRNA-binding protein.<ref>PMID:~~17024178~~</ref> <ref>PMID:~~17692280~~</ref> ~~<ref>PMID:19369340</ref>~~	+	[https://www.uniprot.org/uniprot/R1A_SARS R1A_SARS] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. 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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371).<ref>PMID:23035226</ref> <ref>PMID:30943371</ref> 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.<ref>PMID:19640993</ref> 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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling.<ref>PMID:16271890</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> <ref>PMID:24622840</ref> <ref>PMID:24410069</ref> Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form DMV.<ref>PMID:23943763</ref> <ref>PMID:24410069</ref> Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH.[PROSITE-ProRule:PRU00772]<ref>PMID:16226257</ref> Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). 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 (PubMed:24991833).<ref>PMID:24991833</ref> <ref>PMID:24410069</ref> 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.<ref>PMID:22039154</ref> 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.<ref>PMID:22039154</ref> May participate in viral replication by acting as a ssRNA-binding protein.<ref>PMID:19153232</ref> 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.<ref>PMID:22635272</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 7k0g" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 7k0g" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Virus protease 3D structures\|Virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Hcov-sars]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Battaile~~, K P~~]]	+	[[Category: Severe acute respiratory syndrome-related coronavirus]]
-	[[Category: Chamandi~~, S D~~]]	+	[[Category: Battaile KP]]
-	[[Category: Chang~~, K O~~]]	+	[[Category: Chamandi SD]]
-	[[Category: Groutas~~, W C~~]]	+	[[Category: Chang KO]]
-	[[Category: Kashipathy~~, M M~~]]	+	[[Category: Groutas WC]]
-	[[Category: Kim, Y]]	+	[[Category: Kashipathy MM]]
-	[[Category: Lovell, S]]	+	[[Category: Kim Y]]
-	[[Category: Nguyen~~, H N]]~~	+	[[Category: Lovell S]]
-	~~[[Category: Deuterated hydrolase inhibitor]]~~	+	[[Category: Nguyen HN]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Sars 3cl protease inhhibitor]]~~	+
-	~~[[Category: Severe acute respiratory syndrome coronavirus~~]]	+

OCA at 10:09, 14 July 2021

OCA — Wed, 14 Jul 2021 10:09:06 GMT

←Older revision		Revision as of 10:09, 14 July 2021
Line 1:		Line 1:

	==1.85 A resolution structure of SARS-CoV 3CL protease in complex with deuterated GC376==		==1.85 A resolution structure of SARS-CoV 3CL protease in complex with deuterated GC376==
-	<StructureSection load='7k0g' size='340' side='right'caption='[[7k0g]]' scene=''>	+	<StructureSection load='7k0g' size='340' side='right'caption='[[7k0g]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7k0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hcov-sars Hcov-sars]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K0G FirstGlance]. <br>
-	</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=7k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k0g OCA], [https://pdbe.org/7k0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k0g RCSB], [https://www.ebi.ac.uk/pdbsum/7k0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k0g ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1S:(1R,2S)-2-({N-[(benzyloxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic+acid'>B1S</scene>, <scene name='pdbligand=K36:(1S,2S)-2-({N-[(BENZYLOXY)CARBONYL]-L-LEUCYL}AMINO)-1-HYDROXY-3-[(3S)-2-OXOPYRROLIDIN-3-YL]PROPANE-1-SULFONIC+ACID'>K36</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=694009 HCoV-SARS])</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=7k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k0g OCA], [https://pdbe.org/7k0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k0g RCSB], [https://www.ebi.ac.uk/pdbsum/7k0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k0g ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/R1A_CVHSA R1A_CVHSA]] The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity). Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> Nsp9 is a ssRNA-binding protein.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection continues to be a serious global public health threat. The 3C-like protease (3CLpro) is a virus protease encoded by SARS-CoV-2, which is essential for virus replication. We have previously reported a series of small-molecule 3CLpro inhibitors effective for inhibiting replication of human coronaviruses including SARS-CoV-2 in cell culture and in animal models. Here we generated a series of deuterated variants of a 3CLpro inhibitor, GC376, and evaluated the antiviral effect against SARS-CoV-2. The deuterated GC376 displayed potent inhibitory activity against SARS-CoV-2 in the enzyme- and the cell-based assays. The K18-hACE2 mice develop mild to lethal infection commensurate with SARS-CoV-2 challenge doses and were proposed as a model for efficacy testing of antiviral agents. We treated lethally infected mice with a deuterated derivative of GC376. Treatment of K18-hACE2 mice at 24 h postinfection with a derivative (compound 2) resulted in increased survival of mice compared to vehicle-treated mice. Lung virus titers were decreased, and histopathological changes were ameliorated in compound 2-treated mice compared to vehicle-treated mice. Structural investigation using high-resolution crystallography illuminated binding interactions of 3CLpro of SARS-CoV-2 and SARS-CoV with deuterated variants of GC376. Taken together, deuterated GC376 variants have excellent potential as antiviral agents against SARS-CoV-2.
		+
		+	Postinfection treatment with a protease inhibitor increases survival of mice with a fatal SARS-CoV-2 infection.,Dampalla CS, Zheng J, Perera KD, Wong LR, Meyerholz DK, Nguyen HN, Kashipathy MM, Battaile KP, Lovell S, Kim Y, Perlman S, Groutas WC, Chang KO Proc Natl Acad Sci U S A. 2021 Jul 20;118(29). pii: 2101555118. doi:, 10.1073/pnas.2101555118. PMID:34210738<ref>PMID:34210738</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7k0g" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Hcov-sars]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Battaile KP]]	+	[[Category: Battaile, K P]]
-	[[Category: Chamandi SD]]	+	[[Category: Chamandi, S D]]
-	[[Category: Chang KO]]	+	[[Category: Chang, K O]]
-	[[Category: Groutas WC]]	+	[[Category: Groutas, W C]]
-	[[Category: Kashipathy MM]]	+	[[Category: Kashipathy, M M]]
-	[[Category: Kim Y]]	+	[[Category: Kim, Y]]
-	[[Category: Lovell S]]	+	[[Category: Lovell, S]]
-	[[Category: Nguyen HN]]	+	[[Category: Nguyen, H N]]
		+	[[Category: Deuterated hydrolase inhibitor]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Protease]]
		+	[[Category: Sars 3cl protease inhhibitor]]
		+	[[Category: Severe acute respiratory syndrome coronavirus]]

