7nuk - Revision history

OCA at 12:40, 1 February 2024

OCA — Thu, 01 Feb 2024 12:40:09 GMT

←Older revision		Revision as of 12:40, 1 February 2024
Line 3:		Line 3:
	<StructureSection load='7nuk' size='340' side='right'caption='[[7nuk]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='7nuk' size='340' side='right'caption='[[7nuk]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7nuk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~2019-ncov 2019-ncov~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NUK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7nuk]] is a 2 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=7NUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NUK 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>~~, ~~<scene name='pdbligand=USH:2-~~[~~2-chloranylethanoyl(propyl)amino~~]~~-~{N}-(~~2~~-methoxyphenyl)ethanamide'>USH</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]] 2.19Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ORF1ab ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~2697049 2019-nCoV])</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>, <scene name='pdbligand=USH:2-[2-chloranylethanoyl(propyl)amino]-~{N}-(2-methoxyphenyl)ethanamide'>USH</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/SARS_coronavirus_main_proteinase SARS coronavirus main proteinase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=3.4.22.69 3.4.22.69~~] </~~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=7nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nuk OCA], [https://pdbe.org/7nuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nuk RCSB], [https://www.ebi.ac.uk/pdbsum/7nuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nuk 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=7nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nuk OCA], [https://pdbe.org/7nuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nuk RCSB], [https://www.ebi.ac.uk/pdbsum/7nuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nuk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~R1A_SARS2 R1A_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]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7] 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]	+	[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]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: 2019-ncov]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~SARS~~ coronavirus ~~main proteinase~~]]	+	[[Category: Severe acute respiratory syndrome coronavirus 2]]
-	[[Category: Domling, A]]	+	[[Category: Domling A]]
-	[[Category: Eris, D]]	+	[[Category: Eris D]]
-	[[Category: Groves~~, M R~~]]	+	[[Category: Groves MR]]
-	[[Category: Oerlemans, R]]	+	[[Category: Oerlemans R]]
-	[[Category: Sharpe, M]]	+	[[Category: Sharpe M]]
-	[[Category: Wang, M]]	+	[[Category: Wang M]]
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 09:17, 21 July 2021

OCA — Wed, 21 Jul 2021 09:17:43 GMT

←Older revision		Revision as of 09:17, 21 July 2021
Line 1:		Line 1:

	==Crystal structure of SARS CoV2 main protease in complex with EG009 (modelled using PanDDA event map)==		==Crystal structure of SARS CoV2 main protease in complex with EG009 (modelled using PanDDA event map)==
-	<StructureSection load='7nuk' size='340' side='right'caption='[[7nuk]]' scene=''>	+	<StructureSection load='7nuk' size='340' side='right'caption='[[7nuk]], [[Resolution\|resolution]] 2.19Å' 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=7NUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NUK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7nuk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NUK 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=7nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nuk OCA], [https://pdbe.org/7nuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nuk RCSB], [https://www.ebi.ac.uk/pdbsum/7nuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nuk 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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=USH:2-[2-chloranylethanoyl(propyl)amino]-~{N}-(2-methoxyphenyl)ethanamide'>USH</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ORF1ab ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/SARS_coronavirus_main_proteinase SARS coronavirus main proteinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.69 3.4.22.69] </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=7nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nuk OCA], [https://pdbe.org/7nuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nuk RCSB], [https://www.ebi.ac.uk/pdbsum/7nuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nuk ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/R1A_SARS2 R1A_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]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7] 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]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein-ligand crystallography is widely used to drive advanced stages of drug optimization or to generate starting points for medicinal chemistry by fragment soaking. However, recent progress in protein crystallography could allow for a more integrated role of protein crystallography into the early drug discovery cycle. Here we demonstrate for the first time the interplay of high throughput synthesis and high throughput crystallography. For this we describe a practical multicomponent reaction approach to high diversity acrylamides and esters from diverse building blocks. Surprisingly, in the majority of acrylamides precipitation during the reaction was observed, making library synthesis on a mmol scale and a 96-well format particularly comfortable. The synthesis is also suitable for a high throughput nanoscale format in a highly automated fashion. Moreover, we exemplified the synthesis on a multigram scale featuring good yield and simple work-up. High throughput crystallography of our libraires yielded potent covalent inhibitors of the main protease of the COVID-19 causing agent SARS-CoV-2 in a time efficient manner. Our results demonstrate, that the marriage of in situ HT synthesis of (covalent) libraires and HT crystallography has the potential to accelerate hit finding and to provide meaningful strategies for medicinal chemistry projects.
		+
		+	Marriage of high throughput synthesis and high throughput protein crystallography.,Doemling A, Sutanto F, Shaabani S, Oerlemans R, Deniz E, Patil P, Hadian M, Wang M, Sharpe ME, Groves MR Angew Chem Int Ed Engl. 2021 Jun 7. doi: 10.1002/anie.202105584. PMID:34097796<ref>PMID:34097796</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7nuk" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: 2019-ncov]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Domling A]]	+	[[Category: SARS coronavirus main proteinase]]
-	[[Category: Eris D]]	+	[[Category: Domling, A]]
-	[[Category: Groves MR]]	+	[[Category: Eris, D]]
-	[[Category: Oerlemans R]]	+	[[Category: Groves, M R]]
-	[[Category: Sharpe M]]	+	[[Category: Oerlemans, R]]
-	[[Category: Wang M]]	+	[[Category: Sharpe, M]]
		+	[[Category: Wang, M]]
		+	[[Category: Complex]]
		+	[[Category: Protease]]
		+	[[Category: Viral protein]]