OCA at 09:57, 7 July 2021

OCA — Wed, 07 Jul 2021 09:57:05 GMT

←Older revision		Revision as of 09:57, 7 July 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7k0g ~~is ON HOLD until Paper Publication~~	+	==1.85 A resolution structure of SARS-CoV 3CL protease in complex with deuterated GC376==
-		+	<StructureSection load='7k0g' size='340' side='right'caption='[[7k0g]]' scene=''>
-	~~Authors~~: ~~Lovell, S~~.~~, Kashipathy, M~~.M.~~, Battaile, K~~.P.~~, Chamandi, S~~.D.~~, Nguyen, H~~.N., ~~Kim, Y~~., ~~Chang~~, K.O., ~~Groutas, W~~.C.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K0G FirstGlance]. <br>
-	~~Description~~: 1.~~85 A resolution structure of SARS~~-~~CoV 3CL protease in complex with deuterated GC376~~	+	</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=7k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k0g OCA], [https://pdbe.org/7k0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k0g RCSB], [https://www.ebi.ac.uk/pdbsum/7k0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k0g ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Nguyen, H.N~~]]	+	__TOC__
-	[[Category: ~~Kashipathy, M.M~~]]	+	</StructureSection>
-	[[Category: ~~Battaile, K.P~~]]	+	[[Category: Large Structures]]
-	[[Category: Groutas~~, W.C~~]]	+	[[Category: Battaile KP]]
-	[[Category: ~~Chang, K.O~~]]	+	[[Category: Chamandi SD]]
-	[[Category: Kim, Y]]	+	[[Category: Chang KO]]
-	[[Category: ~~Chamandi,~~ S.D]]	+	[[Category: Groutas WC]]
-	[[Category: ~~Lovell, S~~]]	+	[[Category: Kashipathy MM]]
		+	[[Category: Kim Y]]
		+	[[Category: Lovell S]]
		+	[[Category: Nguyen HN]]

OCA at 05:28, 25 November 2020

OCA — Wed, 25 Nov 2020 05:28:35 GMT

←Older revision		Revision as of 05:28, 25 November 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7k0g is ON HOLD	+	The entry 7k0g is ON HOLD until Paper Publication

	Authors: Lovell, S., Kashipathy, M.M., Battaile, K.P., Chamandi, S.D., Nguyen, H.N., Kim, Y., Chang, K.O., Groutas, W.C.		Authors: Lovell, S., Kashipathy, M.M., Battaile, K.P., Chamandi, S.D., Nguyen, H.N., Kim, Y., Chang, K.O., Groutas, W.C.
Line 7:		Line 7:
	Description: 1.85 A resolution structure of SARS-CoV 3CL protease in complex with deuterated GC376		Description: 1.85 A resolution structure of SARS-CoV 3CL protease in complex with deuterated GC376
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Groutas~~, W.C]]	+	[[Category: Nguyen, H.N]]
		+	[[Category: Kashipathy, M.M]]
	[[Category: Battaile, K.P]]		[[Category: Battaile, K.P]]
-	[[Category: ~~Chamandi~~, S.D]]	+	[[Category: Groutas, W.C]]
	[[Category: Chang, K.O]]		[[Category: Chang, K.O]]
-	[[Category: Kashipathy, M.M]]
	[[Category: Kim, Y]]		[[Category: Kim, Y]]
		+	[[Category: Chamandi, S.D]]
	[[Category: Lovell, S]]		[[Category: Lovell, S]]
-	[[Category: Nguyen, H.N]]

OCA: Protected "7k0g" [edit=sysop:move=sysop]

OCA — Wed, 16 Sep 2020 07:03:26 GMT

Protected "7k0g" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:03, 16 September 2020

OCA: New page: '''Unreleased structure''' The entry 7k0g is ON HOLD Authors: Lovell, S., Kashipathy, M.M., Battaile, K.P., Chamandi, S.D., Nguyen, H.N., Kim, Y., Chang, K.O., Groutas, W.C. Descriptio...

OCA — Wed, 16 Sep 2020 07:03:25 GMT

New page: '''Unreleased structure''' The entry 7k0g is ON HOLD Authors: Lovell, S., Kashipathy, M.M., Battaile, K.P., Chamandi, S.D., Nguyen, H.N., Kim, Y., Chang, K.O., Groutas, W.C. Descriptio...

New page

'''Unreleased structure'''

The entry 7k0g is ON HOLD

Authors: Lovell, S., Kashipathy, M.M., Battaile, K.P., Chamandi, S.D., Nguyen, H.N., Kim, Y., Chang, K.O., Groutas, W.C.

Description: 1.85 A resolution structure of SARS-CoV 3CL protease in complex with deuterated GC376
[[Category: Unreleased Structures]]
[[Category: Groutas, W.C]]
[[Category: Battaile, K.P]]
[[Category: Chamandi, S.D]]
[[Category: Chang, K.O]]
[[Category: Kashipathy, M.M]]
[[Category: Kim, Y]]
[[Category: Lovell, S]]
[[Category: Nguyen, H.N]]