OCA at 14:48, 17 June 2021

OCA — Thu, 17 Jun 2021 14:48:22 GMT

←Older revision		Revision as of 14:48, 17 June 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 7nuk is ON HOLD until Paper Publication~~	+	==Crystal structure of SARS CoV2 main protease in complex with EG009 (modelled using PanDDA event map)==
-		+	<StructureSection load='7nuk' size='340' side='right'caption='[[7nuk]]' scene=''>
-	~~Authors: Oerlemans, R., Eris, D., Wang, M., Sharpe, M., Domling, A., Groves, M.R.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NUK FirstGlance]. <br>
-	~~Description:~~ Crystal structure of SARS CoV2 main protease in complex with EG009 (modelled using PanDDA event map)	+	</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=7nuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nuk OCA], [https://pdbe.org/7nuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nuk RCSB], [https://www.ebi.ac.uk/pdbsum/7nuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nuk ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Wang~~, M]]	+	__TOC__
-	[[Category: ~~Oerlemans, R~~]]	+	</StructureSection>
-	[[Category: Eris, D]]	+	[[Category: Large Structures]]
-	[[Category: ~~Sharpe, M~~]]	+	[[Category: Domling A]]
-	[[Category: ~~Domling, A~~]]	+	[[Category: Eris D]]
-	[[Category: ~~Groves,~~ M.R]]	+	[[Category: Groves MR]]
		+	[[Category: Oerlemans R]]
		+	[[Category: Sharpe M]]
		+	[[Category: Wang M]]

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

OCA — Wed, 24 Mar 2021 05:38:22 GMT

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

←Older revision

Revision as of 05:38, 24 March 2021

OCA: New page: '''Unreleased structure''' The entry 7nuk is ON HOLD until Paper Publication Authors: Oerlemans, R., Eris, D., Wang, M., Sharpe, M., Domling, A., Groves, M.R. Description: Crystal stru...

OCA — Wed, 24 Mar 2021 05:38:21 GMT

New page: '''Unreleased structure''' The entry 7nuk is ON HOLD until Paper Publication Authors: Oerlemans, R., Eris, D., Wang, M., Sharpe, M., Domling, A., Groves, M.R. Description: Crystal stru...

New page

'''Unreleased structure'''

The entry 7nuk is ON HOLD until Paper Publication

Authors: Oerlemans, R., Eris, D., Wang, M., Sharpe, M., Domling, A., Groves, M.R.

Description: Crystal structure of SARS CoV2 main protease in complex with EG009 (modelled using PanDDA event map)
[[Category: Unreleased Structures]]
[[Category: Wang, M]]
[[Category: Oerlemans, R]]
[[Category: Eris, D]]
[[Category: Sharpe, M]]
[[Category: Domling, A]]
[[Category: Groves, M.R]]